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Reviewed, UniProtKB/Swiss-Prot P49841 (GSK3B_HUMAN)

Last modified November 3, 2009. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glycogen synthase kinase-3 beta
      Short name=GSK-3 beta
    EC=2.7.11.26
Gene names
Name: GSK3B
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Participates in the Wnt signaling pathway. Implicated in the hormonal control of several regulatory proteins including glycogen synthase, MYB and the transcription factor JUN. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. Phosphorylates MUC1 in breast cancer cells, and decreases the interaction of MUC1 with CTNNB1/beta-catenin. Phosphorylates CTNNB1/beta-catenin. Ref.5 Ref.24

Catalytic activity

ATP + [tau protein] = ADP + [tau protein] phosphate.

Enzyme regulation

Activated by phosphorylation at Tyr-216. Inhibited when phosphorylated by AKT1. Ref.24

Subunit structure

Monomer By similarity. Interacts with AXIN1, CABYR, MUC1, NIN and PRUNE.

Tissue specificity

Expressed in testis, thymus, prostate and ovary and weakly expressed in lung, brain and kidney.

Post-translational modification

Phosphorylated by AKT1 and ILK1. Activated by phosphorylation at Tyr-216. Ref.24 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processER overload response

Inferred from direct assay. Source: MGI

Wnt receptor signaling pathway through beta-catenin

Inferred by curator. Source: UniProtKB

glycogen metabolic process

Inferred from direct assay. Source: UniProtKB

peptidyl-serine phosphorylation

Inferred from direct assay. Source: UniProtKB

positive regulation of protein complex assembly

Inferred from direct assay. Source: UniProtKB

positive regulation of protein export from nucleus

Inferred from direct assay. Source: MGI

   Cellular componentAxin-APC-beta-catenin-GSK3B complex

Inferred from direct assay. Source: UniProtKB

beta-catenin destruction complex

Inferred from direct assay. Source: UniProtKB

cytosol

Inferred from Experiment. Source: Reactome

nucleus

Inferred from direct assay. Source: MGI

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

NF-kappaB binding

Inferred from physical interaction. Source: UniProtKB

beta-catenin binding

Inferred from physical interaction. Source: UniProtKB

glycogen synthase kinase 3 activity

Inferred from direct assay. Source: UniProtKB

p53 binding

Inferred from direct assay. Source: MGI

protein kinase A catalytic subunit binding

Inferred from physical interaction. Source: UniProtKB

tau-protein kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49841-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P49841-2)

The sequence of this isoform differs from the canonical sequence as follows:
     303-303: K → KDSSGTGHFTSGVR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Glycogen synthase kinase-3 beta
PRO_0000085980

Regions

Domain56 – 340285Protein kinase
Nucleotide binding62 – 709ATP By similarity

Sites

Active site1811Proton acceptor
Binding site851ATP By similarity

Amino acid modifications

Modified residue71Phosphothreonine By similarity
Modified residue91Phosphoserine; by PKB/AKT1 Ref.16 Ref.18
Modified residue2151Phosphoserine By similarity
Modified residue2161Phosphotyrosine Ref.24 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21
Modified residue2191Phosphoserine Ref.18
Modified residue2751Phosphothreonine Ref.18
Modified residue2771Phosphothreonine Ref.18
Modified residue3891Phosphoserine By similarity
Modified residue3901Phosphothreonine Ref.8 Ref.16 Ref.18 Ref.19
Modified residue3921Phosphothreonine Ref.18
Modified residue3951Phosphothreonine By similarity

Natural variations

Alternative sequence3031K → KDSSGTGHFTSGVR in isoform 2.
VSP_004790

Experimental info

Mutagenesis91S → A: Loss of phosphorylation; insensitive to inhibitory phosphorylation.
Sequence conflict281V → G in AAD48517. Ref.4
Sequence conflict3501L → H in AAA66475. Ref.1

Secondary structure

..................................................... 420
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: 4ACC24D00CDBB9C3

FASTA42046,744
        10         20         30         40         50         60 
MSGRPRTTSF AESCKPVQQP SAFGSMKVSR DKDGSKVTTV VATPGQGPDR PQEVSYTDTK 

        70         80         90        100        110        120 
VIGNGSFGVV YQAKLCDSGE LVAIKKVLQD KRFKNRELQI MRKLDHCNIV RLRYFFYSSG 

       130        140        150        160        170        180 
EKKDEVYLNL VLDYVPETVY RVARHYSRAK QTLPVIYVKL YMYQLFRSLA YIHSFGICHR 

       190        200        210        220        230        240 
DIKPQNLLLD PDTAVLKLCD FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDV 

       250        260        270        280        290        300 
WSAGCVLAEL LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP 

       310        320        330        340        350        360 
WTKVFRPRTP PEAIALCSRL LEYTPTARLT PLEACAHSFF DELRDPNVKL PNGRDTPALF 

       370        380        390        400        410        420 
NFTTQELSSN PPLATILIPP HARIQAAAST PTNATAASDA NTGDRGQTNN AASASASNST 

« Hide

Isoform 2.

Checksum: 540F853E1603A080
Show »

FASTA43348,034

References

« Hide 'large scale' references
[1]"Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation."
Stambolic V., Woodgett J.R.
Biochem. J. 303:701-704(1994) [PubMed: 7980435] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Eye and Placenta.
[3]"Radiation hybrid mapping of genes in the lithium-sensitive wnt signaling pathway."
Rhoads A.R., Karkera J.D., Detera-Wadleigh S.D.
Mol. Psychiatry 4:437-442(1999) [PubMed: 10523816] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 185-202.
[4]"Molecular cloning and characterization of the human glycogen synthase kinase-3beta promoter."
Lau K.F., Miller C.C.J., Anderton B.H., Shaw P.C.
Genomics 60:121-128(1999) [PubMed: 10486203] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
[5]"Interaction of glycogen synthase kinase 3beta with the DF3/MUC1 carcinoma-associated antigen and beta-catenin."
Li Y., Bharti A., Chen D., Gong J., Kufe D.
Mol. Cell. Biol. 18:7216-7224(1998) [PubMed: 9819408] [Abstract]
Cited for: INTERACTION WITH MUC1, FUNCTION.
[6]"Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase."
Delcommenne M., Tan C., Gray V., Rue L., Woodgett J.R., Dedhar S.
Proc. Natl. Acad. Sci. U.S.A. 95:11211-11216(1998) [PubMed: 9736715] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Cloning and characterization of a novel human ninein protein that interacts with the glycogen synthase kinase 3beta."
Hong Y.-R., Chen C.-H., Chang J.-H., Wang S.-K., Sy W.-D., Chou C.-K., Howng S.-L.
Biochim. Biophys. Acta 1492:513-516(2000) [PubMed: 11004522] [Abstract]
Cited for: INTERACTION WITH NIN.
[8]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Characterization of two non-testis-specific CABYR variants that bind to GSK3beta with a proline-rich extensin-like domain."
Hsu H.-C., Lee Y.-L., Cheng T.-S., Howng S.-L., Chang L.-K., Lu P.-J., Hong Y.-R.
Biochem. Biophys. Res. Commun. 329:1108-1117(2005) [PubMed: 15752768] [Abstract]
Cited for: INTERACTION WITH CABYR.
[10]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY.
[12]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY.
Tissue: Epithelium.
[13]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY.
Tissue: Epithelium.
[14]"Glycogen synthase kinase 3 and h-prune regulate cell migration by modulating focal adhesions."
Kobayashi T., Hino S., Oue N., Asahara T., Zollo M., Yasui W., Kikuchi A.
Mol. Cell. Biol. 26:898-911(2006) [PubMed: 16428445] [Abstract]
Cited for: INTERACTION WITH PRUNE.
[15]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY.
[16]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; TYR-216 AND THR-390, MASS SPECTROMETRY.
[17]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY.
Tissue: Platelet.
[18]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; TYR-216; SER-219; THR-275; THR-277; THR-390 AND THR-392, MASS SPECTROMETRY.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216 AND THR-390, MASS SPECTROMETRY.
[20]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[22]"Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition."
Dajani R., Fraser E., Roe S.M., Young N., Good V., Dale T.C., Pearl L.H.
Cell 105:721-732(2001) [PubMed: 11440715] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-386.
[23]"The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation."
Bax B., Carter P.S., Lewis C., Guy A.R., Bridges A., Tanner R., Pettman G., Mannix C., Culbert A.A., Brown M.J.B., Smith D.G., Reith A.D.
Structure 9:1143-1152(2001) [PubMed: 11738041] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 27-393 OF PHOSPHORYLATED GSK3B.
[24]"Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex."
Dajani R., Fraser E., Roe S.M., Yeo M., Good V.M., Thompson V., Dale T.C., Pearl L.H.
EMBO J. 22:494-501(2003) [PubMed: 12554650] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 35-384 IN COMPLEX WITH AXIN1, INTERACTION WITH AXIN1 AND FRAT1, FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT TYR-216.
+Additional computationally mapped references.

Cross-references

Sequence databases

L33801 mRNA. Translation: AAA66475.1.
BC000251 mRNA. Translation: AAH00251.1.
BC012760 mRNA. Translation: AAH12760.1.
AF098789 Genomic DNA. Translation: AAC69340.1.
AF074333 Genomic DNA. Translation: AAD48517.1.
IPIIPI00028570.
IPI00216190.
PIRS53324.
RefSeqNP_001139628.1.
NP_002084.2.
UniGeneHs.445733

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GNGX-ray2.60A/B27-393[»]
1H8FX-ray2.80A/B35-386[»]
1I09X-ray2.70A/B1-420[»]
1J1BX-ray1.80A/B1-420[»]
1J1CX-ray2.10A/B1-420[»]
1O9UX-ray2.40A35-384[»]
1PYXX-ray2.40A/B1-420[»]
1Q3DX-ray2.20A/B2-420[»]
1Q3WX-ray2.30A/B2-420[»]
1Q41X-ray2.10A/B2-420[»]
1Q4LX-ray2.77A/B2-420[»]
1Q5KX-ray1.94A/B7-420[»]
1R0EX-ray2.25A/B35-420[»]
1UV5X-ray2.80A35-384[»]
2JDOX-ray1.80C3-12[»]
2JDRX-ray2.30C3-12[»]
2JLDX-ray2.35A/B1-420[»]
2O5KX-ray3.20A29-393[»]
2OW3X-ray2.80A/B35-386[»]
2UW9X-ray2.10C3-12[»]
3CQUX-ray2.20C3-12[»]
3CQWX-ray2.00C3-12[»]
3DU8X-ray2.20A/B1-420[»]
3E87X-ray2.30C/D3-12[»]
3E88X-ray2.50C/D3-12[»]
3E8DX-ray2.70C/D3-12[»]
3F7ZX-ray2.40A/B35-383[»]
3F88X-ray2.60A/B35-383[»]
DisProtDP00385.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:878N.
IntActP49841. 72 interactions.
STRINGP49841.

PTM databases

PhosphoSiteP49841.

Proteomic databases

PRIDEP49841.

Genome annotation databases

EnsemblENST00000264235; ENSP00000264235; ENSG00000082701; Homo sapiens. [Genome view]
ENST00000316626; ENSP00000324806; ENSG00000082701; Homo sapiens. [Genome view]
GeneID2932.
KEGGhsa:2932.
UCSCuc003edn.1. human.
uc003edo.1. human.

Organism-specific databases

CTD2932.
GeneCardsGC03M121028.
H-InvDBHIX0003589.
HGNCHGNC:4617. GSK3B.
HPACAB016263.
MIM605004. gene.
PharmGKBPA29009.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP49841.
OMADQQVEIS.

Enzyme and pathway databases

BRENDA2.7.11.26. 247.
Pathway_Interaction_DBaurora_a_pathway. Aurora A signaling.
bmppathway. BMP receptor signaling.
wnt_canonical_pathway. Canonical Wnt signaling pathway.
pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.
insulin_glucose_pathway. Insulin-mediated glucose transport.
lysophospholipid_pathway. LPA receptor mediated events.
ps1pathway. Presenilin action in Notch and Wnt signaling.
reelinpathway. Reelin signaling pathway.
ar_tf_pathway. Regulation of Androgen receptor activity.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).
pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma.
ReactomeREACT_11045. Signaling by Wnt.
REACT_11061. Signalling by NGF.
REACT_18266. Axon guidance.

Gene expression databases

ArrayExpressP49841.
BgeeP49841.
CleanExHS_GSK3B.
GenevestigatorP49841.
GermOnlineENSG00000082701. Homo sapiens.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01356. Lithium.
NextBio11619.
SOURCESearch...

Entry information

Entry nameGSK3B_HUMAN
AccessionPrimary (citable) accession number: P49841
Secondary accession number(s): Q9BWH3, Q9UL47
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 2, 2002
Last modified: November 3, 2009
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents