- Protein Classification
- Protein Complexes
- Species Selection
 | extracellular side |
| cytoplasmic side |
| ITB1_HUMAN » Integrin beta-1 » Fibronectin receptor subunit beta;Integrin VLA-4 subunit beta; | |
|---|---|
| Hydrophobic Thickness | 35.2 ± 4.0 Å |
| Tilt Angle | 40 ± 0° |
| ΔGtransfer | -31.5 kcal/mol |
| ΔGfold | -23.7 kcal/mol |
| Links | UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, Reactome |
| Topology | Out |
| TM Segments | 729-757 (729-761) |
| Pathways | Arrhythmogenic right ventricular cardiomyopathy (KEGG) Axon guidance (KEGG) Bacterial invasion of epithelial cells (KEGG) Cell adhesion molecules (KEGG) Cell-Cell communication (Reactome) Developmental Biology (Reactome) Dilated cardiomyopathy (KEGG) ECM-receptor interaction (KEGG) Extracellular matrix organization (Reactome) Focal adhesion (KEGG) Hemostasis (Reactome) Hypertrophic cardiomyopathy (KEGG) Immune System (Reactome) Leishmaniasis (KEGG) Leukocyte transendothelial migration (KEGG) NAD salvage pathway II (BioCyc) NAD salvage pathway III (BioCyc) Pathogenic Escherichia coli infection (KEGG) Pathways in cancer (KEGG) Pertussis (KEGG) Phagosome (KEGG) PI3K-Akt signaling pathway (KEGG) Proteoglycans in cancer (KEGG) Regulation of actin cytoskeleton (KEGG) Shigellosis (KEGG) Signal Transduction (Reactome) Small cell lung cancer (KEGG) Toxoplasmosis (KEGG) |
| PDB | 4dx9 (6/7...=784-798), 3t9k (758-769), 3vi3 (B/D=21-465), 3vi4 (B/D=21-465), 4wjk (B=21-465), 4wk0 (B=21-465), 4wk2 (B=21-465), 4wk4 (B=21-465), 3g9w (C/D=752-785) |
| OPM | 3g9w |
| Complexes | |
| Interactions | 4F2, Complex: YLAT2:ITB1:4F2, PubMed ADA12, Complex: ITA9:ITB1:ADA12, PubMed ADA15, Complex: ADA15:ITA9:ITB1, PubMed ADA17, Complex: ADA17:ITB1, PubMed ADAM2, Complex: ADAM2:ITA9:ITB1, PubMed ADAM8, Complex: ITA9:ITB1:ADAM8, PubMed CALX, Complex: CALX:ITB1, PubMed CALX, Complex: CD9:ITB1:CALX, PubMed CD44, Complex: CD44:ITB1, PubMed CSPG4, Complex: ITB1:CSPG4, PubMed DAG1, Complex: ITB1:DAG1, PubMed EGLN, Complex: EGLN:ITB1, PubMed EPHA2, Complex: EPHA2:ITB1 ICAM4, Complex: ICAM4:ITB1, PubMed IGF1R, Complex: IGF1R:ITB1, PubMed IL3RB, Complex: IL3RB:ITB1, PubMed ITA10, Complex: ITB1:ITA10, PubMed ITA11, Complex: ITA11:ITB1, PubMed ITA1, Complex: ITB1:ITA1:CO6A3, PubMed ITA2, Complex: CD47:ITB1:ITA2, PubMed ITA3, Complex: PI4KA:CD81:ITA3:ITB1:CD63, PubMed ITA4, Complex: CD53:ITB1:ITA4, PubMed ITA5, Complex: ITA5:ITB1, PDBID: 3vi3, PubMed ITA6, Complex: CD151:ITB1:ITA6, PubMed ITA7, Complex: CD151:ITB1:ITA7, PubMed ITA8, Complex: ITA8:ITB1, PubMed ITA9, Complex: ITB1:TENA:ITA9, PubMed ITAV, Complex: ITB1:ITAV, PubMed ITB3, Complex: NID1:ITB3:ITB1, PubMed ITB5, Complex: ITB1:KPCE:ITB5, PubMed JAM2, Complex: ITB1:JAM2:ITA4, PubMed MCP, Complex: MCP:ITB1, PubMed NRP1, Complex: ITB1:NRP1 PRLR, Complex: ITB1:PRLR, PubMed PTN2, Complex: ITA1:ITB1:PTN2, PubMed SE1L1, Complex: SE1L1:ITB1 SHPS1, Complex: ITB1:SHPS1, PubMed TGON2, Complex: TGON2:ITB1, PubMed |
| Domains | AA: 25-76, PDBID: 3VI3, Subunit B, Seq Identity:100%, Integrin plexin domain AA: 138-382, PDBID: 3VI3, Subunit B, Seq Identity:100%, Integrin beta chain VWA domain AA: 599-630, PDBID: 1JV2, Subunit B, Seq Identity:60%, EGF-like domain AA: 640-728, PDBID: 1JV2, Subunit B, Seq Identity:33%, Integrin beta tail domain AA: 752-796, PDBID: 3G9W, Subunit C, Seq Identity:100%, Integrin beta cytoplasmic domain |
| UniProt annotation for ITB1_HUMAN » Integrin beta-1 |
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| 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. 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. FUNCTION: Isoform 5: Isoform 5 displaces isoform 1 in striated muscles. SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-1 associates with either alpha-1, alpha-2, alpha-3, alpha-4, alpha- 5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or alpha-V. 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). 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). |
| UniProt features for ITB1_HUMAN » Integrin beta-1 |
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SIGNAL 1 20 CHAIN 21 798 Integrin beta-1. DOMAIN 140 378 VWFA. REPEAT 466 515 I. REPEAT 516 559 II. REPEAT 560 598 III. REPEAT 599 635 IV. REGION 466 635 Cysteine-rich tandem repeats. REGION 785 792 Interaction with ITGB1BP1. DISULFID 27 45 DISULFID 35 464 DISULFID 38 64 DISULFID 48 75 DISULFID 207 213 DISULFID 261 301 DISULFID 401 415 DISULFID 435 462 DISULFID 466 691 Probable. DISULFID 477 489 By similarity. DISULFID 486 525 By similarity. DISULFID 491 500 By similarity. DISULFID 502 516 By similarity. DISULFID 531 536 By similarity. DISULFID 533 568 By similarity. DISULFID 538 553 By similarity. DISULFID 555 560 By similarity. DISULFID 574 579 By similarity. DISULFID 576 607 By similarity. DISULFID 581 590 By similarity. DISULFID 592 599 By similarity. DISULFID 613 618 By similarity. DISULFID 615 661 By similarity. DISULFID 620 630 By similarity. DISULFID 633 636 By similarity. DISULFID 640 649 By similarity. DISULFID 646 723 By similarity. DISULFID 665 699 By similarity. |
| Amino Acid Sequence for ITB1_HUMAN » Integrin beta-1 |
|---|
| MNLQPIFWIG LISSVCCVFA QTDENRCLKA NAKSCGECIQ AGPNCGWCTN STFLQEGMPT SARCDDLEAL KKKGCPPDDI ENPRGSKDIK KNKNVTNRSK GTAEKLKPED ITQIQPQQLV LRLRSGEPQT FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTNKGE VFNELVGKQR ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ CHLENNMYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL SANSSNVIQL IIDAYNSLSS EVILENGKLS EGVTISYKSY CKNGVNGTGE NGRKCSNISI GDEVQFEISI TSNKCPKKDS DSFKIRPLGF TEEVEVILQY ICECECQSEG IPESPKCHEG NGTFECGACR CNEGRVGRHC ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCKCRVCE CNPNYTGSAC DCSLDTSTCE ASNGQICNGR GICECGVCKC TDPKFQGQTC EMCQTCLGVC AEHKECVQCR AFNKGEKKDT CTQECSYFNI TKVESRDKLP QPVQPDPVSH CKEKDVDDCW FYFTYSVNGN NEVMVHVVEN PECPTGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN PIYKSAVTTV VNPKYEGK |
