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Q9UL54 (TAOK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase TAO2

EC=2.7.11.1
Alternative name(s):
Kinase from chicken homolog C
Short name=hKFC-C
Prostate-derived sterile 20-like kinase 1
Short name=PSK-1
Short name=PSK1
Short name=Prostate-derived STE20-like kinase 1
Thousand and one amino acid protein kinase 2
Gene names
Name:TAOK2
Synonyms:KIAA0881, MAP3K17, PSK, PSK1
ORF Names:UNQ2971/PRO7431
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1235 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase involved in different processes such as membrane blebbing and apoptotic bodies formation DNA damage response and MAPK14/p38 MAPK stress-activated MAPK cascade. Phosphorylates itself, MBP, activated MAPK8, MAP2K3, MAP2K6 and tubulins. Activates the MAPK14/p38 MAPK signaling pathway through the specific activation and phosphorylation of the upstream MAP2K3 and MAP2K6 kinases. 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. Isoform 1, but not isoform 2, plays a role in apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation. This function, which requires the activation of MAPK8/JNK and nuclear localization of C-terminally truncated isoform 1, may be linked to the mitochondrial CASP9-associated death pathway. Isoform 1 binds to microtubules and affects their organization and stability independently of its kinase activity. Prevents MAP3K7-mediated activation of CHUK, and thus NF-kappa-B activation, but not that of MAPK8/JNK. May play a role in the osmotic stress-MAPK8 pathway. Isoform 2, but not isoform 1, is required for PCDH8 endocytosis. Following homophilic interactions between PCDH8 extracellular domains, isoform 2 phosphorylates and activates MAPK14/p38 MAPK which in turn phosphorylates isoform 2. This process leads to PCDH8 endocytosis and CDH2 cointernalization. Both isoforms are involved in MAPK14 phosphorylation. Ref.1 Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Selectively inhibited by the enantiopure organoruthenium inhibitor 9E1. Activated following arsenic trioxide (As2O3) treatment. Ref.17 Ref.19

Subunit structure

Interacts with MAP2K3 and MAP2K6 By similarity. Self-associates. Interacts with tubulins through the C-terminal domain. Interacts with MAP3K7 and interfers with MAP3K7-binding to CHUK and thus prevents NF-kappa-B activation. Isoform 2 interacts with PCDH8; this complex may also include CDH2 By similarity. Ref.10 Ref.11 Ref.13

Subcellular location

Cytoplasmic vesicle membrane; Multi-pass membrane protein Potential. Cytoplasmcytoskeleton. Nucleus. Note: Catalytically active full-length phosphorylated isoform 1 localizes to microtubules in the cytoplasm predominantly on microtubule cables positioned around the nucleus. A C-terminally truncated form of isoform 1 is present in the nucleus; isoform 2 and kinase-defective, as well as full-length isoform 1 are excluded from the nucleus. Ref.2 Ref.11 Ref.15

Isoform 2: Cell projectiondendrite. Note: In dendrites, colocalizes with PCDH8 By similarity. Ref.2 Ref.11 Ref.15

Tissue specificity

Ubiquitously expressed, with a higher level of expression in testis and brain. Ref.1 Ref.2

Post-translational modification

Isoforms 1 and 2 are autophosphorylated. Ref.14 Ref.15

C-terminal cleavage of isoform 1 and subsequent nuclear localization requires CASP9 activity.

Autophosphorylated. Phosphorylated by ATM. Ref.14 Ref.15

Isoform 2:Phosphorylated on Ser-1031 by MAPK14. This phosphorylation is required PCDH8 for endocytosis By similarity. Ref.14 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 AAQ89301.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA74904.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2 DNA damage checkpoint

Inferred from mutant phenotype Ref.14. Source: UniProtKB

actin cytoskeleton organization

Inferred from direct assay Ref.1. Source: UniProtKB

activation of MAPKK activity

Inferred from direct assay Ref.1. Source: UniProtKB

apoptotic process

Non-traceable author statement Ref.1. Source: UniProtKB

cell migration

Non-traceable author statement Ref.1. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from direct assay Ref.14. Source: UniProtKB

focal adhesion assembly

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of JNK cascade

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of stress-activated MAPK cascade

Inferred from mutant phenotype Ref.14. Source: UniProtKB

protein targeting to membrane

Non-traceable author statement Ref.1. Source: UniProtKB

regulation of cell growth

Non-traceable author statement Ref.1. Source: UniProtKB

regulation of cell shape

Inferred from direct assay Ref.1. Source: UniProtKB

response to stress

Inferred from direct assay Ref.1. Source: UniProtKB

stress-activated MAPK cascade

Inferred from direct assay Ref.10. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic membrane-bounded vesicle

Inferred from direct assay Ref.1. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitogen-activated protein kinase kinase binding

Inferred from physical interaction Ref.10. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.1Ref.10. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UL54-1)

Also known as: PSK1-alpha; TAO2;

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: Q9UL54-2)

Also known as: PSK1-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     745-1049: VRAGQRPPGL...GVPLGLGAAW → SKELQIKKQF...ILNGSSHFYS
     1050-1235: Missing.
Note: Contains a phosphoserine at position 1031. Contains a phosphoserine at position 1011.
Isoform 3 (identifier: Q9UL54-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-173: Missing.
     174-218: SIMAPANSFV...WSLGITCIEL → MMGTSQGHVA...SPSSLSPFSV
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9UL54-4)

The sequence of this isoform differs from the canonical sequence as follows:
     745-857: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12351235Serine/threonine-protein kinase TAO2
PRO_0000086733

Regions

Transmembrane965 – 98521Helical; Potential
Transmembrane987 – 100721Helical; Potential
Transmembrane1012 – 103221Helical; Potential
Transmembrane1043 – 106321Helical; Potential
Transmembrane1166 – 118621Helical; Potential
Domain28 – 281254Protein kinase
Nucleotide binding34 – 429ATP By similarity
Coiled coil486 – 54762 Potential
Coiled coil574 – 60128 Potential
Coiled coil681 – 71333 Potential
Compositional bias330 – 3367Poly-Glu
Compositional bias347 – 37024Ser-rich
Compositional bias378 – 40629Glu-rich
Compositional bias791 – 907117Glu-rich
Compositional bias943 – 1060118Leu-rich

Sites

Active site1511Proton acceptor By similarity
Binding site571ATP By similarity

Amino acid modifications

Modified residue91Phosphoserine Ref.16 Ref.18
Modified residue1811Phosphoserine Ref.15 Ref.18
Modified residue4861Phosphoserine Ref.18
Modified residue7771Phosphoserine Ref.16
Modified residue8251Phosphoserine Ref.20
Modified residue8271Phosphoserine Ref.20

Natural variations

Alternative sequence1 – 173173Missing in isoform 3.
VSP_015967
Alternative sequence174 – 21845SIMAP…TCIEL → MMGTSQGHVARKSRNWGLNP SRLSSIPLSSTPCHLSPSSL SPFSV in isoform 3.
VSP_015968
Alternative sequence745 – 1049305VRAGQ…LGAAW → SKELQIKKQFQETCKIQTRQ YKALRAHLLETTPKAQHKSL LKRLKEEQTRKLAILAEQYD QSISEMLSSQALRLDETQEA EFQALRQQLQQELELLNAYQ SKIKIRTESQHERELRELEQ RVALRRALLEQRVEEELLAL QTGRSERIRSLLERQAREIE AFDAESMRLGFSSMALGGIP AEAAAQGYPAPPPAPAWPSR PVPRSGAHWSHGPPPPGMPP PAWRQPSLLAPPGPPNWLGP PTQSGTPRGGALLLLRNSPQ PLRRAASGGSGSENVGPPAA AVPGPLSRSTSVASHILNGS SHFYS in isoform 2.
VSP_015969
Alternative sequence745 – 857113Missing in isoform 4.
VSP_044894
Alternative sequence1050 – 1235186Missing in isoform 2.
VSP_015970

Experimental info

Mutagenesis571K → A: Loss of kinase activity. In isoform 1, excluded from the nucleus. No effect on microtubule-binding. Ref.1 Ref.11 Ref.13 Ref.15
Mutagenesis1691D → A: Loss of kinase activity; No effect on MAP3K7-mediated activation of NF-kappa-B. Ref.13
Mutagenesis9191D → N: No effect on kinase activity, nor on JNK activation, but severe reduction in nuclear localization and apoptotic membrane blebbing. Ref.15
Sequence conflict1891M → T in AAI51222. Ref.7
Sequence conflict1891M → T in AAI42664. Ref.7
Sequence conflict12111R → H in AAD45616. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PSK1-alpha) (TAO2) [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 211852E690934307

FASTA1,235138,251
        10         20         30         40         50         60 
MPAGGRAGSL KDPDVAELFF KDDPEKLFSD LREIGHGSFG AVYFARDVRN SEVVAIKKMS 

        70         80         90        100        110        120 
YSGKQSNEKW QDIIKEVRFL QKLRHPNTIQ YRGCYLREHT AWLVMEYCLG SASDLLEVHK 

       130        140        150        160        170        180 
KPLQEVEIAA VTHGALQGLA YLHSHNMIHR DVKAGNILLS EPGLVKLGDF GSASIMAPAN 

       190        200        210        220        230        240 
SFVGTPYWMA PEVILAMDEG QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN 

       250        260        270        280        290        300 
ESPVLQSGHW SEYFRNFVDS CLQKIPQDRP TSEVLLKHRF VLRERPPTVI MDLIQRTKDA 

       310        320        330        340        350        360 
VRELDNLQYR KMKKILFQEA PNGPGAEAPE EEEEAEPYMH RAGTLTSLES SHSVPSMSIS 

       370        380        390        400        410        420 
ASSQSSSVNS LADASDNEEE EEEEEEEEEE EEGPEAREMA MMQEGEHTVT SHSSIIHRLP 

       430        440        450        460        470        480 
GSDNLYDDPY QPEITPSPLQ PPAAPAPTST TSSARRRAYC RNRDHFATIR TASLVSRQIQ 

       490        500        510        520        530        540 
EHEQDSALRE QLSGYKRMRR QHQKQLLALE SRLRGEREEH SARLQRELEA QRAGFGAEAE 

       550        560        570        580        590        600 
KLARRHQAIG EKEARAAQAE ERKFQQHILG QQKKELAALL EAQKRTYKLR KEQLKEELQE 

       610        620        630        640        650        660 
NPSTPKREKA EWLLRQKEQL QQCQAEEEAG LLRRQRQYFE LQCRQYKRKM LLARHSLDQD 

       670        680        690        700        710        720 
LLREDLNKKQ TQKDLECALL LRQHEATREL ELRQLQAVQR TRAELTRLQH QTELGNQLEY 

       730        740        750        760        770        780 
NKRREQELRQ KHAAQVRQQP KSLKVRAGQR PPGLPLPIPG ALGPPNTGTP IEQQPCSPGQ 

       790        800        810        820        830        840 
EAVLDQRMLG EEEEAVGERR ILGKEGATLE PKQQRILGEE SGAPSPSPQK HGSLVDEEVW 

       850        860        870        880        890        900 
GLPEEIEELR VPSLVPQERS IVGQEEAGTW SLWGKEDESL LDEEFELGWV QGPALTPVPE 

       910        920        930        940        950        960 
EEEEEEEGAP IGTPRDPGDG CPSPDIPPEP PPTHLRPCPA SQLPGLLSHG LLAGLSFAVG 

       970        980        990       1000       1010       1020 
SSSGLLPLLL LLLLPLLAAQ GGGGLQAALL ALEVGLVGLG ASYLLLCTAL HLPSSLFLLL 

      1030       1040       1050       1060       1070       1080 
AQGTALGAVL GLSWRRGLMG VPLGLGAAWL LAWPGLALPL VAMAAGGRWV RQQGPRVRRG 

      1090       1100       1110       1120       1130       1140 
ISRLWLRVLL RLSPMAFRAL QGCGAVGDRG LFALYPKTNK DGFRSRLPVP GPRRRNPRTT 

      1150       1160       1170       1180       1190       1200 
QHPLALLARV WVLCKGWNWR LARASQGLAS HLPPWAIHTL ASWGLLRGER PTRIPRLLPR 

      1210       1220       1230 
SQRQLGPPAS RQPLPGTLAG RRSRTRQSRA LPPWR 

« Hide

Isoform 2 (PSK1-beta) [UniParc].

Checksum: D6C5062F47794030
Show »

FASTA1,049119,281
Isoform 3 [UniParc].

Checksum: A4B2B359EEC9CAAD
Show »

FASTA1,062118,780
Isoform 4 [UniParc].

Checksum: 3F00D8F3E84DF679
Show »

FASTA1,122126,204

References

« Hide 'large scale' references
[1]"PSK, a novel STE20-like kinase derived from prostatic carcinoma that activates the JNK MAPK pathway and regulates actin cytoskeletal organisation."
Moore T.M., Garg R., Johnson C., Coptcoat M.J., Ridley A.J., Morris J.D.H.
J. Biol. Chem. 275:4311-4322(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-57.
Tissue: Mammary carcinoma.
[2]"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] (ISOFORM 2), FUNCTION, SELF-ASSOCIATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[3]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal brain.
[5]"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] (ISOFORM 3).
Tissue: Testis.
[6]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORMS 1; 2 AND 4).
[9]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 957-1235 (ISOFORMS 1/3).
[10]"Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2."
Chen Z., Cobb M.H.
J. Biol. Chem. 276:16070-16075(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF MAP2K3 AND MAP2K6, INTERACTION WITH MAP2K3 AND MAP2K6.
[11]"The prostate-derived sterile 20-like kinase (PSK) regulates microtubule organization and stability."
Mitsopoulos C., Zihni C., Garg R., Ridley A.J., Morris J.D.
J. Biol. Chem. 278:18085-18091(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TUBULINS, MUTAGENESIS OF LYS-57.
[12]"TAO (thousand-and-one amino acid) protein kinases mediate signaling from carbachol to p38 mitogen-activated protein kinase and ternary complex factors."
Chen Z., Raman M., Chen L., Lee S.F., Gilman A.G., Cobb M.H.
J. Biol. Chem. 278:22278-22283(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Osmotic stress activates the TAK1-JNK pathway while blocking TAK1-mediated NF-kappaB activation: TAO2 regulates TAK1 pathways."
Huangfu W.C., Omori E., Akira S., Matsumoto K., Ninomiya-Tsuji J.
J. Biol. Chem. 281:28802-28810(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAP3K7, MUTAGENESIS OF LYS-57 AND ASP-169.
[14]"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 BY ATM, INDUCTION.
[15]"Prostate-derived sterile 20-like kinase 1-alpha induces apoptosis. JNK-and caspase-dependent nuclear localization is a requirement for membrane blebbing."
Zihni C., Mitsopoulos C., Tavares I.A., Baum B., Ridley A.J., Morris J.D.
J. Biol. Chem. 282:6484-6493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-181, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-57 AND ASP-919.
[16]"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-9 AND SER-777, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Toward the development of a potent and selective organoruthenium mammalian sterile 20 kinase inhibitor."
Anand R., Maksimoska J., Pagano N., Wong E.Y., Gimotty P.A., Diamond S.L., Meggers E., Marmorstein R.
J. Med. Chem. 52:1602-1611(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[18]"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-9; SER-181 AND SER-486, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1011 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Arsenic trioxide-dependent activation of thousand-and-one amino acid kinase 2 and transforming growth factor-beta-activated kinase 1."
McNeer J.L., Goussetis D.J., Sassano A., Dolniak B., Kroczynska B., Glaser H., Altman J.K., Platanias L.C.
Mol. Pharmacol. 77:828-835(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[20]"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-825 AND SER-827, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061943 mRNA. Translation: AAD45616.1.
AF263313 mRNA. Translation: AAG38503.1.
AB020688 mRNA. Translation: BAA74904.2. Different initiation.
AK291473 mRNA. Translation: BAF84162.1.
AL137701 mRNA. Translation: CAB70882.1.
AC093512 Genomic DNA. No translation available.
CH471238 Genomic DNA. Translation: EAW79963.1.
CH471238 Genomic DNA. Translation: EAW79964.1.
BC136653 mRNA. Translation: AAI36654.1.
BC136655 mRNA. Translation: AAI36656.1.
BC142663 mRNA. Translation: AAI42664.1.
BC144344 mRNA. Translation: AAI44345.1.
BC151221 mRNA. Translation: AAI51222.1.
BC152413 mRNA. Translation: AAI52414.1.
AY358942 mRNA. Translation: AAQ89301.1. Different initiation.
PIRT46444.
RefSeqNP_001238972.1. NM_001252043.1.
NP_004774.1. NM_004783.3.
NP_057235.2. NM_016151.3.
UniGeneHs.291623.

3D structure databases

ProteinModelPortalQ9UL54.
SMRQ9UL54. Positions 12-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114750. 7 interactions.
IntActQ9UL54. 4 interactions.
STRING9606.ENSP00000310094.

Chemistry

BindingDBQ9UL54.
ChEMBLCHEMBL1075195.
GuidetoPHARMACOLOGY2234.

PTM databases

PhosphoSiteQ9UL54.

Polymorphism databases

DMDM116242813.

Proteomic databases

PaxDbQ9UL54.
PRIDEQ9UL54.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000279394; ENSP00000279394; ENSG00000149930. [Q9UL54-2]
ENST00000308893; ENSP00000310094; ENSG00000149930. [Q9UL54-1]
ENST00000416441; ENSP00000393048; ENSG00000149930. [Q9UL54-3]
ENST00000543033; ENSP00000440336; ENSG00000149930. [Q9UL54-4]
GeneID9344.
KEGGhsa:9344.
UCSCuc002dva.2. human. [Q9UL54-1]
uc002dvc.2. human. [Q9UL54-2]
uc002dvd.2. human. [Q9UL54-3]
uc021tgf.1. human.

Organism-specific databases

CTD9344.
GeneCardsGC16P029985.
HGNCHGNC:16835. TAOK2.
HPAHPA010650.
MIM613199. gene.
neXtProtNX_Q9UL54.
PharmGKBPA134907964.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG094024.
InParanoidQ9UL54.
KOK04429.
OMAQETQQNG.
OrthoDBEOG74XS5S.
PhylomeDBQ9UL54.
TreeFamTF351444.

Enzyme and pathway databases

SignaLinkQ9UL54.

Gene expression databases

ArrayExpressQ9UL54.
BgeeQ9UL54.
CleanExHS_TAOK2.
GenevestigatorQ9UL54.

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

GeneWikiTAOK2.
GenomeRNAi9344.
NextBio34999.
PROQ9UL54.
SOURCESearch...

Entry information

Entry nameTAOK2_HUMAN
AccessionPrimary (citable) accession number: Q9UL54
Secondary accession number(s): A5PKY1 expand/collapse secondary AC list , A7MCZ2, B2RN35, B7ZM88, O94957, Q6UW73, Q7LC09, Q9NSW2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 119 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

MIM cross-references

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

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM