Q9H2K8 (TAOK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	898 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	DNA damage DNA repair
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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 negative regulation of JNK cascade Inferred from direct assay Ref.1. Source: HGNC 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 protein autophosphorylation Inferred from direct assay Ref.1. Source: HGNC
Cellular_component	mitochondrion Inferred from direct assay. Source: HPA plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase inhibitor activity Traceable author statement Ref.1. Source: ProtInc protein serine/threonine kinase activity Inferred from direct assay Ref.1. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERN1	O75460	3	EBI-1384100,EBI-371750
TRAF2	Q12933	2	EBI-1384100,EBI-355744

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 898	898	Serine/threonine-protein kinase TAO3		PRO_0000086737
Regions
	Domain	24 – 277	254	Protein kinase
	Nucleotide binding	30 – 38	9	ATP By similarity
	Coiled coil	452 – 502	51	Potential
	Coiled coil	548 – 649	102	Potential
	Coiled coil	754 – 879	126	Potential
	Compositional bias	343 – 393	51	Ser-rich
Sites
	Active site	147	1	Proton acceptor By similarity
	Binding site	53	1	ATP By similarity
Amino acid modifications
	Modified residue	324	1	Phosphoserine; by ATM Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.18
	Modified residue	331	1	Phosphoserine Ref.14
	Modified residue	346	1	Phosphoserine By similarity
	Modified residue	349	1	Phosphoserine By similarity
	Modified residue	442	1	Phosphoserine Ref.13
Natural variations
	Natural variant	20	1	P → T in a lung adenocarcinoma sample; somatic mutation. Ref.19		VAR_041205
	Natural variant	47	1	S → N. Ref.3 Ref.4 Ref.19 Corresponds to variant rs428073 [ dbSNP | Ensembl ].		VAR_023691
	Natural variant	392	1	S → Y in a lung small cell carcinoma sample; somatic mutation. Ref.19		VAR_041206
	Natural variant	727	1	C → Y. Ref.19 Corresponds to variant rs55857273 [ dbSNP | Ensembl ].		VAR_041207
Experimental info
	Mutagenesis	165	1	D → A: Loss of serine/threonine-protein kinase activity. Ref.11
	Mutagenesis	181	1	T → A: No autophosphorylation and no kinase activity; when associated with F-183. Ref.1
	Mutagenesis	183	1	Y → F: No autophosphorylation and no kinase activity; when associated with A-181. Ref.1
	Mutagenesis	324	1	S → A: Inhibits activation of the p38/MAPK14 stress-activated MAPK cascade in response to DNA damage. Ref.11
	Sequence conflict	136	1	A → T in AAG38501. Ref.3
	Sequence conflict	173	1	S → P in AAG38501. Ref.3
	Sequence conflict	356 – 378	23	STGSQ…SSSEL → TWNQPEQGNGQPGQQPFHSK HVR in AAF14559. Ref.1
	Sequence conflict	668	1	Q → R in AAG38501. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9H2K8 [UniParc]. Last modified October 25, 2005. Version 2. Checksum: AE7E30745B09763C	FASTA	898	105,406
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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. , 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.
IPI	IPI00410485.
RefSeq	NP_057365.3. NM_016281.3.
UniGene	Hs.644420.
3D structure databases
ProteinModelPortal	Q9H2K8.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H2K8. 5 interactions.
STRING	9606.ENSP00000376317.
PTM databases
PhosphoSite	Q9H2K8.
Polymorphism databases
DMDM	78099183.
Proteomic databases
PaxDb	Q9H2K8.
PRIDE	Q9H2K8.
Protocols and materials databases
DNASU	51347.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000392533; ENSP00000376317; ENSG00000135090. ENST00000419821; ENSP00000416374; ENSG00000135090.
GeneID	51347.
KEGG	hsa:51347.
UCSC	uc001tww.3. human.
Organism-specific databases
CTD	51347.
GeneCards	GC12M118587.
HGNC	HGNC:18133. TAOK3.
HPA	HPA017160.
neXtProt	NX_Q9H2K8.
PharmGKB	PA134975064.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000236358.
HOVERGEN	HBG088996.
InParanoid	Q9H2K8.
KO	K04429.
OMA	FRGFVDY.
OrthoDB	EOG4THVSD.
PhylomeDB	Q9H2K8.
Enzyme and pathway databases
Pathway_Interaction_DB	p38_mkk3_6pathway. p38 MAPK signaling pathway.
Gene expression databases
ArrayExpress	Q9H2K8.
Bgee	Q9H2K8.
CleanEx	HS_TAOK3.
Genevestigator	Q9H2K8.
GermOnline	ENSG00000135090. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9H2K8.
ChEMBL	CHEMBL5701.
ChiTaRS	TAOK3. human.
GenomeRNAi	51347.
NextBio	54794.

Entry information

Entry name

TAOK3_HUMAN

Accession

Primary (citable) accession number: Q9H2K8
Secondary accession number(s): Q658N1 , Q8IUM4, Q9HC79, Q9NZM9, Q9UHG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	October 25, 2005
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.