P05556 (ITB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Integrin beta-1

Alternative name(s):
Fibronectin receptor subunit beta
Glycoprotein IIa
Short name=GPIIA
VLA-4 subunit beta
CD_antigen=CD29

Gene names

Name:	ITGB1
Synonyms:	FNRB, MDF2, MSK12

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	798 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (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. Ref.8 Ref.27 Ref.29
Subunit structure	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 NMRK2, when associated with alpha-7, but not with alpha-5. Interacts with FGR and HCK By similarity. Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region). Interacts with RAB21. 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 FLNA, FLNB and RANBP9. Isoform Beta-1D interacts with ACE2. Isoform Beta-1A interacts with the C-terminal region of FLNC. Interacts with MYO10. Interacts with DAB2. Interacts with FERMT2. Interacts with ITGB1BP1. Interacts with human cytomegalovirus/HHV-5 envelop glycoprotein B/gB. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.27 Ref.28 Ref.34 Ref.36 Ref.37 Ref.38
Subcellular location	Cell membrane; Single-pass type I membrane protein. Melanosome. Cleavage furrow. 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. Ref.7 Ref.10 Ref.26 Ref.27 Ref.29
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, umbilical 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). Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Post-translational modification	The cysteine residues are involved in intrachain disulfide bonds By similarity.
Sequence similarities	Belongs to the integrin beta chain family. Contains 1 VWFA domain.
Sequence caution	The sequence CAD97649.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell adhesion Host-virus interaction
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Magnesium Metal-binding
Molecular function	Host cell receptor for virus entry Integrin Receptor
PTM	Acetylation Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Inferred by curator PubMed 1715889. Source: BHF-UCL G1/S transition of mitotic cell cycle Inferred from electronic annotation. Source: Compara axon guidance Traceable author statement. Source: Reactome blood coagulation Traceable author statement. Source: Reactome calcium-independent cell-matrix adhesion Inferred from genetic interaction PubMed 19651211. Source: MGI cardiac muscle cell differentiation Inferred from electronic annotation. Source: Compara cell fate specification Inferred from electronic annotation. Source: Compara cell junction assembly Traceable author statement. Source: Reactome cell migration involved in sprouting angiogenesis Inferred from electronic annotation. Source: Compara cell-cell adhesion mediated by integrin Inferred from expression pattern PubMed 17704059. Source: BHF-UCL cellular calcium ion homeostasis Inferred from electronic annotation. Source: Compara cellular defense response Traceable author statement PubMed 10201960. Source: ProtInc cellular response to ionizing radiation Inferred from electronic annotation. Source: Compara cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara cellular response to vitamin D Inferred from electronic annotation. Source: Compara extracellular matrix organization Traceable author statement. Source: Reactome germ cell migration Inferred from electronic annotation. Source: Compara homophilic cell adhesion Traceable author statement PubMed 10201960. Source: ProtInc in utero embryonic development Inferred from electronic annotation. Source: Compara integrin-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW leukocyte cell-cell adhesion Inferred from direct assay PubMed 1715889. Source: BHF-UCL leukocyte migration Traceable author statement. Source: Reactome maternal process involved in female pregnancy Inferred from electronic annotation. Source: Compara negative regulation of anoikis Inferred from mutant phenotype PubMed 15006356. Source: UniProtKB negative regulation of cell projection organization Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of neuron differentiation Inferred from electronic annotation. Source: Compara positive regulation of MAPK cascade Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from genetic interaction PubMed 19364818. Source: MGI positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of cell-substrate adhesion Inferred from electronic annotation. Source: Compara positive regulation of endocytosis Inferred from electronic annotation. Source: Compara positive regulation of neuron differentiation Inferred from electronic annotation. Source: Compara positive regulation of neuron projection development Inferred from electronic annotation. Source: Compara positive regulation of peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara protein transport within lipid bilayer Inferred from electronic annotation. Source: Compara regulation of G-protein coupled receptor protein signaling pathway Inferred from electronic annotation. Source: Compara regulation of cell cycle Inferred from electronic annotation. Source: Compara regulation of immune response Traceable author statement. Source: Reactome response to activity Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to gonadotropin stimulus Inferred from electronic annotation. Source: Compara response to transforming growth factor beta stimulus Inferred from electronic annotation. Source: Compara sarcomere organization Inferred from electronic annotation. Source: Compara tight junction assembly Inferred from electronic annotation. Source: Compara tissue homeostasis Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	acrosomal vesicle Inferred from electronic annotation. Source: Compara alpha3-beta1 integrin complex Inferred from electronic annotation. Source: Compara alpha8-beta1 integrin complex Traceable author statement PubMed 21335239. Source: BHF-UCL alpha9-beta1 integrin complex Inferred from electronic annotation. Source: Compara basement membrane Inferred from electronic annotation. Source: Compara cell surface Inferred from direct assay PubMed 1715889PubMed 21310825. Source: BHF-UCL cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay PubMed 16803572. Source: BHF-UCL external side of plasma membrane Inferred from electronic annotation. Source: Compara filopodium Inferred from direct assay PubMed 16803572. Source: BHF-UCL focal adhesion Inferred from direct assay PubMed 12417594. Source: MGI hemidesmosome Inferred from electronic annotation. Source: Compara intercalated disc Inferred from electronic annotation. Source: Compara melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane raft Inferred from electronic annotation. Source: Compara myelin sheath abaxonal region Inferred from electronic annotation. Source: Compara neuromuscular junction Inferred from direct assay PubMed 9415431. Source: MGI ruffle Traceable author statement PubMed 11919189. Source: HGNC sarcolemma Inferred from direct assay PubMed 9415431. Source: MGI
Molecular_function	actin binding Inferred from direct assay PubMed 16803572. Source: BHF-UCL metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW peptide binding Inferred from electronic annotation. Source: Compara protein heterodimerization activity Non-traceable author statement PubMed 9552005. Source: UniProtKB receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ANGPTL4	Q9BY76	2	EBI-703066,EBI-2968146
CSF2RB	P32927	5	EBI-703066,EBI-1809771
FABP3	P05413	2	EBI-703066,EBI-704216
FLNA	P21333	3	EBI-703066,EBI-350432
ITGA2	P17301	3	EBI-703066,EBI-702960
ITGA4	P13612	3	EBI-703066,EBI-703044
LYN	P07948	4	EBI-703066,EBI-79452
PXN	P49023	2	EBI-6082935,EBI-702209
Rab21	P35282	3	EBI-703066,EBI-1993555	From a different organism.
TLN1	Q9Y490	2	EBI-703066,EBI-2462036

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform Beta-1A (identifier: P05556-1)

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

Isoform Beta-1B (identifier: P05556-2)

The sequence of this isoform differs from the canonical sequence as follows:
     778-798: GENPIYKSAVTTVVNPKYEGK → VSYKTSKKQSGL

Isoform Beta-1C (identifier: P05556-3)

The sequence of this isoform differs from the canonical sequence as follows:
     778-798: GENPIYKSAVTTVVNPKYEGK → SLSVAQPGVQWCDISSLQPLTSRFQQFSCLSLPSTWDYRVKILFIRVP

Isoform Beta-1C-2 (identifier: P05556-4)

The sequence of this isoform differs from the canonical sequence as follows:
     778-798: GENPIYKSAVTTVVNPKYEGK → PGVQWCDISSLQPLTSRFQQFSCLSLPSTWDYRVKILFIRVP

Isoform Beta-1D (identifier: P05556-5)

The sequence of this isoform differs from the canonical sequence as follows:
     778-798: GENPIYKSAVTTVVNPKYEGK → QENPIYKSPINNFKNPNYGRKAGL

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Chain

21 – 798

778

Integrin beta-1

PRO_0000016334

Regions

Topological domain

21 – 728

708

Extracellular Potential

Transmembrane

729 – 751

23

Helical; Potential

Topological domain

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

Region

785 – 792

8

Interaction with ITGB1BP1

Sites

Metal binding

152

1

Magnesium

Metal binding

154

1

Calcium 1; via carbonyl oxygen

Metal binding

156

1

Calcium 1

Metal binding

157

1

Calcium 1

Metal binding

189

1

Calcium 2

Metal binding

244

1

Calcium 2

Metal binding

246

1

Calcium 2

Metal binding

248

1

Calcium 2; via carbonyl oxygen

Metal binding

249

1

Calcium 2

Metal binding

249

1

Magnesium

Metal binding

362

1

Calcium 1; via carbonyl oxygen

Amino acid modifications

Modified residue

186

1

Phosphoserine By similarity

Modified residue

777

1

Phosphothreonine Ref.32

Modified residue

783

1

Phosphotyrosine By similarity

Modified residue

794

1

N6-acetyllysine Ref.33

Glycosylation

50

1

N-linked (GlcNAc...) Potential

Glycosylation

94

1

N-linked (GlcNAc...) Potential

Glycosylation

97

1

N-linked (GlcNAc...) Potential

Glycosylation

212

1

N-linked (GlcNAc...) Ref.30

Glycosylation

269

1

N-linked (GlcNAc...) Ref.37

Glycosylation

363

1

N-linked (GlcNAc...) Potential

Glycosylation

403

1

N-linked (GlcNAc...) Ref.31

Glycosylation

406

1

N-linked (GlcNAc...) Ref.24 Ref.31 Ref.37

Glycosylation

411

1

N-linked (GlcNAc...) Ref.31

Glycosylation

417

1

N-linked (GlcNAc...) Potential

Glycosylation

481

1

N-linked (GlcNAc...) Ref.30

Glycosylation

520

1

N-linked (GlcNAc...) Potential

Glycosylation

584

1

N-linked (GlcNAc...) Potential

Glycosylation

669

1

N-linked (GlcNAc...) Ref.30

Disulfide bond

27 ↔ 45

Ref.37

Disulfide bond

35 ↔ 464

Ref.37

Disulfide bond

38 ↔ 64

Ref.37

Disulfide bond

48 ↔ 75

Ref.37

Disulfide bond

207 ↔ 213

Ref.37

Disulfide bond

261 ↔ 301

Ref.37

Disulfide bond

401 ↔ 415

Ref.37

Disulfide bond

435 ↔ 462

Ref.37

Disulfide bond

466 ↔ 691

Probable

Disulfide bond

477 ↔ 489

By similarity

Disulfide bond

486 ↔ 525

By similarity

Disulfide bond

491 ↔ 500

By similarity

Disulfide bond

502 ↔ 516

By similarity

Disulfide bond

531 ↔ 536

By similarity

Disulfide bond

533 ↔ 568

By similarity

Disulfide bond

538 ↔ 553

By similarity

Disulfide bond

555 ↔ 560

By similarity

Disulfide bond

574 ↔ 579

By similarity

Disulfide bond

576 ↔ 607

By similarity

Disulfide bond

581 ↔ 590

By similarity

Disulfide bond

592 ↔ 599

By similarity

Disulfide bond

613 ↔ 618

By similarity

Disulfide bond

615 ↔ 661

By similarity

Disulfide bond

620 ↔ 630

By similarity

Disulfide bond

633 ↔ 636

By similarity

Disulfide bond

640 ↔ 649

By similarity

Disulfide bond

646 ↔ 723

By similarity

Disulfide bond

665 ↔ 699

By similarity

Natural variations

Alternative sequence

778 – 798

21

GENPI…KYEGK → VSYKTSKKQSGL in isoform Beta-1B.

VSP_002741

Alternative sequence

778 – 798

21

GENPI…KYEGK → SLSVAQPGVQWCDISSLQPL TSRFQQFSCLSLPSTWDYRV KILFIRVP in isoform Beta-1C.

VSP_002742

Alternative sequence

778 – 798

21

GENPI…KYEGK → PGVQWCDISSLQPLTSRFQQ FSCLSLPSTWDYRVKILFIR VP in isoform Beta-1C-2.

VSP_002743

Alternative sequence

778 – 798

21

GENPI…KYEGK → QENPIYKSPINNFKNPNYGR KAGL in isoform Beta-1D.

VSP_002744

Experimental info

Mutagenesis

778

1

G → Q: Loss of beta-1A interaction with FLNA and FLNB. Ref.19

Mutagenesis

786

1

A → P: Loss of beta-1A interaction with FLNA and FLNB. Ref.19

Mutagenesis

788

1

T → D: Strongly reduces ITGB1BP1 binding; when associated with D-790. Ref.38

Mutagenesis

790

1

V → D: Strongly reduces ITGB1BP1 binding; when associated with D-788. Ref.38

Mutagenesis

792

1

N → A: Strongly reduces ITGB1BP1 binding; when associated with A-795. Ref.38

Mutagenesis

795

1

Y → A: Strongly reduces ITGB1BP1 binding; when associated with A-792. Ref.38

Sequence conflict

112

1

T → H in CAA30790. Ref.1

Sequence conflict

215

1

S → T in CAA30790. Ref.1

Sequence conflict

261 – 265

5

CGSLI → VWMLL in AAI13902. Ref.6

Sequence conflict

385 – 386

2

EN → DG in AAI13902. Ref.6

Sequence conflict

463

1

E → V in BAF84386. Ref.2

Secondary structure

1

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798

Helix Strand Turn

Details...

Turn

36 – 38

3

Beta strand

39 – 41

3

Helix

67 – 70

4

Turn

71 – 74

4

Turn

77 – 79

3

Beta strand

86 – 91

6

Turn

108 – 110

3

Beta strand

118 – 123

6

Beta strand

131 – 136

6

Beta strand

143 – 150

8

Helix

153 – 155

3

Helix

156 – 162

7

Helix

165 – 173

9

Turn

174 – 176

3

Beta strand

178 – 187

10

Turn

193 – 195

3

Turn

200 – 204

5

Beta strand

209 – 211

3

Beta strand

218 – 227

10

Helix

229 – 236

8

Beta strand

245 – 249

5

Helix

251 – 260

10

Helix

262 – 265

4

Beta strand

269 – 280

12

Turn

285 – 288

4

Helix

289 – 291

3

Turn

311 – 313

3

Helix

319 – 328

10

Beta strand

331 – 338

8

Helix

339 – 341

3

Helix

342 – 351

10

Beta strand

355 – 360

6

Helix

367 – 379

13

Beta strand

382 – 386

5

Beta strand

393 – 400

8

Helix

402 – 404

3

Beta strand

406 – 408

3

Helix

409 – 413

5

Beta strand

423 – 434

12

Beta strand

438 – 447

10

Beta strand

454 – 460

7

Helix

752 – 769

18

Helix

770 – 772

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Beta-1A [UniParc]. Last modified December 16, 2008. Version 2. Checksum: DE35979C1625578C	FASTA	798	88,415
	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
	Isoform Beta-1B [UniParc]. Checksum: 75834A92490CFBB0	FASTA	789	87,446
	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 MNAKWDTVSY KTSKKQSGL
	Isoform Beta-1C [UniParc]. Checksum: D5DCB510A049FBEC	FASTA	825	91,620
	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 MNAKWDTSLS 790 800 810 820 VAQPGVQWCD ISSLQPLTSR FQQFSCLSLP STWDYRVKIL FIRVP
	Isoform Beta-1C-2 [UniParc]. Checksum: 5838866B6DA6CECC	FASTA	819	91,034
	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 MNAKWDTPGV 790 800 810 QWCDISSLQP LTSRFQQFSC LSLPSTWDYR VKILFIRVP
	Isoform Beta-1D [UniParc]. Checksum: 5A2DA413650A16BE	FASTA	801	88,884
	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 MNAKWDTQEN 790 800 PIYKSPINNF KNPNYGRKAG L

References

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[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1A). Tissue: Placenta.
[3]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1A). Tissue: Endometrium.
[4]	"The DNA sequence and comparative analysis of human chromosome 10." 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. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1A). Tissue: Skin.
[7]	"Expression and functional analysis of a cytoplasmic domain variant of the beta 1 integrin subunit." Balzac F., Belkin A.M., Koteliansky V.E., Balabanov Y.V., Altruda F., Silengo L., Tarone G. J. Cell Biol. 121:171-178(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 717-757, CHARACTERIZATION OF BETA-1B, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]	"Expression of beta 1B integrin isoform in CHO cells results in a dominant negative effect on cell adhesion and motility." Balzac F., Retta S.F., Albini A., Melchiorri A., Koteliansky V.E., Geuna M., Silengo L., Tarone G. J. Cell Biol. 127:557-565(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 717-757, FUNCTION.
[9]	"A human integrin beta 1 subunit with a unique cytoplasmic domain generated by alternative mRNA processing." Altruda F., Cervella P., Tarone G., Botta C., Balzac F., Stefanuto G., Silengo L. Gene 95:261-266(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1B), TISSUE SPECIFICITY. Tissue: Skeletal muscle.
[10]	"An alternative form of the integrin beta 1 subunit with a variant cytoplasmic domain." Languino L.R., Ruoslahti E. J. Biol. Chem. 267:7116-7120(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-1A AND BETA-1C), SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Cervix carcinoma.
[11]	"Novel isoform of beta 1 integrin expressed in skeletal and cardiac muscle." Zhidkova N.I., Belkin A.M., Mayne R. Biochem. Biophys. Res. Commun. 214:279-285(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. Tissue: Skeletal muscle.
[12]	"A novel beta 1 integrin isoform produced by alternative splicing: unique expression in cardiac and skeletal muscle." van der Flier A., Kuikman I., Baudoin C., van der Neut R., Sonnenberg A. FEBS Lett. 369:340-344(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1D), TISSUE SPECIFICITY.
[13]	"Identification of beta1C-2, a novel variant of the integrin beta1 subunit generated by utilization of an alternative splice acceptor site in exon C." Svineng G., Faessler R., Johansson S. Biochem. J. 330:1255-1263(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM BETA-1C-2), TISSUE SPECIFICITY.
[14]	"Interaction of ACE2 and integrin beta1 in failing human heart." Lin Q., Keller R.S., Weaver B., Zisman L.S. Biochim. Biophys. Acta 1689:175-178(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 775-784 (ISOFORM BETA-1D), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ACE2.
[15]	"Infection by echoviruses 1 and 8 depends on the alpha 2 subunit of human VLA-2." Bergelson J.M., St John N., Kawaguchi S., Chan M., Stubdal H., Modlin J., Finberg R.W. J. Virol. 67:6847-6852(1993) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN ECHOVIRUS 1 AND HUMAN ECHOVIRUS 8 CAPSID PROTEINS.
[16]	"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." Sasaki T., Brakebusch C., Engel J., Timpl R. EMBO J. 17:1606-1613(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LGALS3BP.
[17]	"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." Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S., Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B. Blood 94:663-672(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[18]	"A novel muscle-specific beta 1 integrin binding protein (MIBP) that modulates myogenic differentiation." Li J., Mayne R., Wu C. J. Cell Biol. 147:1391-1398(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NMRK2. Tissue: Heart.
[19]	"Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin (beta) subunits." van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T., Shapiro S.S., Sonnenberg A. J. Cell Biol. 156:361-376(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FLNA AND FLNB, MUTAGENESIS OF GLY-778 AND ALA-786.
[20]	"RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1." Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S., Fabbri M., Pardi R., Bianchi E. J. Biol. Chem. 279:13027-13034(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RANBP9.
[21]	"NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin." Fukushi J., Makagiansar I.T., Stallcup W.B. Mol. Biol. Cell 15:3580-3590(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ITGA3; LGALS3 AND CSPG4.
[22]	"Myosin-X provides a motor-based link between integrins and the cytoskeleton." Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A., Cheney R.E., Stromblad S. Nat. Cell Biol. 6:523-531(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYO10.
[23]	"The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins." Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A., Carpen O., Faulkner G., Borradori L. J. Cell Sci. 118:3739-3749(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FLNB AND FLNC.
[24]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406, MASS SPECTROMETRY. Tissue: Plasma.
[25]	"Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic of beta1-integrins." Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M., Ivaska J. J. Cell Biol. 173:767-780(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB21.
[26]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." 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. J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[27]	"Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma NMB7 cells." Chuang N.N., Huang C.C. Biochem. Soc. Trans. 35:1292-1294(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH KRT1, SUBCELLULAR LOCATION.
[28]	"Rab25 associates with alpha5beta1 integrin to promote invasive migration in 3D microenvironments." 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. Dev. Cell 13:496-510(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB25.
[29]	"Integrin trafficking regulated by Rab21 is necessary for cytokinesis." 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. Dev. Cell 15:371-385(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[30]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212; ASN-481 AND ASN-669, MASS SPECTROMETRY. Tissue: Liver.
[31]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-403; ASN-406 AND ASN-411, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[32]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[33]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-794, MASS SPECTROMETRY.
[34]	"The glycoprotein B disintegrin-like domain binds beta 1 integrin to mediate cytomegalovirus entry." Feire A.L., Roy R.M., Manley K., Compton T. J. Virol. 84:10026-10037(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HHV-5 GB.
[35]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]	"Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins." Qu H., Tu Y., Shi X., Larjava H., Saleem M.A., Shattil S.J., Fukuda K., Qin J., Kretzler M., Wu C. J. Cell Sci. 124:879-891(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FERMT2.
[37]	"Crystal structure of alpha5beta1 integrin ectodomain: atomic details of the fibronectin receptor." Nagae M., Re S., Mihara E., Nogi T., Sugita Y., Takagi J. J. Cell Biol. 197:131-140(2012) [PubMed] [Europe PMC] [Abstract] Cited for: 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, SUBUNIT.
[38]	"Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation." Liu W., Draheim K.M., Zhang R., Calderwood D.A., Boggon T.J. Mol. Cell 49:719-729(2013) Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 784-798 IN COMPLEX WITH ITGB1BP1, INTERACTION WITH ITGB1BP1, MUTAGENESIS OF THR-788; VAL-790; ASN-792 AND TYR-795.
+	Additional computationally mapped references.

Web resources

Wikipedia

CD29 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X07979 mRNA. Translation: CAA30790.1.
AK291697 mRNA. Translation: BAF84386.1.
BX537407 mRNA. Translation: CAD97649.1. Different initiation.
AL365203 Genomic DNA. Translation: CAI14426.1.
CH471072 Genomic DNA. Translation: EAW85948.1.
CH471072 Genomic DNA. Translation: EAW85949.1.
CH471072 Genomic DNA. Translation: EAW85950.1.
CH471072 Genomic DNA. Translation: EAW85951.1.
CH471072 Genomic DNA. Translation: EAW85952.1.
CH471072 Genomic DNA. Translation: EAW85953.1.
CH471072 Genomic DNA. Translation: EAW85954.1.
CH471072 Genomic DNA. Translation: EAW85955.1.
CH471072 Genomic DNA. Translation: EAW85957.1.
CH471072 Genomic DNA. Translation: EAW85958.1.
CH471072 Genomic DNA. Translation: EAW85959.1.
BC020057 mRNA. Translation: AAH20057.1.
BC113901 mRNA. Translation: AAI13902.1.
U33879 Genomic DNA. Translation: AAA79832.1.
U33880, U33879 Genomic DNA. Translation: AAA79833.1.
U33882, U33879, U33881 Genomic DNA. Translation: AAA79834.1.
U33882, U33879 Genomic DNA. Translation: AAA79835.1.
M34189 mRNA. Translation: AAA59182.1.
M84237 mRNA. Translation: AAA74402.1.
M84237 mRNA. Translation: AAA74403.1.
U28252 mRNA. Translation: AAA81366.1.

IPI

IPI00217561.
IPI00217562.
IPI00217563.
IPI00293305.
IPI00549336.

PIR

B27079.

RefSeq

NP_002202.2. NM_002211.3.
NP_391988.1. NM_033668.2.
NP_596867.1. NM_133376.2.

UniGene

Hs.643813.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K11	model	-	B	786-797	[»]
1LHA	model	-	A	86-543	[»]
3G9W	X-ray	2.16	C/D	752-785	[»]
3T9K	X-ray	2.30	A/B	758-769	[»]
3VI3	X-ray	2.90	B/D	21-465	[»]
3VI4	X-ray	2.90	B/D	21-465	[»]
4DX9	X-ray	3.00	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	[»]

ProteinModelPortal

P05556.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-312N.

IntAct

P05556. 29 interactions.

MINT

MINT-140089.

PTM databases

PhosphoSite

P05556.

Polymorphism databases

DMDM

218563324.

Proteomic databases

PaxDb

P05556.

PRIDE

P05556.

Protocols and materials databases

DNASU

3688.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302278; ENSP00000303351; ENSG00000150093.
ENST00000374956; ENSP00000364094; ENSG00000150093.
ENST00000396033; ENSP00000379350; ENSG00000150093.
ENST00000423113; ENSP00000388694; ENSG00000150093.

GeneID

3688.

KEGG

hsa:3688.

UCSC

uc001iwr.4. human.
uc001iws.4. human.

Organism-specific databases

CTD

3688.

GeneCards

GC10M033189.

HGNC

HGNC:6153. ITGB1.

HPA

CAB003434.

MIM

135630. gene.

neXtProt

NX_P05556.

PharmGKB

PA29953.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG287997.

HOVERGEN

HBG006190.

KO

K05719.

OMA

KVENRDK.

OrthoDB

EOG4K9BBM.

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_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.
REACT_6900. Immune System.

SignaLink

P05556.

Gene expression databases

ArrayExpress

P05556.

Bgee

P05556.

Genevestigator

P05556.

GermOnline

ENSG00000150093. Homo sapiens.

Family and domain databases

Gene3D

1.20.5.630. 1 hit.
3.40.50.410. 1 hit.

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.
[Graphical view]

PANTHER

PTHR10082. PTHR10082. 1 hit.
PTHR10082:SF28. PTHR10082:SF28. 1 hit.

Pfam

PF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]

PIRSF

PIRSF002512. Integrin_B. 1 hit.

PRINTS

PR01186. INTEGRINB.

SMART

SM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]

SUPFAM

SSF69687. Integrin_bsu_tail. 1 hit.
SSF103575. Plexin-like_fold. 1 hit.

PROSITE

PS00022. EGF_1. 2 hits. Uncertain.
PS00243. INTEGRIN_BETA. 3 hits.
PS50234. VWFA. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P05556.

ChEMBL

CHEMBL1905.

ChiTaRS

ITGB1. human.

EvolutionaryTrace

P05556.

GenomeRNAi

3688.

NextBio

14435.

PMAP-CutDB

Q8WUM6.

SOURCE

Search...

Entry information

Entry name

ITB1_HUMAN

Accession

Primary (citable) accession number: P05556
Secondary accession number(s): A8K6N2 , D3DRX9, D3DRY3, D3DRY4, D3DRY5, P78466, P78467, Q13089, Q13090, Q13091, Q13212, Q14622, Q14647, Q29RW2, Q7Z3V1, Q8WUM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	December 16, 2008
Last modified:	May 29, 2013
This is version 171 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

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