ambiguity in the definition of proteinfamily leads different researchers to wildly varying numbers. Terminology and usage As with many biological terms, the use of proteinfamily is somewhat context .... 35, 2132 2138, 1976. ref Other terms such as protein class , protein group , and protein sub family ... family was conceived at a time when very few protein structures or sequences were known at that time ... sequence when the sequences of a proteinfamily are compared see multiple sequence alignment ... Cdx proteinfamilyProtein structure resources Structural classification of proteins SCOP ... of the family. Ammonium transporter Protein Kinase transmission of biochemical signals Mitogen ... or MHC immune system Immunoglobulin superfamily immunity Globin proteinfamily oxygen binding ... gene regulation Heat Shock protein families stress response HSP60 family HSP70 family HSP90 ... Dynein Transcription factors Cdx proteinfamily External links http www.sanger.ac.uk Software Pfam ... organisms References Reflist DEFAULTSORT ProteinFamily Category Bioinformatics Category Proteins ...File Structural coverage of the human cyclophilin family.png thumb The human cyclophilin family, as represented by the structures of the isomerase domain s of some of its members. A proteinfamily is a group of evolution arily related protein s, and is often nearly synonymous with gene family . The term proteinfamily should not be confused with Family biology family as it is used in taxonomy. Proteins in a family descend from a common ancestor see homology biology homology and typically have similar protein structure three dimensional structures , functions, and significant sequence similarity ... tool for identifying the members of protein families. Currently, over 60,000 protein families have been defined, ref V.Kunin, I. Cases, A.J. Enrigh, V. de Lorenzo, C.A. Ouzounis, Myriads of protein families ..., Dayhoff introduced the concept of a protein superfamily. ref Dayhoff, M.O., Computer analysis ... more details
Pocket proteinfamily consists of three proteins ref name pmid15838516 cite journal author Cobrinik D title Pocket proteins and cell cycle control journal Oncogene volume 24 issue 17 pages 2796 809 year 2005 pmid 15838516 doi 10.1038 sj.onc.1208619 ref RB Retinoblastoma protein p107 Retinoblastoma like protein 1 p130 Retinoblastoma like protein 2 They play crucial roles in the metazoan cell cycle through interaction with members of the E2F transcription factor s family. References reflist protein stub Transcription factors g0 Category Protein families de Pocket Protein Familie es Familia de prote nas pocket ... more details
The WIPI proteinfamily W D repeat protein I nteracting with P hospho I nosides is an evolutionary conserved family of proteins. ref name pmid15602573 cite journal author Proikas Cezanne T, Waddell S, Gaugel A, Frickey T, Lupas A, Nordheim A title WIPI 1alpha WIPI49 , a member of the novel 7 bladed WIPI proteinfamily, is aberrantly expressed in human cancer and is linked to starvation induced autophagy journal Oncogene volume 23 issue 58 pages 9314 25 year 2004 month December pmid 15602573 doi 10.1038 sj.onc.1208331 url issn ref WIPI proteins contain WD repeat domain that fold into 7 bladed beta propeller s that function in autophagy . ref name pmid15602573 Members of this family include class wikitable Protein Gene Aliases Yeast WIPI 1 WIPI1 WIPI49, FLJ10055 Atg18 WIPI 2 WIPI2 Svp1a, DKFZP434J154 WIPI49 like protein 2 Atg21 WIPI 3 WDR45L 628 protein, WIPI49 like protein WIPI 4 WDR45 JM5 protein, WDRX1 References Reflist Protein stub Category Protein families ... more details
The EHD proteinfamily comprises a group of proteins protein that function in vesicle biology intracellular trafficking and that possess a dynamin like structural fold. In humans, four proteins are characterized as belonging to this family EHD1 EHD2 EHD3 EHD4 biochem stub cell biology stub Vesicular transport proteins Category Biochemistry Category Cell biology Category Protein families ... more details
Infobox proteinfamily Symbol DinI Name DinI like family image PDB 1ghh EBI.jpg width caption solution structure of dini Pfam PF06183 Pfam clan InterPro IPR010391 SMART PROSITE MEROPS SCOP 1ghh TCDB OPM family OPM protein CAZy CDD In molecular biology, the DinI like proteinfamily is a proteinfamilyfamily of short proteins . The family includes DNA damage inducible protein I DinI and related protein s. The SOS response , a set of cellular phenomena exhibited by eubacteria , is initiated by various causes that include DNA damage induced replication arrest, and is positively regulated by the co protease activity of RecA . Escherichia coli DinI, a LexA regulated SOS gene product, shuts off the initiation of the SOS response when overexpressed in vivo . Biochemistry Biochemical and genetics genetic studies indicated that DinI physically Proteinprotein interaction interact s with RecA to Enzyme inhibitor inhibit its co protease activity. ref name pmid12626715 cite journal author Yoshimasu M, Aihara H, Ito Y, Rajesh S, Ishibe S, Mikawa T, Yokoyama S, Shibata T title An NMR study on the interaction of Escherichia coli DinI with RecA ssDNA complexes journal Nucleic Acids Res. volume 31 issue 6 pages 1735 43 year 2003 month March pmid 12626715 pmc 152859 doi 10.1093 nar gkg256 url ref The secondary structure structure of DinI is known. ref name pmid11152126 cite journal author Ramirez BE, Voloshin ON, Camerini Otero RD, Bax A title Solution structure of DinI provides insight into its mode of RecA inactivation journal Protein Sci. volume 9 issue 11 pages 2161 9 year 2000 month November pmid 11152126 pmc 2144493 doi 10.1110 ps.9.11.2161 url ref References reflist InterPro content IPR010391 Category Protein families ... more details
Infobox proteinfamily Symbol DsbC N Name Disulfide bond isomerase protein N terminus image PDB 1t3b EBI.jpg width caption x ray structure of dsbc from haemophilus influenzae Pfam PF10411 Pfam clan InterPro IPR018950 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD In molecular biology, the DsbC proteinfamily is a family of prokaryotic disulfide bond isomerases . This family includes DsbC. DsbC is V shaped, where each arm is a DsbC monomer of two protein domain domains linked by a hinge and the N termini of each monomer join to form the protein dimer dimer interface at the base of the V, so are vital for dimerisation. ref name pmid10700276 cite journal author McCarthy AA, Haebel PW, Torronen A, Rybin V, Baker EN, Metcalf P title Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli journal Nat. Struct. Biol. volume 7 issue 3 pages 196 9 year 2000 month March pmid 10700276 doi 10.1038 73295 url ref DsbC is required for disulfide bond formation and functions as a disulfide bond isomerase during oxidative protein folding in bacteria bacterial periplasm . It also has Chaperone protein chaperone activity. ref name pmid16087673 cite journal author Hiniker A, Collet JF, Bardwell JC title Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC journal J. Biol. Chem. volume 280 issue 40 pages 33785 91 year 2005 month October pmid 16087673 doi 10.1074 jbc.M505742200 url ref References reflist InterPro content IPR018950 Category Protein domains ... more details
Infobox proteinfamily Symbol Fic Name Fic DOC family image PDB 2f6s EBI.jpg width caption structure of cell filamentation protein fic from helicobacter pylori Pfam PF02661 Pfam clan InterPro IPR003812 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD In molecular biology, the Fic DOC proteinfamily is a proteinfamilyfamily of proteins which includes the Fic f ilamentation i nduced by c AMP protein and doc d eath o n c uring protein. The Fic protein is involved in cell division and is suggested to be involved in the synthesis of p aminobenzoate or folate , indicating that the Fic protein and Cyclic adenosine monophosphate cAMP are involved in a regulatory mechanism of cell division via folate mmetabolism . ref name pmid1656497 cite journal author Komano T, Utsumi R, Kawamukai M title Functional analysis of the fic gene involved in regulation of cell division journal Res. Microbiol. volume 142 issue 2 3 pages 269 77 year 1991 pmid 1656497 doi url ref This family contains a central conserved sequence conserved protein motif motif HPFXXGNG in most members. The exact molecular function of these protein proteins is uncertain. P1 lysogen s of Escherichia coli carry the prophage as a stable low gene copy number copy number plasmid . The frequency with which viable cell biology cell s cured of prophage are produced is about 10 5 per cell per generation. ref name pmid1656497 cite journal author Komano T, Utsumi R, Kawamukai M title Functional analysis of the fic gene involved in regulation of cell division journal Res. Microbiol. volume 142 issue 2 3 pages 269 77 year 1991 pmid 1656497 doi url ref A significant part of this remarkable stability can be attributed to a plasmid encoded mechanism biology mechanism that causes death of Cell biology cells that have lost ... depends on a gene named doc death on curing that is represented by this family. References reflist InterPro content IPR003812 Category Protein families ... more details
The Cdx proteinfamily is a group of the transcription factor proteins which bind to DNA to regulate the expression of genes. ref M. B land & al. Cdx1 autoregulation is governed by a novel Cdx1 LEF1 transcription complex , Molecular and Cellular Biology 24, 5028 5038, 2004. ref In particular this family of proteins can regulate the Hox genes . Cdx proteins CDX1 Cdx1 protein CDX1 Cdx2 protein Cdx4 protein The human Cdx2 familyprotein has 94 identity with the mouse Cdx2 and the hamster Cdx3. ref G. V. Mallo & al. Molecular cloning, sequencing and expression of the mRNA encoding human Cdx1 and Cdx2 homeobox. Down regulation of Cdx1 and Cdx2 mRNA expression during colorectal carcinogenesis , Int. J. Cancer. 74, 35 44, 1997. ref Cdx proteins and regulation of Hox gene expression Cdx proteins are key regulatiors of Hox genes . The vertebrate Cdx proteins act Upstream and downstream DNA upstream of Hox genes. Cdx genes integrate the posteriorizing Signal physiology signals from retionic acic and Wnt canonical pathways and relay this information to Hox Promoter biology promoter s. ref D. Lohnes. The Cdx1 homeodomain protein an integrator of posterior Signal physiology signaling in the mouse , Bioessays 25, 971 980, 2003. ref Expression in mouse embryo Cdx2 expression begins at 3.5 days and is confined to the trophectoderm , being absent from the inner cell mass. From 8.5 days, Cdx2 begins to be expressed in embryonic tissues, principally in the posterior part of the gut from its earliest formation. ref F. Beck. Expression of Cdx 2 in the mouse embryo and placenta possible role in patterning of the extra embryonic membranes , Developmental Dynamics 204, 219 227, 1995. ref See also ProteinProteinfamily transcription factor Neural tube References reflist External links Category Proteins Category Protein families ar de Cdx Proteine fa fr Prot ines Cdx ... more details
Infobox proteinfamily Symbol Dymeclin Name Dymeclin image width caption Pfam PF09742 Pfam clan CL0456 InterPro IPR019142 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD In molecular biology, the Dymeclin proteinfamily is a family of proteins which includes human DYM Dymeclin . Dymeclin Dyggve Melchior Clausen syndrome protein contains a large number of leucine and isoleucine residues and a total of 17 repeated dileucine protein motif motif s. It is characteristically about 700 amino acids long and present in plants and animal s. In humans, mutations in the gene coding for this protein give rise to a disorder called Dyggve Melchior Clausen syndrome, which is an autosomal recessive disorder characterised by the association of spondylo epi metaphyseal dysplasia and mental retardation . ref name pmid12554689 cite journal author El Ghouzzi V, Dagoneau N, Kinning E, Thauvin Robinet C, Chemaitilly W, Prost Squarcioni C, Al Gazali LI, Verloes A, Le Merrer M, Munnich A, Trembath RC, Cormier Daire V title Mutations in a novel gene Dymeclin FLJ20071 are responsible for Dyggve Melchior Clausen syndrome journal Hum. Mol. Genet. volume 12 issue 3 pages 357 64 year 2003 month February pmid 12554689 doi 10.1093 hmg ddg029 url ref This family of proteins also includes Hid1 high temperature induced dauer formation protein 1 from Caenorhabditis elegans which encodes a novel highly conserved putative transmembrane protein gene expression expressed in neurons . ref name pmid14504222 cite journal author Ailion M, Thomas JH title Isolation and characterization of high temperature induced Dauer formation mutants in Caenorhabditis elegans journal Genetics volume 165 issue 1 pages ... transmembrane domain s separated by regions of low complexity. Functionally this protein might ... protein or be a novel insulin receptor . ref name pmid14504222 References reflist InterPro content IPR019142 Category Protein families ... more details
Infobox proteinfamily Symbol Hyccin Name Hyccin image width caption Pfam PF09790 Pfam clan InterPro IPR018619 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD In molecular biology, the hyccin proteinfamily is a Proteinfamilyfamily of proteins which may have a role in the beta catenin Tcf LEF1 Lef signal transduction signaling pathway, as well as in the process of myelination of the Central nervous system central and peripheral nervous system . One member of this family is hyccin, encoded by the FAM126A gene. Defects in Hyccin are the cause of leukodystrophy hypomyelinating type 5 HLD5 ,this disorder is characterised by congenital cataracts , progressive neurologic impairment, and diffuse myelin deficiency. Affected individuals experience progressive Pyramidal cell pyramidal and cerebellar dysfunction, muscle weakness and wasting prevailing in the lower limbs. ref name pmid16951682 cite journal author Zara F, Biancheri R, Bruno C, Bordo L, Assereto S, Gazzerro E, Sotgia F, Wang XB, Gianotti S, Stringara S, Pedemonte M, Uziel G, Rossi A, Schenone A, Tortori Donati P, van der Knaap MS, Lisanti MP, Minetti C title Deficiency of hyccin, a newly identified membrane protein, causes hypomyelination and congenital cataract journal Nat. Genet. volume 38 issue 10 pages 1111 3 year 2006 month October pmid 16951682 doi 10.1038 ng1870 url ref ref name pmid10910037 cite journal author Kawasoe T, Furukawa Y, Daigo Y, Nishiwaki T, Ishiguro H, Fujita M, Satoh S, Miwa N, Nagasawa Y, Miyoshi Y, Ogawa M, Nakamura Y title Isolation and characterization of a novel human gene, DRCTNNB1A, the expression of which is down regulated by beta catenin journal Cancer Res. volume 60 issue 13 pages 3354 8 year 2000 month July pmid 10910037 doi url ref References reflist External links http www.ncbi.nlm.nih.gov books NBK2587 GeneReviews NCBI NIH UW entry on Hypomyelination and Congenital Cataract InterPro content IPR018619 Category Protein families ... more details
Infobox proteinfamily Symbol LETM1 Name LETM1 image width caption Pfam PF07766 Pfam clan InterPro IPR011685 SMART PROSITE MEROPS SCOP TCDB 8.A.20 OPM family OPM protein CAZy CDD LETM1 like is a Proteinfamilyfamily of evolutionarily related proteins . This is a group of mainly hypothetical eukaryotic protein s. Putative features found in LETM1, such as a transmembrane domain and a CK2 and PKC phosphorylation site, ref name pmid10486213 cite journal author Endele S, Fuhry M, Pak SJ, Zabel BU, Winterpacht A title LETM1, a novel gene encoding a putative EF hand Ca 2 binding protein, flanks the Wolf Hirschhorn syndrome WHS critical region and is deleted in most WHS patients journal Genomics volume 60 issue 2 pages 218 25 year 1999 month September pmid 10486213 doi 10.1006 geno.1999.5881 url ref are relatively conserved sequence conserved throughout the family. dfeletion geneitcs Deletion of LETM1 is thought to be involved in the developmental biology development of Wolf Hirschhorn syndrome in Homo sapiens human s. ref name pmid10486213 cite journal author Endele S, Fuhry M, Pak SJ, Zabel BU, Winterpacht A title LETM1, a novel gene encoding a putative EF hand Ca 2 binding protein, flanks the Wolf Hirschhorn syndrome WHS critical region and is deleted in most WHS patients journal Genomics volume 60 issue 2 pages 218 25 year 1999 month September pmid 10486213 doi 10.1006 geno.1999.5881 url ref A member of this family, http www.uniprot.org uniprot P91927 SWISSPROT , is known to be gene expression expressed in the mitochondria of Drosophila melanogaster , ref name pmid10071211 cite journal author Caggese C, Ragone G, Perrini B, Moschetti R, De Pinto V, Caizzi R, Barsanti P title ... be a group of mitochondrion mitochondrial protein proteins . Examples Human gene encoding members of this family include LETM1 , LETM2 , LETMD1 References reflist InterPro content IPR011685 Category Protein families ... more details
Infobox proteinfamily Symbol ArgJ Name ArgJ image PDB 1vz7 EBI.jpg width caption ornithine acetyltransferase orf6 gene product clavulanic acid biosynthesis from streptomyces clavuligerus Pfam PF01960 Pfam clan InterPro IPR002813 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD In molecular biology, members of the ArgJ proteinfamily are bifunctional protein that catalysis catalyses the first EC number 2.3.1.35 and fifth steps EC number 2.3.1.1 in arginine biosynthesis . ref name pmid8473852 cite journal author Sakanyan V, Charlier D, Legrain C, Kochikyan A, Mett I, Pierard A, Glansdorff N title Primary structure, partial purification and regulation of key enzymes of the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus dual function of ornithine acetyltransferase journal J. Gen. Microbiol. volume 139 issue 3 pages 393 402 year 1993 month March pmid 8473852 doi url ref The secondary structure structure has been determined for glutamic acid glutamate N acetyltransferase 2 ornithine acetyltransferase , an ArgJ like protein from Streptomyces clavuligerus . ref name pmid15352873 cite journal author Elkins JM, Kershaw NJ, Schofield CJ title X ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster journal Biochem. J. volume 385 issue Pt 2 pages 565 73 year 2005 month January pmid 15352873 pmc 1134730 doi 10.1042 BJ20040814 url ref References reflist InterPro content IPR002813 Category Protein families ... more details
Infobox proteinfamily Symbol CodY Name CodY image PDB 2b0l EBI.jpg width caption c terminal dna binding domain of transcriptional pleiotropic repressor cody. Pfam PF06018 Pfam clan CL0161 InterPro IPR010312 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD In molecular biology, the CodY proteinfamily consists of several bacteria bacterial GTP sensing Transcription genetics transcriptional pleiotropic repressor CodY protein s. CodY has been found to repress the dipeptide transport operon dpp of Bacillus subtilis in nutrient rich conditions. ref name pmid7783641 cite journal author Slack FJ, Serror P, Joyce E, Sonenshein AL title A gene required for nutritional repression of the Bacillus subtilis dipeptide permease operon journal Mol. Microbiol. volume 15 issue 4 pages 689 702 year 1995 month February pmid 7783641 doi url ref The CodY protein also has a repressor effect on many genes in Lactococcus lactis during cell growth growth in milk . ref name pmid11401725 cite journal author Guedon E, Serror P, Ehrlich SD, Renault P, Delorme C title Pleiotropic transcriptional repressor CodY senses the intracellular pool of branched chain amino acids in Lactococcus lactis journal Mol. Microbiol. volume 40 issue 5 pages 1227 39 year 2001 month June pmid 11401725 doi 10.1046 j.1365 2958.2001.02470.x url ref References reflist InterPro content IPR010312 Category Protein domains ... more details
Infobox proteinfamily Symbol FHIPEP Name FHIPEP image width caption structure of the cytoplasmic domain of flha from helicobacter pylori Pfam PF00771 Pfam clan InterPro IPR001712 SMART PROSITE PDOC00763 MEROPS SCOP TCDB 3.A.6 OPM family OPM protein CAZy CDD In molecular biology, the FHIPEP proteinfamily F lagellar H r I nvasion P roteins E xport P ore family consists of a number of protein proteins that constitute the type III secretion or signal peptide independent pathway apparatus. ref name pmid8253684 cite journal author Wei ZM, Beer SV title HrpI of Erwinia amylovora functions in secretion of harpin and is a member of a new proteinfamily journal J. Bacteriol. volume 175 issue 24 pages 7958 67 year 1993 month December pmid 8253684 pmc 206975 doi url ref ref name pmid8316211 cite journal author Gough CL, Genin S, Lopes V, Boucher CA title Homology between the HrpO protein of Pseudomonas solanacearum and bacterial proteins implicated in a signal peptide independent secretion mechanism journal Mol. Gen. Genet. volume 239 issue 3 pages 378 92 year 1993 month June pmid 8316211 doi url ref ref name pmid1365398 cite journal author Wandersman C title Secretion across the bacterial outer membrane journal Trends Genet. volume 8 issue 9 pages 317 22 year 1992 month September pmid 1365398 doi 10.1016 0168 9525 92 90264 5 url ref ref name pmid1592799 cite journal author Lory S title Determinants of extracellular protein secretion in gram negative bacteria journal J. Bacteriol. volume 174 issue 11 pages 3423 8 year 1992 month June pmid 1592799 pmc 206022 doi url ref This mechanism ... CA title Homology between the HrpO protein of Pseudomonas solanacearum and bacterial proteins implicated ... 3 pages 378 92 year 1993 month June pmid 8316211 doi url ref An FHIPEP protein is located within the inner ... of TM regions. It is possible that members of the FHIPEP family serve as pores for the export of specific proteins. References reflist InterPro content IPR001712 Category Protein families ... more details
Infobox proteinfamily Symbol Calreticulin Name Calreticulin image PDB 1k91 EBI.jpg width caption solution structure of calreticulin p domain subdomain residues 221 256 Pfam PF00262 Pfam clan InterPro IPR001580 SMART PROSITE PDOC00636 MEROPS SCOP 1jhn TCDB OPM family OPM protein CAZy CDD In molecular biology, the calreticulin proteinfamily is a family of calcium binding proteins . This family includes Calreticulin , Calnexin and CLGN Camlegin . ref name pmid1497605 cite journal author Michalak M, Milner RE, Burns K, Opas M title Calreticulin journal Biochem. J. volume 285 Pt 3 issue pages 681 92 year 1992 month August pmid 1497605 pmc 1132847 doi url ref ref name pmid8203019 cite journal author Bergeron JJ, Brenner MB, Thomas DY, Williams DB title Calnexin a membrane bound chaperone of the endoplasmic reticulum journal Trends Biochem. Sci. volume 19 issue 3 pages 124 8 year 1994 month March pmid 8203019 doi url ref ref name pmid8126001 cite journal author Watanabe D, Yamada K, Nishina Y, Tajima Y, Koshimizu U, Nagata A, Nishimune Y title Molecular cloning of a novel Ca 2 binding protein calmegin specifically expressed during male meiotic germ cell development journal J. Biol. Chem. volume 269 issue 10 pages 7744 9 year 1994 month March pmid 8126001 doi url ref References reflist InterPro content IPR001580 Category Protein families ... more details
Infobox proteinfamily Symbol ASD1 Name ASD1 image width caption Pfam PF08688 Pfam clan InterPro IPR014800 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD Infobox proteinfamily Symbol ASD2 ... TCDB OPM family OPM protein CAZy CDD In molecular biology, the Shroom proteinfamily is a small group of related protein s that are defined by sequence biology sequence similarity and in most cases by some link to the actin cytoskeleton. The Shroom Shrm proteinfamily is found only in animal s. protein Proteins of this family are predicted to be utilised in multiple morphogenic and developmental ... the founding member of the Shrm family is Shrm1 formerly Apx , it appears that this protein is found ... url ref In mice and humans, the Shrm proteinfamilyfamily of proteins consists of Shrm2 formerly Apxl , a protein involved in the morphogenesis, maintenance, and or function of vascular endothelial cell s. Shrm3 formerly Shroom , a protein necessary for neural tube closure in vertebrate developmental ... sapiens human s. This proteinfamily is based on the Conserved sequence conservation of a specific ... the evolutionarily conserved activity of Shroom family proteins journal J. Biol. Chem. volume ... Kiaa1202 is an actin associated protein implicated in cytoskeletal organization journal Cell Motil ... Domain 1 and a C terminal protein motif motif termed ASD2. ref name pmid16684770 cite journal author ... modulates the evolutionarily conserved activity of Shroom family proteins journal J. Biol ... is an actin associated protein implicated in cytoskeletal organization journal Cell Motil. Cytoskeleton ... actin binding protein, is required for neural tube morphogenesis in mice journal Cell volume ... proteins and do not appear in combination with other Conserved sequence conserved protein domain ... conserved activity of Shroom family proteins journal J. Biol. Chem. volume 281 issue 29 pages ... cite journal author Yoder M, Hildebrand JD title Shroom4 Kiaa1202 is an actin associated protein implicated ... more details
Infobox proteinfamily Symbol CAS CSE1 Name CAS CSE protein, C terminus image PDB 1z3h EBI.jpg width caption the exportin cse1 in its cargo free, cytoplasmic state Pfam PF03378 Pfam clan InterPro IPR005043 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD Infobox proteinfamily Symbol Cse1 Name Cse1 image PDB 1z3h EBI.jpg width caption the exportin cse1 in its cargo free, cytoplasmic state Pfam PF08506 Pfam clan CL0020 InterPro IPR013713 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD In molecular biology, the CAS CSE proteinfamily is a family of proteins which includes mammalian cellular apoptosis susceptibility CAS protein s and Saccharomyces cerevisiae yeast chromosome segregation protein, CSE1. ref name pmid7479798 cite journal author Brinkmann U, Brinkmann E, Gallo M, Pastan I title Cloning and characterization of a cellular apoptosis susceptibility gene, the human homologue to the yeast chromosome segregation gene CSE1 journal Proc. Natl. Acad. Sci. U.S.A. volume 92 issue 22 pages 10427 31 year 1995 month October pmid 7479798 pmc 40810 doi 10.1073 pnas.92.22.10427 url ref CAS is involved in both cellular apoptosis and proliferation . ref name pmid8639641 cite journal author Brinkmann U, Brinkmann E, Gallo M, Scherf U, Pastan I title Role of CAS, a human homologue to the yeast chromosome segregation gene CSE1, in toxin and tumor necrosis factor mediated apoptosis journal Biochemistry volume 35 issue 21 pages 6891 9 year 1996 month May pmid 8639641 ... 10.1086 301773 url ref The CAS CSE family of proteins consist of two protein domains domains . An N ... MC, Brinkmann U title The human CAS protein which is homologous to the CSE1 yeast chromosome segregation ... spindle , ref name pmid8610099 as is the protein MEK, which is thought to Transcriptional regulation ... 4 url ref The importin pathway mediates the nuclear transport of several protein s that are necessary ... Protein families ... more details
Orphan date September 2011 Infobox proteinfamily Symbol DSS1 SEM1 Name DSS1 SEM1 image PDB 1miu EBI.jpg width caption structure of a brca2 dss1 complex Pfam PF05160 Pfam clan InterPro IPR007834 SMART PROSITE MEROPS SCOP 1iyj TCDB OPM family OPM protein CAZy CDD In molecular biology, the DSS1 SEM1 proteinfamily is a family of short acidic proteins which includes the 26S proteasome complex subunits SEM1 from Saccharomyces cerevisiae and Drosophila and DSS1 SHFM1 in mammals . In Saccharomyces cerevisiae , SEM1 is a regulator of both exocyst function and pseudohyphal differentiation. ref name pmid9927667 cite journal author Jantti J, Lahdenranta J, Olkkonen VM, Soderlund H, Keranen S title SEM1, a homologue of the split hand split foot malformation candidate gene Dss1, regulates exocytosis and pseudohyphal differentiation in yeast journal Proc. Natl. Acad. Sci. U.S.A. volume 96 issue 3 pages 909 14 year 1999 month February pmid 9927667 pmc 15324 doi 10.1073 pnas.96.3.909 url ref Loss of DSS1 in Homo sapiens human has been associated with split hand split foot malformations. ref name pmid8782053 cite journal author Ignatius J, Knuutila S, Scherer SW, Trask B, Kere J title Split hand split foot malformation, deafness, and mental retardation with a complex cytogenetic rearrangement involving 7q21.3 journal J. Med. Genet. volume 33 issue 6 pages 507 10 year 1996 month June pmid 8782053 pmc 1050639 doi 10.1136 jmg.33.6.507 url ref References reflist InterPro content IPR007834 Category Protein families ... more details
Infobox proteinfamily Symbol CAP Name CAP image PDB 1smb EBI.jpg width caption crystal structure of golgi associated pr 1 protein Pfam PF00188 Pfam clan InterPro IPR014044 SMART PROSITE PDOC00835 MEROPS SCOP 1s0p TCDB OPM family OPM protein CAZy CDD Infobox proteinfamily Symbol Crisp Name Crisp domain image PDB 1rc9 EBI.jpg width caption crystal structure of stecrisp, a member of crisp family from trimeresurus stejnegeri refined at 1.6 angstroms resolution structual relationship of the two domains Pfam PF08562 Pfam clan CL0213 InterPro IPR013871 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD In molecular biology, the CAP proteinfamily c ysteine rich secretory proteins, a ntigen 5, and p athogenesis related 1 proteins CAP is a large family of proteins that are found in a wide range of organisms, including prokaryotes and non vertebrate eukaryotes . ref name pubmed12625841 Cite pmid 12625841 ref ref name pubmed12759345 Cite pmid 12759345 ref The nine subfamilies of the mammalian CAP super family include the human glioma pathogenesis related 1 GLIPR1 , Golgi associated pathogenesis related 1 GAPR1 proteins, peptidase inhibitor 15 PI15 , peptidase inhibitor 16 PI16 , cysteine rich secretory proteins CRISPs , CRISP LCCL domain containing 1 CRISPLD1 , CRISP LCCL domain containing 2 CRISPLD2 , mannose receptor like and the R3H domain containing like proteins. Members are most often secreted and have an extracellular endocrine or paracrine function and are involved ... . The overall protein structural conservation within the CAP super family results in fundamentally ... processes e.g. the CRISP proteins that members of this family are involved in, and also the sequence ... E, Dulhunty AF, O Bryan MK title The cysteine rich secretory protein domain of Tpx 1 is related to ion ... The cysteine rich secretory protein domain of Tpx 1 is related to ion channel toxins and regulates ... InterPro content IPR013871 Category Protein domains ... more details
Infobox proteinfamily Symbol CAP N Name CAP N terminal image PDB 1s0p EBI.jpg width caption structure of the n terminal domain of the adenylyl cyclase associated protein cap from dictyostelium discoideum. Pfam PF01213 Pfam clan InterPro IPR013992 SMART PROSITE PDOC00835 MEROPS SCOP 1s0p TCDB OPM family OPM protein CAZy CDD Infobox proteinfamily Symbol CAP C Name CAP C terminal image PDB 1kq5 EBI.jpg width caption c terminal domain of cyclase associated protein with pro 505 replaced by ser p505s ... family OPM protein CAZy CDD In molecular biology, the cyclase associated proteinfamily CAP is a family of highly conserved actin binding protein s present in a wide range of organism s including yeast, flies, plants, and mammal s. CAPs are multifunctional protein proteins that contain several structural ... family of proteins, because they are the only ones to directly Proteinprotein interaction interact ... Freeman NL, Field J title Mammalian homolog of the yeast cyclase associated protein, CAP Srv2p, regulates ... A title Crystallization of cyclase associated protein from Dictyostelium discoideum journal Acta Crystallogr ... for subsequent rounds of Protein filament filament assembly. ref name pmid17376963 cite journal ... associated protein 1 CAP1 promotes cofilin induced actin dynamics in mammalian nonmuscle cells journal .... Actin exists both as globular G monomeric actin protein subunit subunits and assembled into filamentous ... F actin often regulate F actin assembly and its interaction with other proteins, while proteins that Proteinprotein interaction interact with G actin often control the availability of unpolymerised ... adenylyl cyclase with cyclase associated protein CAP forms a second Ras binding site which mediates ... month January pmid 10594005 pmc 85033 doi url ref S. cerevisiae CAP has four major protein domain domains ... terminal domains as well . The proline rich domain interacts with profilin, a protein that catalysis ... protein CAP from Dictyostelium discoideum journal Structure volume 11 issue 9 pages 1171 8 year ... more details
Infobox proteinfamily Symbol BolA Name BolA image PDB 1ny8 EBI.jpg width caption solution structure of protein yrba from escherichia coli northeast structural genomics consortium target er115 Pfam PF01722 Pfam clan InterPro IPR002634 SMART PROSITE MEROPS SCOP 1v9j TCDB OPM family OPM protein CAZy CDD In molecular biology, the BolA like proteinfamily consists of the morpho protein BolA from Escherichia coli and its various homolog s. In E. coli , over expression of this protein causes round morphology biology morphology and may be involved in switching the cell biology cell between elongation and septation systems during cell cycle cell division . ref name pmid10361282 cite journal author Santos JM, Freire P, Vicente M, Arraiano CM title The stationary phase morphogene bolA from Escherichia coli is induced by stress during early stages of growth journal Mol. Microbiol. volume 32 issue 4 pages 789 98 year 1999 month May pmid 10361282 doi url ref The gene expression expression of BolA is cell growth growth rate regulated and is induced during the transition into the Stationary phase biology stationary phase . ref name pmid10361282 cite journal author Santos JM, Freire P, Vicente M, Arraiano CM title The stationary phase morphogene bolA from Escherichia coli is induced by Stress biology stress during early stages of growth journal Mol. Microbiol. volume 32 issue 4 pages 789 98 year 1999 month May pmid 10361282 doi url ref BolA is also induced by stress during early stages of growth ref name pmid10361282 cite journal author Santos JM, Freire P, Vicente M, Arraiano CM title The stationary phase morphogene bolA from Escherichia coli is induced by stress during early stages of growth journal Mol. Microbiol. volume 32 issue 4 pages 789 98 year 1999 month May pmid 10361282 doi url ref and may have a general role in stress response . It has also been suggested that BolA can ... reflist InterPro content IPR002634 Category Protein families ... more details
Pfam box Symbol ERM Name Ezrin radixin moesin family image 1E5W.png width caption X ray crystallography Crystallographic structure of the N terminal domain of moesin . ref name pmid11401550 PDB 1E5W cite journal author Edwards SD, Keep NH title The 2.7 crystal structure of the activated FERM domain of moesin an analysis of structural changes on activation journal Biochemistry volume 40 issue 24 pages 7061 8 year 2001 month June pmid 11401550 doi 10.1021 bi010419h url ref Pfam PF00769 InterPro IPR011259 SMART PROSITE SCOP 1ef1 TCDB OPM family OPM protein PDB PDB2 1ef1 , PDB2 1e5w , PDB2 1sgh The ERM proteinfamily consists of three closely related protein s, ezrin , ref name pmid6885906 cite journal author Bretscher A title Purification of an 80,000 dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells journal J. Cell Biol. volume 97 issue 2 pages 425 32 year 1983 month August pmid 6885906 pmc 2112519 doi 10.1083 jcb.97.2.425 url ref radixin ref name pmid2500445 cite journal author Tsukita S, Hieda Y, Tsukita S title A new 82 kD barbed end capping protein radixin localized in the cell to cell adherens junction purification and characterization journal J. Cell Biol. volume 108 issue 6 pages 2369 82 year 1989 month June pmid 2500445 pmc 2115614 doi 10.1083 jcb.108.6.2369 url ref and moesin . ref name pmid3046603 cite journal author Lankes W, Griesmacher A, Gr nwald J, Schwartz Albiez R, Keller R title A heparin binding protein involved in inhibition of smooth muscle cell proliferation journal Biochem. J. volume 251 issue 3 pages 831 42 year 1988 month May pmid 3046603 pmc 1149078 doi url ref ref name pmid9048483 ... the following three protein domain domains ref name pmid9048483 N terminus N terminal globular ... prevents either integral protein binding, or actin binding. if this head to tail interaction is disrupted ... of the molecule References Reflist 2 Category Protein families Protein stub ca ERM ... more details
Pfam box Symbol OmpW Name image 2f1v.gif width 200 caption Outer membrane protein W Pfam PF03922 InterPro IPR005618 SMART Prosite SCOP TCDB 1.B.39 OPM family 26 OPM protein 2f1v PDB PDB3 2f1v B 23 212 PDB3 2f1t A 23 212 Outer membrane protein W OmpW family is a Proteinfamilyfamily of evolutionarily related proteins from the outer bacterial membrane. This family includes outer membrane protein W OmpW proteins from a variety of bacterial species. This protein may form the receptor for S4 colicin s in Escherichia coli ref name PUB00008474 cite journal author Braun V, Pil sl H, Smajs D title Characterization of colicin S4 and its receptor, OmpW, a minor protein of the Escherichia coli outer membrane journal J. Bacteriol. volume 181 issue 11 pages 3578 3581 year 1999 pmid 10348872 pmc 93827 ref . References reflist Category Protein domains Category Protein families Category Outer membrane proteins membrane protein stub ... more details
Infobox proteinfamily Symbol HHA Name HHA image PDB 1jw2 EBI.jpg width caption solution structure of hemolysin expression modulating protein hha from escherichia coli. ontario centre for structural proteomics target ec0308 1 72 northeast structural genomics target et88 Pfam PF05321 Pfam clan InterPro IPR007985 SMART PROSITE MEROPS SCOP 1ir6 TCDB OPM family OPM protein CAZy CDD In molecular biology, the haemolysin expression modulating proteinfamily is a proteinfamilyfamily of proteins . This family consists of haemolysin gene expression expression modulating protein Hha from Escherichia coli and its Enterobacteria enterobacterial homologues, such as YmoA from Yersinia enterocolitica , and RmoA encoded on the R100 plasmid . These protein proteins act as modulators of bacteria bacterial gene expression . Members of this family act in conjunction with members of the H NS family, participating in the thermoregulation of different virulence factor s and in plasmid transfer. ref name pmid11890540 cite journal author Madrid C, Nieto JM, Juarez A title Role of the Hha YmoA family of proteins in the thermoregulation of the expression of virulence factors journal Int. J. Med. Microbiol. volume 291 issue 6 7 pages 425 32 year 2002 month February pmid 11890540 doi url ref Hha, along with the chromatin associated protein H NS, is involved in the regulation of expression genetics expression of the toxin alpha haemolysin in response to osmolarity and temperature . ref name pmid11790731 cite journal author Nieto JM, Madrid C, Miquelay E, Parra JL, Rodriguez S, Juarez A title Evidence for direct proteinprotein interaction between members of the enterobacterial Hha YmoA and H NS families ... December pmid 9851035 doi url ref The HHA proteinfamilyfamily of proteins display striking similarity to the oligomerisation protein domain domain of the H NS proteins. References reflist InterPro content IPR007985 Category Protein families ... more details
Infobox proteinfamily Symbol Fe S biosyn Name Fe S biosyn image PDB 1s98 EBI.jpg width caption e.coli isca crystal structure to 2.3 a Pfam PF01521 Pfam clan InterPro IPR000361 SMART PROSITE PDOC00887 MEROPS SCOP 1nwb TCDB OPM family OPM protein CAZy CDD In molecular biology, the iron sulfur cluster biosynthesis proteinfamily of includes proteins involved in Iron sulfur cluster Fe S cluster biogenesis iron sulfur cluster insertion protein, Fe S biogenesis protein . This family includes IscA, HesB, YadR and YfhF like protein s. The hesB gene is gene expression expressed only under nitrogen fixation conditions. ref name pmid10217509 cite journal author Huang TC, Lin RF, Chu MK, Chen HM title Organization and expression of nitrogen fixation genes in the aerobic nitrogen fixing unicellular cyanobacterium Synechococcus sp. strain RF 1 journal Microbiology Reading, Engl. volume 145 Pt 3 issue pages 743 53 year 1999 month March pmid 10217509 doi url ref IscA, an 11 kDa member of the hesB family of proteins, Molecular binding bind s iron and 2Fe 2S clusters, and participates in the biosynthesis of iron sulfur protein s. IscA is able to bind at least 2 iron ion s per protein dimer dimer . ref name pmid15050828 cite journal author Cupp Vickery JR, Silberg JJ, Ta DT, Vickery LE title Crystal structure of IscA, an iron sulfur cluster assembly protein from Escherichia coli journal J. Mol. Biol. volume 338 issue 1 pages 127 37 year 2004 month April pmid 15050828 doi 10.1016 j.jmb.2004.02.027 url ref Other members of this family include various hypothetical proteins that also contain the NifU like protein domain domain suggesting that they too are able to bind iron and are involved in Fe S cluster biogenesis. The HesB family are found in species as divergent as Homo sapiens Human and Haemophilus ..., a nitrogen fixation cluster protein, is highly conserved in evolution journal J. Mol. Evol. volume ... reflist InterPro content IPR000361 Category Protein families ... more details
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