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Protein

Serine/threonine-protein kinase TAO2

Gene

TAOK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Selectively inhibited by the enantiopure organoruthenium inhibitor 9E1. Activated following arsenic trioxide (As2O3) treatment.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571ATPPROSITE-ProRule annotation
Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 429ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • MAP kinase kinase kinase activity Source: GO_Central
  • mitogen-activated protein kinase kinase binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • activation of MAPKK activity Source: UniProtKB
  • apoptotic process Source: UniProtKB
  • cell migration Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • focal adhesion assembly Source: UniProtKB
  • G2 DNA damage checkpoint Source: UniProtKB
  • nervous system development Source: GO_Central
  • positive regulation of JNK cascade Source: UniProtKB
  • positive regulation of stress-activated MAPK cascade Source: UniProtKB
  • protein targeting to membrane Source: UniProtKB
  • regulation of apoptotic process Source: GO_Central
  • regulation of cell growth Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of mitotic cell cycle Source: GO_Central
  • response to stress Source: UniProtKB
  • stress-activated MAPK cascade Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9UL54.

Names & Taxonomyi

Protein namesi
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 namesi
Name:TAOK2
Synonyms:KIAA0881, MAP3K17, PSK, PSK1
ORF Names:UNQ2971/PRO7431
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:16835. TAOK2.

Subcellular locationi

  • Cytoplasmic vesicle membrane Curated; Multi-pass membrane protein Curated
  • 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.
Isoform 2 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei965 – 98521HelicalSequence AnalysisAdd
BLAST
Transmembranei987 – 100721HelicalSequence AnalysisAdd
BLAST
Transmembranei1012 – 103221HelicalSequence AnalysisAdd
BLAST
Transmembranei1043 – 106321HelicalSequence AnalysisAdd
BLAST
Transmembranei1166 – 118621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytoplasmic membrane-bounded vesicle Source: UniProtKB
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • cytoskeleton Source: UniProtKB-SubCell
  • dendrite Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • nucleolus Source: HPA
  • nucleus Source: HPA
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571K → A: Loss of kinase activity. In isoform 1, excluded from the nucleus. No effect on microtubule-binding. 4 Publications
Mutagenesisi169 – 1691D → A: Loss of kinase activity; No effect on MAP3K7-mediated activation of NF-kappa-B. 1 Publication
Mutagenesisi919 – 9191D → N: No effect on kinase activity, nor on JNK activation, but severe reduction in nuclear localization and apoptotic membrane blebbing. 1 Publication

Organism-specific databases

PharmGKBiPA134907964.

Polymorphism and mutation databases

BioMutaiTAOK2.
DMDMi116242813.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12351235Serine/threonine-protein kinase TAO2PRO_0000086733Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine2 Publications
Modified residuei181 – 1811Phosphoserine2 Publications
Modified residuei414 – 4141Phosphoserine1 Publication
Modified residuei777 – 7771Phosphoserine1 Publication
Modified residuei825 – 8251Phosphoserine1 Publication
Modified residuei827 – 8271Phosphoserine1 Publication

Post-translational modificationi

Isoforms 1 and 2 are autophosphorylated.
C-terminal cleavage of isoform 1 and subsequent nuclear localization requires CASP9 activity.
Autophosphorylated. Phosphorylated by ATM.
Isoform 2: Phosphorylated on Ser-1031 by MAPK14. This phosphorylation is required PCDH8 for endocytosis (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UL54.
PaxDbiQ9UL54.
PRIDEiQ9UL54.

PTM databases

PhosphoSiteiQ9UL54.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9UL54.
CleanExiHS_TAOK2.
GenevestigatoriQ9UL54.

Organism-specific databases

HPAiHPA010650.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi114750. 11 interactions.
IntActiQ9UL54. 7 interactions.
STRINGi9606.ENSP00000310094.

Structurei

3D structure databases

ProteinModelPortaliQ9UL54.
SMRiQ9UL54. Positions 12-320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 281254Protein kinasePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili486 – 54762Sequence AnalysisAdd
BLAST
Coiled coili574 – 60128Sequence AnalysisAdd
BLAST
Coiled coili681 – 71333Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi330 – 3367Poly-Glu
Compositional biasi347 – 37024Ser-richAdd
BLAST
Compositional biasi378 – 40629Glu-richAdd
BLAST
Compositional biasi791 – 907117Glu-richAdd
BLAST
Compositional biasi943 – 1060118Leu-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118848.
HOGENOMiHOG000236358.
HOVERGENiHBG094024.
InParanoidiQ9UL54.
KOiK04429.
OMAiLNHRFLC.
OrthoDBiEOG74XS5S.
PhylomeDBiQ9UL54.
TreeFamiTF351444.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UL54-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPAGGRAGSL KDPDVAELFF KDDPEKLFSD LREIGHGSFG AVYFARDVRN
60 70 80 90 100
SEVVAIKKMS YSGKQSNEKW QDIIKEVRFL QKLRHPNTIQ YRGCYLREHT
110 120 130 140 150
AWLVMEYCLG SASDLLEVHK KPLQEVEIAA VTHGALQGLA YLHSHNMIHR
160 170 180 190 200
DVKAGNILLS EPGLVKLGDF GSASIMAPAN SFVGTPYWMA PEVILAMDEG
210 220 230 240 250
QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN ESPVLQSGHW
260 270 280 290 300
SEYFRNFVDS CLQKIPQDRP TSEVLLKHRF VLRERPPTVI MDLIQRTKDA
310 320 330 340 350
VRELDNLQYR KMKKILFQEA PNGPGAEAPE EEEEAEPYMH RAGTLTSLES
360 370 380 390 400
SHSVPSMSIS ASSQSSSVNS LADASDNEEE EEEEEEEEEE EEGPEAREMA
410 420 430 440 450
MMQEGEHTVT SHSSIIHRLP GSDNLYDDPY QPEITPSPLQ PPAAPAPTST
460 470 480 490 500
TSSARRRAYC RNRDHFATIR TASLVSRQIQ EHEQDSALRE QLSGYKRMRR
510 520 530 540 550
QHQKQLLALE SRLRGEREEH SARLQRELEA QRAGFGAEAE KLARRHQAIG
560 570 580 590 600
EKEARAAQAE ERKFQQHILG QQKKELAALL EAQKRTYKLR KEQLKEELQE
610 620 630 640 650
NPSTPKREKA EWLLRQKEQL QQCQAEEEAG LLRRQRQYFE LQCRQYKRKM
660 670 680 690 700
LLARHSLDQD LLREDLNKKQ TQKDLECALL LRQHEATREL ELRQLQAVQR
710 720 730 740 750
TRAELTRLQH QTELGNQLEY NKRREQELRQ KHAAQVRQQP KSLKVRAGQR
760 770 780 790 800
PPGLPLPIPG ALGPPNTGTP IEQQPCSPGQ EAVLDQRMLG EEEEAVGERR
810 820 830 840 850
ILGKEGATLE PKQQRILGEE SGAPSPSPQK HGSLVDEEVW GLPEEIEELR
860 870 880 890 900
VPSLVPQERS IVGQEEAGTW SLWGKEDESL LDEEFELGWV QGPALTPVPE
910 920 930 940 950
EEEEEEEGAP IGTPRDPGDG CPSPDIPPEP PPTHLRPCPA SQLPGLLSHG
960 970 980 990 1000
LLAGLSFAVG SSSGLLPLLL LLLLPLLAAQ GGGGLQAALL ALEVGLVGLG
1010 1020 1030 1040 1050
ASYLLLCTAL HLPSSLFLLL AQGTALGAVL GLSWRRGLMG VPLGLGAAWL
1060 1070 1080 1090 1100
LAWPGLALPL VAMAAGGRWV RQQGPRVRRG ISRLWLRVLL RLSPMAFRAL
1110 1120 1130 1140 1150
QGCGAVGDRG LFALYPKTNK DGFRSRLPVP GPRRRNPRTT QHPLALLARV
1160 1170 1180 1190 1200
WVLCKGWNWR LARASQGLAS HLPPWAIHTL ASWGLLRGER PTRIPRLLPR
1210 1220 1230
SQRQLGPPAS RQPLPGTLAG RRSRTRQSRA LPPWR
Length:1,235
Mass (Da):138,251
Last modified:October 17, 2006 - v2
Checksum:i211852E690934307
GO
Isoform 2 (identifier: Q9UL54-2) [UniParc]FASTAAdd to basket

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 (By similarity). Contains a phosphoserine at position 1011.By similarity1 Publication

Show »
Length:1,049
Mass (Da):119,281
Checksum:iD6C5062F47794030
GO
Isoform 3 (identifier: Q9UL54-3) [UniParc]FASTAAdd to basket

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.

Show »
Length:1,062
Mass (Da):118,780
Checksum:iA4B2B359EEC9CAAD
GO
Isoform 4 (identifier: Q9UL54-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     745-857: Missing.

Note: No experimental confirmation available.

Show »
Length:1,122
Mass (Da):126,204
Checksum:i3F00D8F3E84DF679
GO

Sequence cautioni

The sequence AAQ89301.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA74904.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1891M → T in AAI51222 (Ref. 7) Curated
Sequence conflicti189 – 1891M → T in AAI42664 (Ref. 7) Curated
Sequence conflicti1211 – 12111R → H in AAD45616 (PubMed:10660600).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 173173Missing in isoform 3. 1 PublicationVSP_015967Add
BLAST
Alternative sequencei174 – 21845SIMAP…TCIEL → MMGTSQGHVARKSRNWGLNP SRLSSIPLSSTPCHLSPSSL SPFSV in isoform 3. 1 PublicationVSP_015968Add
BLAST
Alternative sequencei745 – 1049305VRAGQ…LGAAW → SKELQIKKQFQETCKIQTRQ YKALRAHLLETTPKAQHKSL LKRLKEEQTRKLAILAEQYD QSISEMLSSQALRLDETQEA EFQALRQQLQQELELLNAYQ SKIKIRTESQHERELRELEQ RVALRRALLEQRVEEELLAL QTGRSERIRSLLERQAREIE AFDAESMRLGFSSMALGGIP AEAAAQGYPAPPPAPAWPSR PVPRSGAHWSHGPPPPGMPP PAWRQPSLLAPPGPPNWLGP PTQSGTPRGGALLLLRNSPQ PLRRAASGGSGSENVGPPAA AVPGPLSRSTSVASHILNGS SHFYS in isoform 2. 4 PublicationsVSP_015969Add
BLAST
Alternative sequencei745 – 857113Missing in isoform 4. 1 PublicationVSP_044894Add
BLAST
Alternative sequencei1050 – 1235186Missing in isoform 2. 4 PublicationsVSP_015970Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10662.1. [Q9UL54-2]
CCDS10663.1. [Q9UL54-1]
CCDS58448.1. [Q9UL54-4]
PIRiT46444.
RefSeqiNP_001238972.1. NM_001252043.1. [Q9UL54-4]
NP_004774.1. NM_004783.3. [Q9UL54-2]
NP_057235.2. NM_016151.3. [Q9UL54-1]
UniGeneiHs.291623.

Genome annotation databases

EnsembliENST00000279394; ENSP00000279394; ENSG00000149930. [Q9UL54-2]
ENST00000308893; ENSP00000310094; ENSG00000149930. [Q9UL54-1]
ENST00000416441; ENSP00000393048; ENSG00000149930. [Q9UL54-3]
ENST00000543033; ENSP00000440336; ENSG00000149930. [Q9UL54-4]
GeneIDi9344.
KEGGihsa:9344.
UCSCiuc002dva.2. human. [Q9UL54-1]
uc002dvc.2. human. [Q9UL54-2]
uc002dvd.2. human. [Q9UL54-3]
uc021tgf.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10662.1. [Q9UL54-2]
CCDS10663.1. [Q9UL54-1]
CCDS58448.1. [Q9UL54-4]
PIRiT46444.
RefSeqiNP_001238972.1. NM_001252043.1. [Q9UL54-4]
NP_004774.1. NM_004783.3. [Q9UL54-2]
NP_057235.2. NM_016151.3. [Q9UL54-1]
UniGeneiHs.291623.

3D structure databases

ProteinModelPortaliQ9UL54.
SMRiQ9UL54. Positions 12-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114750. 11 interactions.
IntActiQ9UL54. 7 interactions.
STRINGi9606.ENSP00000310094.

Chemistry

BindingDBiQ9UL54.
ChEMBLiCHEMBL1075195.
GuidetoPHARMACOLOGYi2234.

PTM databases

PhosphoSiteiQ9UL54.

Polymorphism and mutation databases

BioMutaiTAOK2.
DMDMi116242813.

Proteomic databases

MaxQBiQ9UL54.
PaxDbiQ9UL54.
PRIDEiQ9UL54.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000279394; ENSP00000279394; ENSG00000149930. [Q9UL54-2]
ENST00000308893; ENSP00000310094; ENSG00000149930. [Q9UL54-1]
ENST00000416441; ENSP00000393048; ENSG00000149930. [Q9UL54-3]
ENST00000543033; ENSP00000440336; ENSG00000149930. [Q9UL54-4]
GeneIDi9344.
KEGGihsa:9344.
UCSCiuc002dva.2. human. [Q9UL54-1]
uc002dvc.2. human. [Q9UL54-2]
uc002dvd.2. human. [Q9UL54-3]
uc021tgf.1. human.

Organism-specific databases

CTDi9344.
GeneCardsiGC16P029985.
HGNCiHGNC:16835. TAOK2.
HPAiHPA010650.
MIMi613199. gene.
neXtProtiNX_Q9UL54.
PharmGKBiPA134907964.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118848.
HOGENOMiHOG000236358.
HOVERGENiHBG094024.
InParanoidiQ9UL54.
KOiK04429.
OMAiLNHRFLC.
OrthoDBiEOG74XS5S.
PhylomeDBiQ9UL54.
TreeFamiTF351444.

Enzyme and pathway databases

SignaLinkiQ9UL54.

Miscellaneous databases

GeneWikiiTAOK2.
GenomeRNAii9344.
NextBioi34999.
PROiQ9UL54.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UL54.
CleanExiHS_TAOK2.
GenevestigatoriQ9UL54.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-181, 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTAOK2_HUMAN
AccessioniPrimary (citable) accession number: Q9UL54
Secondary accession number(s): A5PKY1
, A7MCZ2, B2RN35, B7ZM88, O94957, Q6UW73, Q7LC09, Q9NSW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 17, 2006
Last modified: May 27, 2015
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.