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Q9H2K8 (TAOK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Serine/threonine-protein kinase TAO3

EC=2.7.11.1
Alternative name(s):
Cutaneous T-cell lymphoma-associated antigen HD-CL-09
Short name=CTCL-associated antigen HD-CL-09
Dendritic cell-derived protein kinase
JNK/SAPK-inhibitory kinase
Jun kinase-inhibitory kinase
Kinase from chicken homolog A
Short name=hKFC-A
Thousand and one amino acid protein 3
Gene names
Name:TAOK3
Synonyms:DPK, JIK, KDS, MAP3K18
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length898 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that acts as a regulator of the p38/MAPK14 stress-activated MAPK cascade and of the MAPK8/JNK cascade. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. Inhibits basal activity of MAPK8/JNK cascade and diminishes its activation in response epidermal growth factor (EGF). Ref.1 Ref.2 Ref.11

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Self-associates. Interacts with ERN1 and TRAF2. Interaction with TRAF2 is facilitated under ER stress conditions, such as treatment with tunicamycin, and may promote TRAF2 phosphorylation. Ref.10

Subcellular location

Cytoplasm. Cell membrane; Peripheral membrane protein. Note: Also localized to the peripheral cell membrane. Ref.3

Tissue specificity

Ubiquitously expressed at a low level, and highly expressed in peripheral blood leukocytes (PBLs), thymus, spleen, kidney, skeletal muscle, heart and liver. Ref.2 Ref.3

Post-translational modification

Autophosphorylated. Phosphorylation at Ser-324 by ATM following DNA damage is required for activation of the p38/MAPK14 stress-activated MAPK cascade. Phosphorylated by LRRK2. Ref.1 Ref.11 Ref.15

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAN09723.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

G2 DNA damage checkpoint

Inferred from mutant phenotype Ref.11. Source: UniProtKB

MAPK cascade

Inferred from mutant phenotype Ref.2. Source: HGNC

activation of MAPKK activity

Inferred from Biological aspect of Ancestor. Source: GOC

cellular response to DNA damage stimulus

Inferred from direct assay Ref.11. Source: UniProtKB

negative regulation of JNK cascade

Inferred from direct assay Ref.1. Source: HGNC

negative regulation of protein kinase activity

Traceable author statement Ref.1. Source: GOC

positive regulation of JNK cascade

Inferred from mutant phenotype Ref.2. Source: HGNC

positive regulation of JUN kinase activity

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of stress-activated MAPK cascade

Inferred from mutant phenotype Ref.11. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.1. Source: HGNC

protein phosphorylation

Inferred from mutant phenotype Ref.10. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein kinase inhibitor activity

Traceable author statement Ref.1. Source: ProtInc

protein serine/threonine kinase activity

Inferred from direct assay Ref.1. Source: HGNC

transferase activity

Inferred from direct assay Ref.1. Source: HGNC

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 898898Serine/threonine-protein kinase TAO3
PRO_0000086737

Regions

Domain24 – 277254Protein kinase
Nucleotide binding30 – 389ATP By similarity
Coiled coil452 – 50251 Potential
Coiled coil548 – 649102 Potential
Coiled coil754 – 879126 Potential
Compositional bias343 – 39351Ser-rich

Sites

Active site1471Proton acceptor By similarity
Binding site531ATP By similarity

Amino acid modifications

Modified residue3241Phosphoserine; by ATM Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.18
Modified residue3311Phosphoserine Ref.14
Modified residue4421Phosphoserine Ref.13
Modified residue8301N6-acetyllysine By similarity

Natural variations

Natural variant201P → T in a lung adenocarcinoma sample; somatic mutation. Ref.19
VAR_041205
Natural variant471S → N. Ref.3 Ref.4 Ref.19
Corresponds to variant rs428073 [ dbSNP | Ensembl ].
VAR_023691
Natural variant3921S → Y in a lung small cell carcinoma sample; somatic mutation. Ref.19
VAR_041206
Natural variant7271C → Y. Ref.19
Corresponds to variant rs55857273 [ dbSNP | Ensembl ].
VAR_041207

Experimental info

Mutagenesis1651D → A: Loss of serine/threonine-protein kinase activity. Ref.11
Mutagenesis1811T → A: No autophosphorylation and no kinase activity; when associated with F-183. Ref.1
Mutagenesis1831Y → F: No autophosphorylation and no kinase activity; when associated with A-181. Ref.1
Mutagenesis3241S → A: Inhibits activation of the p38/MAPK14 stress-activated MAPK cascade in response to DNA damage. Ref.11
Sequence conflict1361A → T in AAG38501. Ref.3
Sequence conflict1731S → P in AAG38501. Ref.3
Sequence conflict356 – 37823STGSQ…SSSEL → TWNQPEQGNGQPGQQPFHSK HVR in AAF14559. Ref.1
Sequence conflict6681Q → R in AAG38501. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9H2K8 [UniParc].

Last modified October 25, 2005. Version 2.
Checksum: AE7E30745B09763C

FASTA898105,406
        10         20         30         40         50         60 
MRKGVLKDPE IADLFYKDDP EELFIGLHEI GHGSFGAVYF ATNAHTSEVV AIKKMSYSGK 

        70         80         90        100        110        120 
QTHEKWQDIL KEVKFLRQLK HPNTIEYKGC YLKEHTAWLV MEYCLGSASD LLEVHKKPLQ 

       130        140        150        160        170        180 
EVEIAAITHG ALHGLAYLHS HALIHRDIKA GNILLTEPGQ VKLADFGSAS MASPANSFVG 

       190        200        210        220        230        240 
TPYWMAPEVI LAMDEGQYDG KVDIWSLGIT CIELAERKPP LFNMNAMSAL YHIAQNDSPT 

       250        260        270        280        290        300 
LQSNEWTDSF RRFVDYCLQK IPQERPTSAE LLRHDFVRRD RPLRVLIDLI QRTKDAVREL 

       310        320        330        340        350        360 
DNLQYRKMKK ILFQETRNGP LNESQEDEED SEHGTSLNRE MDSLGSNHSI PSMSVSTGSQ 

       370        380        390        400        410        420 
SSSVNSMQEV MDESSSELVM MHDDESTINS SSSVVHKKDH VFIRDEAGHG DPRPEPRPTQ 

       430        440        450        460        470        480 
SVQSQALHYR NRERFATIKS ASLVTRQIHE HEQENELREQ MSGYKRMRRQ HQKQLIALEN 

       490        500        510        520        530        540 
KLKAEMDEHR LKLQKEVETH ANNSSIELEK LAKKQVAIIE KEAKVAAADE KKFQQQILAQ 

       550        560        570        580        590        600 
QKKDLTTFLE SQKKQYKICK EKIKEEMNED HSTPKKEKQE RISKHKENLQ HTQAEEEAHL 

       610        620        630        640        650        660 
LTQQRLYYDK NCRFFKRKIM IKRHEVEQQN IREELNKKRT QKEMEHAMLI RHDESTRELE 

       670        680        690        700        710        720 
YRQLHTLQKL RMDLIRLQHQ TELENQLEYN KRRERELHRK HVMELRQQPK NLKAMEMQIK 

       730        740        750        760        770        780 
KQFQDTCKVQ TKQYKALKNH QLEVTPKNEH KTILKTLKDE QTRKLAILAE QYEQSINEMM 

       790        800        810        820        830        840 
ASQALRLDEA QEAECQALRL QLQQEMELLN AYQSKIKMQT EAQHERELQK LEQRVSLRRA 

       850        860        870        880        890 
HLEQKIEEEL AALQKERSER IKNLLERQER EIETFDMESL RMGFGNLVTL DFPKEDYR 

« Hide

References

« Hide 'large scale' references
[1]"Human JIK, a novel member of the STE20 kinase family that inhibits JNK and is negatively regulated by epidermal growth factor."
Tassi E., Biesova Z., Di Fiore P.P., Gutkind J.S., Wong W.T.
J. Biol. Chem. 274:33287-33295(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, MUTAGENESIS OF THR-181 AND TYR-183, FUNCTION.
[2]"Cloning of DPK, a novel dendritic cell-derived protein kinase activating the ERK1/ERK2 and JNK/SAPK pathways."
Zhang W., Chen T., Wan T., He L., Li N., Yuan Z., Cao X.
Biochem. Biophys. Res. Commun. 274:872-879(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Dendritic cell.
[3]"Comparative studies of a new subfamily of human Ste20-like kinases: homodimerization, subcellular localization, and selective activation of MKK3 and p38."
Yustein J.T., Xia L., Kahlenburg J.M., Robinson D., Templeton D., Kung H.-J.
Oncogene 22:6129-6141(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SELF-ASSOCIATION, TISSUE SPECIFICITY, VARIANT ASN-47, SUBCELLULAR LOCATION.
[4]"KDS and TAO1, two related proteins with kinase domain homology to STE20, differentially relocate in mitogen stimulated T lymphocytes."
Carter T.G., Benton B., Fruhling D., Monks C.R.F., Windmiller D., Kupfer A., Manfredi J., Johnson G.L., Pleiman C.M.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-47.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Placenta.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-898.
Tissue: Stomach.
[9]"SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma."
Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.
Br. J. Dermatol. 150:252-258(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 304-898.
Tissue: T-cell lymphoma.
[10]"Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress."
Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T., Tohyama M.
J. Biol. Chem. 276:13935-13940(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERN1 AND TRAF2.
[11]"TAO kinases mediate activation of p38 in response to DNA damage."
Raman M., Earnest S., Zhang K., Zhao Y., Cobb M.H.
EMBO J. 26:2005-2014(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-324, INDUCTION, MUTAGENESIS OF ASP-165 AND SER-324.
[12]"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-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Signal transduction protein array analysis links LRRK2 to Ste20 kinases and PKC zeta that modulate neuronal plasticity."
Zach S., Felk S., Gillardon F.
PLoS ONE 5:E13191-E13191(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY LRRK2.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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: VARIANTS [LARGE SCALE ANALYSIS] THR-20; ASN-47; TYR-392 AND TYR-727.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF179867 mRNA. Translation: AAF14559.1.
AF135158 mRNA. Translation: AAG09131.1.
AF263311 mRNA. Translation: AAG38501.1.
AF181985 mRNA. Translation: AAF25817.1.
BT007185 mRNA. Translation: AAP35849.1.
AC026366 Genomic DNA. No translation available.
BC002756 mRNA. Translation: AAH02756.1.
AL833731 mRNA. Translation: CAH56239.1.
AF328731 mRNA. Translation: AAN09723.1. Different initiation.
RefSeqNP_057365.3. NM_016281.3.
UniGeneHs.644420.

3D structure databases

ProteinModelPortalQ9H2K8.
SMRQ9H2K8. Positions 8-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119490. 8 interactions.
IntActQ9H2K8. 5 interactions.
MINTMINT-5005619.
STRING9606.ENSP00000376317.

Chemistry

BindingDBQ9H2K8.
ChEMBLCHEMBL5701.
GuidetoPHARMACOLOGY2235.

PTM databases

PhosphoSiteQ9H2K8.

Polymorphism databases

DMDM78099183.

Proteomic databases

PaxDbQ9H2K8.
PRIDEQ9H2K8.

Protocols and materials databases

DNASU51347.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392533; ENSP00000376317; ENSG00000135090.
ENST00000419821; ENSP00000416374; ENSG00000135090.
GeneID51347.
KEGGhsa:51347.
UCSCuc001tww.3. human.

Organism-specific databases

CTD51347.
GeneCardsGC12M118587.
HGNCHGNC:18133. TAOK3.
HPAHPA017160.
neXtProtNX_Q9H2K8.
PharmGKBPA134975064.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000236358.
HOVERGENHBG088996.
InParanoidQ9H2K8.
KOK04429.
OMAFIDLHEI.
OrthoDBEOG74XS5S.
PhylomeDBQ9H2K8.
TreeFamTF351444.

Enzyme and pathway databases

SignaLinkQ9H2K8.

Gene expression databases

ArrayExpressQ9H2K8.
BgeeQ9H2K8.
CleanExHS_TAOK3.
GenevestigatorQ9H2K8.

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

ChiTaRSTAOK3. human.
GeneWikiTAOK3.
GenomeRNAi51347.
NextBio54794.
PROQ9H2K8.

Entry information

Entry nameTAOK3_HUMAN
AccessionPrimary (citable) accession number: Q9H2K8
Secondary accession number(s): Q658N1 expand/collapse secondary AC list , Q8IUM4, Q9HC79, Q9NZM9, Q9UHG7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: April 16, 2014
This is version 113 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

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 12

Human chromosome 12: entries, gene names and cross-references to MIM