UniProt Accession

 ITB1_HUMAN; P05556; A8K6N2; D3DRX9; D3DRY3; D3DRY4; D3DRY5; P78466; P78467; Q13089; Q13090; Q13091; Q13212; Q14622; Q14647; Q29RW2; Q7Z3V1; Q8WUM6 

Genbank Protein ID

 X07979; AK291697; BX537407; AL365203; CH471072; CH471072; CH471072; CH471072; CH471072; CH471072; CH471072; CH471072; CH471072; CH471072; CH471072; BC020057; BC113901; U33879; U33880; U33879; U33882; U33879; U33881; U33882; U33879; M34189; M84237; M84237; U28252 

Genbank Nucleotide ID

 CAA30790.1; BAF84386.1; CAD97649.1; CAI14426.1; EAW85948.1; EAW85949.1; EAW85950.1; EAW85951.1; EAW85952.1; EAW85953.1; EAW85954.1; EAW85955.1; EAW85957.1; EAW85958.1; EAW85959.1; AAH20057.1; AAI13902.1; AAA79832.1; AAA79833.1; AAA79833.1; AAA79834.1; AAA79834.1; AAA79834.1; AAA79835.1; AAA79835.1; AAA59182.1; AAA74402.1; AAA74403.1; AAA81366.1 

Protein Name

 Integrin beta-1 

Protein Synonyms/Alias

 Fibronectin receptor subunit beta; Glycoprotein IIa; GPIIA; VLA-4 subunit beta; CD29 

Gene Name

 ITGB1 

Gene Synonyms/Alias

 FNRB; MDF2; MSK12 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
107	KGTAEKLKPEDITQI	ubiquitination	[1]
134	EPQTFTLKFKRAEDY	ubiquitination	[2]
163	KDDLENVKSLGTDLM	ubiquitination	[1]
190	GFGSFVEKTVMPYIS	ubiquitination	[1, 2, 3]
202	YISTTPAKLRNPCTS	ubiquitination	[1, 2, 3, 4]
228	NVLSLTNKGEVFNEL	ubiquitination	[1, 2, 3, 4, 5]
238	VFNELVGKQRISGNL	ubiquitination	[1, 2]
346	EEFQPVYKELKNLIP	ubiquitination	[1, 2]
575	CGGNGVCKCRVCECN	ubiquitination	[4]
672	CSYFNITKVESRDKL	ubiquitination	[1]
774	EKEKMNAKWDTGENP	acetylation	[6]
774	EKEKMNAKWDTGENP	ubiquitination	[1, 2, 3, 4, 5, 7, 8, 9, 10, 11]
784	TGENPIYKSAVTTVV	ubiquitination	[1, 2, 3, 4, 5, 7, 8, 9, 10, 11, 12]
794	VTTVVNPKYEGK***	acetylation	[6, 13]
794	VTTVVNPKYEGK***	ubiquitination	[1, 2, 3, 4, 5, 9, 11]
798	VNPKYEGK*******	ubiquitination	[2, 5, 11]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [10] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [11] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [12] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [13] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 

Functional Description

 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. 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 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. 

Sequence Annotation

 DOMAIN 140 378 VWFA.
 REPEAT 466 515 I.
 REPEAT 516 559 II.
 REPEAT 560 598 III.
 REPEAT 599 635 IV.
 REGION 466 635 Cysteine-rich tandem repeats.
 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 186 186 Phosphoserine (By similarity).
 MOD_RES 777 777 Phosphothreonine.
 MOD_RES 783 783 Phosphotyrosine (By similarity).
 MOD_RES 794 794 N6-acetyllysine.
 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...).
 CARBOHYD 363 363 N-linked (GlcNAc...) (Potential).
 CARBOHYD 403 403 N-linked (GlcNAc...); atypical.
 CARBOHYD 406 406 N-linked (GlcNAc...).
 CARBOHYD 411 411 N-linked (GlcNAc...); atypical.
 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 45
 DISULFID 35 464
 DISULFID 38 64
 DISULFID 48 75
 DISULFID 207 213
 DISULFID 261 301
 DISULFID 401 415
 DISULFID 435 462
 DISULFID 466 691 Probable.
 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.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Calcium; Cell adhesion; Cell membrane; Cell projection; Complete proteome; Direct protein sequencing; Disulfide bond; Glycoprotein; Host cell receptor for virus entry; Host-virus interaction; Integrin; Magnesium; Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 798 AA 

Protein Sequence

Gene Ontology

 GO:0001669; C:acrosomal vesicle; IEA:Compara.
 GO:0034667; C:alpha3-beta1 integrin complex; IEA:Compara.
 GO:0034678; C:alpha8-beta1 integrin complex; TAS:BHF-UCL.
 GO:0034679; C:alpha9-beta1 integrin complex; IEA:Compara.
 GO:0005604; C:basement membrane; IEA:Compara.
 GO:0009986; C:cell surface; IDA:BHF-UCL.
 GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IDA:BHF-UCL.
 GO:0009897; C:external side of plasma membrane; IEA:Compara.
 GO:0030175; C:filopodium; IDA:BHF-UCL.
 GO:0005925; C:focal adhesion; IDA:MGI.
 GO:0030056; C:hemidesmosome; IEA:Compara.
 GO:0014704; C:intercalated disc; IEA:Compara.
 GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0045121; C:membrane raft; IEA:Compara.
 GO:0035748; C:myelin sheath abaxonal region; IEA:Compara.
 GO:0031594; C:neuromuscular junction; IDA:MGI.
 GO:0001726; C:ruffle; TAS:HGNC.
 GO:0042383; C:sarcolemma; IDA:MGI.
 GO:0003779; F:actin binding; IDA:BHF-UCL.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0042277; F:peptide binding; IEA:Compara.
 GO:0046982; F:protein heterodimerization activity; NAS:UniProtKB.
 GO:0004872; F:receptor activity; IEA:InterPro.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0030183; P:B cell differentiation; IC:BHF-UCL.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0007161; P:calcium-independent cell-matrix adhesion; IGI:MGI.
 GO:0055007; P:cardiac muscle cell differentiation; IEA:Compara.
 GO:0001708; P:cell fate specification; IEA:Compara.
 GO:0034329; P:cell junction assembly; TAS:Reactome.
 GO:0002042; P:cell migration involved in sprouting angiogenesis; IEA:Compara.
 GO:0033631; P:cell-cell adhesion mediated by integrin; IEP:BHF-UCL.
 GO:0006874; P:cellular calcium ion homeostasis; IEA:Compara.
 GO:0006968; P:cellular defense response; TAS:ProtInc.
 GO:0071479; P:cellular response to ionizing radiation; IEA:Compara.
 GO:0071260; P:cellular response to mechanical stimulus; IEA:Compara.
 GO:0071305; P:cellular response to vitamin D; IEA:Compara.
 GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Compara.
 GO:0008354; P:germ cell migration; IEA:Compara.
 GO:0007156; P:homophilic cell adhesion; TAS:ProtInc.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
 GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
 GO:0050900; P:leukocyte migration; TAS:Reactome.
 GO:0060135; P:maternal process involved in female pregnancy; IEA:Compara.
 GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
 GO:0031345; P:negative regulation of cell projection organization; IEA:Compara.
 GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
 GO:0045665; P:negative regulation of neuron differentiation; IEA:Compara.
 GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
 GO:0030335; P:positive regulation of cell migration; IEA:Compara.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Compara.
 GO:0045807; P:positive regulation of endocytosis; IEA:Compara.
 GO:0043410; P:positive regulation of MAPK cascade; IEA:Compara.
 GO:0045666; P:positive regulation of neuron differentiation; IEA:Compara.
 GO:0010976; P:positive regulation of neuron projection development; IEA:Compara.
 GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Compara.
 GO:0032594; P:protein transport within lipid bilayer; IEA:Compara.
 GO:0051726; P:regulation of cell cycle; IEA:Compara.
 GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; IEA:Compara.
 GO:0050776; P:regulation of immune response; TAS:Reactome.
 GO:0014823; P:response to activity; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0034698; P:response to gonadotropin stimulus; IEA:Compara.
 GO:0071559; P:response to transforming growth factor beta stimulus; IEA:Compara.
 GO:0045214; P:sarcomere organization; IEA:Compara.
 GO:0070830; P:tight junction assembly; IEA:Compara.
 GO:0001894; P:tissue homeostasis; IEA:Compara.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 IPR013111; EGF_extracell.
 IPR027071; Integrin_beta-1.
 IPR015812; Integrin_bsu.
 IPR014836; Integrin_bsu_cyt_dom.
 IPR002369; Integrin_bsu_N.
 IPR012896; Integrin_bsu_tail.
 IPR003659; Plexin-like.
 IPR016201; Plexin-like_fold.
 IPR002035; VWF_A. 

Pfam

 PF07974; EGF_2
 PF08725; Integrin_b_cyt
 PF07965; Integrin_B_tail
 PF00362; Integrin_beta 

SMART

 SM00187; INB
 SM00423; PSI
 SM00327; VWA 

PROSITE

 PS00022; EGF_1
 PS00243; INTEGRIN_BETA
 PS50234; VWFA 

PRINTS

 PR01186; INTEGRINB.