Q7L7X3 (TAOK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1001 AA.
Sequence status	Complete.
Protein existence	Evidence 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.13 Ref.16 Ref.17 Ref.18 Ref.26 Ref.27
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.14
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.16
Post-translational modification	Proteolytically processed by caspase-3 (CASP3). Autophosphorylated By similarity. Phosphorylated by ATM in response to DNA damage. Phosphorylated by LRRK2. Ref.11 Ref.12 Ref.15 Ref.16 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.28
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.17). 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.26 and Ref.27).
Sequence caution	The sequence BAA92599.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Apoptosis DNA damage DNA repair
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing 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/M transition DNA damage checkpoint Inferred from mutant phenotype Ref.16. Source: UniProtKB apoptotic process Inferred from direct assay Ref.13. Source: UniProtKB mitotic prometaphase Traceable author statement. Source: Reactome positive regulation of JNK cascade Inferred from direct assay Ref.13. Source: UniProtKB positive regulation of stress-activated MAPK cascade Inferred from mutant phenotype Ref.16. Source: UniProtKB regulation of cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	ATP binding Non-traceable author statement. Source: HGNC protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1001	1001	Serine/threonine-protein kinase TAO1		PRO_0000086728
Regions
	Domain	28 – 281	254	Protein kinase
	Nucleotide binding	34 – 42	9	ATP By similarity
	Coiled coil	458 – 651	194	Potential
	Coiled coil	754 – 877	124	Potential
	Compositional bias	330 – 334	5	Poly-Glu
	Compositional bias	347 – 379	33	Ser-rich
Sites
	Active site	151	1	Proton acceptor By similarity
	Binding site	57	1	ATP Probable
Amino acid modifications
	Modified residue	9	1	Phosphoserine Ref.22 Ref.24
	Modified residue	43	1	Phosphotyrosine Ref.24
	Modified residue	177	1	Phosphoserine Ref.24
	Modified residue	181	1	Phosphoserine Ref.24
	Modified residue	421	1	Phosphoserine Ref.11 Ref.15 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25
	Modified residue	445	1	Phosphoserine Ref.22 Ref.24
	Modified residue	480	1	Phosphothreonine Ref.24
	Modified residue	669	1	Phosphothreonine Ref.24
	Modified residue	958	1	Phosphoserine Ref.24
	Modified residue	959	1	Phosphoserine Ref.12 Ref.24
	Modified residue	965	1	Phosphoserine Ref.19 Ref.24
Natural variations
	Alternative sequence	1 – 174	174	Missing in isoform 2.		VSP_015964
	Alternative sequence	569 – 572	4	ELNE → VLMS in isoform 2.		VSP_015965
	Alternative sequence	573 – 1001	429	Missing in isoform 2.		VSP_015966
	Natural variant	855	1	A → T. Ref.29 Corresponds to variant rs34151057 [ dbSNP | Ensembl ].		VAR_041204
Experimental info
	Mutagenesis	57	1	K → A: Abolishes kinase activity, ability to activite the MAPK8/JNK cascade and cleavage by caspase-3 (CASP3). Ref.13
	Mutagenesis	169	1	D → A: Loss of serine/threonine-protein kinase activity. Ref.16
	Mutagenesis	376	1	D → N: Does not abolish cleavage by caspase-3 (CASP3). Ref.13
	Mutagenesis	643	1	T → A: Abolishes phosphorylation by ATM; when associated with A-785 and A-990. Ref.16
	Mutagenesis	785	1	T → A: Abolishes phosphorylation by ATM; when associated with A-643 and A-990. Ref.16
	Mutagenesis	990	1	S → A: Abolishes phosphorylation by ATM; when associated with A-643 and A-785. Ref.16
	Sequence conflict	251	1	S → T in BAB14901. Ref.5
	Sequence conflict	257	1	F → S in AAG38502. Ref.1
	Sequence conflict	860	1	R → C in AAG38502. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 82941DEAEADC7651	FASTA	1,001	116,070
	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
	Isoform 2 [UniParc]. Checksum: B2744BCA14C7E63F	FASTA	398	46,163
	10 20 30 40 50 60 MASPANSFVG TPYWMAPEVI LAMDEGQYDG KVDVWSLGIT CIELAERKPP LFNMNAMSAL 70 80 90 100 110 120 YHIAQNESPT LQSNEWSDYF RNFVDSCLQK IPQDRPTSEE LLKHIFVLRE RPETVLIDLI 130 140 150 160 170 180 QRTKDAVREL DNLQYRKMKK LLFQEAHNGP AVEAQEEEEE QDHGVGRTGT VNSVGSNQSI 190 200 210 220 230 240 PSMSISASSQ SSSVNSLPDV SDDKSELDMM EGDHTVMSNS SVIHLKPEEE NYREEGDPRT 250 260 270 280 290 300 RASDPQSPPQ VSRHKSHYRN REHFATIRTA SLVTRQMQEH EQDSELREQM SGYKRMRRQH 310 320 330 340 350 360 QKQLMTLENK LKAEMDEHRL RLDKDLETQR NNFAAEMEKL IKKHQAAMEK EAKVMSNEEK 370 380 390 KFQQHIQAQQ KKELNSFLES QKREYKLRKE QLKEVLMS

References

	« Hide 'large scale' referencesShow '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: 13679851] [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: 10718198] [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. , 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: 14702039] [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. , 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: 16625196] [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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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: 9786855] [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: 12665513] [Abstract] Cited for: FUNCTION.
[11]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-959, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 16407310] [Abstract] Cited for: FUNCTION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF LYS-57 AND ASP-376.
[14]	"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: 16893890] [Abstract] Cited for: INTERACTION WITH MAP3K7.
[15]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: 17396146] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION BY ATM, INDUCTION, MUTAGENESIS OF ASP-169; THR-643; THR-785 AND SER-990.
[17]	"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: 17417629] [Abstract] Cited for: POSSIBLE ROLE IN SPINDLE CHECKPOINT.
[18]	"Human TAO kinase 1 induces apoptosis in SH-SY5Y cells." Wu M.F., Wang S.G. Cell Biol. Int. 32:151-156(2008) [PubMed: 17900936] [Abstract] Cited for: FUNCTION.
[19]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-965, MASS SPECTROMETRY. Tissue: Platelet.
[20]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-421 AND SER-445, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[24]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; TYR-43; SER-177; SER-181; SER-421; SER-445; THR-480; THR-669; SER-958; SER-959 AND SER-965, MASS SPECTROMETRY.
[25]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"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: 19904549] [Abstract] Cited for: LACK OF ROLE IN SPINDLE CHECKPOINT.
[27]	"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: 20162290] [Abstract] Cited for: LACK OF ROLE IN SPINDLE CHECKPOINT.
[28]	"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: 20949042] [Abstract] Cited for: PHOSPHORYLATION BY LRRK2.
[29]	"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: 17344846] [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. AC068588 Genomic DNA. No translation available. AC090698 Genomic DNA. No translation available. CH471159 Genomic DNA. Translation: EAW51188.1. BC133039 mRNA. Translation: AAI33040.1.
IPI	IPI00002232. IPI00654673.
RefSeq	NP_065842.1. NM_020791.2.
UniGene	Hs.597434.
3D structure databases
ProteinModelPortal	Q7L7X3.
SMR	Q7L7X3. Positions 12-320.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-39709N.
IntAct	Q7L7X3. 1 interaction.
STRING	Q7L7X3.
PTM databases
PhosphoSite	Q7L7X3.
Polymorphism databases
DMDM	74759012.
Proteomic databases
PeptideAtlas	Q7L7X3.
PRIDE	Q7L7X3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261716; ENSP00000261716; ENSG00000160551.
GeneID	57551.
KEGG	hsa:57551.
UCSC	uc002hdz.1. human. uc002heb.1. human.
Organism-specific databases
CTD	57551.
GeneCards	GC17P027717.
H-InvDB	HIX0013678.
HGNC	HGNC:29259. TAOK1.
HPA	HPA007669.
MIM	610266. gene.
neXtProt	NX_Q7L7X3.
PharmGKB	PA134872946.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00600000084021.
HOGENOM	HBG382294.
HOVERGEN	HBG088996.
InParanoid	Q7L7X3.
OMA	RASEPQS.
OrthoDB	EOG41VK27.
PhylomeDB	Q7L7X3.
Enzyme and pathway databases
Pathway_Interaction_DB	p38_mkk3_6pathway. p38 MAPK signaling pathway.
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_383. DNA Replication.
Gene expression databases
ArrayExpress	Q7L7X3.
Bgee	Q7L7X3.
CleanEx	HS_TAOK1.
Genevestigator	Q7L7X3.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K04429.
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
NextBio	64014.
SOURCE	Search...

Entry information

Entry name

TAOK1_HUMAN

Accession

Primary (citable) accession number: Q7L7X3
Secondary accession number(s): A2RUT8 , Q96L75, Q9H2K7, Q9H7S5, Q9P2I6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 82 of the entry and version 1 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.