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P59113

- FERM1_MOUSE

UniProt

P59113 - FERM1_MOUSE

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Protein

Fermitin family homolog 1

Gene
Fermt1, Kind1, Urp1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 By similarity.

GO - Biological processi

  1. cell adhesion Source: UniProtKB
  2. establishment of epithelial cell polarity Source: UniProtKB
  3. keratinocyte migration Source: UniProtKB
  4. keratinocyte proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Fermitin family homolog 1
Alternative name(s):
Kindlin-1
Unc-112-related protein 1
Gene namesi
Name:Fermt1
Synonyms:Kind1, Urp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:2443583. Fermt1.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Cell junctionfocal adhesion By similarity. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side By similarity
Note: Colocalizes with filamentous actin. Constituent of focal adhesions By similarity. Localized at the basal aspect of skin keratinocytes, close to the cell membrane By similarity. Upon TGFB1 treatment, it localizes to membrane ruffles By similarity.

GO - Cellular componenti

  1. cell junction Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-SubCell
  3. cytosol Source: UniProtKB
  4. focal adhesion Source: MGI
  5. ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are born with the expected Mendelian distribution and appear normal at birth, but fail to thrive, become dehydrated and die after three to five days. They develop skin atrophy and die due to a lethal intestinal epithelial dysfunction. The colon is shortened and swollen and presents signs of acute inflammation. At the time of death, about 80% of the colonic epithelium is detached.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 677677Fermitin family homolog 1PRO_0000219453Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei170 – 1701Phosphoserine By similarity
Modified residuei179 – 1791Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP59113.
PaxDbiP59113.
PRIDEiP59113.

PTM databases

PhosphoSiteiP59113.

Expressioni

Gene expression databases

BgeeiP59113.
GenevestigatoriP59113.

Interactioni

Subunit structurei

Interacts with the cytoplasmic domain of integrins ITGB1 and ITGB3 By similarity.

Protein-protein interaction databases

IntActiP59113. 1 interaction.
MINTiMINT-4139673.

Structurei

Secondary structure

677
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 55
Beta strandi12 – 198
Beta strandi26 – 338
Helixi39 – 5012
Beta strandi57 – 637
Turni64 – 674
Beta strandi68 – 703
Helixi77 – 804
Beta strandi88 – 925
Beta strandi372 – 3798
Beta strandi390 – 3978
Beta strandi400 – 4067
Helixi407 – 4093
Beta strandi415 – 4195
Beta strandi424 – 4307
Turni431 – 4344
Beta strandi435 – 44410
Beta strandi447 – 45711
Helixi458 – 47215
Helixi482 – 49615

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KMCNMR-A1-96[»]
4BBKX-ray2.10A364-509[»]
DisProtiDP00655.
ProteinModelPortaliP59113.
SMRiP59113. Positions 1-96, 370-497, 525-651.

Miscellaneous databases

EvolutionaryTraceiP59113.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini96 – 653558FERMAdd
BLAST
Domaini377 – 47397PHAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi147 – 1548Poly-Lys

Domaini

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 By similarity.1 Publication

Sequence similaritiesi

Belongs to the kindlin family.
Contains 1 FERM domain.
Contains 1 PH domain.

Phylogenomic databases

eggNOGiNOG238024.
GeneTreeiENSGT00390000013444.
HOGENOMiHOG000231715.
HOVERGENiHBG020688.
InParanoidiA2ANX1.
KOiK17082.
OMAiVSPRCAK.
OrthoDBiEOG7T7GSC.
TreeFamiTF314677.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 2 hits.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00295. B41. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
PROSITEiPS00661. FERM_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P59113-1 [UniParc]FASTAAdd to Basket

« Hide

MLSSGDLTSA SWELVVRVDH ANGEQQTEIT LRVSGDLHIG GVMLKLVEQM    50
NIAQDWSDYA LWWEQKRCWL LKTHWTLDKC GVQADANLLF TPQHKMLRLR 100
LPNAKTVRLR VSFSAVVFKA VADICKVLNI RRPEELSLLK PSSDYCKKKK 150
KKEKNSKEPV IEDILNLESS STSSGSPVSP GLYSKTMTPT YDPINGTPAL 200
STMTWFGDSP LTEQNCSVLA FSQPPPSPDV LADMFQPRSL VDKAKMNAGW 250
LDSSRSLMEQ SIQEDEQLQL RFKYYTFFDL NPKYDAVRIN QLYEQARWAV 300
LLEEIDCTEE EMLIFAALQY HISKLSQCAE IQDFATKSEV DEVEAALSSL 350
EVTLEGGKAD NTLEDITDIP KLADYLKLFR PKKLMLKACK QYWFVFKDTS 400
IAYFKNKELE QGEPIEKLNL RGCEIVPDVN VSGRKFGIKL LIPVADGMNE 450
VYLRCDHEDQ YARWMAACIL ASKGKTMADS SYQPEVISIL SFLKMKNRNS 500
SPLVASSLEN MDMNPECLVS PCCAKKHKSK QLAARILEAH HNVAQMPLVE 550
AKLQFIQAWQ SLPEFGLTYY LVRFKGSKKD DILGVAYNRL IRIDAVTGIP 600
VTTWRFANMK QWNVNWEIRQ VAIEFDQNVS IAFTCLSADC KIVHEYIGGY 650
IFLSTRSKDQ NETLDEDLFH KLTGGQD 677
Length:677
Mass (Da):76,941
Last modified:July 27, 2011 - v4
Checksum:i9B8B1876FA7621EE
GO

Sequence cautioni

The sequence AAH29093.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti522 – 5221C → R in AAH29093. 1 Publication
Sequence conflicti586 – 5861A → S in AAH29093. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL831763 Genomic DNA. Translation: CAM20382.1.
BC029093 mRNA. Translation: AAH29093.1. Different initiation.
BC042792 mRNA. No translation available.
AK050804 mRNA. Translation: BAC34417.1.
CCDSiCCDS38248.1.
RefSeqiNP_932146.2. NM_198029.2.
UniGeneiMm.209784.

Genome annotation databases

EnsembliENSMUST00000038280; ENSMUSP00000047616; ENSMUSG00000027356.
GeneIDi241639.
KEGGimmu:241639.
UCSCiuc008mno.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL831763 Genomic DNA. Translation: CAM20382.1 .
BC029093 mRNA. Translation: AAH29093.1 . Different initiation.
BC042792 mRNA. No translation available.
AK050804 mRNA. Translation: BAC34417.1 .
CCDSi CCDS38248.1.
RefSeqi NP_932146.2. NM_198029.2.
UniGenei Mm.209784.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KMC NMR - A 1-96 [» ]
4BBK X-ray 2.10 A 364-509 [» ]
DisProti DP00655.
ProteinModelPortali P59113.
SMRi P59113. Positions 1-96, 370-497, 525-651.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P59113. 1 interaction.
MINTi MINT-4139673.

PTM databases

PhosphoSitei P59113.

Proteomic databases

MaxQBi P59113.
PaxDbi P59113.
PRIDEi P59113.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000038280 ; ENSMUSP00000047616 ; ENSMUSG00000027356 .
GeneIDi 241639.
KEGGi mmu:241639.
UCSCi uc008mno.1. mouse.

Organism-specific databases

CTDi 55612.
MGIi MGI:2443583. Fermt1.

Phylogenomic databases

eggNOGi NOG238024.
GeneTreei ENSGT00390000013444.
HOGENOMi HOG000231715.
HOVERGENi HBG020688.
InParanoidi A2ANX1.
KOi K17082.
OMAi VSPRCAK.
OrthoDBi EOG7T7GSC.
TreeFami TF314677.

Miscellaneous databases

EvolutionaryTracei P59113.
NextBioi 385110.
PROi P59113.
SOURCEi Search...

Gene expression databases

Bgeei P59113.
Genevestigatori P59113.

Family and domain databases

Gene3Di 1.20.80.10. 2 hits.
2.30.29.30. 2 hits.
InterProi IPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view ]
Pfami PF00373. FERM_M. 1 hit.
PF00169. PH. 1 hit.
[Graphical view ]
SMARTi SM00295. B41. 1 hit.
SM00233. PH. 1 hit.
[Graphical view ]
SUPFAMi SSF47031. SSF47031. 1 hit.
PROSITEi PS00661. FERM_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "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] OF 1-152 AND 448-677.
    Tissue: Mammary fibroblast.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-677.
    Strain: C57BL/6J.
  4. "Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction."
    Ussar S., Moser M., Widmaier M., Rognoni E., Harrer C., Genzel-Boroviczeny O., Fassler R.
    PLoS Genet. 4:E1000289-E1000289(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  5. "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: STRUCTURE BY NMR OF 1-96, DOMAIN FERM.

Entry informationi

Entry nameiFERM1_MOUSE
AccessioniPrimary (citable) accession number: P59113
Secondary accession number(s): A2ANX1, Q8BQG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 107 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi