Q9BQL6 (FERM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fermitin family homolog 1

Alternative name(s):
Kindlerin
Kindlin syndrome protein
Kindlin-1
Unc-112-related protein 1

Gene names

Name:	FERMT1
Synonyms:	C20orf42, KIND1, URP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	677 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in cell adhesion. Contributes to integrin activation. When coexpressed with talin, potentiates activation of ITGA2B. Required for normal keratinocyte proliferation. Required for normal polarization of basal keratinocytes in skin, and for normal cell shape. Required for normal adhesion of keratinocytes to fibronectin and laminin, and for normal keratinocyte migration to wound sites. May mediate TGF-beta 1 signaling in tumor progression. Ref.8 Ref.9 Ref.11
Subunit structure	Interacts with the cytoplasmic domain of integrins ITGB1 and ITGB3. Ref.8
Subcellular location	Cytoplasm › cytoskeleton. Cell junction › focal adhesion. Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Note: Constituent of focal adhesions. Localized at the basal aspect of skin keratinocytes, close to the cell membrane. Colocalizes with filamentous actin. Upon TGFB1 treatment, it localizes to membrane ruffles. Ref.2 Ref.8 Ref.9 Ref.11
Tissue specificity	Expressed in brain, skeletal muscle, kidney, colon, adrenal gland, prostate, and placenta. Weakly or not expressed in heart, thymus, spleen, liver, small intestine, bone marrow, lung and peripheral blood leukocytes. Overexpressed in some colon and lung tumors. In skin, it is localized within the epidermis and particularly in basal keratocytes. Not detected in epidermal melanocytes and dermal fibroblasts. Ref.1 Ref.2 Ref.7 Ref.8 Ref.9
Induction	By TGFB1. Ref.8
Domain	The FERM domain is not correctly detected by PROSITE or Pfam techniques because it contains the insertion of a PH domain. The FERM domain contains the subdomains F1, F2 and F3. It is preceded by a F0 domain with a ubiquitin-like fold. The F0 domain is required for integrin activation and for localization at focal adhesions. Ref.11
Involvement in disease	Kindler syndrome (KINDS) [MIM:173650]: Autosomal recessive skin disorder characterized by skin blistering, photosensitivity, progressive poikiloderma, and extensive skin atrophy. Additional clinical features include gingival erosions, ocular, esophageal, gastrointestinal and urogenital involvement, and an increased risk of mucocutaneous malignancy. Note: The disease is caused by mutations affecting the gene represented in this entry. Although most FERMT1 mutations are predicted to lead to premature termination of translation, and to loss of FERMT1 function, significant clinical variability is observed among patients. There is an association of FERMT1 missense and in-frame deletion mutations with milder disease phenotypes, and later onset of complications (Ref.14). Ref.2 Ref.7 Ref.14
Sequence similarities	Belongs to the kindlin family. Contains 1 FERM domain. Contains 1 PH domain.
Sequence caution	The sequence BAA91358.1 differs from that shown. Reason: Erroneous initiation. The sequence BAC03826.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from direct assay Ref.9. Source: UniProtKB establishment of epithelial cell polarity Inferred from direct assay Ref.9. Source: UniProtKB keratinocyte migration Inferred from direct assay Ref.9. Source: UniProtKB keratinocyte proliferation Inferred from direct assay Ref.9. Source: UniProtKB
Cellular_component	cell junction Inferred from direct assay Ref.9. Source: UniProtKB cytosol Inferred from direct assay Ref.9. Source: UniProtKB filamentous actin Inferred from electronic annotation. Source: Compara focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BQL6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9BQL6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     541-554: QNVAQMPLVEAKLR → LQAPFHSYRSLSHL
     555-677: Missing.

Isoform 3 (identifier: Q9BQL6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-447: Missing.

Isoform 4 (identifier: Q9BQL6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     458-495: ENQYAQWMAA...VLNILSFLRM → VSKTPKILSH...ALLCHSAIAL
     496-677: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 677	677	Fermitin family homolog 1		PRO_0000219452
Regions
	Domain	96 – 653	558	FERM
	Domain	377 – 473	97	PH
	Compositional bias	147 – 154	8	Poly-Lys
Amino acid modifications
	Modified residue	170	1	Phosphoserine Ref.10
	Modified residue	179	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	1 – 447	447	Missing in isoform 3.		VSP_003809
	Alternative sequence	458 – 495	38	ENQYA…SFLRM → VSKTPKILSHFTSTKPKSKT QKCFHKFRALLCHSAIAL in isoform 4.		VSP_009224
	Alternative sequence	496 – 677	182	Missing in isoform 4.		VSP_009225
	Alternative sequence	541 – 554	14	QNVAQ…EAKLR → LQAPFHSYRSLSHL in isoform 2.		VSP_003810
	Alternative sequence	555 – 677	123	Missing in isoform 2.		VSP_003811
	Natural variant	100	1	Missing in KINDS. Ref.14		VAR_066942
	Natural variant	160	1	I → T. Corresponds to variant rs16991866 [ dbSNP | Ensembl ].		VAR_048368
	Natural variant	241	1	V → A. Corresponds to variant rs55666319 [ dbSNP | Ensembl ].		VAR_061035
	Natural variant	400	1	S → P in KINDS. Ref.14		VAR_066943
	Natural variant	526	1	R → K. Ref.1 Ref.3 Corresponds to variant rs2232074 [ dbSNP | Ensembl ].		VAR_014398
	Natural variant	534	1	A → T. Corresponds to variant rs2232078 [ dbSNP | Ensembl ].		VAR_014399
	Natural variant	559	1	W → R in KINDS. Ref.14		VAR_066944
	Natural variant	623	1	Missing in KINDS. Ref.14		VAR_066945
Experimental info
	Sequence conflict	117	1	V → A in BAC03826. Ref.4
	Sequence conflict	262	1	I → T in BAC03826. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 7354DCD84C516F90	FASTA	677	77,437
	10 20 30 40 50 60 MLSSTDFTFA SWELVVRVDH PNEEQQKDVT LRVSGDLHVG GVMLKLVEQI NISQDWSDFA 70 80 90 100 110 120 LWWEQKHCWL LKTHWTLDKY GVQADAKLLF TPQHKMLRLR LPNLKMVRLR VSFSAVVFKA 130 140 150 160 170 180 VSDICKILNI RRSEELSLLK PSGDYFKKKK KKDKNNKEPI IEDILNLESS PTASGSSVSP 190 200 210 220 230 240 GLYSKTMTPI YDPINGTPAS STMTWFSDSP LTEQNCSILA FSQPPQSPEA LADMYQPRSL 250 260 270 280 290 300 VDKAKLNAGW LDSSRSLMEQ GIQEDEQLLL RFKYYSFFDL NPKYDAVRIN QLYEQARWAI 310 320 330 340 350 360 LLEEIDCTEE EMLIFAALQY HISKLSLSAE TQDFAGESEV DEIEAALSNL EVTLEGGKAD 370 380 390 400 410 420 SLLEDITDIP KLADNLKLFR PKKLLPKAFK QYWFIFKDTS IAYFKNKELE QGEPLEKLNL 430 440 450 460 470 480 RGCEVVPDVN VAGRKFGIKL LIPVADGMNE MYLRCDHENQ YAQWMAACML ASKGKTMADS 490 500 510 520 530 540 SYQPEVLNIL SFLRMKNRNS ASQVASSLEN MDMNPECFVS PRCAKRHKSK QLAARILEAH 550 560 570 580 590 600 QNVAQMPLVE AKLRFIQAWQ SLPEFGLTYY LVRFKGSKKD DILGVSYNRL IKIDAATGIP 610 620 630 640 650 660 VTTWRFTNIK QWNVNWETRQ VVIEFDQNVF TAFTCLSADC KIVHEYIGGY IFLSTRSKDQ 670 NETLDEDLFH KLTGGQD
	Isoform 2 [UniParc]. Checksum: 51FE18BC2DFE0542	FASTA	554	63,235
	10 20 30 40 50 60 MLSSTDFTFA SWELVVRVDH PNEEQQKDVT LRVSGDLHVG GVMLKLVEQI NISQDWSDFA 70 80 90 100 110 120 LWWEQKHCWL LKTHWTLDKY GVQADAKLLF TPQHKMLRLR LPNLKMVRLR VSFSAVVFKA 130 140 150 160 170 180 VSDICKILNI RRSEELSLLK PSGDYFKKKK KKDKNNKEPI IEDILNLESS PTASGSSVSP 190 200 210 220 230 240 GLYSKTMTPI YDPINGTPAS STMTWFSDSP LTEQNCSILA FSQPPQSPEA LADMYQPRSL 250 260 270 280 290 300 VDKAKLNAGW LDSSRSLMEQ GIQEDEQLLL RFKYYSFFDL NPKYDAVRIN QLYEQARWAI 310 320 330 340 350 360 LLEEIDCTEE EMLIFAALQY HISKLSLSAE TQDFAGESEV DEIEAALSNL EVTLEGGKAD 370 380 390 400 410 420 SLLEDITDIP KLADNLKLFR PKKLLPKAFK QYWFIFKDTS IAYFKNKELE QGEPLEKLNL 430 440 450 460 470 480 RGCEVVPDVN VAGRKFGIKL LIPVADGMNE MYLRCDHENQ YAQWMAACML ASKGKTMADS 490 500 510 520 530 540 SYQPEVLNIL SFLRMKNRNS ASQVASSLEN MDMNPECFVS PRCAKRHKSK QLAARILEAH 550 LQAPFHSYRS LSHL
	Isoform 3 [UniParc]. Checksum: 90D6CC89DBCA8BC6	FASTA	230	26,498
	10 20 30 40 50 60 MNEMYLRCDH ENQYAQWMAA CMLASKGKTM ADSSYQPEVL NILSFLRMKN RNSASQVASS 70 80 90 100 110 120 LENMDMNPEC FVSPRCAKRH KSKQLAARIL EAHQNVAQMP LVEAKLRFIQ AWQSLPEFGL 130 140 150 160 170 180 TYYLVRFKGS KKDDILGVSY NRLIKIDAAT GIPVTTWRFT NIKQWNVNWE TRQVVIEFDQ 190 200 210 220 230 NVFTAFTCLS ADCKIVHEYI GGYIFLSTRS KDQNETLDED LFHKLTGGQD
	Isoform 4 [UniParc]. Checksum: 2DD52A11D0630636	FASTA	495	56,516
	10 20 30 40 50 60 MLSSTDFTFA SWELVVRVDH PNEEQQKDVT LRVSGDLHVG GVMLKLVEQI NISQDWSDFA 70 80 90 100 110 120 LWWEQKHCWL LKTHWTLDKY GVQADAKLLF TPQHKMLRLR LPNLKMVRLR VSFSAVVFKA 130 140 150 160 170 180 VSDICKILNI RRSEELSLLK PSGDYFKKKK KKDKNNKEPI IEDILNLESS PTASGSSVSP 190 200 210 220 230 240 GLYSKTMTPI YDPINGTPAS STMTWFSDSP LTEQNCSILA FSQPPQSPEA LADMYQPRSL 250 260 270 280 290 300 VDKAKLNAGW LDSSRSLMEQ GIQEDEQLLL RFKYYSFFDL NPKYDAVRIN QLYEQARWAI 310 320 330 340 350 360 LLEEIDCTEE EMLIFAALQY HISKLSLSAE TQDFAGESEV DEIEAALSNL EVTLEGGKAD 370 380 390 400 410 420 SLLEDITDIP KLADNLKLFR PKKLLPKAFK QYWFIFKDTS IAYFKNKELE QGEPLEKLNL 430 440 450 460 470 480 RGCEVVPDVN VAGRKFGIKL LIPVADGMNE MYLRCDHVSK TPKILSHFTS TKPKSKTQKC 490 FHKFRALLCH SAIAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"URP1: a member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas." Weinstein E.J., Bourner M., Head R., Zakeri H., Bauer C., Mazzarella R. Biochim. Biophys. Acta 1637:207-216(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT LYS-526. Tissue: Colon cancer.
[2]	"Loss of kindlin-1, a human homolog of the Caenorhabditis elegans actin-extracellular-matrix linker protein UNC-112, causes Kindler syndrome." Siegel D.H., Ashton G.H.S., Penagos H.G., Lee J.V., Feiler H.S., Wilhelmsen K.C., South A.P., Smith F.J.D., Prescott A.R., Wessagowit V., Oyama N., Akiyama M., Al-Aboud D., Al-Aboud K., Al-Githami A., Al-Hawsawi K., Al-Ismaily A., Al-Suwaid R. , Atherton D.J., Caputo R., Fine J.-D., Frieden I.J., Fuchs E., Haber R.M., Harada T., Kitajima Y., Mallory S.B., Ogawa H., Sahin S., Shimizu H., Suga Y., Tadini G., Tsuchiya K., Wiebe C.B., Wojnarowska F., Zaghloul A.B., Hamada T., Mallipeddi R., Eady R.A.J., McLean W.H.I., McGrath J.A., Epstein E.H. Jr. Am. J. Hum. Genet. 73:174-187(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN KINDS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT LYS-526. Tissue: Colon, Hepatoma and Teratocarcinoma.
[4]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Brain.
[7]	"Identification of mutations in a new gene encoding a FERM family protein with a pleckstrin homology domain in Kindler syndrome." Jobard F., Bouadjar B., Caux F., Hadj-Rabia S., Has C., Matsuda F., Weissenbach J., Lathrop M., Prud'homme J.-F., Fischer J. Hum. Mol. Genet. 12:925-935(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN KINDS, TISSUE SPECIFICITY.
[8]	"The Kindler syndrome protein is regulated by transforming growth factor-beta and involved in integrin-mediated adhesion." Kloeker S., Major M.B., Calderwood D.A., Ginsberg M.H., Jones D.A., Beckerle M.C. J. Biol. Chem. 279:6824-6833(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH ITGB1 AND ITGB3.
[9]	"Kindlin-1 is a phosphoprotein involved in regulation of polarity, proliferation, and motility of epidermal keratinocytes." Herz C., Aumailley M., Schulte C., Schlotzer-Schrehardt U., Bruckner-Tuderman L., Has C. J. Biol. Chem. 281:36082-36090(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-179, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"The structure of the N-terminus of kindlin-1: a domain important for alphaIIbbeta3 integrin activation." Goult B.T., Bouaouina M., Harburger D.S., Bate N., Patel B., Anthis N.J., Campbell I.D., Calderwood D.A., Barsukov I.L., Roberts G.C., Critchley D.R. J. Mol. Biol. 394:944-956(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN.
[12]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Kindler syndrome: extension of FERMT1 mutational spectrum and natural history." Has C., Castiglia D., del Rio M., Diez M.G., Piccinni E., Kiritsi D., Kohlhase J., Itin P., Martin L., Fischer J., Zambruno G., Bruckner-Tuderman L. Hum. Mutat. 32:1204-1212(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS KINDS ARG-100 DEL; PRO-400; ARG-559 AND ILE-623 DEL.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF443278 mRNA. Translation: AAN75822.1. AY137240 mRNA. Translation: AAM94174.1. AK000123 mRNA. Translation: BAA90957.1. AK000747 mRNA. Translation: BAA91358.1. Different initiation. AK092195 mRNA. Translation: BAC03826.1. Different initiation. AL118505 Genomic DNA. Translation: CAC03433.2. CH471133 Genomic DNA. Translation: EAX10392.1. CH471133 Genomic DNA. Translation: EAX10393.1. BC035882 mRNA. Translation: AAH35882.1.
IPI	IPI00220602. IPI00304754. IPI00383562. IPI00643475.
RefSeq	NP_060141.3. NM_017671.4.
UniGene	Hs.472054.
3D structure databases
ProteinModelPortal	Q9BQL6.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000217289.
PTM databases
PhosphoSite	Q9BQL6.
Polymorphism databases
DMDM	26392456.
Proteomic databases
PaxDb	Q9BQL6.
PRIDE	Q9BQL6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000217289; ENSP00000217289; ENSG00000101311.
GeneID	55612.
KEGG	hsa:55612.
UCSC	uc002wmq.3. human. uc002wmr.3. human. uc002wms.3. human.
Organism-specific databases
CTD	55612.
GeneCards	GC20M006055.
H-InvDB	HIX0015632.
HGNC	HGNC:15889. FERMT1.
HPA	HPA039778. HPA041966.
MIM	173650. phenotype. 607900. gene.
neXtProt	NX_Q9BQL6.
Orphanet	2907. Hereditary acrokeratotic poikiloderma, Weary type. 2908. Kindler syndrome.
PharmGKB	PA162388314.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG238024.
HOGENOM	HOG000231715.
HOVERGEN	HBG020688.
InParanoid	Q9BQL6.
OMA	ADSSYQP.
OrthoDB	EOG4RBQJ4.
PhylomeDB	Q9BQL6.
Gene expression databases
ArrayExpress	Q9BQL6.
Bgee	Q9BQL6.
CleanEx	HS_FERMT1.
Genevestigator	Q9BQL6.
GermOnline	ENSG00000101311. Homo sapiens.
Family and domain databases
Gene3D	1.20.80.10. 2 hits. 2.30.29.30. 2 hits.
InterPro	IPR019749. Band_41_domain. IPR014352. FERM/acyl-CoA-bd_prot_3-hlx. IPR019748. FERM_central. IPR018979. FERM_N. IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. [Graphical view]
Pfam	PF00373. FERM_M. 1 hit. PF09379. FERM_N. 1 hit. [Graphical view]
SMART	SM00295. B41. 1 hit. SM00233. PH. 1 hit. [Graphical view]
SUPFAM	SSF47031. FERM_3-hlx. 1 hit.
PROSITE	PS00660. FERM_1. False negative. PS00661. FERM_2. 1 hit. PS50057. FERM_3. False negative. PS50003. PH_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	55612.
NextBio	60184.
SOURCE	Search...

Entry information

Entry name

FERM1_HUMAN

Accession

Primary (citable) accession number: Q9BQL6
Secondary accession number(s): D3DW10 , Q8IX34, Q8IYH2, Q9NWM2, Q9NXQ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.