ID FERM1_HUMAN Reviewed; 677 AA. AC Q9BQL6; D3DW10; Q8IX34; Q8IYH2; Q9NWM2; Q9NXQ3; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 02-SEP-2026, entry version 210. DE RecName: Full=Fermitin family homolog 1; DE AltName: Full=Kindlerin; DE AltName: Full=Kindlin syndrome protein; DE AltName: Full=Kindlin-1; DE AltName: Full=Unc-112-related protein 1; GN Name=FERMT1; Synonyms=C20orf42, KIND1, URP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT RP LYS-526. RC TISSUE=Colon cancer; RX PubMed=12697302; DOI=10.1016/s0925-4439(03)00035-8; RA Weinstein E.J., Bourner M., Head R., Zakeri H., Bauer C., Mazzarella R.; RT "URP1: a member of a novel family of PH and FERM domain-containing RT membrane-associated proteins is significantly over-expressed in lung and RT colon carcinomas."; RL Biochim. Biophys. Acta 1637:207-216(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN KNDLRS, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12789646; DOI=10.1086/376609; RA Siegel D.H., Ashton G.H.S., Penagos H.G., Lee J.V., Feiler H.S., RA Wilhelmsen K.C., South A.P., Smith F.J.D., Prescott A.R., Wessagowit V., RA Oyama N., Akiyama M., Al-Aboud D., Al-Aboud K., Al-Githami A., RA Al-Hawsawi K., Al-Ismaily A., Al-Suwaid R., Atherton D.J., Caputo R., RA Fine J.-D., Frieden I.J., Fuchs E., Haber R.M., Harada T., Kitajima Y., RA Mallory S.B., Ogawa H., Sahin S., Shimizu H., Suga Y., Tadini G., RA Tsuchiya K., Wiebe C.B., Wojnarowska F., Zaghloul A.B., Hamada T., RA Mallipeddi R., Eady R.A.J., McLean W.H.I., McGrath J.A., Epstein E.H. Jr.; RT "Loss of kindlin-1, a human homolog of the Caenorhabditis elegans actin- RT extracellular-matrix linker protein UNC-112, causes Kindler syndrome."; RL Am. J. Hum. Genet. 73:174-187(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), PARTIAL NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT LYS-526. RC TISSUE=Colon, Hepatoma, and Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP INVOLVEMENT IN KNDLRS, AND TISSUE SPECIFICITY. RX PubMed=12668616; DOI=10.1093/hmg/ddg097; RA Jobard F., Bouadjar B., Caux F., Hadj-Rabia S., Has C., Matsuda F., RA Weissenbach J., Lathrop M., Prud'homme J.-F., Fischer J.; RT "Identification of mutations in a new gene encoding a FERM family protein RT with a pleckstrin homology domain in Kindler syndrome."; RL Hum. Mol. Genet. 12:925-935(2003). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND RP INTERACTION WITH ITGB1 AND ITGB3. RX PubMed=14634021; DOI=10.1074/jbc.m307978200; RA Kloeker S., Major M.B., Calderwood D.A., Ginsberg M.H., Jones D.A., RA Beckerle M.C.; RT "The Kindler syndrome protein is regulated by transforming growth factor- RT beta and involved in integrin-mediated adhesion."; RL J. Biol. Chem. 279:6824-6833(2004). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION. RX PubMed=17012746; DOI=10.1074/jbc.m606259200; RA Herz C., Aumailley M., Schulte C., Schlotzer-Schrehardt U., RA Bruckner-Tuderman L., Has C.; RT "Kindlin-1 is a phosphoprotein involved in regulation of polarity, RT proliferation, and motility of epidermal keratinocytes."; RL J. Biol. Chem. 281:36082-36090(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-179, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=19804783; DOI=10.1016/j.jmb.2009.09.061; RA Goult B.T., Bouaouina M., Harburger D.S., Bate N., Patel B., Anthis N.J., RA Campbell I.D., Calderwood D.A., Barsukov I.L., Roberts G.C., RA Critchley D.R.; RT "The structure of the N-terminus of kindlin-1: a domain important for RT alphaIIbbeta3 integrin activation."; RL J. Mol. Biol. 394:944-956(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP VARIANTS KNDLRS ARG-100 DEL; PRO-400; ARG-559 AND ILE-623 DEL. RX PubMed=21936020; DOI=10.1002/humu.21576; RA Has C., Castiglia D., del Rio M., Diez M.G., Piccinni E., Kiritsi D., RA Kohlhase J., Itin P., Martin L., Fischer J., Zambruno G., RA Bruckner-Tuderman L.; RT "Kindler syndrome: extension of FERMT1 mutational spectrum and natural RT history."; RL Hum. Mutat. 32:1204-1212(2011). CC -!- FUNCTION: Involved in cell adhesion. Contributes to integrin CC activation. When coexpressed with talin, potentiates activation of CC ITGA2B. Required for normal keratinocyte proliferation. Required for CC normal polarization of basal keratinocytes in skin, and for normal cell CC shape. Required for normal adhesion of keratinocytes to fibronectin and CC laminin, and for normal keratinocyte migration to wound sites. May CC mediate TGF-beta 1 signaling in tumor progression. CC {ECO:0000269|PubMed:14634021, ECO:0000269|PubMed:17012746, CC ECO:0000269|PubMed:19804783}. CC -!- SUBUNIT: Interacts with the cytoplasmic domain of integrins ITGB1 and CC ITGB3. {ECO:0000269|PubMed:14634021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, focal CC adhesion. Cell projection, ruffle membrane; Peripheral membrane CC protein; Cytoplasmic side. Note=Constituent of focal adhesions. CC Localized at the basal aspect of skin keratinocytes, close to the cell CC membrane. Colocalizes with filamentous actin. Upon TGFB1 treatment, it CC localizes to membrane ruffles. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9BQL6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BQL6-2; Sequence=VSP_003810, VSP_003811; CC Name=3; CC IsoId=Q9BQL6-3; Sequence=VSP_003809; CC Name=4; CC IsoId=Q9BQL6-4; Sequence=VSP_009224, VSP_009225; CC -!- TISSUE SPECIFICITY: Expressed in brain, skeletal muscle, kidney, colon, CC adrenal gland, prostate, and placenta. Weakly or not expressed in CC heart, thymus, spleen, liver, small intestine, bone marrow, lung and CC peripheral blood leukocytes. Overexpressed in some colon and lung CC tumors. In skin, it is localized within the epidermis and particularly CC in basal keratocytes. Not detected in epidermal melanocytes and dermal CC fibroblasts. {ECO:0000269|PubMed:12668616, ECO:0000269|PubMed:12697302, CC ECO:0000269|PubMed:12789646, ECO:0000269|PubMed:14634021, CC ECO:0000269|PubMed:17012746}. CC -!- INDUCTION: By TGFB1. {ECO:0000269|PubMed:14634021}. CC -!- DOMAIN: The FERM domain is not correctly detected by PROSITE or Pfam CC techniques because it contains the insertion of a PH domain. The FERM CC domain contains the subdomains F1, F2 and F3. It is preceded by a F0 CC domain with a ubiquitin-like fold. The F0 domain is required for CC integrin activation and for localization at focal adhesions. CC {ECO:0000269|PubMed:19804783}. CC -!- DISEASE: Kindler syndrome (KNDLRS) [MIM:173650]: An autosomal recessive CC skin disorder characterized by skin blistering, photosensitivity, CC progressive poikiloderma, and extensive skin atrophy. Additional CC clinical features include gingival erosions, ocular, esophageal, CC gastrointestinal and urogenital involvement, and an increased risk of CC mucocutaneous malignancy. {ECO:0000269|PubMed:12668616, CC ECO:0000269|PubMed:12789646, ECO:0000269|PubMed:21936020}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. Although most FERMT1 mutations are predicted to lead to CC premature termination of translation, and to loss of FERMT1 function, CC significant clinical variability is observed among patients. There is CC an association of FERMT1 missense and in-frame deletion mutations with CC milder disease phenotypes, and later onset of complications CC (PubMed:21936020). {ECO:0000269|PubMed:21936020}. CC -!- SIMILARITY: Belongs to the kindlin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91358.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC03826.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF443278; AAN75822.1; -; mRNA. DR EMBL; AY137240; AAM94174.1; -; mRNA. DR EMBL; AK000123; BAA90957.1; -; mRNA. DR EMBL; AK000747; BAA91358.1; ALT_INIT; mRNA. DR EMBL; AK092195; BAC03826.1; ALT_INIT; mRNA. DR EMBL; AL118505; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10392.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10393.1; -; Genomic_DNA. DR EMBL; BC035882; AAH35882.1; -; mRNA. DR CCDS; CCDS13098.1; -. [Q9BQL6-1] DR RefSeq; NP_060141.3; NM_017671.5. [Q9BQL6-1] DR RefSeq; XP_024307703.1; XM_024451935.2. [Q9BQL6-1] DR RefSeq; XP_047296215.1; XM_047440259.1. [Q9BQL6-1] DR RefSeq; XP_054179606.1; XM_054323631.1. [Q9BQL6-1] DR RefSeq; XP_054179607.1; XM_054323632.1. [Q9BQL6-1] DR AlphaFoldDB; Q9BQL6; -. DR SMR; Q9BQL6; -. DR BioGRID; 120752; 43. DR FunCoup; Q9BQL6; 480. DR IntAct; Q9BQL6; 18. DR MINT; Q9BQL6; -. DR NDEx; IQUERY-CP-FERMT1; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000217289; -. DR BindingDB; Q9BQL6; -. DR ChEMBL; CHEMBL5465350; -. DR TCDB; 8.A.25.1.8; the ezrin/radixin/moesin (ezrin) family. DR GlyGen; Q9BQL6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BQL6; -. DR PhosphoSitePlus; Q9BQL6; -. DR SwissPalm; Q9BQL6; -. DR BioMuta; FERMT1; -. DR DMDM; 26392456; -. DR jPOST; Q9BQL6; -. DR MassIVE; Q9BQL6; -. DR PaxDb; 9606-ENSP00000217289; -. DR PeptideAtlas; Q9BQL6; -. DR ProteomicsDB; 78697; -. [Q9BQL6-1] DR ProteomicsDB; 78698; -. [Q9BQL6-2] DR ProteomicsDB; 78699; -. [Q9BQL6-3] DR ProteomicsDB; 78700; -. [Q9BQL6-4] DR Pumba; Q9BQL6; -. DR Antibodypedia; 8379; 235 antibodies from 28 providers. DR DNASU; 55612; -. DR Ensembl; ENST00000217289.9; ENSP00000217289.4; ENSG00000101311.18. [Q9BQL6-1] DR Ensembl; ENST00000699095.1; ENSP00000514127.1; ENSG00000101311.18. [Q9BQL6-1] DR Ensembl; ENST00000855451.1; ENSP00000525510.1; ENSG00000101311.18. [Q9BQL6-1] DR Ensembl; ENST00000855452.1; ENSP00000525511.1; ENSG00000101311.18. [Q9BQL6-1] DR Ensembl; ENST00000936598.1; ENSP00000606657.1; ENSG00000101311.18. [Q9BQL6-1] DR Ensembl; ENST00000936599.1; ENSP00000606658.1; ENSG00000101311.18. [Q9BQL6-1] DR Ensembl; ENST00000936600.1; ENSP00000606659.1; ENSG00000101311.18. [Q9BQL6-1] DR GeneID; 55612; -. DR KEGG; hsa:55612; -. DR MANE-Select; ENST00000217289.9; ENSP00000217289.4; NM_017671.5; NP_060141.3. DR UCSC; uc002wmr.3; human. [Q9BQL6-1] DR AGR; HGNC:15889; -. DR ClinPGx; PA162388314; -. DR CTD; 55612; -. DR DisGeNET; 55612; -. DR GeneCards; FERMT1; -. DR GeneReviews; FERMT1; -. DR HGNC; HGNC:15889; FERMT1. DR HPA; ENSG00000101311; Tissue enhanced (intestine). DR MalaCards; FERMT1; -. DR MIM; 173650; phenotype. DR MIM; 607900; gene. DR OpenTargets; ENSG00000101311; -. DR Orphanet; 2908; Kindler epidermolysis bullosa. DR VEuPathDB; HostDB:ENSG00000101311; -. DR eggNOG; KOG3727; Eukaryota. DR GeneTree; ENSGT00390000013444; -. DR HOGENOM; CLU_011611_0_0_1; -. DR InParanoid; Q9BQL6; -. DR OMA; GMFFCAP; -. DR OrthoDB; 10057618at2759; -. DR PAN-GO; Q9BQL6; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q9BQL6; -. DR PathwayCommons; Q9BQL6; -. DR SignaLink; Q9BQL6; -. DR SIGNOR; Q9BQL6; -. DR Agora; ENSG00000101311; -. DR BioGRID-ORCS; 55612; 44 hits in 1158 CRISPR screens. DR ChiTaRS; FERMT1; human. DR GeneWiki; C20orf42; -. DR GenomeRNAi; 55612; -. DR Pharos; Q9BQL6; Tbio. DR PRO; PR:Q9BQL6; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q9BQL6; protein. DR Bgee; ENSG00000101311; Expressed in mucosa of sigmoid colon and 166 other cell types or tissues. DR ExpressionAtlas; Q9BQL6; baseline and differential. DR GO; GO:0030054; C:cell junction; IDA:UniProtKB. DR GO; GO:0071944; C:cell periphery; IDA:ARUK-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:ARUK-UCL. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl. DR GO; GO:0005178; F:integrin binding; IBA:GO_Central. DR GO; GO:0071711; P:basement membrane organization; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB. DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central. DR GO; GO:0090162; P:establishment of epithelial cell polarity; IDA:UniProtKB. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:InterPro. DR GO; GO:0051546; P:keratinocyte migration; IDA:UniProtKB. DR GO; GO:0043616; P:keratinocyte proliferation; IDA:UniProtKB. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IEA:Ensembl. DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl. DR GO; GO:0051886; P:negative regulation of timing of anagen; IEA:Ensembl. DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IEA:Ensembl. DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IEA:Ensembl. DR GO; GO:0033625; P:positive regulation of integrin activation; IGI:ARUK-UCL. DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IEA:Ensembl. DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl. DR GO; GO:1903691; P:positive regulation of wound healing, spreading of epidermal cells; IGI:ARUK-UCL. DR CDD; cd14473; FERM_B-lobe; 1. DR CDD; cd13205; FERM_C_fermitin; 1. DR CDD; cd17180; FERM_F0_KIND1; 1. DR CDD; cd17183; FERM_F1_KIND1; 1. DR CDD; cd01237; PH_fermitin; 1. DR FunFam; 2.30.29.30:FF:000037; Fermitin family homolog 2; 1. DR FunFam; 2.30.29.30:FF:000057; Fermitin family homolog 2 (Drosophila); 1. DR FunFam; 3.10.20.90:FF:000035; Fermitin family homolog 2 (Drosophila); 1. DR Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 2. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR035963; FERM_2. DR InterPro; IPR019748; FERM_central. DR InterPro; IPR037843; Kindlin/fermitin. DR InterPro; IPR040790; Kindlin_2_N. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR037837; PH_Kindlin/fermitin. DR PANTHER; PTHR16160; FERMITIN 2-RELATED; 1. DR PANTHER; PTHR16160:SF12; FERMITIN FAMILY HOMOLOG 1; 1. DR Pfam; PF00373; FERM_M; 2. DR Pfam; PF18124; Kindlin_2_N; 1. DR SMART; SM00295; B41; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF50729; PH domain-like; 2. DR SUPFAM; SSF47031; Second domain of FERM; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane; KW Cell projection; Cytoplasm; Cytoskeleton; Disease variant; Membrane; KW Phosphoprotein; Proteomics identification; Reference proteome. FT CHAIN 1..677 FT /note="Fermitin family homolog 1" FT /id="PRO_0000219452" FT DOMAIN 96..653 FT /note="FERM" FT DOMAIN 377..473 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT MOD_RES 170 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 179 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 361 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..447 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_003809" FT VAR_SEQ 458..495 FT /note="ENQYAQWMAACMLASKGKTMADSSYQPEVLNILSFLRM -> VSKTPKILSH FT FTSTKPKSKTQKCFHKFRALLCHSAIAL (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009224" FT VAR_SEQ 496..677 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009225" FT VAR_SEQ 541..554 FT /note="QNVAQMPLVEAKLR -> LQAPFHSYRSLSHL (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_003810" FT VAR_SEQ 555..677 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_003811" FT VARIANT 100 FT /note="Missing (in KNDLRS)" FT /evidence="ECO:0000269|PubMed:21936020" FT /id="VAR_066942" FT VARIANT 160 FT /note="I -> T (in dbSNP:rs16991866)" FT /id="VAR_048368" FT VARIANT 241 FT /note="V -> A (in dbSNP:rs55666319)" FT /id="VAR_061035" FT VARIANT 400 FT /note="S -> P (in KNDLRS; dbSNP:rs869312718)" FT /evidence="ECO:0000269|PubMed:21936020" FT /id="VAR_066943" FT VARIANT 526 FT /note="R -> K (in dbSNP:rs2232074)" FT /evidence="ECO:0000269|PubMed:12697302, FT ECO:0000269|PubMed:14702039" FT /id="VAR_014398" FT VARIANT 534 FT /note="A -> T (in dbSNP:rs2232078)" FT /id="VAR_014399" FT VARIANT 559 FT /note="W -> R (in KNDLRS; dbSNP:rs869312719)" FT /evidence="ECO:0000269|PubMed:21936020" FT /id="VAR_066944" FT VARIANT 623 FT /note="Missing (in KNDLRS; dbSNP:rs869312721)" FT /evidence="ECO:0000269|PubMed:21936020" FT /id="VAR_066945" FT CONFLICT 117 FT /note="V -> A (in Ref. 4; BAC03826)" FT /evidence="ECO:0000305" FT CONFLICT 262 FT /note="I -> T (in Ref. 4; BAC03826)" FT /evidence="ECO:0000305" SQ SEQUENCE 677 AA; 77437 MW; 7354DCD84C516F90 CRC64; MLSSTDFTFA SWELVVRVDH PNEEQQKDVT LRVSGDLHVG GVMLKLVEQI NISQDWSDFA LWWEQKHCWL LKTHWTLDKY GVQADAKLLF TPQHKMLRLR LPNLKMVRLR VSFSAVVFKA VSDICKILNI RRSEELSLLK PSGDYFKKKK KKDKNNKEPI IEDILNLESS PTASGSSVSP GLYSKTMTPI YDPINGTPAS STMTWFSDSP LTEQNCSILA FSQPPQSPEA LADMYQPRSL VDKAKLNAGW LDSSRSLMEQ GIQEDEQLLL RFKYYSFFDL NPKYDAVRIN QLYEQARWAI LLEEIDCTEE EMLIFAALQY HISKLSLSAE TQDFAGESEV DEIEAALSNL EVTLEGGKAD SLLEDITDIP KLADNLKLFR PKKLLPKAFK QYWFIFKDTS IAYFKNKELE QGEPLEKLNL RGCEVVPDVN VAGRKFGIKL LIPVADGMNE MYLRCDHENQ YAQWMAACML ASKGKTMADS SYQPEVLNIL SFLRMKNRNS ASQVASSLEN MDMNPECFVS PRCAKRHKSK QLAARILEAH QNVAQMPLVE AKLRFIQAWQ SLPEFGLTYY LVRFKGSKKD DILGVSYNRL IKIDAATGIP VTTWRFTNIK QWNVNWETRQ VVIEFDQNVF TAFTCLSADC KIVHEYIGGY IFLSTRSKDQ NETLDEDLFH KLTGGQD //