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Q7L7X3 (TAOK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 TAO1

EC=2.7.11.1
Alternative name(s):
Kinase from chicken homolog B
Short name=hKFC-B
MARK Kinase
Short name=MARKK
Prostate-derived sterile 20-like kinase 2
Short name=PSK-2
Short name=PSK2
Short name=Prostate-derived STE20-like kinase 2
Thousand and one amino acid protein kinase 1
Short name=TAOK1
Short name=hTAOK1
Gene names
Name:TAOK1
Synonyms:KIAA1361, MAP3K16, MARKK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1001 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. 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 MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade. Ref.1 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.23 Ref.24

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Serine/threonine-protein kinase activity is inhibited by SPRED1.

Subunit structure

Self-associates. Interacts with MAP2K3 By similarity. Interacts with SPRED1 and TESK1. Interacts with MAP3K7. Ref.12

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Highly expressed in the testis, and to a lower extent also expressed in brain, placenta, colon and skeletal muscle. Ref.1 Ref.9

Induction

In response to DNA damage. Ref.14

Post-translational modification

Proteolytically processed by caspase-3 (CASP3).

Autophosphorylated By similarity. Phosphorylated by ATM in response to DNA damage. Phosphorylated by LRRK2. Ref.14 Ref.25

Sequence similarities

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

Contains 1 protein kinase domain.

Caution

Was initially thought to play a role in the spindle checkpoint (Ref.15). However, it was later shown that it is not the case and that phenotypes initially observed are the cause of the siRNA used that has an off-target effect resulting in MAD2L1 inhibition (Ref.23 and Ref.24).

Sequence caution

The sequence BAA92599.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processApoptosis
DNA damage
DNA repair
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   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.14. Source: UniProtKB

MAPK cascade

Inferred from Biological aspect of Ancestor. Source: GOC

activation of MAPKK activity

Inferred from Biological aspect of Ancestor. Source: GOC

cellular response to DNA damage stimulus

Inferred from direct assay Ref.14. Source: UniProtKB

execution phase of apoptosis

Inferred from direct assay Ref.11. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of JNK cascade

Inferred from direct assay Ref.11. Source: UniProtKB

positive regulation of stress-activated MAPK cascade

Inferred from mutant phenotype Ref.14. Source: UniProtKB

protein phosphorylation

Non-traceable author statement PubMed 14517247. Source: HGNC

regulation of cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

   Molecular_functionATP binding

Non-traceable author statement PubMed 14517247. Source: HGNC

MAP kinase kinase kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

kinase activity

Non-traceable author statement PubMed 14517247. Source: HGNC

protein binding

Inferred from physical interaction PubMed 11733138. Source: WormBase

protein kinase activity

Non-traceable author statement PubMed 14517247. Source: HGNC

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transferase activity

Non-traceable author statement PubMed 14517247. Source: HGNC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7L7X3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q7L7X3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: Missing.
     569-572: ELNE → VLMS
     573-1001: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q7L7X3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     569-716: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10011001Serine/threonine-protein kinase TAO1
PRO_0000086728

Regions

Domain28 – 281254Protein kinase
Nucleotide binding34 – 429ATP By similarity
Coiled coil458 – 651194 Potential
Coiled coil754 – 877124 Potential
Compositional bias330 – 3345Poly-Glu
Compositional bias347 – 37933Ser-rich

Sites

Active site1511Proton acceptor By similarity
Binding site571ATP Probable

Amino acid modifications

Modified residue91Phosphoserine Ref.21 Ref.22
Modified residue4211Phosphoserine Ref.13 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.27
Modified residue4451Phosphoserine Ref.19
Modified residue6691Phosphothreonine Ref.21
Modified residue9651Phosphoserine Ref.17

Natural variations

Alternative sequence1 – 174174Missing in isoform 2.
VSP_015964
Alternative sequence569 – 716148Missing in isoform 3.
VSP_043706
Alternative sequence569 – 5724ELNE → VLMS in isoform 2.
VSP_015965
Alternative sequence573 – 1001429Missing in isoform 2.
VSP_015966
Natural variant8551A → T. Ref.28
Corresponds to variant rs34151057 [ dbSNP | Ensembl ].
VAR_041204

Experimental info

Mutagenesis571K → A: Abolishes kinase activity, ability to activate the MAPK8/JNK cascade and cleavage by caspase-3 (CASP3). Ref.11
Mutagenesis1691D → A: Loss of serine/threonine-protein kinase activity. Ref.14
Mutagenesis3761D → N: Does not abolish cleavage by caspase-3 (CASP3). Ref.11
Mutagenesis6431T → A: Abolishes phosphorylation by ATM; when associated with A-785 and A-990. Ref.14
Mutagenesis7851T → A: Abolishes phosphorylation by ATM; when associated with A-643 and A-990. Ref.14
Mutagenesis9901S → A: Abolishes phosphorylation by ATM; when associated with A-643 and A-785. Ref.14
Sequence conflict2511S → T in BAB14901. Ref.5
Sequence conflict2571F → S in AAG38502. Ref.1
Sequence conflict8601R → C in AAG38502. Ref.1

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: 82941DEAEADC7651

FASTA1,001116,070
        10         20         30         40         50         60 
MPSTNRAGSL KDPEIAELFF KEDPEKLFTD LREIGHGSFG AVYFARDVRT NEVVAIKKMS 

        70         80         90        100        110        120 
YSGKQSTEKW QDIIKEVKFL QRIKHPNSIE YKGCYLREHT AWLVMEYCLG SASDLLEVHK 

       130        140        150        160        170        180 
KPLQEVEIAA ITHGALQGLA YLHSHTMIHR DIKAGNILLT EPGQVKLADF GSASMASPAN 

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

       250        260        270        280        290        300 
ESPTLQSNEW SDYFRNFVDS CLQKIPQDRP TSEELLKHIF VLRERPETVL IDLIQRTKDA 

       310        320        330        340        350        360 
VRELDNLQYR KMKKLLFQEA HNGPAVEAQE EEEEQDHGVG RTGTVNSVGS NQSIPSMSIS 

       370        380        390        400        410        420 
ASSQSSSVNS LPDVSDDKSE LDMMEGDHTV MSNSSVIHLK PEEENYREEG DPRTRASDPQ 

       430        440        450        460        470        480 
SPPQVSRHKS HYRNREHFAT IRTASLVTRQ MQEHEQDSEL REQMSGYKRM RRQHQKQLMT 

       490        500        510        520        530        540 
LENKLKAEMD EHRLRLDKDL ETQRNNFAAE MEKLIKKHQA AMEKEAKVMS NEEKKFQQHI 

       550        560        570        580        590        600 
QAQQKKELNS FLESQKREYK LRKEQLKEEL NENQSTPKKE KQEWLSKQKE NIQHFQAEEE 

       610        620        630        640        650        660 
ANLLRRQRQY LELECRRFKR RMLLGRHNLE QDLVREELNK RQTQKDLEHA MLLRQHESMQ 

       670        680        690        700        710        720 
ELEFRHLNTI QKMRCELIRL QHQTELTNQL EYNKRREREL RRKHVMEVRQ QPKSLKSKEL 

       730        740        750        760        770        780 
QIKKQFQDTC KIQTRQYKAL RNHLLETTPK SEHKAVLKRL KEEQTRKLAI LAEQYDHSIN 

       790        800        810        820        830        840 
EMLSTQALRL DEAQEAECQV LKMQLQQELE LLNAYQSKIK MQAEAQHDRE LRELEQRVSL 

       850        860        870        880        890        900 
RRALLEQKIE EEMLALQNER TERIRSLLER QAREIEAFDS ESMRLGFSNM VLSNLSPEAF 

       910        920        930        940        950        960 
SHSYPGASGW SHNPTGGPGP HWGHPMGGPP QAWGHPMQGG PQPWGHPSGP MQGVPRGSSM 

       970        980        990       1000 
GVRNSPQALR RTASGGRTEQ GMSRSTSVTS QISNGSHMSY T 

« Hide

Isoform 2 [UniParc].

Checksum: B2744BCA14C7E63F
Show »

FASTA39846,163
Isoform 3 [UniParc].

Checksum: 15DE595D707B9E34
Show »

FASTA85397,526

References

« Hide 'large scale' references
[1]"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 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]"Characterization of human TAO1."
Jenkins S.G., D'Andrea R.J., Gamble J.R., Vadas M.A.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"T cell activating gene."
Matsuda A., Yoneta S.
Patent number WO2004058805, 15-JUL-2004
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"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: Placenta.
[6]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [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 AND 3).
Tissue: Brain.
[9]"Isolation of TAO1, a protein kinase that activates MEKs in stress-activated protein kinase cascades."
Hutchison M., Berman K.S., Cobb M.H.
J. Biol. Chem. 273:28625-28632(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"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.
[11]"Prostate-derived sterile 20-like kinase 2 (PSK2) regulates apoptotic morphology via C-Jun N-terminal kinase and Rho kinase-1."
Zihni C., Mitsopoulos C., Tavares I.A., Ridley A.J., Morris J.D.
J. Biol. Chem. 281:7317-7323(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF LYS-57 AND ASP-376.
[12]"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: INTERACTION WITH MAP3K7.
[13]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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, MUTAGENESIS OF ASP-169; THR-643; THR-785 AND SER-990.
[15]"A functional genomic screen identifies a role for TAO1 kinase in spindle-checkpoint signalling."
Draviam V.M., Stegmeier F., Nalepa G., Sowa M.E., Chen J., Liang A., Hannon G.J., Sorger P.K., Harper J.W., Elledge S.J.
Nat. Cell Biol. 9:556-564(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE ROLE IN SPINDLE CHECKPOINT.
[16]"Human TAO kinase 1 induces apoptosis in SH-SY5Y cells."
Wu M.F., Wang S.G.
Cell Biol. Int. 32:151-156(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-965, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[18]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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-421 AND THR-669, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[23]"Re-examination of siRNA specificity questions role of PICH and Tao1 in the spindle checkpoint and identifies Mad2 as a sensitive target for small RNAs."
Hubner N.C., Wang L.H., Kaulich M., Descombes P., Poser I., Nigg E.A.
Chromosoma 119:149-165(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: LACK OF ROLE IN SPINDLE CHECKPOINT.
[24]"Re-evaluating the role of Tao1 in the spindle checkpoint."
Westhorpe F.G., Diez M.A., Gurden M.D., Tighe A., Taylor S.S.
Chromosoma 119:371-379(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: LACK OF ROLE IN SPINDLE CHECKPOINT.
[25]"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.
[26]"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].
[27]"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-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"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] THR-855.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF263312 mRNA. Translation: AAG38502.1.
AY049015 mRNA. Translation: AAL12217.1.
CQ834802 mRNA. Translation: CAH05616.1.
AB037782 mRNA. Translation: BAA92599.1. Different initiation.
AK024376 mRNA. Translation: BAB14901.1.
AC068025 Genomic DNA. No translation available.
AC068588 Genomic DNA. No translation available.
AC090698 Genomic DNA. No translation available.
CH471159 Genomic DNA. Translation: EAW51188.1.
BC133039 mRNA. Translation: AAI33040.1.
BC144067 mRNA. Translation: AAI44068.1.
CCDSCCDS32601.1. [Q7L7X3-1]
CCDS56024.1. [Q7L7X3-3]
RefSeqNP_065842.1. NM_020791.2. [Q7L7X3-1]
NP_079418.1. NM_025142.1. [Q7L7X3-3]
UniGeneHs.597434.
Hs.735869.

3D structure databases

ProteinModelPortalQ7L7X3.
SMRQ7L7X3. Positions 12-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121607. 11 interactions.
DIPDIP-39709N.
IntActQ7L7X3. 9 interactions.
MINTMINT-5006389.
STRING9606.ENSP00000261716.

Chemistry

BindingDBQ7L7X3.
ChEMBLCHEMBL5261.
GuidetoPHARMACOLOGY2233.

PTM databases

PhosphoSiteQ7L7X3.

Polymorphism databases

DMDM74759012.

Proteomic databases

MaxQBQ7L7X3.
PaxDbQ7L7X3.
PeptideAtlasQ7L7X3.
PRIDEQ7L7X3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261716; ENSP00000261716; ENSG00000160551. [Q7L7X3-1]
ENST00000536202; ENSP00000438819; ENSG00000160551. [Q7L7X3-3]
GeneID57551.
KEGGhsa:57551.
UCSCuc002hdz.2. human. [Q7L7X3-1]
uc002heb.1. human. [Q7L7X3-2]
uc010wbe.2. human. [Q7L7X3-3]

Organism-specific databases

CTD57551.
GeneCardsGC17P027717.
HGNCHGNC:29259. TAOK1.
HPAHPA007669.
MIM610266. gene.
neXtProtNX_Q7L7X3.
PharmGKBPA134872946.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000236358.
HOVERGENHBG088996.
InParanoidQ7L7X3.
KOK04429.
OMAAGPHWGH.
OrthoDBEOG74XS5S.
PhylomeDBQ7L7X3.
TreeFamTF351444.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
SignaLinkQ7L7X3.

Gene expression databases

ArrayExpressQ7L7X3.
BgeeQ7L7X3.
CleanExHS_TAOK1.
GenevestigatorQ7L7X3.

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

ChiTaRSTAOK1. human.
GeneWikiTAOK1.
GenomeRNAi57551.
NextBio64014.
PROQ7L7X3.
SOURCESearch...

Entry information

Entry nameTAOK1_HUMAN
AccessionPrimary (citable) accession number: Q7L7X3
Secondary accession number(s): A2RUT8 expand/collapse secondary AC list , B7ZLV6, Q96L75, Q9H2K7, Q9H7S5, Q9P2I6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 108 of the entry and version 1 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 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 17

Human chromosome 17: entries, gene names and cross-references to MIM