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Protein

Integrin beta-1

Gene

Itgb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 and 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. 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. 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. 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 RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi152MagnesiumBy similarity1
Metal bindingi154Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi156Calcium 1By similarity1
Metal bindingi157Calcium 1By similarity1
Metal bindingi189Calcium 2By similarity1
Metal bindingi244Calcium 2By similarity1
Metal bindingi246Calcium 2By similarity1
Metal bindingi248Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi249Calcium 2By similarity1
Metal bindingi249MagnesiumBy similarity1

GO - Molecular functioni

  • actin binding Source: RGD
  • alpha-actinin binding Source: RGD
  • collagen binding Source: RGD
  • fibronectin binding Source: RGD
  • glycoprotein binding Source: RGD
  • integrin binding Source: RGD
  • kinase binding Source: RGD
  • laminin binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • peptide binding Source: RGD
  • protease binding Source: RGD
  • protein complex binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein kinase binding Source: RGD
  • receptor activity Source: InterPro
  • receptor binding Source: RGD

GO - Biological processi

  • bicellular tight junction assembly Source: RGD
  • cell adhesion Source: RGD
  • cell adhesion mediated by integrin Source: UniProtKB
  • cell-matrix adhesion Source: InterPro
  • cellular calcium ion homeostasis Source: RGD
  • cellular response to ionizing radiation Source: RGD
  • cellular response to low-density lipoprotein particle stimulus Source: UniProtKB
  • cellular response to mechanical stimulus Source: RGD
  • cellular response to vitamin D Source: RGD
  • integrin-mediated signaling pathway Source: RGD
  • maternal process involved in female pregnancy Source: RGD
  • negative regulation of cell projection organization Source: RGD
  • negative regulation of cell proliferation Source: RGD
  • negative regulation of neuron differentiation Source: RGD
  • positive regulation of cell migration Source: RGD
  • positive regulation of cell-substrate adhesion Source: RGD
  • positive regulation of endocytosis Source: RGD
  • positive regulation of establishment of protein localization to plasma membrane Source: UniProtKB
  • positive regulation of MAPK cascade Source: RGD
  • positive regulation of neuron differentiation Source: RGD
  • positive regulation of neuron projection development Source: RGD
  • positive regulation of peptidyl-tyrosine phosphorylation Source: RGD
  • protein transport within lipid bilayer Source: RGD
  • receptor internalization Source: UniProtKB
  • regulation of collagen catabolic process Source: UniProtKB
  • regulation of G-protein coupled receptor protein signaling pathway Source: RGD
  • response to activity Source: RGD
  • response to drug Source: RGD
  • response to gonadotropin Source: RGD
  • response to nutrient levels Source: RGD
  • response to transforming growth factor beta Source: RGD
  • tissue homeostasis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin beta-1
Alternative name(s):
Beta oligodendroglia
Short name:
Beta OL
Fibronectin receptor subunit beta
VLA-4 subunit beta
CD_antigen: CD29
Gene namesi
Name:Itgb1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2927. Itgb1.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Cell projectioninvadopodium membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Cell projectionruffle membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Recycling endosome By similarity
  • Melanosome By similarity
  • Cell projectionlamellipodium By similarity
  • Cell projectionruffle By similarity
  • Cell junctionfocal adhesion By similarity
  • Cell surface By similarity

  • Note: Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. 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 to fibrillar adhesions in an ITGB1BP1-dependent manner.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 729ExtracellularSequence analysisAdd BLAST709
Transmembranei730 – 752HelicalSequence analysisAdd BLAST23
Topological domaini753 – 799CytoplasmicSequence analysisAdd BLAST47

GO - Cellular componenti

  • acrosomal vesicle Source: RGD
  • adherens junction Source: RGD
  • basement membrane Source: RGD
  • cell-cell junction Source: RGD
  • cell surface Source: RGD
  • focal adhesion Source: RGD
  • hemidesmosome Source: RGD
  • integrin alpha3-beta1 complex Source: RGD
  • integrin alpha9-beta1 complex Source: RGD
  • integrin complex Source: RGD
  • invadopodium membrane Source: UniProtKB
  • lamellipodium Source: UniProtKB-SubCell
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: RGD
  • membrane raft Source: RGD
  • plasma membrane Source: Reactome
  • recycling endosome Source: UniProtKB-SubCell
  • ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20By similarityAdd BLAST20
ChainiPRO_000001633621 – 798Integrin beta-1Add BLAST778

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 45By similarity
Disulfide bondi35 ↔ 465By similarity
Disulfide bondi38 ↔ 75By similarity
Disulfide bondi48 ↔ 64By similarity
Glycosylationi50N-linked (GlcNAc...)Sequence analysis1
Glycosylationi94N-linked (GlcNAc...)Sequence analysis1
Glycosylationi97N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi207 ↔ 213By similarity
Glycosylationi212N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi261 ↔ 301By similarity
Glycosylationi269N-linked (GlcNAc...)Sequence analysis1
Glycosylationi363N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi401 ↔ 415By similarity
Glycosylationi406N-linked (GlcNAc...)Sequence analysis1
Glycosylationi417N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi435 ↔ 463By similarity
Disulfide bondi467 ↔ 692By similarity
Disulfide bondi478 ↔ 490By similarity
Glycosylationi482N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi487 ↔ 526By similarity
Disulfide bondi492 ↔ 501By similarity
Disulfide bondi503 ↔ 517By similarity
Glycosylationi521N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi532 ↔ 537By similarity
Disulfide bondi534 ↔ 569By similarity
Disulfide bondi539 ↔ 554By similarity
Disulfide bondi556 ↔ 561By similarity
Disulfide bondi575 ↔ 580By similarity
Disulfide bondi577 ↔ 608By similarity
Disulfide bondi582 ↔ 591By similarity
Glycosylationi585N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi593 ↔ 600By similarity
Disulfide bondi614 ↔ 619By similarity
Disulfide bondi616 ↔ 662By similarity
Disulfide bondi621 ↔ 631By similarity
Disulfide bondi634 ↔ 637By similarity
Disulfide bondi641 ↔ 650By similarity
Disulfide bondi647 ↔ 724By similarity
Disulfide bondi666 ↔ 700By similarity
Glycosylationi670N-linked (GlcNAc...)Sequence analysis1
Modified residuei778PhosphothreonineBy similarity1
Modified residuei784PhosphotyrosineBy similarity1
Modified residuei786PhosphoserineBy similarity1
Modified residuei790PhosphothreonineBy similarity1
Modified residuei795N6-acetyllysine; alternateBy similarity1
Cross-linki795Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP49134.
PRIDEiP49134.

PTM databases

iPTMnetiP49134.
PhosphoSitePlusiP49134.

Expressioni

Gene expression databases

BgeeiENSRNOG00000010966.

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. Binds LGALS3BP and NMRK2, when associated with alpha-7, but not with alpha-5. Interacts with FLNA, FLNB, FLNC and RANBP9. Interacts with KRT1 in the presence of RACK1 and SRC. Interacts with JAML; integrin alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by controlling JAML homodimerization. Interacts with RAB21. Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region). Interacts with FGR and HCK. Interacts with MYO10. Interacts with DAB2. Interacts with ITGB1BP1 (via C-terminal region); the interaction is a prerequisite for focal adhesion disassembly. Interacts with FERMT2; the interaction is inhibited in presence of ITGB1BP1. Interacts with TLN1; the interaction is prevented by competitive binding of ITGB1BP1. Interacts with ACAP1; required for ITGB1 recycling. Interacts with ASAP3. Interacts with seprase FAP (seprase); the interaction occurs at the cell surface of invadopodia membrane in a collagen-dependent manner. Interacts with EMP2; the interaction may be direct or indirect and ITGB1 has a heterodimer form (By similarity). ITGA5:ITGB1 interacts with NOV. ITGA4:ITGB1 is found in a ternary complex with CX3CR1 and CX3CL1. ITGA5:ITGB1 interacts with FBN1.By similarity

GO - Molecular functioni

  • actin binding Source: RGD
  • alpha-actinin binding Source: RGD
  • collagen binding Source: RGD
  • fibronectin binding Source: RGD
  • integrin binding Source: RGD
  • kinase binding Source: RGD
  • laminin binding Source: RGD
  • protease binding Source: RGD
  • protein complex binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein kinase binding Source: RGD
  • receptor binding Source: RGD

Protein-protein interaction databases

BioGridi246668. 6 interactors.
IntActiP49134. 4 interactors.
MINTiMINT-122445.
STRINGi10116.ENSRNOP00000014785.

Structurei

3D structure databases

ProteinModelPortaliP49134.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini140 – 378VWFAAdd BLAST239
Repeati467 – 516IAdd BLAST50
Repeati517 – 560IIAdd BLAST44
Repeati561 – 599IIIAdd BLAST39
Repeati600 – 636IVAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni207 – 213CX3CL1-bindingBy similarity7
Regioni295 – 314CX3CL1-bindingBy similarityAdd BLAST20
Regioni467 – 636Cysteine-rich tandem repeatsAdd BLAST170
Regioni763 – 768Signal for sorting from recycling endosomes; interaction with ACAP1By similarity6
Regioni786 – 793Interaction with ITGB1BP1By similarity8

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1226. Eukaryota.
ENOG410XP60. LUCA.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiP49134.
KOiK05719.
PhylomeDBiP49134.
TreeFamiTF105392.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR013111. EGF_extracell.
IPR033760. Integin_beta_N.
IPR027071. Integrin_beta-1.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR012896. Integrin_bsu_tail.
IPR002369. Integrin_bsu_VWA.
IPR032695. Integrin_dom.
IPR016201. PSI.
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.
PF17205. PSI_integrin. 1 hit.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM01241. Integrin_b_cyt. 1 hit.
SM01242. Integrin_B_tail. 1 hit.
SM00423. PSI. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 2 hits.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P49134-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLQLVFWIG LISLICSVFG QTDKNRCLKA NAKSCGECIQ AGPNCGWCTN
60 70 80 90 100
TTFLQEGMPT SARCDDLEAL KKKGCHPSDI ENPRGSQTIK KNKNVTNRSK
110 120 130 140 150
GMAEKLRPED ITQIQPQQLL LKLRSGEPQK FTLKFKRAED YPIDLYYLMD
160 170 180 190 200
LSYSMKDDLE NVKSLGTDLM NEMRRITSDF RIGFGSFVEK TVMPYISTTP
210 220 230 240 250
AKLRNPCTSE QNCTSPFSYK NVLSLTDRGE FFNELVGQQR ISGNLDSPEG
260 270 280 290 300
GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
310 320 330 340 350
CHLENNVYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN
360 370 380 390 400
LIPKSAVGTL SGNSSNVIQL IIDAYNSLSS EVILENSKLP DGVTINYKSY
410 420 430 440 450
CKNGVNGTGE NGRKCSNISI GDEVQFEISI TANKCPNKES ENQLKLNPLG
460 470 480 490 500
FTEEVEVVLQ FICKCNCQSH GIPASPKCHE GNGTFECGAC RCNEGRVGRH
510 520 530 540 550
CECSTDEVNS EDMDAYCRKE NSSEICSNNG ECVCGQCVCR KRENTNEIYS
560 570 580 590 600
GKFCECDNFN CDRSNGLICG GNGVCRCRVC ECYPNYTGSA CDCSLDTVPC
610 620 630 640 650
VATNGQICNG RGICECGACK CTDPKFQGPT CETCQTCLGV CAEHKECVQC
660 670 680 690 700
RAFNKGEKKD TCAQECSHFN LTKVESREKL PQPVQVDPVT HCKEKDIDDC
710 720 730 740 750
WFYFTYSVNS KGEAHVHVVE TPDCPTGPDI IPIVAGVVAG IVLIGLALLL
760 770 780 790
IWKLLMIIHD RREFAKFEKE KMNAKWDTGE NPIYKSAVTT VVNPKYEGK
Length:799
Mass (Da):88,495
Last modified:February 1, 1996 - v1
Checksum:iF4475202EB8A3EA6
GO

Sequence cautioni

The sequence AAI31846 differs from that shown. Reason: Frameshift at positions 442, 443 and 447.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti76H → Q in AAI31846 (PubMed:15489334).Curated1
Sequence conflicti711K → N in AAI31846 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12309 mRNA. Translation: AAA86669.1.
BC131845 mRNA. Translation: AAI31846.1. Frameshift.
PIRiJC4126.
RefSeqiNP_058718.2. NM_017022.2.
UniGeneiRn.25733.

Genome annotation databases

GeneIDi24511.
KEGGirno:24511.
UCSCiRGD:2927. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12309 mRNA. Translation: AAA86669.1.
BC131845 mRNA. Translation: AAI31846.1. Frameshift.
PIRiJC4126.
RefSeqiNP_058718.2. NM_017022.2.
UniGeneiRn.25733.

3D structure databases

ProteinModelPortaliP49134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246668. 6 interactors.
IntActiP49134. 4 interactors.
MINTiMINT-122445.
STRINGi10116.ENSRNOP00000014785.

PTM databases

iPTMnetiP49134.
PhosphoSitePlusiP49134.

Proteomic databases

PaxDbiP49134.
PRIDEiP49134.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24511.
KEGGirno:24511.
UCSCiRGD:2927. rat.

Organism-specific databases

CTDi3688.
RGDi2927. Itgb1.

Phylogenomic databases

eggNOGiKOG1226. Eukaryota.
ENOG410XP60. LUCA.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiP49134.
KOiK05719.
PhylomeDBiP49134.
TreeFamiTF105392.

Miscellaneous databases

PROiP49134.

Gene expression databases

BgeeiENSRNOG00000010966.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR013111. EGF_extracell.
IPR033760. Integin_beta_N.
IPR027071. Integrin_beta-1.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR012896. Integrin_bsu_tail.
IPR002369. Integrin_bsu_VWA.
IPR032695. Integrin_dom.
IPR016201. PSI.
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.
PF17205. PSI_integrin. 1 hit.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM01241. Integrin_b_cyt. 1 hit.
SM01242. Integrin_B_tail. 1 hit.
SM00423. PSI. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 2 hits.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiITB1_RAT
AccessioniPrimary (citable) accession number: P49134
Secondary accession number(s): A2RRT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.