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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › 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 2 interferes with isoform 1 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. Ref.8 Ref.24 Ref.28 Ref.33 Ref.35 Ref.36 Ref.44 Isoform 5:Isoform 5 displaces isoform 1 in striated muscles By similarity. Ref.8 Ref.24 Ref.28 Ref.33 Ref.35 Ref.36 Ref.44
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. 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 AMICA1; integrin alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by controlling AMICA1 homodimerization. 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 5 interacts with ACE2. Isoform 1 interacts with the C-terminal region of FLNC. Interacts with MYO10. Interacts with DAB2. Interacts with FERMT2; the interaction is inhibited in presence of ITGB1BP1. Interacts with ITGB1BP1 (via C-terminus region); the interaction is a prerequisite for focal adhesion disassembly. Interacts with TLN1; the interaction is prevented by competitive binding of ITGB1BP1. Interacts with human cytomegalovirus/HHV-5 envelope glycoprotein B/gB. Interacts with ACAP1; required for ITGB1 recycling. Interacts with ASAP3. Isoform 5 interacts with alpha-7A and alpha-7B in adult skeletal muscle. Isoform 5 interacts with alpha-7B in cardiomyocytes of adult heart. Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.33 Ref.34 Ref.36 Ref.41 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48
Subcellular location	Cell membrane; Single-pass type I membrane protein. Recycling endosome. Melanosome. Cleavage furrow. Cell projection › lamellipodium. Cell projection › ruffle. Note: Isoform 2 does not localize to focal adhesions. Highly enriched in stage I melanosomes. Located on plasma membrane of neuroblastoma NMB7 cells. In a lung cancer cell line, in prometaphase and metaphase, localizes diffusely at the membrane and in a few intracellular vesicles. In early telophase, detected mainly on the matrix-facing side of the cells. By mid-telophase, concentrated to the ingressing cleavage furrow, mainly to the basal side of the furrow. In late telophase, concentrated to the extending protrusions formed at the opposite ends of the spreading daughter cells, in vesicles at the base of the lamellipodia formed by the separating daughter cells. Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen. Translocates from peripheral focal adhesions sites to fibrillar adhesions in a ITGB1BP1-dependent manner. Ref.7 Ref.10 Ref.16 Ref.21 Ref.28 Ref.32 Ref.33 Ref.35 Ref.46 Isoform 5: Cell membrane › sarcolemma By similarity. Cell junction By similarity. Note: In cardiac muscle, isoform 5 is found in costameres and intercalated disks By similarity. Ref.7 Ref.10 Ref.16 Ref.21 Ref.28 Ref.32 Ref.33 Ref.35 Ref.46
Tissue specificity	Isoform 1 is widely expressed, other isoforms are generally coexpressed with a more restricted distribution. Isoform 2 is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbilical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoform 3 and isoform 4 are expressed in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein endothelial cells, fibroblast cells, embryonal kidney cells, platelets and several blood cell lines. Isoform 4, rather than isoform 3, is selectively expressed in peripheral T-cells. Isoform 3 is expressed in non-proliferating and differentiated prostate gland epithelial cells and in platelets, on the surface of erythroleukemia cells and in various hematopoietic cell lines. Isoform 5 is expressed specifically in striated muscle (skeletal and cardiac muscle). 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 junction Cell membrane Cell projection Endosome 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: Ensembl 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: Ensembl cell fate specification Inferred from electronic annotation. Source: Ensembl cell junction assembly Traceable author statement. Source: Reactome cell migration Traceable author statement Ref.21. Source: HGNC cell migration involved in sprouting angiogenesis Inferred from electronic annotation. Source: Ensembl cell-cell adhesion mediated by integrin Inferred from expression pattern PubMed 17704059. Source: BHF-UCL cell-matrix adhesion Inferred from mutant phenotype PubMed 18156211. Source: BHF-UCL cellular calcium ion homeostasis Inferred from electronic annotation. Source: Ensembl cellular defense response Traceable author statement PubMed 10201960. Source: ProtInc cellular response to ionizing radiation Inferred from electronic annotation. Source: Ensembl cellular response to mechanical stimulus Inferred from electronic annotation. Source: Ensembl cellular response to vitamin D Inferred from electronic annotation. Source: Ensembl extracellular matrix organization Traceable author statement. Source: Reactome formation of radial glial scaffolds Inferred from electronic annotation. Source: Ensembl germ cell migration Inferred from electronic annotation. Source: Ensembl homophilic cell adhesion Traceable author statement PubMed 10201960. Source: ProtInc in utero embryonic development Inferred from electronic annotation. Source: Ensembl 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: Ensembl negative regulation of anoikis Inferred from mutant phenotype PubMed 15006356. Source: UniProtKB negative regulation of cell projection organization Inferred from electronic annotation. Source: Ensembl negative regulation of cell proliferation Inferred from electronic annotation. Source: Ensembl negative regulation of neuron differentiation Inferred from electronic annotation. Source: Ensembl positive regulation of MAPK cascade Inferred from electronic annotation. Source: Ensembl positive regulation of apoptotic process Inferred from genetic interaction PubMed 19364818. Source: MGI positive regulation of cell migration Inferred from electronic annotation. Source: Ensembl positive regulation of cell proliferation Inferred from electronic annotation. Source: Ensembl positive regulation of cell-substrate adhesion Inferred from electronic annotation. Source: Ensembl positive regulation of endocytosis Inferred from electronic annotation. Source: Ensembl positive regulation of neuron differentiation Inferred from electronic annotation. Source: Ensembl positive regulation of neuron projection development Inferred from electronic annotation. Source: Ensembl positive regulation of peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Ensembl protein transport within lipid bilayer Inferred from electronic annotation. Source: Ensembl regulation of G-protein coupled receptor protein signaling pathway Inferred from electronic annotation. Source: Ensembl regulation of cell cycle Inferred from electronic annotation. Source: Ensembl regulation of immune response Traceable author statement. Source: Reactome response to activity Inferred from electronic annotation. Source: Ensembl response to drug Inferred from electronic annotation. Source: Ensembl response to gonadotropin Inferred from electronic annotation. Source: Ensembl response to transforming growth factor beta Inferred from electronic annotation. Source: Ensembl sarcomere organization Inferred from electronic annotation. Source: Ensembl tight junction assembly Inferred from electronic annotation. Source: Ensembl tissue homeostasis Inferred from electronic annotation. Source: Ensembl viral process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	acrosomal vesicle Inferred from electronic annotation. Source: Ensembl alpha3-beta1 integrin complex Inferred from electronic annotation. Source: Ensembl alpha7-beta1 integrin complex Inferred from electronic annotation. Source: Ensembl alpha8-beta1 integrin complex Traceable author statement PubMed 21335239. Source: BHF-UCL alpha9-beta1 integrin complex Inferred from electronic annotation. Source: Ensembl basement membrane Inferred from electronic annotation. Source: Ensembl 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: Ensembl extracellular vesicular exosome Inferred from direct assay PubMed 19056867. Source: UniProt 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: Ensembl integrin complex Non-traceable author statement PubMed 9552005. Source: UniProtKB intercalated disc Inferred from electronic annotation. Source: Ensembl lamellipodium Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane raft Inferred from direct assay PubMed 14559243. Source: BHF-UCL myelin sheath abaxonal region Inferred from electronic annotation. Source: Ensembl neuromuscular junction Inferred from direct assay PubMed 9415431. Source: MGI plasma membrane Inferred from direct assay PubMed 12869515. Source: UniProtKB receptor complex Inferred from direct assay PubMed 23382219. Source: MGI recycling endosome Inferred from electronic annotation. Source: UniProtKB-SubCell ruffle Traceable author statement Ref.21. Source: HGNC sarcolemma Inferred from direct assay PubMed 9415431. Source: MGI
Molecular_function	actin binding Inferred from direct assay PubMed 16803572. Source: BHF-UCL cell adhesion molecule binding Inferred from physical interaction PubMed 12869515. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW peptide binding Inferred from electronic annotation. Source: Ensembl protein heterodimerization activity Non-traceable author statement PubMed 9552005. Source: UniProtKB virus receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ANGPTL4	Q9BY76	2	EBI-703066,EBI-2968146
CSF2RB	P32927	5	EBI-703066,EBI-1809771
ENG	P17813	3	EBI-703066,EBI-2834630
FABP3	P05413	2	EBI-703066,EBI-704216
FLNA	P21333	5	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
PTPN1	P18031	2	EBI-703066,EBI-968788
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 1 (identifier: P05556-1)

Also known as: Beta-1A;

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 2 (identifier: P05556-2)

Also known as: Beta-1B;

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

Isoform 3 (identifier: P05556-3)

Also known as: Beta-1C;

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

Isoform 4 (identifier: P05556-4)

Also known as: Beta-1C-2;

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

Isoform 5 (identifier: P05556-5)

Also known as: Beta-1D;

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

762 – 767

6

Signal for sorting from recycling endosomes; interaction with ACAP1

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

777

1

Phosphothreonine Ref.39

Modified residue

783

1

Phosphotyrosine By similarity

Modified residue

794

1

N6-acetyllysine Ref.40

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.37

Glycosylation

269

1

N-linked (GlcNAc...) Ref.47

Glycosylation

363

1

N-linked (GlcNAc...) Potential

Glycosylation

403

1

N-linked (GlcNAc...); atypical Ref.38

Glycosylation

406

1

N-linked (GlcNAc...) Ref.30 Ref.38 Ref.47

Glycosylation

411

1

N-linked (GlcNAc...); atypical Ref.38

Glycosylation

417

1

N-linked (GlcNAc...) Potential

Glycosylation

481

1

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

Glycosylation

520

1

N-linked (GlcNAc...) Potential

Glycosylation

584

1

N-linked (GlcNAc...) Potential

Glycosylation

669

1

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

Disulfide bond

27 ↔ 45

Ref.47

Disulfide bond

35 ↔ 464

Ref.47

Disulfide bond

38 ↔ 64

Ref.47

Disulfide bond

48 ↔ 75

Ref.47

Disulfide bond

207 ↔ 213

Ref.47

Disulfide bond

261 ↔ 301

Ref.47

Disulfide bond

401 ↔ 415

Ref.47

Disulfide bond

435 ↔ 462

Ref.47

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 2.

VSP_002741

Alternative sequence

778 – 798

21

GENPI…KYEGK → SLSVAQPGVQWCDISSLQPL TSRFQQFSCLSLPSTWDYRV KILFIRVP in isoform 3.

VSP_002742

Alternative sequence

778 – 798

21

GENPI…KYEGK → PGVQWCDISSLQPLTSRFQQ FSCLSLPSTWDYRVKILFIR VP in isoform 4.

VSP_002743

Alternative sequence

778 – 798

21

GENPI…KYEGK → QENPIYKSPINNFKNPNYGR KAGL in isoform 5.

VSP_002744

Experimental info

Mutagenesis

760 – 761

2

RR → AA: No effect on interaction with ACAP1.

Mutagenesis

762 – 767

6

EFAKFE → AAAAAA: Strongly reduces interaction with ACAP1 and ability to recycle; does not affect heterodimerization with ITGA5. Ref.46

Mutagenesis

762 – 763

2

EF → AA: Slightly reduces interaction with ACAP1.

Mutagenesis

765

1

K → A: Reduces interaction with ACAP1.

Mutagenesis

766 – 767

2

FE → AA: Slightly reduces interaction with ACAP1.

Mutagenesis

768 – 769

2

KE → AA: No effect on interaction with ACAP1.

Mutagenesis

778

1

G → Q: Loss of beta-1A interaction with FLNA and FLNB. Ref.22

Mutagenesis

786 – 791

6

AVTTVV → PINNFK: Does not interact with ITGB1BP1. Ref.22 Ref.23

Mutagenesis

786

1

A → P: Loss of beta-1A interaction with FLNA and FLNB. Ref.22

Mutagenesis

787

1

V → T: Reduces interaction with ITGB1BP1, but not with FERMT2 or TLN1. Inhibits fibronectin deposition and mineralized bone nodules formation. Ref.44

Mutagenesis

788

1

T → D: Strongly reduces ITGB1BP1 binding; when associated with D-790. Ref.48

Mutagenesis

790

1

V → D: Strongly reduces ITGB1BP1 binding; when associated with D-788. Ref.48

Mutagenesis

792

1

N → A: Strongly reduces ITGB1BP1 binding; when associated with A-795. Ref.48

Mutagenesis

795

1

Y → A: Strongly reduces ITGB1BP1 binding; when associated with A-792. Ref.48

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 1 (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 2 (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 3 (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 4 (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 5 (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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[1]	"Amino acid sequence of the human fibronectin receptor." Argraves W.S., Suzuki S., Arai H., Thompson K., Pierschbacher M.D., Ruoslahti E. J. Cell Biol. 105:1183-1190(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[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 1). 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 1). 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 1). 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 2), 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 1 AND 3), 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 5), 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 4), 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 5), 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]	"Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells." Belkin A.M., Zhidkova N.I., Balzac F., Altruda F., Tomatis D., Maier A., Tarone G., Koteliansky V.E., Burridge K. J. Cell Biol. 132:211-226(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"Interaction between krit1 and icap1alpha infers perturbation of integrin beta1-mediated angiogenesis in the pathogenesis of cerebral cavernous malformation." Zhang J., Clatterbuck R.E., Rigamonti D., Chang D.D., Dietz H.C. Hum. Mol. Genet. 10:2953-2960(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ITGB1BP1.
[21]	"Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement." Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C., Block M.R., Albiges-Rizo C. J. Biol. Chem. 277:20895-20902(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[22]	"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.
[23]	"The integrin cytoplasmic domain-associated protein ICAP-1 binds and regulates Rho family GTPases during cell spreading." Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F., Silengo L., Eva A., Tarone G. J. Cell Biol. 156:377-387(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ITGB1BP1, MUTAGENESIS OF 786-ALA--VAL-791.
[24]	"Disruption of focal adhesions by integrin cytoplasmic domain-associated protein-1 alpha." Bouvard D., Vignoud L., Dupe-Manet S., Abed N., Fournier H.N., Vincent-Monegat C., Retta S.F., Fassler R., Block M.R. J. Biol. Chem. 278:6567-6574(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ITGB1BP1.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin beta1 to control cell migration." Li J., Ballif B.A., Powelka A.M., Dai J., Gygi S.P., Hsu V.W. Dev. Cell 9:663-673(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ACAP1, SUBCELLULAR LOCATION.
[29]	"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.
[30]	"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. Tissue: Plasma.
[31]	"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.
[32]	"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]. Tissue: Melanoma.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"JAM-L-mediated leukocyte adhesion to endothelial cells is regulated in cis by alpha4beta1 integrin activation." Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O., Bourdoulous S. J. Cell Biol. 183:1159-1173(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN LEUKOCYTE TO ENDOTHELIAL CELLS ADHESION, INTERACTION WITH AMICA1.
[37]	"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. Tissue: Liver.
[38]	"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. Tissue: Leukemic T-cell.
[39]	"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[40]	"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]	"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.
[42]	"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].
[43]	"ACAP4 protein cooperates with Grb2 protein to orchestrate epidermal growth factor-stimulated integrin beta1 recycling in cell migration." Yu X., Wang F., Liu H., Adams G., Aikhionbare F., Liu D., Cao X., Fan L., Hu G., Chen Y., Frost A., Partridge E., Ding X., Yao X. J. Biol. Chem. 286:43735-43747(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ASAP3.
[44]	"Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition." Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D., Block M.R., Albiges-Rizo C., Bouvard D. J. Cell Biol. 194:307-322(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH FERMT2 AND TLN1, MUTAGENESIS OF VAL-787.
[45]	"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.
[46]	"Mechanistic insights into regulated cargo binding by ACAP1 protein." Bai M., Pang X., Lou J., Zhou Q., Zhang K., Ma J., Li J., Sun F., Hsu V.W. J. Biol. Chem. 287:28675-28685(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 758-769 IN COMPLEX WITH ACAP1, INTERACTION WITH ACAP1 AND ITGA5, SUBCELLULAR LOCATION, MUTAGENESIS OF 760-ARG-ARG-761; 762-GLU--PHE-767 AND 768-LYS-GLU-769.
[47]	"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.
[48]	"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.

PIR

B27079.

RefSeq

NP_002202.2. NM_002211.3.
NP_391988.1. NM_033668.2.
NP_596867.1. NM_133376.2.
XP_005252505.1. XM_005252448.1.

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.

SMR

P05556. Positions 23-797.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

109894. 61 interactions.

DIP

DIP-312N.

IntAct

P05556. 38 interactions.

MINT

MINT-140089.

Chemistry

BindingDB

P05556.

ChEMBL

CHEMBL1907599.

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. [P05556-1]
ENST00000374956; ENSP00000364094; ENSG00000150093. [P05556-3]
ENST00000396033; ENSP00000379350; ENSG00000150093. [P05556-1]
ENST00000423113; ENSP00000388694; ENSG00000150093. [P05556-5]

GeneID

3688.

KEGG

hsa:3688.

UCSC

uc001iwr.4. human. [P05556-5]
uc001iws.4. human. [P05556-1]

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

ENNVYTM.

OrthoDB

EOG7T7GSB.

PhylomeDB

P05556.

TreeFam

TF105392.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.
REACT_6900. Immune System.

SABIO-RK

P05556.

SignaLink

P05556.

Gene expression databases

ArrayExpress

P05556.

Bgee

P05556.

Genevestigator

P05556.

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.
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

SSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69687. SSF69687. 1 hit.

PROSITE

PS00022. EGF_1. 2 hits.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ITGB1. human.

EvolutionaryTrace

P05556.

GeneWiki

CD29.

GenomeRNAi

3688.

NextBio

14435.

PMAP-CutDB

Q8WUM6.

PRO

P05556.

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:	April 16, 2014
This is version 181 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.