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Protein

Catenin beta-1

Gene

Ctnnb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell adhesion, Neurogenesis, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_274349. formation of the beta-catenin:TCF transactivating complex.
REACT_275454. Ca2+ pathway.
REACT_280475. VEGFR2 mediated vascular permeability.
REACT_287155. CDO in myogenesis.
REACT_289020. Degradation of beta-catenin by the destruction complex.
REACT_292827. TCF dependent signaling in response to WNT.
REACT_312354. Adherens junctions interactions.
REACT_313206. Apoptotic cleavage of cell adhesion proteins.
REACT_341833. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_344709. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_345252. deactivation of the beta-catenin transactivating complex.
REACT_345474. Beta-catenin phosphorylation cascade.
REACT_362399. RHO GTPases activate IQGAPs.

Names & Taxonomyi

Protein namesi
Recommended name:
Catenin beta-1
Alternative name(s):
Beta-catenin
Gene namesi
Name:Ctnnb1
Synonyms:Catnb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi70487. Ctnnb1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cytoplasmcytoskeleton 1 Publication
  • Nucleus 1 Publication
  • Cell junctionadherens junction By similarity
  • Cell junction By similarity
  • Cell membrane 1 Publication
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
  • Cytoplasmcytoskeletonspindle pole By similarity

  • Note: Cytoplasmic when it is unstabilized (high level of phosphorylation) or bound to CDH1. Translocates to the nucleus when it is stabilized (low level of phosphorylation). Interaction with GLIS2 promotes nuclear translocation. Interaction with EMD inhibits nuclear localization. The majority of beta- catenin is localized to the cell membrane. In interphase, colocalizes with CROCC between CEP250 puncta at the proximal end of centrioles, and this localization is dependent on CROCC and CEP250. In mitosis, when NEK2 activity increases, it localizes to centrosomes at spindle poles independent of CROCC. Colocalizes with CDK5 in the cell-cell contacts and plasma membrane of undifferentiated and differentiated neuroblastoma cells. Colocalized with RAPGEF2 and TJP1 at cell-cell contacts (By similarity).By similarity

GO - Cellular componenti

  • apical part of cell Source: Ensembl
  • basolateral plasma membrane Source: Ensembl
  • beta-catenin destruction complex Source: UniProtKB
  • beta-catenin-TCF7L2 complex Source: UniProtKB
  • bicellular tight junction Source: Ensembl
  • catenin complex Source: UniProtKB
  • cell-cell adherens junction Source: RGD
  • cell-cell junction Source: UniProtKB
  • cell cortex Source: UniProtKB
  • cell junction Source: UniProtKB
  • cell periphery Source: BHF-UCL
  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: RGD
  • dendritic shaft Source: RGD
  • extracellular exosome Source: Ensembl
  • fascia adherens Source: Ensembl
  • focal adhesion Source: Ensembl
  • lamellipodium Source: Ensembl
  • lateral plasma membrane Source: Ensembl
  • membrane Source: UniProtKB
  • microvillus membrane Source: Ensembl
  • nuclear euchromatin Source: Ensembl
  • nucleus Source: RGD
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • protein complex Source: RGD
  • protein-DNA complex Source: UniProtKB
  • Scrib-APC-beta-catenin complex Source: Ensembl
  • spindle pole Source: UniProtKB-SubCell
  • synapse Source: RGD
  • transcription factor complex Source: UniProtKB
  • Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 781780Catenin beta-1PRO_0000064273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei23 – 231Phosphoserine; by GSK3-beta; alternateBy similarity
Glycosylationi23 – 231O-linked (GlcNAc); alternateBy similarity
Modified residuei29 – 291Phosphoserine; by GSK3-betaBy similarity
Modified residuei33 – 331Phosphoserine; by GSK3-beta and HIPK2By similarity
Modified residuei37 – 371Phosphoserine; by GSK3-beta and HIPK2By similarity
Modified residuei41 – 411Phosphothreonine; by GSK3-betaBy similarity
Modified residuei45 – 451PhosphoserineBy similarity
Modified residuei49 – 491N6-acetyllysineBy similarity
Modified residuei64 – 641Phosphotyrosine; by PTK6By similarity
Modified residuei86 – 861Phosphotyrosine; by CSKBy similarity
Modified residuei142 – 1421Phosphotyrosine; by FYN and PTK6By similarity
Modified residuei191 – 1911Phosphoserine; by CDK5By similarity
Modified residuei246 – 2461Phosphoserine; by CDK5By similarity
Modified residuei331 – 3311PhosphotyrosineBy similarity
Modified residuei552 – 5521Phosphoserine; by AMPKBy similarity
Modified residuei556 – 5561PhosphothreonineBy similarity
Modified residuei619 – 6191S-nitrosocysteineBy similarity
Modified residuei654 – 6541Phosphotyrosine; by CSKBy similarity
Modified residuei675 – 6751Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding. Phosphorylated on Ser-33 and Ser-37 by HIPK2; this phosphorylation triggers proteasomal degradation. Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription. Phosphorylation on Ser-191 and Ser-246 by CDK5. Phosphorylation by CDK2 regulates insulin internalization (By similarity). Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331 and/or Tyr-333 with the predominant site at Tyr-64 is not essential for inhibition of transcriptional activity (By similarity).By similarity
Ubiquitinated by the SCF(BTRC) E3 ligase complex when phosphorylated by GSK3B, leading to its degradation. Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent proteasomal degradation (By similarity).By similarity
S-nitrosylation at Cys-619 within adherens junctions promotes VEGF-induced, NO-dependent endothelial cell permeability by disrupting interaction with E-cadherin, thus mediating disassembly adherens junctions.By similarity
O-glycosylation at Ser-23 decreases nuclear localization and transcriptional activity, and increases localization to the plasma membrane and interaction with E-cadherin CDH1.By similarity
Deacetylated at Lys-49 by SIRT1.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

PaxDbiQ9WU82.
PRIDEiQ9WU82.

PTM databases

PhosphoSiteiQ9WU82.

Expressioni

Tissue specificityi

Expressed in the testis.

Developmental stagei

Highly expressed at E30-60 day DPC in the testis. Reduced expression at E90 day DPC.

Gene expression databases

ExpressionAtlasiQ9WU82. baseline and differential.
GenevisibleiQ9WU82. RN.

Interactioni

Subunit structurei

Two separate complex-associated pools are found in the cytoplasm. The majority is present as component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1 and beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Another cytoplasmic pool is part of a large complex containing AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 Interacts directly with AXIN1; the interaction is regulated by CK2 via BTRC and its subsequent degradation by the proteasome. Interacts directly with AXIN1;the interaction is regulated by CDK2 phosphorylation. Wnt-dependent activation of DVL antagonizes the action of GSK3B. When GSK3B activity is inhibited the complex dissociates, CTNNB1 is dephosphorylated and is no longer targeted for destruction. The stabilized protein translocates to the nucleus, where it binds TCF/LEF-1 family members, TBP, BCL9, BCL9L and possibly also RUVBL1 and CHD8. Binds CTNNBIP and EP300. CTNNB1 forms a ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1 binding. Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits the transcriptional activity of CTNNB1. Interacts with AJAP1, BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds SLC9A3R1. Interacts with GLIS2. Interacts with XIRP1. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain) and with SLC30A9. Interacts with EMD. Interacts with SCRIB. Interacts with TNIK and TCF7L2. Interacts with SESTD1 and TRPC4. Interacts directly with AXIN1; the interaction is regulated by CDK2 phosphorylation of AXIN1. Interacts with CAV1. Interacts with TRPV4. The TRPV4 and CTNNB1 complex can interact with CDH1. Interacts with VCL. Interacts with PTPRJ. Interacts with PKT7. Interacts with NANOS1. Interacts with CDK2, NDRG2, NEK2 and CDK5. Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B. Interacts with PTK6. Interacts with SOX7; this interaction may lead to proteasomal degradation of active CTNNB1 and thus inhibition of Wnt/beta-catenin-stimulated transcription. Identified in a complex with HINT1 and MITF. Interacts with FHIT. The CTNNB1 and TCF4 complex interacts with PML. Interacts with FERMT2. Identified in a complex with TCF4 and FERMT2. Interacts with RAPGEF2. Interacts with FAT1 (via the cytoplasmic domain). Interacts with RORA. May interact with P-cadherin/CDH3. Interacts with RNF220 (By similarity). Interacts with Interacts with CTNND2 (By similarity).By similarity3 Publications

Protein-protein interaction databases

BioGridi249913. 11 interactions.
DIPiDIP-37053N.
IntActiQ9WU82. 4 interactions.
MINTiMINT-87458.
STRINGi10116.ENSRNOP00000026016.

Structurei

3D structure databases

ProteinModelPortaliQ9WU82.
SMRiQ9WU82. Positions 19-44, 118-682.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati151 – 19141ARM 1Add
BLAST
Repeati193 – 23442ARM 2Add
BLAST
Repeati235 – 27642ARM 3Add
BLAST
Repeati277 – 31842ARM 4Add
BLAST
Repeati319 – 36042ARM 5Add
BLAST
Repeati361 – 38929ARM 6Add
BLAST
Repeati400 – 44142ARM 7Add
BLAST
Repeati442 – 48443ARM 8Add
BLAST
Repeati489 – 53042ARM 9Add
BLAST
Repeati531 – 57141ARM 10Add
BLAST
Repeati594 – 63643ARM 11Add
BLAST
Repeati637 – 66630ARM 12Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2322Interaction with VCLBy similarityAdd
BLAST
Regioni156 – 17823Interaction with BCL9By similarityAdd
BLAST
Regioni772 – 78110Interaction with SCRIBBy similarity

Sequence similaritiesi

Belongs to the beta-catenin family.Curated
Contains 12 ARM repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG297695.
HOGENOMiHOG000230958.
HOVERGENiHBG000919.
InParanoidiQ9WU82.
KOiK02105.
OrthoDBiEOG7X9G6B.
PhylomeDBiQ9WU82.
TreeFamiTF317997.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamiPF00514. Arm. 4 hits.
[Graphical view]
PRINTSiPR01869. BCATNINFAMLY.
SMARTiSM00185. ARM. 12 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9WU82-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG
60 70 80 90 100
NPEEEDVDTS QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP
110 120 130 140 150
ETLDEGMQIP STQFDAAHPT NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT
160 170 180 190 200
RAIPELTKLL NDEDQVVVNK AAVMVHQLSK KEASRHAIMR SPQMVSAIVR
210 220 230 240 250
TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL VKMLGSPVDS
260 270 280 290 300
VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC
310 320 330 340 350
LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC
360 370 380 390 400
SSNKPAIVEA GGMQALGPHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG
410 420 430 440 450
LLGTLVQLLG SDDINVVTCA AGILSNLTCN NYKNKMMVCQ VGGIEALVRT
460 470 480 490 500
VLRAGDREDI TEPAICALRH LTSRHQEAEM AQNAVRLHYG LPVVVKLLHP
510 520 530 540 550
PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL VRAHQDTQRR
560 570 580 590 600
TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV
610 620 630 640 650
QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG
660 670 680 690 700
VATYAAAVLF RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI
710 720 730 740 750
GAQGEALGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV
760 770 780
DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L
Length:781
Mass (Da):85,455
Last modified:November 1, 1999 - v1
Checksum:i9C29186B6DD54B87
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti368 – 3681P → L in AAK85253 (PubMed:11867232).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121265 mRNA. Translation: AAD28504.1.
AF397179 Genomic DNA. Translation: AAK85253.1.
RefSeqiNP_445809.2. NM_053357.2.
XP_008764913.1. XM_008766691.1.
UniGeneiRn.112601.

Genome annotation databases

GeneIDi84353.
KEGGirno:84353.
UCSCiRGD:70487. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121265 mRNA. Translation: AAD28504.1.
AF397179 Genomic DNA. Translation: AAK85253.1.
RefSeqiNP_445809.2. NM_053357.2.
XP_008764913.1. XM_008766691.1.
UniGeneiRn.112601.

3D structure databases

ProteinModelPortaliQ9WU82.
SMRiQ9WU82. Positions 19-44, 118-682.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249913. 11 interactions.
DIPiDIP-37053N.
IntActiQ9WU82. 4 interactions.
MINTiMINT-87458.
STRINGi10116.ENSRNOP00000026016.

PTM databases

PhosphoSiteiQ9WU82.

Proteomic databases

PaxDbiQ9WU82.
PRIDEiQ9WU82.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi84353.
KEGGirno:84353.
UCSCiRGD:70487. rat.

Organism-specific databases

CTDi1499.
RGDi70487. Ctnnb1.

Phylogenomic databases

eggNOGiNOG297695.
HOGENOMiHOG000230958.
HOVERGENiHBG000919.
InParanoidiQ9WU82.
KOiK02105.
OrthoDBiEOG7X9G6B.
PhylomeDBiQ9WU82.
TreeFamiTF317997.

Enzyme and pathway databases

ReactomeiREACT_274349. formation of the beta-catenin:TCF transactivating complex.
REACT_275454. Ca2+ pathway.
REACT_280475. VEGFR2 mediated vascular permeability.
REACT_287155. CDO in myogenesis.
REACT_289020. Degradation of beta-catenin by the destruction complex.
REACT_292827. TCF dependent signaling in response to WNT.
REACT_312354. Adherens junctions interactions.
REACT_313206. Apoptotic cleavage of cell adhesion proteins.
REACT_341833. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_344709. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_345252. deactivation of the beta-catenin transactivating complex.
REACT_345474. Beta-catenin phosphorylation cascade.
REACT_362399. RHO GTPases activate IQGAPs.

Miscellaneous databases

NextBioi616667.
PROiQ9WU82.

Gene expression databases

ExpressionAtlasiQ9WU82. baseline and differential.
GenevisibleiQ9WU82. RN.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamiPF00514. Arm. 4 hits.
[Graphical view]
PRINTSiPR01869. BCATNINFAMLY.
SMARTiSM00185. ARM. 12 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Study on the formation of specialized inter-Sertoli cell junctions in vitro."
    Chung S.S.W., Lee W.M., Cheng C.Y.
    J. Cell. Physiol. 181:258-272(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Testis.
  2. "Sequencing of the rat beta-catenin gene (Ctnnb1) and mutational analysis of liver tumors induced by 2-amino-3-methylimidazo[4,5-f]quinoline."
    Li Q., Dixon B.M., Al-Fageeh M., Blum C.A., Dashwood R.H.
    Gene 283:255-262(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Fischer 344.
  3. "The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt signaling pathway."
    Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.
    Genes Dev. 20:1933-1945(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH MACF1; APC; AXIN1 AND GSK3B.
  4. "The Fat1 cadherin integrates vascular smooth muscle cell growth and migration signals."
    Hou R., Liu L., Anees S., Hiroyasu S., Sibinga N.E.
    J. Cell Biol. 173:417-429(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAT1.
  5. "A novel beta-catenin-binding protein inhibits beta-catenin-dependent Tcf activation and axis formation."
    Sakamoto I., Kishida S., Fukui A., Kishida M., Yamamoto H., Hino S., Michiue T., Takada S., Asashima M., Kikuchi A.
    J. Biol. Chem. 275:32871-32878(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHD8.
  6. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCTNB1_RAT
AccessioniPrimary (citable) accession number: Q9WU82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 145 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

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.