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P49840 (GSK3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycogen synthase kinase-3 alpha

Short name=GSK-3 alpha
EC=2.7.11.26
Alternative name(s):
Serine/threonine-protein kinase GSK3A
EC=2.7.11.1
Gene names
Name:GSK3A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), CTNNB1/beta-catenin, APC and AXIN1. Requires primed phosphorylation of the majority of its substrates. Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. Regulates glycogen metabolism in liver, but not in muscle. May also mediate the development of insulin resistance by regulating activation of transcription factors. In Wnt signaling, regulates the level and transcriptional activity of nuclear CTNNB1/beta-catenin. Facilitates amyloid precursor protein (APP) processing and the generation of APP-derived amyloid plaques found in Alzheimer disease. May be involved in the regulation of replication in pancreatic beta-cells. Is necessary for the establishment of neuronal polarity and axon outgrowth. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. Ref.6 Ref.7

Catalytic activity

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

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by phosphorylation at Tyr-279. In response to insulin, inhibited by phosphorylation at Ser-21 by PKB/AKT1; phosphorylation at this site causes a conformational change, preventing access of substrates to the active site. Inhibited by lithium. Ref.8 Ref.13

Subunit structure

Monomer. Interacts with ARRB2 By similarity. Interacts with AXIN1 and CTNNB1/beta-catenin. Ref.7

Post-translational modification

Phosphorylated by AKT1 at Ser-21: upon insulin-mediated signaling, the activated PKB/AKT1 protein kinase phosphorylates and desactivates GSK3A, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-279.

Miscellaneous

Higher expression and activity of GSK3A are found in the skeletal muscle (vastus lateralis) of patients with type 2 diabetes (Ref.5). Several potent GSK3 (GSK3A and GSK3B) inhibitors have been identified and characterized in preclinical models for treatments of type 2 diabetes (Ref.13).

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 processCarbohydrate metabolism
Glycogen metabolism
Neurogenesis
Wnt signaling pathway
   Coding sequence diversityPolymorphism
   DiseaseAlzheimer disease
Diabetes mellitus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Signal transduction inhibitor
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Wnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

cardiac left ventricle morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to insulin stimulus

Inferred from mutant phenotype PubMed 17569761. Source: BHF-UCL

cellular response to interleukin-3

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from sequence or structural similarity. Source: UniProtKB

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

glycogen metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Inferred from sequence or structural similarity PubMed 18285345. Source: BHF-UCL

negative regulation of TOR signaling

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of UDP-glucose catabolic process

Inferred by curator PubMed 11035810. Source: UniProtKB

negative regulation of canonical Wnt signaling pathway

Traceable author statement Ref.13. Source: UniProtKB

negative regulation of cell growth involved in cardiac muscle cell development

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of glucose import

Inferred from mutant phenotype PubMed 17569761. Source: BHF-UCL

negative regulation of glycogen (starch) synthase activity

Traceable author statement Ref.13. Source: UniProtKB

negative regulation of glycogen biosynthetic process

Traceable author statement Ref.13. Source: UniProtKB

negative regulation of insulin receptor signaling pathway

Inferred from mutant phenotype PubMed 17569761. Source: BHF-UCL

negative regulation of transferase activity

Inferred from mutant phenotype PubMed 17569761. Source: BHF-UCL

negative regulation of type B pancreatic cell development

Traceable author statement Ref.13. Source: UniProtKB

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

positive regulation of adrenergic receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cAMP biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of glycogen (starch) synthase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of heart contraction

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein catabolic process

Non-traceable author statement PubMed 19759537. Source: BHF-UCL

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 11035810. Source: BHF-UCL

regulation of systemic arterial blood pressure

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentbeta-catenin destruction complex

Traceable author statement Ref.13. Source: UniProtKB

cytosol

Traceable author statement PubMed 11035810. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase A catalytic subunit binding

Inferred from physical interaction PubMed 11035810. Source: BHF-UCL

protein serine/threonine kinase activity

Inferred from direct assay PubMed 11035810. Source: BHF-UCL

tau-protein kinase activity

Traceable author statement Ref.13. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 483482Glycogen synthase kinase-3 alpha
PRO_0000085978

Regions

Domain119 – 403285Protein kinase
Nucleotide binding125 – 1339ATP By similarity
Compositional bias3 – 8381Gly-rich

Sites

Active site2441Proton acceptor By similarity
Binding site1481ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.12 Ref.14
Modified residue21Phosphoserine Ref.10 Ref.14
Modified residue211Phosphoserine; by PKB/AKT1
Modified residue721Phosphoserine Ref.10
Modified residue771Phosphoserine Ref.14
Modified residue971Phosphoserine Ref.14
Modified residue2791Phosphotyrosine By similarity

Natural variations

Natural variant1091Q → E.
Corresponds to variant rs35978177 [ dbSNP | Ensembl ].
VAR_051625
Natural variant4611L → F. Ref.17
Corresponds to variant rs35454502 [ dbSNP | Ensembl ].
VAR_040539

Experimental info

Sequence conflict4491A → S in AAA62432. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49840 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: F18C012C03B7D786

FASTA48350,981
        10         20         30         40         50         60 
MSGGGPSGGG PGGSGRARTS SFAEPGGGGG GGGGGPGGSA SGPGGTGGGK ASVGAMGGGV 

        70         80         90        100        110        120 
GASSSGGGPG GSGGGGSGGP GAGTSFPPPG VKLGRDSGKV TTVVATLGQG PERSQEVAYT 

       130        140        150        160        170        180 
DIKVIGNGSF GVVYQARLAE TRELVAIKKV LQDKRFKNRE LQIMRKLDHC NIVRLRYFFY 

       190        200        210        220        230        240 
SSGEKKDELY LNLVLEYVPE TVYRVARHFT KAKLTIPILY VKVYMYQLFR SLAYIHSQGV 

       250        260        270        280        290        300 
CHRDIKPQNL LVDPDTAVLK LCDFGSAKQL VRGEPNVSYI CSRYYRAPEL IFGATDYTSS 

       310        320        330        340        350        360 
IDVWSAGCVL AELLLGQPIF PGDSGVDQLV EIIKVLGTPT REQIREMNPN YTEFKFPQIK 

       370        380        390        400        410        420 
AHPWTKVFKS RTPPEAIALC SSLLEYTPSS RLSPLEACAH SFFDELRCLG TQLPNNRPLP 

       430        440        450        460        470        480 
PLFNFSAGEL SIQPSLNAIL IPPHLRSPAG TTTLTPSSQA LTETPTSSDW QSTDATPTLT 


NSS 

« Hide

References

« Hide 'large scale' references
[1]"Glycogen synthase kinase 3 and dorsoventral patterning in Xenopus embryos."
He X., Saint-Jeannet J.P., Woodgett J.R., Varmus H.E., Dawid I.B.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Foreskin.
[2]"Isolation of cDNA clones for human glycogen synthase kinase 3alpha."
Hoshino T., Kondo K., Ishiguro K., Takashima A., Imahori K.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Eye and Pancreas.
[5]"Potential role of glycogen synthase kinase-3 in skeletal muscle insulin resistance of type 2 diabetes."
Nikoulina S.E., Ciaraldi T.P., Mudaliar S., Mohideen P., Carter L., Henry R.R.
Diabetes 49:263-271(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH DIABETES MELLITUS.
[6]"GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides."
Phiel C.J., Wilson C.A., Lee V.M., Klein P.S.
Nature 423:435-439(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH ALZHEIMER DISEASE, FUNCTION.
[7]"GSK3alpha exhibits beta-catenin and tau directed kinase activities that are modulated by Wnt."
Asuni A.A., Hooper C., Reynolds C.H., Lovestone S., Anderton B.H., Killick R.
Eur. J. Neurosci. 24:3387-3392(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN WNT SIGNALING, INTERACTION WITH AXIN1 AND CTNNB1/BETA-CATENIN.
[8]"Glycogen synthase kinase-3: properties, functions, and regulation."
Ali A., Hoeflich K.P., Woodgett J.R.
Chem. Rev. 101:2527-2540(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION, ENZYME REGULATION.
[9]"The role of GSK3 in glucose homeostasis and the development of insulin resistance."
Lee J., Kim M.S.
Diabetes Res. Clin. Pract. 77:S49-S57(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[10]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Glycogen synthase kinase 3: more than a namesake."
Rayasam G.V., Tulasi V.K., Sodhi R., Davis J.A., Ray A.
Br. J. Pharmacol. 156:885-898(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION, ENZYME REGULATION.
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-77 AND SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-461.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L40027 mRNA. Translation: AAA62432.1.
D63424 mRNA. Translation: BAA23608.1.
AC006486 Genomic DNA. Translation: AAD11986.1.
BC027984 mRNA. Translation: AAH27984.1.
BC051865 mRNA. Translation: AAH51865.1.
RefSeqNP_063937.2. NM_019884.2.
UniGeneHs.466828.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DFMmodel-A98-449[»]
ProteinModelPortalP49840.
SMRP49840. Positions 99-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109186. 50 interactions.
IntActP49840. 34 interactions.
MINTMINT-1688290.
STRING9606.ENSP00000222330.

Chemistry

BindingDBP49840.
ChEMBLCHEMBL2850.
GuidetoPHARMACOLOGY2029.

PTM databases

PhosphoSiteP49840.

Polymorphism databases

DMDM12644292.

Proteomic databases

PaxDbP49840.
PeptideAtlasP49840.
PRIDEP49840.

Protocols and materials databases

DNASU2931.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222330; ENSP00000222330; ENSG00000105723.
ENST00000453535; ENSP00000412663; ENSG00000105723.
GeneID2931.
KEGGhsa:2931.
UCSCuc002otb.1. human.

Organism-specific databases

CTD2931.
GeneCardsGC19M042734.
HGNCHGNC:4616. GSK3A.
HPACAB004422.
HPA028423.
MIM606784. gene.
neXtProtNX_P49840.
PharmGKBPA29008.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233017.
HOVERGENHBG014652.
InParanoidP49840.
KOK08822.
OMADELRCHG.
OrthoDBEOG7TF78V.
PhylomeDBP49840.
TreeFamTF101104.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_6900. Immune System.
SignaLinkP49840.

Gene expression databases

ArrayExpressP49840.
BgeeP49840.
CleanExHS_GSK3A.
GenevestigatorP49840.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGSK3A. human.
GeneWikiGSK3A.
GenomeRNAi2931.
NextBio11615.
PROP49840.
SOURCESearch...

Entry information

Entry nameGSK3A_HUMAN
AccessionPrimary (citable) accession number: P49840
Secondary accession number(s): O14959
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM