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Protein

Integrin beta-1

Gene

ITGB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion.8 Publications
Isoform 5: Isoform 5 displaces isoform 1 in striated muscles.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi152 – 1521Magnesium
Metal bindingi154 – 1541Calcium 1; via carbonyl oxygen
Metal bindingi156 – 1561Calcium 1
Metal bindingi157 – 1571Calcium 1
Metal bindingi189 – 1891Calcium 2
Metal bindingi244 – 2441Calcium 2
Metal bindingi246 – 2461Calcium 2
Metal bindingi248 – 2481Calcium 2; via carbonyl oxygen
Metal bindingi249 – 2491Calcium 2
Metal bindingi249 – 2491Magnesium
Metal bindingi362 – 3621Calcium 1; via carbonyl oxygen

GO - Molecular functioni

  • actin binding Source: BHF-UCL
  • cell adhesion molecule binding Source: UniProtKB
  • collagen binding involved in cell-matrix adhesion Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • peptide binding Source: Ensembl
  • protease binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Integrin, Receptor

Keywords - Biological processi

Cell adhesion, Host-virus interaction

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_12051. Cell surface interactions at the vascular wall.
REACT_1230. Platelet Adhesion to exposed collagen.
REACT_12560. Basigin interactions.
REACT_13552. Integrin cell surface interactions.
REACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.
REACT_160131. Fibronectin matrix formation.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.
REACT_169262. Laminin interactions.
REACT_19200. Other semaphorin interactions.
REACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
REACT_22272. Signal transduction by L1.
REACT_22292. CHL1 interactions.
REACT_355252. RHO GTPases Activate Formins.
SABIO-RKP05556.
SignaLinkiP05556.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ITGB1
Synonyms:FNRB, MDF2, MSK12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:6153. ITGB1.

Subcellular locationi

Isoform 5 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 728708ExtracellularSequence AnalysisAdd
BLAST
Transmembranei729 – 75123HelicalSequence AnalysisAdd
BLAST
Topological domaini752 – 79847CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • acrosomal vesicle Source: Ensembl
  • basement membrane Source: Ensembl
  • cell surface Source: UniProtKB
  • cleavage furrow Source: UniProtKB-SubCell
  • cytoplasm Source: BHF-UCL
  • dendritic spine Source: Ensembl
  • external side of plasma membrane Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • filopodium Source: BHF-UCL
  • focal adhesion Source: UniProtKB
  • hemidesmosome Source: Ensembl
  • integrin alpha10-beta1 complex Source: UniProtKB
  • integrin alpha11-beta1 complex Source: UniProtKB
  • integrin alpha1-beta1 complex Source: UniProtKB
  • integrin alpha2-beta1 complex Source: UniProtKB
  • integrin alpha3-beta1 complex Source: UniProtKB
  • integrin alpha7-beta1 complex Source: Ensembl
  • integrin alpha8-beta1 complex Source: BHF-UCL
  • integrin alpha9-beta1 complex Source: Ensembl
  • integrin complex Source: UniProtKB
  • intercalated disc Source: Ensembl
  • invadopodium membrane Source: UniProtKB
  • lamellipodium Source: UniProtKB-SubCell
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • membrane raft Source: BHF-UCL
  • myelin sheath abaxonal region Source: Ensembl
  • neuromuscular junction Source: MGI
  • plasma membrane Source: UniProtKB
  • receptor complex Source: MGI
  • recycling endosome Source: UniProtKB-SubCell
  • ruffle Source: HGNC
  • ruffle membrane Source: UniProtKB
  • sarcolemma Source: MGI
  • synaptic membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi760 – 7612RR → AA: No effect on interaction with ACAP1. 1 Publication
Mutagenesisi762 – 7676EFAKFE → AAAAAA: Strongly reduces interaction with ACAP1 and ability to recycle; does not affect heterodimerization with ITGA5. 1 Publication
Mutagenesisi762 – 7632EF → AA: Slightly reduces interaction with ACAP1.
Mutagenesisi765 – 7651K → A: Reduces interaction with ACAP1.
Mutagenesisi766 – 7672FE → AA: Slightly reduces interaction with ACAP1.
Mutagenesisi768 – 7692KE → AA: No effect on interaction with ACAP1. 1 Publication
Mutagenesisi778 – 7781G → Q: Loss of beta-1A interaction with FLNA and FLNB. 1 Publication
Mutagenesisi786 – 7916AVTTVV → PINNFK: Does not interact with ITGB1BP1. 1 Publication
Mutagenesisi786 – 7861A → P: Loss of beta-1A interaction with FLNA and FLNB. 1 Publication
Mutagenesisi787 – 7871V → T: Reduces interaction with ITGB1BP1, but not with FERMT2 or TLN1. Inhibits fibronectin deposition and mineralized bone nodules formation. 1 Publication
Mutagenesisi788 – 7881T → D: Strongly reduces ITGB1BP1 binding; when associated with D-790. 1 Publication
Mutagenesisi790 – 7901V → D: Strongly reduces ITGB1BP1 binding; when associated with D-788. 1 Publication
Mutagenesisi792 – 7921N → A: Strongly reduces ITGB1BP1 binding; when associated with A-795. 1 Publication
Mutagenesisi795 – 7951Y → A: Strongly reduces ITGB1BP1 binding; when associated with A-792. 1 Publication

Organism-specific databases

PharmGKBiPA29953.

Chemistry

DrugBankiDB00098. Antithymocyte globulin.

Polymorphism and mutation databases

BioMutaiITGB1.
DMDMi218563324.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 798778Integrin beta-1PRO_0000016334Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 451 Publication
Disulfide bondi35 ↔ 4641 Publication
Disulfide bondi38 ↔ 641 Publication
Disulfide bondi48 ↔ 751 Publication
Glycosylationi50 – 501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi207 ↔ 2131 Publication
Glycosylationi212 – 2121N-linked (GlcNAc...)1 Publication
Disulfide bondi261 ↔ 3011 Publication
Glycosylationi269 – 2691N-linked (GlcNAc...)1 Publication
Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi401 ↔ 4151 Publication
Glycosylationi403 – 4031N-linked (GlcNAc...); atypical1 Publication
Glycosylationi406 – 4061N-linked (GlcNAc...)3 Publications
Glycosylationi411 – 4111N-linked (GlcNAc...); atypical1 Publication
Glycosylationi417 – 4171N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi435 ↔ 4621 Publication
Disulfide bondi466 ↔ 6911 Publication
Disulfide bondi477 ↔ 489By similarity
Glycosylationi481 – 4811N-linked (GlcNAc...)1 Publication
Disulfide bondi486 ↔ 525By similarity
Disulfide bondi491 ↔ 500By similarity
Disulfide bondi502 ↔ 516By similarity
Glycosylationi520 – 5201N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi531 ↔ 536By similarity
Disulfide bondi533 ↔ 568By similarity
Disulfide bondi538 ↔ 553By similarity
Disulfide bondi555 ↔ 560By similarity
Disulfide bondi574 ↔ 579By similarity
Disulfide bondi576 ↔ 607By similarity
Disulfide bondi581 ↔ 590By similarity
Glycosylationi584 – 5841N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi592 ↔ 599By similarity
Disulfide bondi613 ↔ 618By similarity
Disulfide bondi615 ↔ 661By similarity
Disulfide bondi620 ↔ 630By similarity
Disulfide bondi633 ↔ 636By similarity
Disulfide bondi640 ↔ 649By similarity
Disulfide bondi646 ↔ 723By similarity
Disulfide bondi665 ↔ 699By similarity
Glycosylationi669 – 6691N-linked (GlcNAc...)1 Publication
Modified residuei777 – 7771Phosphothreonine1 Publication
Modified residuei783 – 7831PhosphotyrosineBy similarity
Modified residuei785 – 7851Phosphoserine1 Publication
Modified residuei789 – 7891Phosphothreonine1 Publication
Modified residuei794 – 7941N6-acetyllysine1 Publication

Post-translational modificationi

The cysteine residues are involved in intrachain disulfide bonds.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP05556.
PaxDbiP05556.
PRIDEiP05556.

PTM databases

PhosphoSiteiP05556.

Miscellaneous databases

PMAP-CutDBQ8WUM6.

Expressioni

Tissue specificityi

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).6 Publications

Gene expression databases

BgeeiP05556.
ExpressionAtlasiP05556. baseline and differential.
GenevestigatoriP05556.

Organism-specific databases

HPAiCAB003434.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Beta-1 associates with either alpha-1, alpha-2, alpha-3, alpha-4, alpha-5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or alpha-V. Interacts with seprase FAP (seprase); the interaction occurs at the cell surface of invadopodia membrane in a collagen-dependent manner. Binds LGALS3BP and NMRK2, when associated with alpha-7, but not with alpha-5. Interacts with FGR and HCK. Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region). Interacts with RAB21. Interacts with KRT1 in the presence of 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-terminal region); the interaction is a prerequisite for focal adhesion disassembly. Interacts with TLN1; the interaction is prevented by competitive binding of ITGB1BP1. Interacts with 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. Interacts with EMP2; the interaction may be direct or indirect and ITGB1 has an heterodimer form (By similarity).By similarity26 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ANGPTL4Q9BY762EBI-703066,EBI-2968146
BMRF2P031922EBI-703066,EBI-9348955From a different organism.
CSF2RBP329275EBI-703066,EBI-1809771
ENGP178133EBI-703066,EBI-2834630
FABP3P054132EBI-703066,EBI-704216
FLNAP213335EBI-703066,EBI-350432
ITGA2P173013EBI-703066,EBI-702960
ITGA4P136123EBI-703066,EBI-703044
LYNP079484EBI-703066,EBI-79452
PTPN1P180312EBI-703066,EBI-968788
PXNP490232EBI-6082935,EBI-702209
Rab21P352823EBI-703066,EBI-1993555From a different organism.
TLN1Q9Y4902EBI-703066,EBI-2462036

Protein-protein interaction databases

BioGridi109894. 72 interactions.
DIPiDIP-312N.
IntActiP05556. 39 interactions.
MINTiMINT-140089.

Structurei

Secondary structure

1
798
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni26 – 316Combined sources
Helixi35 – 406Combined sources
Beta strandi45 – 473Combined sources
Helixi61 – 633Combined sources
Beta strandi64 – 663Combined sources
Helixi67 – 715Combined sources
Turni72 – 743Combined sources
Turni77 – 793Combined sources
Beta strandi86 – 916Combined sources
Helixi108 – 1103Combined sources
Beta strandi118 – 1247Combined sources
Beta strandi129 – 1368Combined sources
Beta strandi143 – 1508Combined sources
Helixi153 – 1553Combined sources
Helixi156 – 1616Combined sources
Helixi162 – 1643Combined sources
Helixi165 – 1739Combined sources
Turni174 – 1763Combined sources
Beta strandi180 – 1878Combined sources
Turni193 – 1953Combined sources
Helixi200 – 2045Combined sources
Beta strandi209 – 2113Combined sources
Beta strandi218 – 22710Combined sources
Helixi229 – 2368Combined sources
Beta strandi245 – 2495Combined sources
Helixi251 – 26010Combined sources
Helixi262 – 2643Combined sources
Beta strandi269 – 28012Combined sources
Helixi287 – 2915Combined sources
Turni311 – 3133Combined sources
Helixi319 – 32810Combined sources
Beta strandi331 – 3377Combined sources
Helixi339 – 3413Combined sources
Helixi342 – 35110Combined sources
Beta strandi352 – 3598Combined sources
Beta strandi362 – 3643Combined sources
Helixi367 – 37913Combined sources
Beta strandi382 – 3865Combined sources
Beta strandi393 – 4008Combined sources
Helixi402 – 4043Combined sources
Beta strandi406 – 4083Combined sources
Helixi409 – 4135Combined sources
Beta strandi423 – 43210Combined sources
Beta strandi437 – 4393Combined sources
Beta strandi441 – 4477Combined sources
Beta strandi454 – 4618Combined sources
Helixi752 – 76918Combined sources
Helixi770 – 7723Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K11model-B786-797[»]
1LHAmodel-A86-543[»]
3G9WX-ray2.16C/D752-785[»]
3T9KX-ray2.30A/B758-769[»]
3VI3X-ray2.90B/D21-465[»]
3VI4X-ray2.90B/D21-465[»]
4DX9X-ray3.006/7/8/9/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/z784-798[»]
4WJKX-ray1.85B21-465[»]
4WK0X-ray1.78B21-465[»]
4WK2X-ray2.50B21-465[»]
4WK4X-ray2.50B21-465[»]
ProteinModelPortaliP05556.
SMRiP05556. Positions 24-787.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05556.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini140 – 378239VWFAAdd
BLAST
Repeati466 – 51550IAdd
BLAST
Repeati516 – 55944IIAdd
BLAST
Repeati560 – 59839IIIAdd
BLAST
Repeati599 – 63537IVAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni466 – 635170Cysteine-rich tandem repeatsAdd
BLAST
Regioni762 – 7676Signal for sorting from recycling endosomes; interaction with ACAP1
Regioni785 – 7928Interaction with ITGB1BP1

Sequence similaritiesi

Belongs to the integrin beta chain family.Curated
Contains 1 VWFA domain.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG287997.
GeneTreeiENSGT00760000119064.
HOVERGENiHBG006190.
InParanoidiP05556.
KOiK05719.
OMAiENNVYTM.
OrthoDBiEOG7T7GSB.
PhylomeDBiP05556.
TreeFamiTF105392.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR013111. 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]
PANTHERiPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF28. PTHR10082:SF28. 1 hit.
PfamiPF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 2 hits.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P05556-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MNLQPIFWIG LISSVCCVFA QTDENRCLKA NAKSCGECIQ AGPNCGWCTN
60 70 80 90 100
STFLQEGMPT SARCDDLEAL KKKGCPPDDI ENPRGSKDIK KNKNVTNRSK
110 120 130 140 150
GTAEKLKPED ITQIQPQQLV LRLRSGEPQT FTLKFKRAED YPIDLYYLMD
160 170 180 190 200
LSYSMKDDLE NVKSLGTDLM NEMRRITSDF RIGFGSFVEK TVMPYISTTP
210 220 230 240 250
AKLRNPCTSE QNCTSPFSYK NVLSLTNKGE VFNELVGKQR ISGNLDSPEG
260 270 280 290 300
GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
310 320 330 340 350
CHLENNMYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN
360 370 380 390 400
LIPKSAVGTL SANSSNVIQL IIDAYNSLSS EVILENGKLS EGVTISYKSY
410 420 430 440 450
CKNGVNGTGE NGRKCSNISI GDEVQFEISI TSNKCPKKDS DSFKIRPLGF
460 470 480 490 500
TEEVEVILQY ICECECQSEG IPESPKCHEG NGTFECGACR CNEGRVGRHC
510 520 530 540 550
ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK RDNTNEIYSG
560 570 580 590 600
KFCECDNFNC DRSNGLICGG NGVCKCRVCE CNPNYTGSAC DCSLDTSTCE
610 620 630 640 650
ASNGQICNGR GICECGVCKC TDPKFQGQTC EMCQTCLGVC AEHKECVQCR
660 670 680 690 700
AFNKGEKKDT CTQECSYFNI TKVESRDKLP QPVQPDPVSH CKEKDVDDCW
710 720 730 740 750
FYFTYSVNGN NEVMVHVVEN PECPTGPDII PIVAGVVAGI VLIGLALLLI
760 770 780 790
WKLLMIIHDR REFAKFEKEK MNAKWDTGEN PIYKSAVTTV VNPKYEGK
Length:798
Mass (Da):88,415
Last modified:December 16, 2008 - v2
Checksum:iDE35979C1625578C
GO
Isoform 2 (identifier: P05556-2) [UniParc]FASTAAdd to basket

Also known as: Beta-1B

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

Show »
Length:789
Mass (Da):87,446
Checksum:i75834A92490CFBB0
GO
Isoform 3 (identifier: P05556-3) [UniParc]FASTAAdd to basket

Also known as: Beta-1C

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

Show »
Length:825
Mass (Da):91,620
Checksum:iD5DCB510A049FBEC
GO
Isoform 4 (identifier: P05556-4) [UniParc]FASTAAdd to basket

Also known as: Beta-1C-2

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

Show »
Length:819
Mass (Da):91,034
Checksum:i5838866B6DA6CECC
GO
Isoform 5 (identifier: P05556-5) [UniParc]FASTAAdd to basket

Also known as: Beta-1D

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

Show »
Length:801
Mass (Da):88,884
Checksum:i5A2DA413650A16BE
GO

Sequence cautioni

The sequence CAD97649.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121T → H in CAA30790 (PubMed:2958481).Curated
Sequence conflicti215 – 2151S → T in CAA30790 (PubMed:2958481).Curated
Sequence conflicti261 – 2655CGSLI → VWMLL in AAI13902 (PubMed:15489334).Curated
Sequence conflicti385 – 3862EN → DG in AAI13902 (PubMed:15489334).Curated
Sequence conflicti463 – 4631E → V in BAF84386 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei778 – 79821GENPI…KYEGK → VSYKTSKKQSGL in isoform 2. CuratedVSP_002741Add
BLAST
Alternative sequencei778 – 79821GENPI…KYEGK → SLSVAQPGVQWCDISSLQPL TSRFQQFSCLSLPSTWDYRV KILFIRVP in isoform 3. CuratedVSP_002742Add
BLAST
Alternative sequencei778 – 79821GENPI…KYEGK → PGVQWCDISSLQPLTSRFQQ FSCLSLPSTWDYRVKILFIR VP in isoform 4. CuratedVSP_002743Add
BLAST
Alternative sequencei778 – 79821GENPI…KYEGK → QENPIYKSPINNFKNPNYGR KAGL in isoform 5. CuratedVSP_002744Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7174.1. [P05556-1]
PIRiB27079.
RefSeqiNP_002202.2. NM_002211.3. [P05556-1]
NP_391988.1. NM_033668.2. [P05556-5]
NP_596867.1. NM_133376.2. [P05556-1]
XP_005252505.1. XM_005252448.1. [P05556-5]
UniGeneiHs.643813.

Genome annotation databases

EnsembliENST00000302278; ENSP00000303351; ENSG00000150093. [P05556-1]
ENST00000396033; ENSP00000379350; ENSG00000150093. [P05556-1]
ENST00000423113; ENSP00000388694; ENSG00000150093. [P05556-5]
GeneIDi3688.
KEGGihsa:3688.
UCSCiuc001iwr.4. human. [P05556-5]
uc001iws.4. human. [P05556-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

CD29 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7174.1. [P05556-1]
PIRiB27079.
RefSeqiNP_002202.2. NM_002211.3. [P05556-1]
NP_391988.1. NM_033668.2. [P05556-5]
NP_596867.1. NM_133376.2. [P05556-1]
XP_005252505.1. XM_005252448.1. [P05556-5]
UniGeneiHs.643813.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K11model-B786-797[»]
1LHAmodel-A86-543[»]
3G9WX-ray2.16C/D752-785[»]
3T9KX-ray2.30A/B758-769[»]
3VI3X-ray2.90B/D21-465[»]
3VI4X-ray2.90B/D21-465[»]
4DX9X-ray3.006/7/8/9/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/z784-798[»]
4WJKX-ray1.85B21-465[»]
4WK0X-ray1.78B21-465[»]
4WK2X-ray2.50B21-465[»]
4WK4X-ray2.50B21-465[»]
ProteinModelPortaliP05556.
SMRiP05556. Positions 24-787.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109894. 72 interactions.
DIPiDIP-312N.
IntActiP05556. 39 interactions.
MINTiMINT-140089.

Chemistry

BindingDBiP05556.
ChEMBLiCHEMBL2111407.
DrugBankiDB00098. Antithymocyte globulin.

PTM databases

PhosphoSiteiP05556.

Polymorphism and mutation databases

BioMutaiITGB1.
DMDMi218563324.

Proteomic databases

MaxQBiP05556.
PaxDbiP05556.
PRIDEiP05556.

Protocols and materials databases

DNASUi3688.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302278; ENSP00000303351; ENSG00000150093. [P05556-1]
ENST00000396033; ENSP00000379350; ENSG00000150093. [P05556-1]
ENST00000423113; ENSP00000388694; ENSG00000150093. [P05556-5]
GeneIDi3688.
KEGGihsa:3688.
UCSCiuc001iwr.4. human. [P05556-5]
uc001iws.4. human. [P05556-1]

Organism-specific databases

CTDi3688.
GeneCardsiGC10M033189.
HGNCiHGNC:6153. ITGB1.
HPAiCAB003434.
MIMi135630. gene.
neXtProtiNX_P05556.
PharmGKBiPA29953.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG287997.
GeneTreeiENSGT00760000119064.
HOVERGENiHBG006190.
InParanoidiP05556.
KOiK05719.
OMAiENNVYTM.
OrthoDBiEOG7T7GSB.
PhylomeDBiP05556.
TreeFamiTF105392.

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_12051. Cell surface interactions at the vascular wall.
REACT_1230. Platelet Adhesion to exposed collagen.
REACT_12560. Basigin interactions.
REACT_13552. Integrin cell surface interactions.
REACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.
REACT_160131. Fibronectin matrix formation.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.
REACT_169262. Laminin interactions.
REACT_19200. Other semaphorin interactions.
REACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
REACT_22272. Signal transduction by L1.
REACT_22292. CHL1 interactions.
REACT_355252. RHO GTPases Activate Formins.
SABIO-RKP05556.
SignaLinkiP05556.

Miscellaneous databases

ChiTaRSiITGB1. human.
EvolutionaryTraceiP05556.
GeneWikiiCD29.
GenomeRNAii3688.
NextBioi14435.
PMAP-CutDBQ8WUM6.
PROiP05556.
SOURCEiSearch...

Gene expression databases

BgeeiP05556.
ExpressionAtlasiP05556. baseline and differential.
GenevestigatoriP05556.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR013111. 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]
PANTHERiPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF28. PTHR10082:SF28. 1 hit.
PfamiPF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 2 hits.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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. 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. Cited for: FUNCTION, SUBUNIT, INTERACTION WITH FAP, SUBCELLULAR LOCATION.
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. "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.
  25. "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.
  26. "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.
  27. "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.
  28. "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.
  29. "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.
  30. "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.
  31. "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.
  32. "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.
  33. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  34. "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.
  35. "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.
  36. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  37. "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.
  38. "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.
  39. "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.
  40. "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.
  41. "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].
  42. "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.
  43. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  44. "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.
  45. "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.
  46. "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.
  47. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-785 AND THR-789, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  48. "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.
  49. "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.
  50. "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) [PubMed] [Europe PMC] [Abstract]
    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.

Entry informationi

Entry nameiITB1_HUMAN
AccessioniPrimary (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 historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: December 16, 2008
Last modified: May 27, 2015
This is version 194 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.