[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1A). TISSUE=Placenta; DOI=10.1083/jcb.105.3.1183; PubMed=2958481 [NCBI, ExPASy, EBI, Israel, Japan] 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 BETA-1A). TISSUE=Placenta; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] 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 BETA-1A). TISSUE=Endometrium; DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan] Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder 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]. DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan] 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 BETA-1A). TISSUE=Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1083/jcb.121.1.171; PubMed=7681433 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1083/jcb.127.2.557; PubMed=7523423 [NCBI, ExPASy, EBI, Israel, Japan] 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 BETA-1B), AND TISSUE SPECIFICITY. TISSUE=Skeletal muscle; DOI=10.1016/0378-1119(90)90369-3; PubMed=2249781 [NCBI, ExPASy, EBI, Israel, Japan] 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 BETA-1A AND BETA-1C), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. TISSUE=Cervix carcinoma; PubMed=1551917 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1006/bbrc.1995.2285; PubMed=7545396 [NCBI, ExPASy, EBI, Israel, Japan] 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 BETA-1D), AND TISSUE SPECIFICITY. DOI=10.1016/0014-5793(95)00814-P; PubMed=7544298 [NCBI, ExPASy, EBI, Israel, Japan] 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 BETA-1C-2), AND TISSUE SPECIFICITY. PubMed=9494094 [NCBI, ExPASy, EBI, Israel, Japan] 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 BETA-1D), IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH ACE2. DOI=10.1016/j.bbadis.2004.05.005; PubMed=15276642 [NCBI, ExPASy, EBI, Israel, Japan] 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]	INTERACTION WITH HUMAN ECHOVIRUS 1 AND HUMAN ECHOVIRUS 8 CAPSID PROTEINS. PubMed=8411387 [NCBI, ExPASy, EBI, Israel, Japan] 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]	INTERACTION WITH LGALS3BP. DOI=10.1093/emboj/17.6.1606; PubMed=9501082 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[17]	INTERACTION WITH HIV-1 TAT. PubMed=10397733 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[18]	INTERACTION WITH ITGB1BP3. TISSUE=Heart; DOI=10.1083/jcb.147.7.1391; PubMed=10613898 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[19]	INTERACTION WITH FLNA AND FLNB, AND MUTAGENESIS OF GLY-778 AND ALA-786. DOI=10.1083/jcb.200103037; PubMed=11807098 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[20]	INTERACTION WITH RANBP9. DOI=10.1074/jbc.M313515200; PubMed=14722085 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[21]	INTERACTION WITH ITGA3; LGALS3 AND CSPG4. DOI=10.1091/mbc.E04-03-0236; PubMed=15181153 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[22]	INTERACTION WITH FLNB AND FLNC. DOI=10.1242/jcs.02484; PubMed=16076904 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[23]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[24]	INTERACTION WITH RAB21. DOI=10.1083/jcb.200509019; PubMed=16754960 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[25]	SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[26]	FUNCTION, INTERACTION WITH KRT1, AND SUBCELLULAR LOCATION. DOI=10.1042/BST0351292; PubMed=17956333 [NCBI, ExPASy, EBI, Israel, Japan] Chuang N.N., Huang C.C.; "Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma NMB7 cells."; Biochem. Soc. Trans. 35:1292-1294(2007).
[27]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783, AND MASS SPECTROMETRY. DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan] Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."; Cell 131:1190-1203(2007).
[28]	FUNCTION, AND SUBCELLULAR LOCATION. DOI=10.1016/j.devcel.2008.08.001; PubMed=18804435 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[29]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[30]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212; ASN-481 AND ASN-669, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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 beta-1B interferes with isoform beta-1A resulting in a dominant negative effect on cell adhesion and migration (in vitro). In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and GNB2L1/RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis.
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. Binds LGALS3BP and ITGB1BP3, when associated with alpha-7, but not with alpha-5. Interacts with FLNA, FLNB and RANBP9. Isoform Beta-1D interacts with ACE2. Isoform Beta-1A interacts with the C-terminal region of FLNC. Interacts with KRT1 in the presence of GNB2L1 and SRC. Interacts with HIV-1 Tat. Binds to human echoviruses 1 and 8 capsid proteins and acts as a receptor for these viruses. Interacts with RAB21.
INTERACTION:
Self; NbExp=2; IntAct=EBI-703066, EBI-703066;
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Melanosome. Note=Isoform beta-1B 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 afew 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.

ALTERNATIVE PRODUCTS: 5 named isoforms [FASTA] produced by alternative splicing.

Name	Beta-1A
Isoform ID	P05556-1
This is the isoform sequence displayed in this entry.

Name	Beta-1B
Isoform ID	P05556-2
Features which should be applied to build the isoform sequence: VSP_002741.

Name	Beta-1C
Isoform ID	P05556-3
Features which should be applied to build the isoform sequence: VSP_002742.

Name	Beta-1C-2
Isoform ID	P05556-4
Features which should be applied to build the isoform sequence: VSP_002743.

Name	Beta-1D
Isoform ID	P05556-5
Features which should be applied to build the isoform sequence: VSP_002744.

TISSUE SPECIFICITY: Isoform beta-1A is widely expressed, other isoforms are generally coexpressed with a more restricted distribution. Isoform beta-1B is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbelical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoform beta-1C and isoform beta-1C-2 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 beta-C-2, rather than isoform beta-1C, is selectively expressed in peripheral T-cells. Isoform beta-1C 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 beta-1D is expressed specifically in striated muscle (skeletal and cardiac muscle).
PTM: The cysteine residues are involved in intrachain disulfide bonds (By similarity).
SIMILARITY: Belongs to the integrin beta chain family.
SIMILARITY: Contains 1 VWFA domain.
WEB RESOURCE: Name=Wikipedia; Note=CD29 entry; URL="http://en.wikipedia.org/wiki/CD29";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X07979; CAA30790.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291697; BAF84386.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX537407; CAD97649.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365203; CAI14426.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471072; EAW85948.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020057; AAH20057.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC113901; AAI13902.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U33879; AAA79832.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U33880; AAA79833.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U33879; AAA79833.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U33882; AAA79834.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U33879; AAA79834.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U33881; AAA79834.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U33882; AAA79835.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U33879; AAA79835.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M34189; AAA59182.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M84237; AAA74402.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M84237; AAA74403.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U28252; AAA81366.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00217561; -.
IPI00217562; -.
IPI00217563; -.
IPI00293305; -.
IPI00549336; -.

PIR

B27079; B27079.

RefSeq

NP_002202.2; -.
NP_389647.1; -.
NP_391987.1; -.
NP_391988.1; -.
NP_391989.1; -.
NP_596867.1; -.

UniGene

Hs.713531

3D structure databases

PDB

1K11; Model; -; B=786-797.	[ExPASy / RCSB / EBI]
1LHA; Model; -; A=86-543.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1K11; -.
1LHA; -.

ModBase

P05556.

Protein-protein interaction databases

IntAct

P05556; 6.

PTM databases

PhosphoSite

P05556; -.

Enzyme and pathway databases

Pathway_Interaction_DB

a4b1_a4b7_pathway; a4b1 and a4b7 Integrin signaling.
a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
arf6_traffickingpathway; Arf6 trafficking events.
a4b1_paxdep_pathway; Paxillin-dependent events mediated by a4b1.
a4b1_paxindep_pathway; Paxillin-independent events mediated by a4b1 and a4b7.
reelinpathway; Reelin signaling pathway.
prlsignalingeventspathway; Signaling events mediated by PRL.
syndecan_2_pathway; Syndecan-2-mediated signaling events.
syndecan_4_pathway; Syndecan-4-mediated signaling events.
lymphangiogenesis_pathway; VEGFR3 signaling in lymphatic endothelium.

Reactome

REACT_13552; Integrin cell surface interactions.
REACT_604; Hemostasis.
REACT_6900; Signaling in Immune system.

Organism-specific databases

GC10M033229; -.

HGNC:6153; ITGB1.

CAB003434; -.

135630; gene. [NCBI / EBI]

PharmGKB

PA29953; -.

Gene expression databases

ArrayExpress

P05556; -.

Bgee

P05556; -.

GermOnline

ENSG00000150093; Homo sapiens.

Ontologies

GO:0009986;	Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0008305;	Cellular component: integrin complex (non-traceable author statement from UniProtKB).
GO:0042470;	Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0031594;	Cellular component: neuromuscular junction (inferred from direct assay from MGI).
GO:0001726;	Cellular component: ruffle (traceable author statement from HGNC).
GO:0042383;	Cellular component: sarcolemma (inferred from direct assay from MGI).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0046982;	Molecular function: protein heterodimerization activity (non-traceable author statement from UniProtKB).
GO:0004872;	Molecular function: receptor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0030183;	Biological process: B cell differentiation (inferred by curator from UniProtKB).
GO:0033631;	Biological process: cell-cell adhesion mediated by integrin (inferred from expression pattern from UniProtKB).
GO:0007160;	Biological process: cell-matrix adhesion (inferred from electronic annotation from InterPro).
GO:0006968;	Biological process: cellular defense response (traceable author statement from ProtInc).
GO:0007156;	Biological process: homophilic cell adhesion (traceable author statement from ProtInc).
GO:0007229;	Biological process: integrin-mediated signaling pathway (inferred from electronic annotation from UniProtKB-KW).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0007159;	Biological process: leukocyte adhesion (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR013032; EGF-like_reg_CS.
IPR013111; EGF_extracell.
IPR015812; Integrin_bsu.
IPR015438; Integrin_bsu-1_C.
IPR001169; Integrin_bsu_C.
IPR014836; Integrin_bsu_cyt.
IPR002369; Integrin_bsu_N.
IPR012012; Integrin_bsu_subgr.
IPR012896; Integrin_bsu_tail.
IPR003659; Plexin-like.
IPR002035; VWF_A.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.5.630; Integrin_bsu_cyt; 1.

PANTHER

PTHR10082; Integrin_beta_C; 1.
PTHR10082:SF14; Integrin_bsu-1_C; 1.

Pfam

PF07974; EGF_2; 3.
PF08725; Integrin_b_cyt; 1.
PF07965; Integrin_B_tail; 1.
PF00362; Integrin_beta; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF002512; Integrin_B; 1.

PRINTS

PR01186; INTEGRINB.

SMART

SM00187; INB; 1.
SM00423; PSI; 1.
SM00327; VWA; 1.
SMART graphical view of domain structure.

PROSITE

PS00022; EGF_1; UNKNOWN_2.
PS00243; INTEGRIN_BETA; 3.
PS50234; VWFA; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P05556; -.

Genome annotation databases

Ensembl

ENSG00000150093; Homo sapiens. [Contig view]

GeneID

3688; -.

Phylogenomic databases

HOVERGEN

P05556; -.

OMA

P05556; AKLRNPC.

Other

ITGB1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein; Host-virus interaction; Integrin; Membrane; Phosphoprotein; Receptor; Repeat; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`
`CHAIN`	`21 798`	`778`	`Integrin beta-1.`	`PRO_0000016334`
`TOPO_DOM`	`21 728`	`708`	`Extracellular (Potential).`
`TRANSMEM`	`729 751`	`23`	`Potential.`
`TOPO_DOM`	`752 798`	`47`	`Cytoplasmic (Potential).`
`DOMAIN`	`140 378`	`239`	`VWFA.`
`REPEAT`	`466 515`	`50`	`I.`
`REPEAT`	`516 559`	`44`	`II.`
`REPEAT`	`560 598`	`39`	`III.`
`REPEAT`	`599 635`	`37`	`IV.`
`REGION`	`466 635`	`170`	`Cysteine-rich tandem repeats.`
`MOD_RES`	`186 186`		`Phosphoserine (By similarity).`
`MOD_RES`	`777 777`		`Phosphothreonine (By similarity).`
`MOD_RES`	`783 783`		`Phosphotyrosine.`
`CARBOHYD`	`50 50`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`94 94`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`97 97`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`212 212`		`N-linked (GlcNAc...).`
`CARBOHYD`	`269 269`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`363 363`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`406 406`		`N-linked (GlcNAc...).`
`CARBOHYD`	`417 417`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`481 481`		`N-linked (GlcNAc...).`
`CARBOHYD`	`520 520`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`584 584`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`669 669`		`N-linked (GlcNAc...).`
`DISULFID`	`27 464`		`By similarity.`
`DISULFID`	`35 45`		`By similarity.`
`DISULFID`	`38 75`		`By similarity.`
`DISULFID`	`48 64`		`By similarity.`
`DISULFID`	`207 213`		`By similarity.`
`DISULFID`	`261 301`		`By similarity.`
`DISULFID`	`401 415`		`By similarity.`
`DISULFID`	`435 691`		`By similarity.`
`DISULFID`	`462 466`		`By similarity.`
`DISULFID`	`477 489`		`By similarity.`
`DISULFID`	`486 525`		`By similarity.`
`DISULFID`	`491 500`		`By similarity.`
`DISULFID`	`502 516`		`By similarity.`
`DISULFID`	`531 536`		`By similarity.`
`DISULFID`	`533 568`		`By similarity.`
`DISULFID`	`538 553`		`By similarity.`
`DISULFID`	`555 560`		`By similarity.`
`DISULFID`	`574 579`		`By similarity.`
`DISULFID`	`576 607`		`By similarity.`
`DISULFID`	`581 590`		`By similarity.`
`DISULFID`	`592 599`		`By similarity.`
`DISULFID`	`613 618`		`By similarity.`
`DISULFID`	`615 661`		`By similarity.`
`DISULFID`	`620 630`		`By similarity.`
`DISULFID`	`633 636`		`By similarity.`
`DISULFID`	`640 649`		`By similarity.`
`DISULFID`	`646 723`		`By similarity.`
`DISULFID`	`665 699`		`By similarity.`
`VAR_SEQ`	`778 798`		`GENPIYKSAVTTVVNPKYEGK -> VSYKTSKKQSGL (in isoform Beta-1B).`	`VSP_002741`
`VAR_SEQ`	`778 798`		`GENPIYKSAVTTVVNPKYEGK -> SLSVAQPGVQWCDISSLQPLTSRFQQFSCLSLPSTWDYRV` `KILFIRVP (in isoform Beta-1C).`	`VSP_002742`
`VAR_SEQ`	`778 798`		`GENPIYKSAVTTVVNPKYEGK -> PGVQWCDISSLQPLTSRFQQFSCLSLPSTWDYRVKIL` `FIRVP (in isoform Beta-1C-2).`	`VSP_002743`
`VAR_SEQ`	`778 798`		`GENPIYKSAVTTVVNPKYEGK -> QENPIYKSPINNFKNPNYGRKAGL (in isoform Beta-1D).`	`VSP_002744`
`MUTAGEN`	`778 778`		`G->Q: Loss of beta-1A interaction with FLNA and FLNB.`
`MUTAGEN`	`786 786`		`A->P: Loss of beta-1A interaction with FLNA and FLNB.`
`CONFLICT`	`112 112`		`T -> H (in Ref. 1; CAA30790).`
`CONFLICT`	`215 215`		`S -> T (in Ref. 1; CAA30790).`
`CONFLICT`	`261 265`		`CGSLI -> VWMLL (in Ref. 6; AAI13902).`
`CONFLICT`	`385 386`		`EN -> DG (in Ref. 6; AAI13902).`
`CONFLICT`	`463 463`		`E -> V (in Ref. 2; BAF84386).`
`STRAND`	`107 109`	`3`
`STRAND`	`113 115`	`3`
`STRAND`	`117 123`	`7`
`STRAND`	`128 131`	`4`
`STRAND`	`134 136`	`3`
`STRAND`	`143 150`	`8`
`HELIX`	`153 155`	`3`
`TURN`	`156 162`	`7`
`HELIX`	`167 174`	`8`
`STRAND`	`178 187`	`10`
`TURN`	`193 197`	`5`
`STRAND`	`199 203`	`5`
`STRAND`	`218 220`	`3`
`STRAND`	`225 227`	`3`
`HELIX`	`231 237`	`7`
`STRAND`	`245 249`	`5`
`HELIX`	`252 260`	`9`
`HELIX`	`262 265`	`4`
`STRAND`	`272 280`	`9`
`HELIX`	`287 289`	`3`
`TURN`	`290 292`	`3`
`STRAND`	`303 308`	`6`
`HELIX`	`309 312`	`4`
`HELIX`	`319 328`	`10`
`STRAND`	`333 338`	`6`
`HELIX`	`339 341`	`3`
`HELIX`	`342 351`	`10`
`STRAND`	`356 360`	`5`
`HELIX`	`365 367`	`3`
`HELIX`	`368 378`	`11`
`STRAND`	`384 387`	`4`
`STRAND`	`391 393`	`3`
`STRAND`	`423 425`	`3`
`STRAND`	`428 434`	`7`
`STRAND`	`442 447`	`6`
`STRAND`	`454 460`	`7`
`HELIX`	`510 512`	`3`
`STRAND`	`514 516`	`3`
`HELIX`	`525 527`	`3`
`STRAND`	`529 532`	`4`
`STRAND`	`535 538`	`4`
`STRAND`	`787 791`	`5`

Sequence information

Length: 798 AA [This is the length of the unprocessed precursor]

Molecular weight: 88415 Da [This is the MW of the unprocessed precursor]

CRC64: DE35979C1625578C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNLQPIFWIG LISSVCCVFA QTDENRCLKA NAKSCGECIQ AGPNCGWCTN STFLQEGMPT 

        70         80         90        100        110        120 
SARCDDLEAL KKKGCPPDDI ENPRGSKDIK KNKNVTNRSK GTAEKLKPED ITQIQPQQLV 

       130        140        150        160        170        180 
LRLRSGEPQT FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF 

       190        200        210        220        230        240 
RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTNKGE VFNELVGKQR 

       250        260        270        280        290        300 
ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ 

       310        320        330        340        350        360 
CHLENNMYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL 

       370        380        390        400        410        420 
SANSSNVIQL IIDAYNSLSS EVILENGKLS EGVTISYKSY CKNGVNGTGE NGRKCSNISI 

       430        440        450        460        470        480 
GDEVQFEISI TSNKCPKKDS DSFKIRPLGF TEEVEVILQY ICECECQSEG IPESPKCHEG 

       490        500        510        520        530        540 
NGTFECGACR CNEGRVGRHC ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK 

       550        560        570        580        590        600 
RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCKCRVCE CNPNYTGSAC DCSLDTSTCE 

       610        620        630        640        650        660 
ASNGQICNGR GICECGVCKC TDPKFQGQTC EMCQTCLGVC AEHKECVQCR AFNKGEKKDT 

       670        680        690        700        710        720 
CTQECSYFNI TKVESRDKLP QPVQPDPVSH CKEKDVDDCW FYFTYSVNGN NEVMVHVVEN 

       730        740        750        760        770        780 
PECPTGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN 

       790 
PIYKSAVTTV VNPKYEGK

P05556 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools