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Integrin beta-1 (Fibronectin receptor subunit beta) (Glycoprotein IIa) (GPIIA) (VLA-4 subunit beta) (CD antigen CD29)

 ITB1_HUMAN              Reviewed;         798 AA.
P05556; A8K6N2; D3DRX9; D3DRY3; D3DRY4; D3DRY5; P78466; P78467;
Q13089; Q13090; Q13091; Q13212; Q14622; Q14647; Q29RW2; Q7Z3V1;
Q8WUM6;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 2.
25-OCT-2017, entry version 221.
RecName: Full=Integrin beta-1;
AltName: Full=Fibronectin receptor subunit beta;
AltName: Full=Glycoprotein IIa;
Short=GPIIA;
AltName: Full=VLA-4 subunit beta;
AltName: CD_antigen=CD29;
Flags: Precursor;
Name=ITGB1; Synonyms=FNRB, MDF2, MSK12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=2958481; DOI=10.1083/jcb.105.3.1183;
Argraves W.S., Suzuki S., Arai H., Thompson K., Pierschbacher M.D.,
Ruoslahti E.;
"Amino acid sequence of the human fibronectin receptor.";
J. Cell Biol. 105:1183-1190(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Endometrium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 717-757, CHARACTERIZATION OF
BETA-1B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=7681433; DOI=10.1083/jcb.121.1.171;
Balzac F., Belkin A.M., Koteliansky V.E., Balabanov Y.V., Altruda F.,
Silengo L., Tarone G.;
"Expression and functional analysis of a cytoplasmic domain variant of
the beta 1 integrin subunit.";
J. Cell Biol. 121:171-178(1993).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 717-757, AND FUNCTION.
PubMed=7523423; DOI=10.1083/jcb.127.2.557;
Balzac F., Retta S.F., Albini A., Melchiorri A., Koteliansky V.E.,
Geuna M., Silengo L., Tarone G.;
"Expression of beta 1B integrin isoform in CHO cells results in a
dominant negative effect on cell adhesion and motility.";
J. Cell Biol. 127:557-565(1994).
[9]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE
SPECIFICITY.
TISSUE=Skeletal muscle;
PubMed=2249781; DOI=10.1016/0378-1119(90)90369-3;
Altruda F., Cervella P., Tarone G., Botta C., Balzac F., Stefanuto G.,
Silengo L.;
"A human integrin beta 1 subunit with a unique cytoplasmic domain
generated by alternative mRNA processing.";
Gene 95:261-266(1990).
[10]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=1551917;
Languino L.R., Ruoslahti E.;
"An alternative form of the integrin beta 1 subunit with a variant
cytoplasmic domain.";
J. Biol. Chem. 267:7116-7120(1992).
[11]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
TISSUE=Skeletal muscle;
PubMed=7545396; DOI=10.1006/bbrc.1995.2285;
Zhidkova N.I., Belkin A.M., Mayne R.;
"Novel isoform of beta 1 integrin expressed in skeletal and cardiac
muscle.";
Biochem. Biophys. Res. Commun. 214:279-285(1995).
[12]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND TISSUE
SPECIFICITY.
PubMed=7544298; DOI=10.1016/0014-5793(95)00814-P;
van der Flier A., Kuikman I., Baudoin C., van der Neut R.,
Sonnenberg A.;
"A novel beta 1 integrin isoform produced by alternative splicing:
unique expression in cardiac and skeletal muscle.";
FEBS Lett. 369:340-344(1995).
[13]
PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 4), AND TISSUE SPECIFICITY.
PubMed=9494094; DOI=10.1042/bj3301255;
Svineng G., Faessler R., Johansson S.;
"Identification of beta1C-2, a novel variant of the integrin beta1
subunit generated by utilization of an alternative splice acceptor
site in exon C.";
Biochem. J. 330:1255-1263(1998).
[14]
PROTEIN SEQUENCE OF 775-784 (ISOFORM 5), IDENTIFICATION BY MASS
SPECTROMETRY, AND INTERACTION WITH ACE2.
PubMed=15276642; DOI=10.1016/j.bbadis.2004.05.005;
Lin Q., Keller R.S., Weaver B., Zisman L.S.;
"Interaction of ACE2 and integrin beta1 in failing human heart.";
Biochim. Biophys. Acta 1689:175-178(2004).
[15]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ECHOVIRUS 1
AND HUMAN ECHOVIRUS 8 CAPSID PROTEINS.
PubMed=8411387;
Bergelson J.M., St John N., Kawaguchi S., Chan M., Stubdal H.,
Modlin J., Finberg R.W.;
"Infection by echoviruses 1 and 8 depends on the alpha 2 subunit of
human VLA-2.";
J. Virol. 67:6847-6852(1993).
[16]
SUBCELLULAR LOCATION.
PubMed=8567725; DOI=10.1083/jcb.132.1.211;
Belkin A.M., Zhidkova N.I., Balzac F., Altruda F., Tomatis D.,
Maier A., Tarone G., Koteliansky V.E., Burridge K.;
"Beta 1D integrin displaces the beta 1A isoform in striated muscles:
localization at junctional structures and signaling potential in
nonmuscle cells.";
J. Cell Biol. 132:211-226(1996).
[17]
INTERACTION WITH LGALS3BP.
PubMed=9501082; DOI=10.1093/emboj/17.6.1606;
Sasaki T., Brakebusch C., Engel J., Timpl R.;
"Mac-2 binding protein is a cell-adhesive protein of the extracellular
matrix which self-assembles into ring-like structures and binds beta1
integrins, collagens and fibronectin.";
EMBO J. 17:1606-1613(1998).
[18]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 TAT.
PubMed=10397733;
Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S.,
Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.;
"The Tat protein of human immunodeficiency virus type-1 promotes
vascular cell growth and locomotion by engaging the alpha5beta1 and
alphavbeta3 integrins and by mobilizing sequestered basic fibroblast
growth factor.";
Blood 94:663-672(1999).
[19]
FUNCTION, SUBUNIT, INTERACTION WITH FAP, AND SUBCELLULAR LOCATION.
PubMed=10455171; DOI=10.1074/jbc.274.35.24947;
Mueller S.C., Ghersi G., Akiyama S.K., Sang Q.X., Howard L.,
Pineiro-Sanchez M., Nakahara H., Yeh Y., Chen W.T.;
"A novel protease-docking function of integrin at invadopodia.";
J. Biol. Chem. 274:24947-24952(1999).
[20]
INTERACTION WITH NMRK2.
TISSUE=Heart;
PubMed=10613898; DOI=10.1083/jcb.147.7.1391;
Li J., Mayne R., Wu C.;
"A novel muscle-specific beta 1 integrin binding protein (MIBP) that
modulates myogenic differentiation.";
J. Cell Biol. 147:1391-1398(1999).
[21]
INTERACTION WITH ITGB1BP1.
PubMed=11741838; DOI=10.1093/hmg/10.25.2953;
Zhang J., Clatterbuck R.E., Rigamonti D., Chang D.D., Dietz H.C.;
"Interaction between krit1 and icap1alpha infers perturbation of
integrin beta1-mediated angiogenesis in the pathogenesis of cerebral
cavernous malformation.";
Hum. Mol. Genet. 10:2953-2960(2001).
[22]
SUBCELLULAR LOCATION.
PubMed=11919189; DOI=10.1074/jbc.M200200200;
Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C.,
Block M.R., Albiges-Rizo C.;
"Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha)
interacts directly with the metastasis suppressor nm23-H2, and both
proteins are targeted to newly formed cell adhesion sites upon
integrin engagement.";
J. Biol. Chem. 277:20895-20902(2002).
[23]
INTERACTION WITH FLNA AND FLNB, AND MUTAGENESIS OF GLY-778 AND
ALA-786.
PubMed=11807098; DOI=10.1083/jcb.200103037;
van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M.,
Takafuta T., Shapiro S.S., Sonnenberg A.;
"Different splice variants of filamin-B affect myogenesis, subcellular
distribution, and determine binding to integrin (beta) subunits.";
J. Cell Biol. 156:361-376(2002).
[24]
INTERACTION WITH ITGB1BP1, AND MUTAGENESIS OF 786-ALA--VAL-791.
PubMed=11807099; DOI=10.1083/jcb.200108030;
Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F.,
Silengo L., Eva A., Tarone G.;
"The integrin cytoplasmic domain-associated protein ICAP-1 binds and
regulates Rho family GTPases during cell spreading.";
J. Cell Biol. 156:377-387(2002).
[25]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN PARVOVIRUS
B19 CAPSID PROTEIN.
PubMed=12907437; DOI=10.1182/blood-2003-05-1522;
Weigel-Kelley K.A., Yoder M.C., Srivastava A.;
"Alpha5beta1 integrin as a cellular coreceptor for human parvovirus
B19: requirement of functional activation of beta1 integrin for viral
entry.";
Blood 102:3927-3933(2003).
[26]
FUNCTION, AND INTERACTION WITH ITGB1BP1.
PubMed=12473654; DOI=10.1074/jbc.M211258200;
Bouvard D., Vignoud L., Dupe-Manet S., Abed N., Fournier H.N.,
Vincent-Monegat C., Retta S.F., Fassler R., Block M.R.;
"Disruption of focal adhesions by integrin cytoplasmic domain-
associated protein-1 alpha.";
J. Biol. Chem. 278:6567-6574(2003).
[27]
INTERACTION WITH NOV.
PubMed=12695522; DOI=10.1074/jbc.M302028200;
Lin C.G., Leu S.J., Chen N., Tebeau C.M., Lin S.X., Yeung C.Y.,
Lau L.F.;
"CCN3 (NOV) is a novel angiogenic regulator of the CCN protein
family.";
J. Biol. Chem. 278:24200-24208(2003).
[28]
FUNCTION, AND INTERACTION WITH FBN1.
PubMed=12807887; DOI=10.1074/jbc.M303159200;
Bax D.V., Bernard S.E., Lomas A., Morgan A., Humphries J.,
Shuttleworth C.A., Humphries M.J., Kielty C.M.;
"Cell adhesion to fibrillin-1 molecules and microfibrils is mediated
by alpha 5 beta 1 and alpha v beta 3 integrins.";
J. Biol. Chem. 278:34605-34616(2003).
[29]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ROTAVIRUS
VP4 PROTEIN.
PubMed=12941907; DOI=10.1128/JVI.77.18.9969-9978.2003;
Graham K.L., Halasz P., Tan Y., Hewish M.J., Takada Y., Mackow E.R.,
Robinson M.K., Coulson B.S.;
"Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain
via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by
using VP7 during cell entry.";
J. Virol. 77:9969-9978(2003).
[30]
INTERACTION WITH RANBP9.
PubMed=14722085; DOI=10.1074/jbc.M313515200;
Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S.,
Fabbri M., Pardi R., Bianchi E.;
"RanBPM is a phosphoprotein that associates with the plasma membrane
and interacts with the integrin LFA-1.";
J. Biol. Chem. 279:13027-13034(2004).
[31]
INTERACTION WITH ITGA3; LGALS3 AND CSPG4.
PubMed=15181153; DOI=10.1091/mbc.E04-03-0236;
Fukushi J., Makagiansar I.T., Stallcup W.B.;
"NG2 proteoglycan promotes endothelial cell motility and angiogenesis
via engagement of galectin-3 and alpha3beta1 integrin.";
Mol. Biol. Cell 15:3580-3590(2004).
[32]
INTERACTION WITH MYO10.
PubMed=15156152; DOI=10.1038/ncb1136;
Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A.,
Cheney R.E., Stromblad S.;
"Myosin-X provides a motor-based link between integrins and the
cytoskeleton.";
Nat. Cell Biol. 6:523-531(2004).
[33]
FUNCTION, INTERACTION WITH ACAP1, AND SUBCELLULAR LOCATION.
PubMed=16256741; DOI=10.1016/j.devcel.2005.09.012;
Li J., Ballif B.A., Powelka A.M., Dai J., Gygi S.P., Hsu V.W.;
"Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent
recycling of integrin beta1 to control cell migration.";
Dev. Cell 9:663-673(2005).
[34]
INTERACTION WITH FLNB AND FLNC.
PubMed=16076904; DOI=10.1242/jcs.02484;
Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A.,
Carpen O., Faulkner G., Borradori L.;
"The Z-disc proteins myotilin and FATZ-1 interact with each other and
are connected to the sarcolemma via muscle-specific filamins.";
J. Cell Sci. 118:3739-3749(2005).
[35]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[36]
INTERACTION WITH RAB21.
PubMed=16754960; DOI=10.1083/jcb.200509019;
Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M.,
Ivaska J.;
"Small GTPase Rab21 regulates cell adhesion and controls endosomal
traffic of beta1-integrins.";
J. Cell Biol. 173:767-780(2006).
[37]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[38]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MAMMALIAN
REOVIRUS CAPSID PROTEINS.
PubMed=16501085; DOI=10.1128/JVI.80.6.2760-2770.2006;
Maginnis M.S., Forrest J.C., Kopecky-Bromberg S.A., Dickeson S.K.,
Santoro S.A., Zutter M.M., Nemerow G.R., Bergelson J.M., Dermody T.S.;
"Beta1 integrin mediates internalization of mammalian reovirus.";
J. Virol. 80:2760-2770(2006).
[39]
FUNCTION, INTERACTION WITH KRT1, AND SUBCELLULAR LOCATION.
PubMed=17956333; DOI=10.1042/BST0351292;
Chuang N.N., Huang C.C.;
"Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma
NMB7 cells.";
Biochem. Soc. Trans. 35:1292-1294(2007).
[40]
INTERACTION WITH RAB25.
PubMed=17925226; DOI=10.1016/j.devcel.2007.08.012;
Caswell P.T., Spence H.J., Parsons M., White D.P., Clark K.,
Cheng K.W., Mills G.B., Humphries M.J., Messent A.J., Anderson K.I.,
McCaffrey M.W., Ozanne B.W., Norman J.C.;
"Rab25 associates with alpha5beta1 integrin to promote invasive
migration in 3D microenvironments.";
Dev. Cell 13:496-510(2007).
[41]
FUNCTION, INTERACTION WITH FBN1, AND SUBCELLULAR LOCATION.
PubMed=17158881; DOI=10.1074/jbc.M607008200;
Jovanovic J., Takagi J., Choulier L., Abrescia N.G., Stuart D.I.,
van der Merwe P.A., Mardon H.J., Handford P.A.;
"alphaVbeta6 is a novel receptor for human fibrillin-1. Comparative
studies of molecular determinants underlying integrin-rgd affinity and
specificity.";
J. Biol. Chem. 282:6743-6751(2007).
[42]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18804435; DOI=10.1016/j.devcel.2008.08.001;
Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H.,
Grosse R., Kitzing T., Rantala J.K., Kallioniemi O., Faessler R.,
Kallio M., Ivaska J.;
"Integrin trafficking regulated by Rab21 is necessary for
cytokinesis.";
Dev. Cell 15:371-385(2008).
[43]
FUNCTION.
PubMed=18635536; DOI=10.1074/jbc.M804835200;
Saegusa J., Akakura N., Wu C.Y., Hoogland C., Ma Z., Lam K.S.,
Liu F.T., Takada Y.K., Takada Y.;
"Pro-inflammatory secretory phospholipase A2 type IIA binds to
integrins alphavbeta3 and alpha4beta1 and induces proliferation of
monocytic cells in an integrin-dependent manner.";
J. Biol. Chem. 283:26107-26115(2008).
[44]
FUNCTION IN LEUKOCYTE TO ENDOTHELIAL CELLS ADHESION, AND INTERACTION
WITH JAML.
PubMed=19064666; DOI=10.1083/jcb.200805061;
Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O.,
Bourdoulous S.;
"JAM-L-mediated leukocyte adhesion to endothelial cells is regulated
in cis by alpha4beta1 integrin activation.";
J. Cell Biol. 183:1159-1173(2008).
[45]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EPSTEIN-BARR
VIRUS/HHV-4 GB PROTEIN.
PubMed=17945327; DOI=10.1016/j.virol.2007.09.012;
Xiao J., Palefsky J.M., Herrera R., Berline J., Tugizov S.M.;
"The Epstein-Barr virus BMRF-2 protein facilitates virus attachment to
oral epithelial cells.";
Virology 370:430-442(2008).
[46]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212; ASN-481 AND ASN-669.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[47]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-403; ASN-406 AND ASN-411.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[48]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[49]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-794, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[50]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HHV-5 GB.
PubMed=20660204; DOI=10.1128/JVI.00710-10;
Feire A.L., Roy R.M., Manley K., Compton T.;
"The glycoprotein B disintegrin-like domain binds beta 1 integrin to
mediate cytomegalovirus entry.";
J. Virol. 84:10026-10037(2010).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[52]
INTERACTION WITH ASAP3.
PubMed=22027826; DOI=10.1074/jbc.M111.278770;
Yu X., Wang F., Liu H., Adams G., Aikhionbare F., Liu D., Cao X.,
Fan L., Hu G., Chen Y., Frost A., Partridge E., Ding X., Yao X.;
"ACAP4 protein cooperates with Grb2 protein to orchestrate epidermal
growth factor-stimulated integrin beta1 recycling in cell migration.";
J. Biol. Chem. 286:43735-43747(2011).
[53]
FUNCTION, INTERACTION WITH FERMT2 AND TLN1, AND MUTAGENESIS OF
VAL-787.
PubMed=21768292; DOI=10.1083/jcb.201007108;
Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A.,
Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.;
"Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
fibronectin deposition.";
J. Cell Biol. 194:307-322(2011).
[54]
INTERACTION WITH FERMT2.
PubMed=21325030; DOI=10.1242/jcs.076976;
Qu H., Tu Y., Shi X., Larjava H., Saleem M.A., Shattil S.J.,
Fukuda K., Qin J., Kretzler M., Wu C.;
"Kindlin-2 regulates podocyte adhesion and fibronectin matrix
deposition through interactions with phosphoinositides and
integrins.";
J. Cell Sci. 124:879-891(2011).
[55]
FUNCTION, BINDING TO CX3CL1, IDENTIFICATION IN A COMPLEX WITH CX3CR1
AND CX3CL1, AND CX3CL1-BINDING REGION.
PubMed=23125415; DOI=10.4049/jimmunol.1200889;
Fujita M., Takada Y.K., Takada Y.;
"Integrins alphavbeta3 and alpha4beta1 act as coreceptors for
fractalkine, and the integrin-binding defective mutant of fractalkine
is an antagonist of CX3CR1.";
J. Immunol. 189:5809-5819(2012).
[56]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[57]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-785 AND THR-789, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[58]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-794, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[59]
FUNCTION.
PubMed=25398877; DOI=10.1074/jbc.M114.579946;
Fujita M., Zhu K., Fujita C.K., Zhao M., Lam K.S., Kurth M.J.,
Takada Y.K., Takada Y.;
"Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces
integrin activation through direct binding to a newly identified
binding site (site 2) in integrins alphavbeta3, alpha4beta1, and
alpha5beta1.";
J. Biol. Chem. 290:259-271(2015).
[60]
BINDING TO CX3CL1, AND CX3CL1-BINDING REGION.
PubMed=24789099; DOI=10.1371/journal.pone.0096372;
Fujita M., Takada Y.K., Takada Y.;
"The chemokine fractalkine can activate integrins without CX3CR1
through direct binding to a ligand-binding site distinct from the
classical RGD-binding site.";
PLoS ONE 9:E96372-E96372(2014).
[61]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[62]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 758-769 IN COMPLEX WITH
ACAP1, INTERACTION WITH ACAP1 AND ITGA5, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 760-ARG-ARG-761; 762-GLU--PHE-767 AND 768-LYS-GLU-769.
PubMed=22645133; DOI=10.1074/jbc.M112.378810;
Bai M., Pang X., Lou J., Zhou Q., Zhang K., Ma J., Li J., Sun F.,
Hsu V.W.;
"Mechanistic insights into regulated cargo binding by ACAP1 protein.";
J. Biol. Chem. 287:28675-28685(2012).
[63]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-465 IN COMPLEX WITH
ANTIBODY; ITGA5 AND RGD PEPTIDE, DISULFIDE BONDS, GLYCOSYLATION AT
ASN-269 AND ASN-406, METAL-BINDING SITES, AND SUBUNIT.
PubMed=22451694; DOI=10.1083/jcb.201111077;
Nagae M., Re S., Mihara E., Nogi T., Sugita Y., Takagi J.;
"Crystal structure of alpha5beta1 integrin ectodomain: atomic details
of the fibronectin receptor.";
J. Cell Biol. 197:131-140(2012).
[64]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 784-798 IN COMPLEX WITH
ITGB1BP1, INTERACTION WITH ITGB1BP1, AND MUTAGENESIS OF THR-788;
VAL-790; ASN-792 AND TYR-795.
PubMed=23317506; DOI=10.1016/j.molcel.2012.12.005;
Liu W., Draheim K.M., Zhang R., Calderwood D.A., Boggon T.J.;
"Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin
activation.";
Mol. Cell 49:719-729(2013).
-!- FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-
1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-
1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated
sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-
3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-
10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for
fibronectin. Alpha-4/beta-1 recognizes one or more domains within
the alternatively spliced CS-1 and CS-5 regions of fibronectin.
Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin
alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1
are receptors for lamimin. Integrin alpha-4/beta-1 is a receptor
for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin
alpha-9/beta-1 is a receptor for VCAM1, cytotactin and
osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in
cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin,
thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3
the stimulation by CSPG4 of endothelial cells migration. Integrin
alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins
recognize the sequence R-G-D in a wide array of ligands. Isoform 2
interferes with isoform 1 resulting in a dominant negative effect
on cell adhesion and migration (in vitro). When associated with
alpha-7/beta-1 integrin, regulates cell adhesion and laminin
matrix deposition. Involved in promoting endothelial cell motility
and angiogenesis. Involved in osteoblast compaction through the
fibronectin fibrillogenesis cell-mediated matrix assembly process
and the formation of mineralized bone nodules. May be involved in
up-regulation of the activity of kinases such as PKC via binding
to KRT1. Together with KRT1 and RACK1, serves as a platform for
SRC activation or inactivation. Plays a mechanistic adhesive role
during telophase, required for the successful completion of
cytokinesis. Integrin alpha-3/beta-1 provides a docking site for
FAP (seprase) at invadopodia plasma membranes in a collagen-
dependent manner and hence may participate in the adhesion,
formation of invadopodia and matrix degradation processes,
promoting cell invasion. ITGA4:ITGB1 binds to fractalkine (CX3CL1)
and may act as its coreceptor in CX3CR1-dependent fractalkine
signaling (PubMed:23125415, PubMed:24789099). ITGA4:ITGB1 and
ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct
from the classical ligand-binding site (site 1) and this induces
integrin conformational changes and enhanced ligand binding to
site 1 (PubMed:18635536, PubMed:25398877). ITGA5:ITGB1 acts as a
receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell
adhesion to FBN1 (PubMed:12807887, PubMed:17158881).
{ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:12473654,
ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:16256741,
ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:18635536,
ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:19064666,
ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:23125415,
ECO:0000269|PubMed:24789099, ECO:0000269|PubMed:25398877,
ECO:0000269|PubMed:7523423}.
-!- FUNCTION: Isoform 5: Isoform 5 displaces isoform 1 in striated
muscles. {ECO:0000250}.
-!- FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a
receptor for human echoviruses 1 and 8 (PubMed:8411387). Acts as a
receptor for cytomegalovirus/HHV-5 (PubMed:20660204). Acts as a
receptor for Epstein-Barr virus/HHV-4 (PubMed:17945327). Integrin
ITGA5:ITGB1 acts as a receptor for human parvovirus B19
(PubMed:12907437). Integrin ITGA2:ITGB1 acts as a receptor for
human rotavirus (PubMed:12941907). Acts as a receptor for
mammalian reovirus (PubMed:16501085). In case of HIV-1 infection,
integrin ITGA5:ITGB1 binding to extracellular viral Tat protein
seems to enhance angiogenesis in Kaposi's sarcoma lesions
(PubMed:10397733). {ECO:0000269|PubMed:10397733,
ECO:0000269|PubMed:12907437, ECO:0000269|PubMed:12941907,
ECO:0000269|PubMed:16501085, ECO:0000269|PubMed:17945327,
ECO:0000269|PubMed:20660204, ECO:0000269|PubMed:8411387}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-1
associates with either alpha-1, alpha-2, alpha-3, alpha-4, alpha-
5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or
alpha-V. Interacts with seprase FAP (seprase); the interaction
occurs at the cell surface of invadopodia membrane in a collagen-
dependent manner. Binds LGALS3BP and NMRK2, when associated with
alpha-7, but not with alpha-5. Interacts with FGR and HCK.
Interacts (via the cytoplasmic region) with RAB25 (via the
hypervariable C-terminal region). Interacts with RAB21. Interacts
with KRT1 in the presence of RACK1 and SRC. Interacts with JAML;
integrin alpha-4/beta-1 may regulate leukocyte to endothelial
cells adhesion by controlling JAML homodimerization. Interacts
with FLNA, FLNB and RANBP9. Isoform 5 interacts with ACE2. Isoform
1 interacts with the C-terminal region of FLNC. Interacts with
MYO10. Interacts with DAB2. Interacts with FERMT2; the interaction
is inhibited in presence of ITGB1BP1. Interacts with ITGB1BP1 (via
C-terminal region); the interaction is a prerequisite for focal
adhesion disassembly. Interacts with TLN1; the interaction is
prevented by competitive binding of ITGB1BP1. Interacts with
ACAP1; required for ITGB1 recycling. Interacts with ASAP3. Isoform
5 interacts with alpha-7A and alpha-7B in adult skeletal muscle.
Isoform 5 interacts with alpha-7B in cardiomyocytes of adult
heart. Interacts with EMP2; the interaction may be direct or
indirect and ITGB1 has an heterodimer form (By similarity).
ITGA5:ITGB1 interacts with NOV. ITGA4:ITGB1 is found in a ternary
complex with CX3CR1 and CX3CL1 (PubMed:23125415). ITGA5:ITGB1
interacts with FBN1 (PubMed:12807887, PubMed:17158881).
{ECO:0000250|UniProtKB:P09055, ECO:0000269|PubMed:10455171,
ECO:0000269|PubMed:10613898, ECO:0000269|PubMed:11741838,
ECO:0000269|PubMed:11807098, ECO:0000269|PubMed:11807099,
ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:12695522,
ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:14722085,
ECO:0000269|PubMed:15156152, ECO:0000269|PubMed:15181153,
ECO:0000269|PubMed:15276642, ECO:0000269|PubMed:16076904,
ECO:0000269|PubMed:16256741, ECO:0000269|PubMed:16754960,
ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:17925226,
ECO:0000269|PubMed:19064666, ECO:0000269|PubMed:21325030,
ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:22027826,
ECO:0000269|PubMed:22451694, ECO:0000269|PubMed:22645133,
ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:23317506,
ECO:0000269|PubMed:9501082}.
-!- SUBUNIT: (Microbial infection) Integrin ITGA2:ITGB1 interacts with
human echoviruses 1 and 8 capsid proteins.
{ECO:0000269|PubMed:8411387}.
-!- SUBUNIT: (Microbial infection) Interacts with human
cytomegalovirus/HHV-5 envelope glycoprotein B/gB.
{ECO:0000269|PubMed:20660204}.
-!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr
virus/HHV-4 gB protein. {ECO:0000269|PubMed:17945327}.
-!- SUBUNIT: (Microbial infection) Integrin ITGA5:ITGB1 interacts with
human parvovirus B19 capsid protein.
{ECO:0000269|PubMed:12907437}.
-!- SUBUNIT: (Microbial infection) Integrin ITGA2:ITGB1 interacts with
human rotavirus VP4 protein. {ECO:0000269|PubMed:12941907}.
-!- SUBUNIT: (Microbial infection) Interacts with mammalian reovirus
capsid proteins. {ECO:0000269|PubMed:16501085}.
-!- SUBUNIT: (Microbial infection) Integrin ITGA5:ITGB1 interacts with
HIV-1 Tat. {ECO:0000269|PubMed:10397733}.
-!- INTERACTION:
Q9BY76:ANGPTL4; NbExp=2; IntAct=EBI-703066, EBI-2968146;
P03192:BMRF2 (xeno); NbExp=2; IntAct=EBI-703066, EBI-9348955;
P46109:CRKL; NbExp=2; IntAct=EBI-703066, EBI-910;
P32927:CSF2RB; NbExp=5; IntAct=EBI-703066, EBI-1809771;
P78423:CX3CL1; NbExp=2; IntAct=EBI-703066, EBI-15188013;
P17813:ENG; NbExp=3; IntAct=EBI-703066, EBI-2834630;
P05413:FABP3; NbExp=2; IntAct=EBI-703066, EBI-704216;
P21333:FLNA; NbExp=5; IntAct=EBI-703066, EBI-350432;
P17301:ITGA2; NbExp=3; IntAct=EBI-703066, EBI-702960;
P13612:ITGA4; NbExp=4; IntAct=EBI-703066, EBI-703044;
P08648:ITGA5; NbExp=5; IntAct=EBI-703066, EBI-1382311;
P07948:LYN; NbExp=4; IntAct=EBI-703066, EBI-79452;
P18031:PTPN1; NbExp=2; IntAct=EBI-703066, EBI-968788;
P49023:PXN; NbExp=2; IntAct=EBI-6082935, EBI-702209;
P35282:Rab21 (xeno); NbExp=3; IntAct=EBI-703066, EBI-1993555;
Q9Y490:TLN1; NbExp=2; IntAct=EBI-703066, EBI-2462036;
P26039:Tln1 (xeno); NbExp=2; IntAct=EBI-703066, EBI-1039593;
Q71LX4:Tln2 (xeno); NbExp=3; IntAct=EBI-7208579, EBI-2255655;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:10455171};
Single-pass type I membrane protein {ECO:0000255}. Cell
projection, invadopodium membrane {ECO:0000269|PubMed:10455171};
Single-pass type I membrane protein {ECO:0000255}. Cell
projection, ruffle membrane {ECO:0000303|PubMed:10455171}; Single-
pass type I membrane protein {ECO:0000255}. Recycling endosome
{ECO:0000269|PubMed:16256741}. Melanosome
{ECO:0000269|PubMed:17081065}. Cleavage furrow
{ECO:0000269|PubMed:17956333}. Cell projection, lamellipodium
{ECO:0000269|PubMed:11919189}. Cell projection, ruffle
{ECO:0000269|PubMed:11919189}. Cell junction, focal adhesion
{ECO:0000269|PubMed:17158881}. Cell surface
{ECO:0000269|PubMed:17158881}. Note=Isoform 2 does not localize to
focal adhesions. Highly enriched in stage I melanosomes. Located
on plasma membrane of neuroblastoma NMB7 cells. In a lung cancer
cell line, in prometaphase and metaphase, localizes diffusely at
the membrane and in a few intracellular vesicles. In early
telophase, detected mainly on the matrix-facing side of the cells.
By mid-telophase, concentrated to the ingressing cleavage furrow,
mainly to the basal side of the furrow. In late telophase,
concentrated to the extending protrusions formed at the opposite
ends of the spreading daughter cells, in vesicles at the base of
the lamellipodia formed by the separating daughter cells.
Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2
at the edge or peripheral ruffles and lamellipodia during the
early stages of cell spreading on fibronectin or collagen.
Translocates from peripheral focal adhesions sites to fibrillar
adhesions in a ITGB1BP1-dependent manner. Enriched preferentially
at invadopodia, cell membrane protrusions that correspond to sites
of cell invasion, in a collagen-dependent manner. Localized at
plasma and ruffle membranes in a collagen-independent manner.
{ECO:0000269|PubMed:10455171, ECO:0000303|PubMed:10455171}.
-!- SUBCELLULAR LOCATION: Isoform 5: Cell membrane, sarcolemma
{ECO:0000250}. Cell junction {ECO:0000250}. Note=In cardiac
muscle, isoform 5 is found in costameres and intercalated disks.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=Beta-1A;
IsoId=P05556-1; Sequence=Displayed;
Name=2; Synonyms=Beta-1B;
IsoId=P05556-2; Sequence=VSP_002741;
Name=3; Synonyms=Beta-1C;
IsoId=P05556-3; Sequence=VSP_002742;
Name=4; Synonyms=Beta-1C-2;
IsoId=P05556-4; Sequence=VSP_002743;
Name=5; Synonyms=Beta-1D;
IsoId=P05556-5; Sequence=VSP_002744;
-!- TISSUE SPECIFICITY: Isoform 1 is widely expressed, other isoforms
are generally coexpressed with a more restricted distribution.
Isoform 2 is expressed in skin, liver, skeletal muscle, cardiac
muscle, placenta, umbilical vein endothelial cells, neuroblastoma
cells, lymphoma cells, hepatoma cells and astrocytoma cells.
Isoform 3 and isoform 4 are expressed in muscle, kidney, liver,
placenta, cervical epithelium, umbilical vein endothelial cells,
fibroblast cells, embryonal kidney cells, platelets and several
blood cell lines. Isoform 4, rather than isoform 3, is selectively
expressed in peripheral T-cells. Isoform 3 is expressed in non-
proliferating and differentiated prostate gland epithelial cells
and in platelets, on the surface of erythroleukemia cells and in
various hematopoietic cell lines. Isoform 5 is expressed
specifically in striated muscle (skeletal and cardiac muscle).
{ECO:0000269|PubMed:1551917, ECO:0000269|PubMed:2249781,
ECO:0000269|PubMed:7544298, ECO:0000269|PubMed:7545396,
ECO:0000269|PubMed:7681433, ECO:0000269|PubMed:9494094}.
-!- PTM: The cysteine residues are involved in intrachain disulfide
bonds. {ECO:0000250}.
-!- SIMILARITY: Belongs to the integrin beta chain family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAD97649.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=CD29 entry;
URL="https://en.wikipedia.org/wiki/CD29";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X07979; CAA30790.1; -; mRNA.
EMBL; AK291697; BAF84386.1; -; mRNA.
EMBL; BX537407; CAD97649.1; ALT_INIT; mRNA.
EMBL; AL365203; CAI14426.1; -; Genomic_DNA.
EMBL; CH471072; EAW85948.1; -; Genomic_DNA.
EMBL; CH471072; EAW85949.1; -; Genomic_DNA.
EMBL; CH471072; EAW85950.1; -; Genomic_DNA.
EMBL; CH471072; EAW85951.1; -; Genomic_DNA.
EMBL; CH471072; EAW85952.1; -; Genomic_DNA.
EMBL; CH471072; EAW85953.1; -; Genomic_DNA.
EMBL; CH471072; EAW85954.1; -; Genomic_DNA.
EMBL; CH471072; EAW85955.1; -; Genomic_DNA.
EMBL; CH471072; EAW85957.1; -; Genomic_DNA.
EMBL; CH471072; EAW85958.1; -; Genomic_DNA.
EMBL; CH471072; EAW85959.1; -; Genomic_DNA.
EMBL; BC020057; AAH20057.1; -; mRNA.
EMBL; BC113901; AAI13902.1; -; mRNA.
EMBL; U33879; AAA79832.1; -; Genomic_DNA.
EMBL; U33880; AAA79833.1; -; Genomic_DNA.
EMBL; U33879; AAA79833.1; JOINED; Genomic_DNA.
EMBL; U33882; AAA79834.1; -; Genomic_DNA.
EMBL; U33879; AAA79834.1; JOINED; Genomic_DNA.
EMBL; U33881; AAA79834.1; JOINED; Genomic_DNA.
EMBL; U33882; AAA79835.1; -; Genomic_DNA.
EMBL; U33879; AAA79835.1; JOINED; Genomic_DNA.
EMBL; M34189; AAA59182.1; -; mRNA.
EMBL; M84237; AAA74402.1; -; mRNA.
EMBL; M84237; AAA74403.1; -; mRNA.
EMBL; U28252; AAA81366.1; -; mRNA.
CCDS; CCDS7174.1; -. [P05556-1]
PIR; B27079; B27079.
RefSeq; NP_002202.2; NM_002211.3. [P05556-1]
RefSeq; NP_391988.1; NM_033668.2. [P05556-5]
RefSeq; NP_596867.1; NM_133376.2. [P05556-1]
UniGene; Hs.643813; -.
PDB; 1K11; Model; -; B=786-797.
PDB; 1LHA; Model; -; A=86-543.
PDB; 3G9W; X-ray; 2.16 A; C/D=752-785.
PDB; 3T9K; X-ray; 2.30 A; A/B=758-769.
PDB; 3VI3; X-ray; 2.90 A; B/D=21-465.
PDB; 3VI4; X-ray; 2.90 A; B/D=21-465.
PDB; 4DX9; X-ray; 3.00 A; 6/7/8/9/B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f/h/j/l/n/p/r/t/v/x/z=784-798.
PDB; 4WJK; X-ray; 1.85 A; B=21-465.
PDB; 4WK0; X-ray; 1.78 A; B=21-465.
PDB; 4WK2; X-ray; 2.50 A; B=21-465.
PDB; 4WK4; X-ray; 2.50 A; B=21-465.
PDBsum; 1K11; -.
PDBsum; 1LHA; -.
PDBsum; 3G9W; -.
PDBsum; 3T9K; -.
PDBsum; 3VI3; -.
PDBsum; 3VI4; -.
PDBsum; 4DX9; -.
PDBsum; 4WJK; -.
PDBsum; 4WK0; -.
PDBsum; 4WK2; -.
PDBsum; 4WK4; -.
ProteinModelPortal; P05556; -.
SMR; P05556; -.
BioGrid; 109894; 96.
CORUM; P05556; -.
DIP; DIP-312N; -.
ELM; P05556; -.
IntAct; P05556; 65.
MINT; MINT-140089; -.
STRING; 9606.ENSP00000303351; -.
BindingDB; P05556; -.
ChEMBL; CHEMBL1905; -.
DrugBank; DB00098; Anti-thymocyte Globulin (Rabbit).
GuidetoPHARMACOLOGY; 2455; -.
TCDB; 9.B.87.1.8; the selenoprotein p receptor (selp-receptor) family.
iPTMnet; P05556; -.
PhosphoSitePlus; P05556; -.
SwissPalm; P05556; -.
UniCarbKB; P05556; -.
BioMuta; ITGB1; -.
DMDM; 218563324; -.
EPD; P05556; -.
MaxQB; P05556; -.
PaxDb; P05556; -.
PeptideAtlas; P05556; -.
PRIDE; P05556; -.
DNASU; 3688; -.
Ensembl; ENST00000302278; ENSP00000303351; ENSG00000150093. [P05556-1]
Ensembl; ENST00000396033; ENSP00000379350; ENSG00000150093. [P05556-1]
Ensembl; ENST00000423113; ENSP00000388694; ENSG00000150093. [P05556-5]
GeneID; 3688; -.
KEGG; hsa:3688; -.
UCSC; uc001iwr.5; human. [P05556-1]
CTD; 3688; -.
DisGeNET; 3688; -.
EuPathDB; HostDB:ENSG00000150093.18; -.
GeneCards; ITGB1; -.
HGNC; HGNC:6153; ITGB1.
HPA; CAB003434; -.
MIM; 135630; gene.
neXtProt; NX_P05556; -.
OpenTargets; ENSG00000150093; -.
PharmGKB; PA29953; -.
eggNOG; KOG1226; Eukaryota.
eggNOG; ENOG410XP60; LUCA.
GeneTree; ENSGT00760000119064; -.
HOVERGEN; HBG006190; -.
InParanoid; P05556; -.
KO; K05719; -.
OMA; FFDEDDC; -.
OrthoDB; EOG091G029W; -.
PhylomeDB; P05556; -.
TreeFam; TF105392; -.
Reactome; R-HSA-1566948; Elastic fibre formation.
Reactome; R-HSA-1566977; Fibronectin matrix formation.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-210991; Basigin interactions.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000157; Laminin interactions.
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-416700; Other semaphorin interactions.
Reactome; R-HSA-445144; Signal transduction by L1.
Reactome; R-HSA-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
Reactome; R-HSA-447041; CHL1 interactions.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
Reactome; R-HSA-8875513; MET interacts with TNS proteins.
SABIO-RK; P05556; -.
SignaLink; P05556; -.
SIGNOR; P05556; -.
ChiTaRS; ITGB1; human.
EvolutionaryTrace; P05556; -.
GeneWiki; CD29; -.
GenomeRNAi; 3688; -.
PMAP-CutDB; Q8WUM6; -.
PRO; PR:P05556; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000150093; -.
ExpressionAtlas; P05556; baseline and differential.
Genevisible; P05556; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0034665; C:integrin alpha1-beta1 complex; IDA:UniProtKB.
GO; GO:0034680; C:integrin alpha10-beta1 complex; IDA:UniProtKB.
GO; GO:0034681; C:integrin alpha11-beta1 complex; IDA:UniProtKB.
GO; GO:0034666; C:integrin alpha2-beta1 complex; IDA:UniProtKB.
GO; GO:0034667; C:integrin alpha3-beta1 complex; IDA:UniProtKB.
GO; GO:0034677; C:integrin alpha7-beta1 complex; IEA:Ensembl.
GO; GO:0034678; C:integrin alpha8-beta1 complex; TAS:BHF-UCL.
GO; GO:0008305; C:integrin complex; NAS:UniProtKB.
GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
GO; GO:0071438; C:invadopodium membrane; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0035748; C:myelin sheath abaxonal region; IEA:Ensembl.
GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0001726; C:ruffle; TAS:HGNC.
GO; GO:0032587; C:ruffle membrane; NAS:UniProtKB.
GO; GO:0042383; C:sarcolemma; IDA:MGI.
GO; GO:0097060; C:synaptic membrane; IEA:Ensembl.
GO; GO:0003779; F:actin binding; IDA:BHF-UCL.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:UniProtKB.
GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IMP:UniProtKB.
GO; GO:0015026; F:coreceptor activity; TAS:UniProtKB.
GO; GO:0001968; F:fibronectin binding; IPI:UniProtKB.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0043236; F:laminin binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0032403; F:protein complex binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0048675; P:axon extension; IEA:Ensembl.
GO; GO:0030183; P:B cell differentiation; IC:BHF-UCL.
GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
GO; GO:0007161; P:calcium-independent cell-matrix adhesion; IGI:MGI.
GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
GO; GO:0016477; P:cell migration; TAS:HGNC.
GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IEA:Ensembl.
GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IEP:BHF-UCL.
GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0021943; P:formation of radial glial scaffolds; IEA:Ensembl.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0008354; P:germ cell migration; IEA:Ensembl.
GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; TAS:ProtInc.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0050901; P:leukocyte tethering or rolling; IMP:UniProtKB.
GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB.
GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
GO; GO:0010710; P:regulation of collagen catabolic process; IDA:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 1.20.5.630; -; 1.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR013111; EGF_extracell.
InterPro; IPR027071; Integrin_beta-1.
InterPro; IPR033760; Integrin_beta_N.
InterPro; IPR015812; Integrin_bsu.
InterPro; IPR014836; Integrin_bsu_cyt_dom.
InterPro; IPR037076; Integrin_bsu_cyt_dom_sf.
InterPro; IPR012896; Integrin_bsu_tail.
InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
InterPro; IPR002369; Integrin_bsu_VWA.
InterPro; IPR032695; Integrin_dom.
InterPro; IPR016201; PSI.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR10082; PTHR10082; 1.
PANTHER; PTHR10082:SF28; PTHR10082:SF28; 1.
Pfam; PF07974; EGF_2; 1.
Pfam; PF08725; Integrin_b_cyt; 1.
Pfam; PF07965; Integrin_B_tail; 1.
Pfam; PF00362; Integrin_beta; 1.
Pfam; PF17205; PSI_integrin; 1.
PIRSF; PIRSF002512; Integrin_B; 1.
PRINTS; PR01186; INTEGRINB.
SMART; SM00187; INB; 1.
SMART; SM01241; Integrin_b_cyt; 1.
SMART; SM01242; Integrin_B_tail; 1.
SMART; SM00423; PSI; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 1.
SUPFAM; SSF69687; SSF69687; 1.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS00243; INTEGRIN_BETA; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Calcium;
Cell adhesion; Cell junction; Cell membrane; Cell projection;
Complete proteome; Direct protein sequencing; Disulfide bond;
Endosome; Glycoprotein; Host cell receptor for virus entry;
Host-virus interaction; Integrin; Isopeptide bond; Magnesium;
Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 20
CHAIN 21 798 Integrin beta-1.
/FTId=PRO_0000016334.
TOPO_DOM 21 728 Extracellular. {ECO:0000255}.
TRANSMEM 729 751 Helical. {ECO:0000255}.
TOPO_DOM 752 798 Cytoplasmic. {ECO:0000255}.
DOMAIN 140 378 VWFA.
REPEAT 466 515 I.
REPEAT 516 559 II.
REPEAT 560 598 III.
REPEAT 599 635 IV.
REGION 207 213 CX3CL1-binding.
{ECO:0000269|PubMed:23125415}.
REGION 295 314 CX3CL1-binding.
{ECO:0000269|PubMed:24789099}.
REGION 466 635 Cysteine-rich tandem repeats.
REGION 762 767 Signal for sorting from recycling
endosomes; interaction with ACAP1.
REGION 785 792 Interaction with ITGB1BP1.
METAL 152 152 Magnesium.
METAL 154 154 Calcium 1; via carbonyl oxygen.
METAL 156 156 Calcium 1.
METAL 157 157 Calcium 1.
METAL 189 189 Calcium 2.
METAL 244 244 Calcium 2.
METAL 246 246 Calcium 2.
METAL 248 248 Calcium 2; via carbonyl oxygen.
METAL 249 249 Calcium 2.
METAL 249 249 Magnesium.
METAL 362 362 Calcium 1; via carbonyl oxygen.
MOD_RES 777 777 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 783 783 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 785 785 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 789 789 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 794 794 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22451694}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 403 403 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:22451694}.
CARBOHYD 411 411 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 481 481 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 520 520 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 584 584 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 669 669 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 27 45 {ECO:0000269|PubMed:22451694}.
DISULFID 35 464 {ECO:0000269|PubMed:22451694}.
DISULFID 38 64 {ECO:0000269|PubMed:22451694}.
DISULFID 48 75 {ECO:0000269|PubMed:22451694}.
DISULFID 207 213 {ECO:0000269|PubMed:22451694}.
DISULFID 261 301 {ECO:0000269|PubMed:22451694}.
DISULFID 401 415 {ECO:0000269|PubMed:22451694}.
DISULFID 435 462 {ECO:0000269|PubMed:22451694}.
DISULFID 466 691 {ECO:0000305|PubMed:22451694}.
DISULFID 477 489 {ECO:0000250}.
DISULFID 486 525 {ECO:0000250}.
DISULFID 491 500 {ECO:0000250}.
DISULFID 502 516 {ECO:0000250}.
DISULFID 531 536 {ECO:0000250}.
DISULFID 533 568 {ECO:0000250}.
DISULFID 538 553 {ECO:0000250}.
DISULFID 555 560 {ECO:0000250}.
DISULFID 574 579 {ECO:0000250}.
DISULFID 576 607 {ECO:0000250}.
DISULFID 581 590 {ECO:0000250}.
DISULFID 592 599 {ECO:0000250}.
DISULFID 613 618 {ECO:0000250}.
DISULFID 615 661 {ECO:0000250}.
DISULFID 620 630 {ECO:0000250}.
DISULFID 633 636 {ECO:0000250}.
DISULFID 640 649 {ECO:0000250}.
DISULFID 646 723 {ECO:0000250}.
DISULFID 665 699 {ECO:0000250}.
CROSSLNK 794 794 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
VAR_SEQ 778 798 GENPIYKSAVTTVVNPKYEGK -> VSYKTSKKQSGL (in
isoform 2). {ECO:0000305}.
/FTId=VSP_002741.
VAR_SEQ 778 798 GENPIYKSAVTTVVNPKYEGK -> SLSVAQPGVQWCDISS
LQPLTSRFQQFSCLSLPSTWDYRVKILFIRVP (in
isoform 3). {ECO:0000305}.
/FTId=VSP_002742.
VAR_SEQ 778 798 GENPIYKSAVTTVVNPKYEGK -> PGVQWCDISSLQPLTS
RFQQFSCLSLPSTWDYRVKILFIRVP (in isoform
4). {ECO:0000305}.
/FTId=VSP_002743.
VAR_SEQ 778 798 GENPIYKSAVTTVVNPKYEGK -> QENPIYKSPINNFKNP
NYGRKAGL (in isoform 5). {ECO:0000305}.
/FTId=VSP_002744.
MUTAGEN 760 761 RR->AA: No effect on interaction with
ACAP1. {ECO:0000269|PubMed:22645133}.
MUTAGEN 762 767 EFAKFE->AAAAAA: Strongly reduces
interaction with ACAP1 and ability to
recycle; does not affect
heterodimerization with ITGA5.
{ECO:0000269|PubMed:22645133}.
MUTAGEN 762 763 EF->AA: Slightly reduces interaction with
ACAP1.
MUTAGEN 765 765 K->A: Reduces interaction with ACAP1.
MUTAGEN 766 767 FE->AA: Slightly reduces interaction with
ACAP1.
MUTAGEN 768 769 KE->AA: No effect on interaction with
ACAP1. {ECO:0000269|PubMed:22645133}.
MUTAGEN 778 778 G->Q: Loss of beta-1A interaction with
FLNA and FLNB.
{ECO:0000269|PubMed:11807098}.
MUTAGEN 786 791 AVTTVV->PINNFK: Does not interact with
ITGB1BP1. {ECO:0000269|PubMed:11807099}.
MUTAGEN 786 786 A->P: Loss of beta-1A interaction with
FLNA and FLNB.
{ECO:0000269|PubMed:11807098}.
MUTAGEN 787 787 V->T: Reduces interaction with ITGB1BP1,
but not with FERMT2 or TLN1. Inhibits
fibronectin deposition and mineralized
bone nodules formation.
{ECO:0000269|PubMed:21768292}.
MUTAGEN 788 788 T->D: Strongly reduces ITGB1BP1 binding;
when associated with D-790.
{ECO:0000269|PubMed:23317506}.
MUTAGEN 790 790 V->D: Strongly reduces ITGB1BP1 binding;
when associated with D-788.
{ECO:0000269|PubMed:23317506}.
MUTAGEN 792 792 N->A: Strongly reduces ITGB1BP1 binding;
when associated with A-795.
{ECO:0000269|PubMed:23317506}.
MUTAGEN 795 795 Y->A: Strongly reduces ITGB1BP1 binding;
when associated with A-792.
{ECO:0000269|PubMed:23317506}.
CONFLICT 112 112 T -> H (in Ref. 1; CAA30790).
{ECO:0000305}.
CONFLICT 215 215 S -> T (in Ref. 1; CAA30790).
{ECO:0000305}.
CONFLICT 261 265 CGSLI -> VWMLL (in Ref. 6; AAI13902).
{ECO:0000305}.
CONFLICT 385 386 EN -> DG (in Ref. 6; AAI13902).
{ECO:0000305}.
CONFLICT 463 463 E -> V (in Ref. 2; BAF84386).
{ECO:0000305}.
TURN 26 31 {ECO:0000244|PDB:4WK0}.
HELIX 35 40 {ECO:0000244|PDB:4WK0}.
STRAND 45 47 {ECO:0000244|PDB:4WK0}.
HELIX 61 63 {ECO:0000244|PDB:4WK0}.
STRAND 64 66 {ECO:0000244|PDB:4WK0}.
HELIX 67 71 {ECO:0000244|PDB:4WK0}.
TURN 72 74 {ECO:0000244|PDB:4WK0}.
TURN 77 79 {ECO:0000244|PDB:4WK0}.
STRAND 86 91 {ECO:0000244|PDB:4WK0}.
HELIX 108 110 {ECO:0000244|PDB:4WK0}.
STRAND 118 124 {ECO:0000244|PDB:4WK0}.
STRAND 129 136 {ECO:0000244|PDB:4WK0}.
STRAND 143 150 {ECO:0000244|PDB:4WK0}.
HELIX 153 155 {ECO:0000244|PDB:4WK0}.
HELIX 156 161 {ECO:0000244|PDB:4WK0}.
HELIX 162 164 {ECO:0000244|PDB:4WK0}.
HELIX 165 173 {ECO:0000244|PDB:4WK0}.
TURN 174 176 {ECO:0000244|PDB:4WK0}.
STRAND 180 187 {ECO:0000244|PDB:4WK0}.
TURN 193 195 {ECO:0000244|PDB:4WK0}.
HELIX 200 204 {ECO:0000244|PDB:4WK0}.
STRAND 209 211 {ECO:0000244|PDB:4WK0}.
STRAND 218 227 {ECO:0000244|PDB:4WK0}.
HELIX 229 236 {ECO:0000244|PDB:4WK0}.
STRAND 245 249 {ECO:0000244|PDB:4WK0}.
HELIX 251 260 {ECO:0000244|PDB:4WK0}.
HELIX 262 264 {ECO:0000244|PDB:4WK0}.
STRAND 269 280 {ECO:0000244|PDB:4WK0}.
HELIX 287 291 {ECO:0000244|PDB:4WK0}.
TURN 311 313 {ECO:0000244|PDB:4WK0}.
HELIX 319 328 {ECO:0000244|PDB:4WK0}.
STRAND 331 337 {ECO:0000244|PDB:4WK0}.
HELIX 339 341 {ECO:0000244|PDB:4WK0}.
HELIX 342 351 {ECO:0000244|PDB:4WK0}.
STRAND 352 359 {ECO:0000244|PDB:4WK0}.
STRAND 362 364 {ECO:0000244|PDB:4WK4}.
HELIX 367 379 {ECO:0000244|PDB:4WK0}.
STRAND 382 386 {ECO:0000244|PDB:4WK0}.
STRAND 393 400 {ECO:0000244|PDB:4WK0}.
HELIX 402 404 {ECO:0000244|PDB:4WK0}.
STRAND 406 408 {ECO:0000244|PDB:4WJK}.
HELIX 409 413 {ECO:0000244|PDB:4WK0}.
STRAND 423 432 {ECO:0000244|PDB:4WK0}.
STRAND 437 439 {ECO:0000244|PDB:4WJK}.
STRAND 441 447 {ECO:0000244|PDB:4WK0}.
STRAND 454 461 {ECO:0000244|PDB:4WK0}.
HELIX 752 769 {ECO:0000244|PDB:3G9W}.
HELIX 770 772 {ECO:0000244|PDB:3G9W}.
SEQUENCE 798 AA; 88415 MW; DE35979C1625578C CRC64;
MNLQPIFWIG LISSVCCVFA QTDENRCLKA NAKSCGECIQ AGPNCGWCTN STFLQEGMPT
SARCDDLEAL KKKGCPPDDI ENPRGSKDIK KNKNVTNRSK GTAEKLKPED ITQIQPQQLV
LRLRSGEPQT FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF
RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTNKGE VFNELVGKQR
ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
CHLENNMYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL
SANSSNVIQL IIDAYNSLSS EVILENGKLS EGVTISYKSY CKNGVNGTGE NGRKCSNISI
GDEVQFEISI TSNKCPKKDS DSFKIRPLGF TEEVEVILQY ICECECQSEG IPESPKCHEG
NGTFECGACR CNEGRVGRHC ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK
RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCKCRVCE CNPNYTGSAC DCSLDTSTCE
ASNGQICNGR GICECGVCKC TDPKFQGQTC EMCQTCLGVC AEHKECVQCR AFNKGEKKDT
CTQECSYFNI TKVESRDKLP QPVQPDPVSH CKEKDVDDCW FYFTYSVNGN NEVMVHVVEN
PECPTGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN
PIYKSAVTTV VNPKYEGK


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