Q9UL54 (TAOK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	1235 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton. 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 projection › dendrite. 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. Isoform 2 is phosphorylated at 'Ser-1031' by MAPK14. This phosphorylation is required PCDH8 for endocytosis By similarity. Autophosphorylated. Phosphorylated by ATM. 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 component	Cell projection Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2 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 focal adhesion assembly Inferred from direct assay Ref.1. Source: UniProtKB positive regulation of JNK cascade Inferred from direct assay Ref.1. 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 stress-activated MAPK cascade Inferred from direct assay Ref.10. Source: UniProtKB
Cellular_component	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 to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleolus Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1235	1235	Serine/threonine-protein kinase TAO2		PRO_0000086733
Regions
	Transmembrane	965 – 985	21	Helical; Potential
	Transmembrane	987 – 1007	21	Helical; Potential
	Transmembrane	1012 – 1032	21	Helical; Potential
	Transmembrane	1043 – 1063	21	Helical; Potential
	Transmembrane	1166 – 1186	21	Helical; Potential
	Domain	28 – 281	254	Protein kinase
	Nucleotide binding	34 – 42	9	ATP By similarity
	Coiled coil	486 – 547	62	Potential
	Coiled coil	574 – 601	28	Potential
	Coiled coil	681 – 713	33	Potential
	Compositional bias	330 – 336	7	Poly-Glu
	Compositional bias	347 – 370	24	Ser-rich
	Compositional bias	378 – 406	29	Glu-rich
	Compositional bias	791 – 907	117	Glu-rich
	Compositional bias	943 – 1060	118	Leu-rich
Sites
	Active site	151	1	Proton acceptor By similarity
	Binding site	57	1	ATP By similarity
Amino acid modifications
	Modified residue	9	1	Phosphoserine Ref.16 Ref.18
	Modified residue	43	1	Phosphotyrosine By similarity
	Modified residue	181	1	Phosphoserine Ref.15 Ref.18
	Modified residue	486	1	Phosphoserine Ref.18
	Modified residue	777	1	Phosphoserine Ref.16
	Modified residue	825	1	Phosphoserine Ref.20
	Modified residue	827	1	Phosphoserine Ref.20
Natural variations
	Alternative sequence	1 – 173	173	Missing in isoform 3.		VSP_015967
	Alternative sequence	174 – 218	45	SIMAP…TCIEL → MMGTSQGHVARKSRNWGLNP SRLSSIPLSSTPCHLSPSSL SPFSV in isoform 3.		VSP_015968
	Alternative sequence	745 – 1049	305	VRAGQ…LGAAW → SKELQIKKQFQETCKIQTRQ YKALRAHLLETTPKAQHKSL LKRLKEEQTRKLAILAEQYD QSISEMLSSQALRLDETQEA EFQALRQQLQQELELLNAYQ SKIKIRTESQHERELRELEQ RVALRRALLEQRVEEELLAL QTGRSERIRSLLERQAREIE AFDAESMRLGFSSMALGGIP AEAAAQGYPAPPPAPAWPSR PVPRSGAHWSHGPPPPGMPP PAWRQPSLLAPPGPPNWLGP PTQSGTPRGGALLLLRNSPQ PLRRAASGGSGSENVGPPAA AVPGPLSRSTSVASHILNGS SHFYS in isoform 2.		VSP_015969
	Alternative sequence	745 – 857	113	Missing in isoform 4.		VSP_044894
	Alternative sequence	1050 – 1235	186	Missing in isoform 2.		VSP_015970
Experimental info
	Mutagenesis	57	1	K → 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
	Mutagenesis	169	1	D → A: Loss of kinase activity; No effect on MAP3K7-mediated activation of NF-kappa-B. Ref.13
	Mutagenesis	919	1	D → N: No effect on kinase activity, nor on JNK activation, but severe reduction in nuclear localization and apoptotic membrane blebbing. Ref.15
	Sequence conflict	189	1	M → T in AAI51222. Ref.7
	Sequence conflict	189	1	M → T in AAI42664. Ref.7
	Sequence conflict	1211	1	R → H in AAD45616. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PSK1-alpha) (TAO2) [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 211852E690934307	FASTA	1,235	138,251
	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
	Isoform 2 (PSK1-beta) [UniParc]. Checksum: D6C5062F47794030	FASTA	1,049	119,281
	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 KSLKSKELQI KKQFQETCKI QTRQYKALRA HLLETTPKAQ 790 800 810 820 830 840 HKSLLKRLKE EQTRKLAILA EQYDQSISEM LSSQALRLDE TQEAEFQALR QQLQQELELL 850 860 870 880 890 900 NAYQSKIKIR TESQHERELR ELEQRVALRR ALLEQRVEEE LLALQTGRSE RIRSLLERQA 910 920 930 940 950 960 REIEAFDAES MRLGFSSMAL GGIPAEAAAQ GYPAPPPAPA WPSRPVPRSG AHWSHGPPPP 970 980 990 1000 1010 1020 GMPPPAWRQP SLLAPPGPPN WLGPPTQSGT PRGGALLLLR NSPQPLRRAA SGGSGSENVG 1030 1040 PPAAAVPGPL SRSTSVASHI LNGSSHFYS
	Isoform 3 [UniParc]. Checksum: A4B2B359EEC9CAAD	FASTA	1,062	118,780
	10 20 30 40 50 60 MMGTSQGHVA RKSRNWGLNP SRLSSIPLSS TPCHLSPSSL SPFSVAERKP PLFNMNAMSA 70 80 90 100 110 120 LYHIAQNESP VLQSGHWSEY FRNFVDSCLQ KIPQDRPTSE VLLKHRFVLR ERPPTVIMDL 130 140 150 160 170 180 IQRTKDAVRE LDNLQYRKMK KILFQEAPNG PGAEAPEEEE EAEPYMHRAG TLTSLESSHS 190 200 210 220 230 240 VPSMSISASS QSSSVNSLAD ASDNEEEEEE EEEEEEEEEG PEAREMAMMQ EGEHTVTSHS 250 260 270 280 290 300 SIIHRLPGSD NLYDDPYQPE ITPSPLQPPA APAPTSTTSS ARRRAYCRNR DHFATIRTAS 310 320 330 340 350 360 LVSRQIQEHE QDSALREQLS GYKRMRRQHQ KQLLALESRL RGEREEHSAR LQRELEAQRA 370 380 390 400 410 420 GFGAEAEKLA RRHQAIGEKE ARAAQAEERK FQQHILGQQK KELAALLEAQ KRTYKLRKEQ 430 440 450 460 470 480 LKEELQENPS TPKREKAEWL LRQKEQLQQC QAEEEAGLLR RQRQYFELQC RQYKRKMLLA 490 500 510 520 530 540 RHSLDQDLLR EDLNKKQTQK DLECALLLRQ HEATRELELR QLQAVQRTRA ELTRLQHQTE 550 560 570 580 590 600 LGNQLEYNKR REQELRQKHA AQVRQQPKSL KVRAGQRPPG LPLPIPGALG PPNTGTPIEQ 610 620 630 640 650 660 QPCSPGQEAV LDQRMLGEEE EAVGERRILG KEGATLEPKQ QRILGEESGA PSPSPQKHGS 670 680 690 700 710 720 LVDEEVWGLP EEIEELRVPS LVPQERSIVG QEEAGTWSLW GKEDESLLDE EFELGWVQGP 730 740 750 760 770 780 ALTPVPEEEE EEEEGAPIGT PRDPGDGCPS PDIPPEPPPT HLRPCPASQL PGLLSHGLLA 790 800 810 820 830 840 GLSFAVGSSS GLLPLLLLLL LPLLAAQGGG GLQAALLALE VGLVGLGASY LLLCTALHLP 850 860 870 880 890 900 SSLFLLLAQG TALGAVLGLS WRRGLMGVPL GLGAAWLLAW PGLALPLVAM AAGGRWVRQQ 910 920 930 940 950 960 GPRVRRGISR LWLRVLLRLS PMAFRALQGC GAVGDRGLFA LYPKTNKDGF RSRLPVPGPR 970 980 990 1000 1010 1020 RRNPRTTQHP LALLARVWVL CKGWNWRLAR ASQGLASHLP PWAIHTLASW GLLRGERPTR 1030 1040 1050 1060 IPRLLPRSQR QLGPPASRQP LPGTLAGRRS RTRQSRALPP WR
	Isoform 4 [UniParc]. Checksum: 3F00D8F3E84DF679	FASTA	1,122	126,204
	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 KSLKERSIVG QEEAGTWSLW GKEDESLLDE EFELGWVQGP 790 800 810 820 830 840 ALTPVPEEEE EEEEGAPIGT PRDPGDGCPS PDIPPEPPPT HLRPCPASQL PGLLSHGLLA 850 860 870 880 890 900 GLSFAVGSSS GLLPLLLLLL LPLLAAQGGG GLQAALLALE VGLVGLGASY LLLCTALHLP 910 920 930 940 950 960 SSLFLLLAQG TALGAVLGLS WRRGLMGVPL GLGAAWLLAW PGLALPLVAM AAGGRWVRQQ 970 980 990 1000 1010 1020 GPRVRRGISR LWLRVLLRLS PMAFRALQGC GAVGDRGLFA LYPKTNKDGF RSRLPVPGPR 1030 1040 1050 1060 1070 1080 RRNPRTTQHP LALLARVWVL CKGWNWRLAR ASQGLASHLP PWAIHTLASW GLLRGERPTR 1090 1100 1110 1120 IPRLLPRSQR QLGPPASRQP LPGTLAGRRS RTRQSRALPP WR

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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, MASS SPECTROMETRY. 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), MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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.
IPI	IPI00006283. IPI00465168. IPI00641071. IPI00922624.
PIR	T46444.
RefSeq	NP_001238972.1. NM_001252043.1. NP_004774.1. NM_004783.3. NP_057235.2. NM_016151.3.
UniGene	Hs.291623.
3D structure databases
ProteinModelPortal	Q9UL54.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UL54. 4 interactions.
STRING	9606.ENSP00000310094.
PTM databases
PhosphoSite	Q9UL54.
Polymorphism databases
DMDM	116242813.
Proteomic databases
PaxDb	Q9UL54.
PRIDE	Q9UL54.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000279394; ENSP00000279394; ENSG00000149930. ENST00000308893; ENSP00000310094; ENSG00000149930. ENST00000416441; ENSP00000393048; ENSG00000149930. ENST00000543033; ENSP00000440336; ENSG00000149930.
GeneID	9344.
KEGG	hsa:9344.
UCSC	uc002dva.2. human. uc002dvc.2. human. uc002dvd.2. human.
Organism-specific databases
CTD	9344.
GeneCards	GC16P029985.
HGNC	HGNC:16835. TAOK2.
HPA	HPA010650.
MIM	613199. gene.
neXtProt	NX_Q9UL54.
PharmGKB	PA134907964.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG094024.
InParanoid	Q9UL54.
KO	K04429.
OMA	QETQQNG.
OrthoDB	EOG4Q58NS.
PhylomeDB	Q9UL54.
Enzyme and pathway databases
Pathway_Interaction_DB	p38_mkk3_6pathway. p38 MAPK signaling pathway.
Gene expression databases
ArrayExpress	Q9UL54.
Bgee	Q9UL54.
CleanEx	HS_TAOK2.
Genevestigator	Q9UL54.
GermOnline	ENSG00000149930. 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	Q9UL54.
ChEMBL	CHEMBL1075195.
GenomeRNAi	9344.
NextBio	34999.
SOURCE	Search...

Entry information

Entry name

TAOK2_HUMAN

Accession

Primary (citable) accession number: Q9UL54
Secondary accession number(s): A5PKY1 , 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:	May 1, 2013
This is version 109 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.