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Q9UL54

- TAOK2_HUMAN

UniProt

Q9UL54 - TAOK2_HUMAN

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Protein
Serine/threonine-protein kinase TAO2
Gene
TAOK2, KIAA0881, MAP3K17, PSK, PSK1, UNQ2971/PRO7431
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Magnesium 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 – 571ATP By similarity
Active sitei151 – 1511Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 429ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase kinase kinase activity Source: RefGenome
  3. mitogen-activated protein kinase kinase binding Source: UniProtKB
  4. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. G2 DNA damage checkpoint Source: UniProtKB
  2. actin cytoskeleton organization Source: UniProtKB
  3. activation of MAPKK activity Source: UniProtKB
  4. apoptotic process Source: UniProtKB
  5. cell migration Source: UniProtKB
  6. cellular response to DNA damage stimulus Source: UniProtKB
  7. focal adhesion assembly Source: UniProtKB
  8. positive regulation of JNK cascade Source: UniProtKB
  9. positive regulation of stress-activated MAPK cascade Source: UniProtKB
  10. protein targeting to membrane Source: UniProtKB
  11. regulation of cell growth Source: UniProtKB
  12. regulation of cell shape Source: UniProtKB
  13. response to stress Source: UniProtKB
  14. 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: Chromosome 16

Organism-specific databases

HGNCiHGNC:16835. TAOK2.

Subcellular locationi

Cytoplasmic vesicle membrane; Multi-pass membrane protein Reviewed prediction. 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.3 Publications
Isoform 2 : Cell projectiondendrite
Note: In dendrites, colocalizes with PCDH8 By similarity.3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei965 – 98521Helical; Reviewed prediction
Add
BLAST
Transmembranei987 – 100721Helical; Reviewed prediction
Add
BLAST
Transmembranei1012 – 103221Helical; Reviewed prediction
Add
BLAST
Transmembranei1043 – 106321Helical; Reviewed prediction
Add
BLAST
Transmembranei1166 – 118621Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoplasmic membrane-bounded vesicle Source: UniProtKB
  3. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  4. cytoskeleton Source: UniProtKB-SubCell
  5. dendrite Source: UniProtKB-SubCell
  6. integral component of membrane Source: UniProtKB-KW
  7. nucleolus Source: HPA
  8. nucleus Source: HPA
  9. 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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12351235Serine/threonine-protein kinase TAO2
PRO_0000086733Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine2 Publications
Modified residuei181 – 1811Phosphoserine2 Publications
Modified residuei486 – 4861Phosphoserine1 Publication
Modified residuei777 – 7771Phosphoserine1 Publication
Modified residuei825 – 8251Phosphoserine1 Publication
Modified residuei827 – 8271Phosphoserine1 Publication

Post-translational modificationi

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

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

ArrayExpressiQ9UL54.
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.3 Publications

Protein-protein interaction databases

BioGridi114750. 7 interactions.
IntActiQ9UL54. 4 interactions.
STRINGi9606.ENSP00000310094.

Structurei

3D structure databases

ProteinModelPortaliQ9UL54.
SMRiQ9UL54. Positions 12-320.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 281254Protein kinase
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili486 – 54762 Reviewed prediction
Add
BLAST
Coiled coili574 – 60128 Reviewed prediction
Add
BLAST
Coiled coili681 – 71333 Reviewed prediction
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG094024.
InParanoidiQ9UL54.
KOiK04429.
OMAiWGKEDES.
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_dom.
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. Align

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

MPAGGRAGSL KDPDVAELFF KDDPEKLFSD LREIGHGSFG AVYFARDVRN     50
SEVVAIKKMS YSGKQSNEKW QDIIKEVRFL QKLRHPNTIQ YRGCYLREHT 100
AWLVMEYCLG SASDLLEVHK KPLQEVEIAA VTHGALQGLA YLHSHNMIHR 150
DVKAGNILLS EPGLVKLGDF GSASIMAPAN SFVGTPYWMA PEVILAMDEG 200
QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN ESPVLQSGHW 250
SEYFRNFVDS CLQKIPQDRP TSEVLLKHRF VLRERPPTVI MDLIQRTKDA 300
VRELDNLQYR KMKKILFQEA PNGPGAEAPE EEEEAEPYMH RAGTLTSLES 350
SHSVPSMSIS ASSQSSSVNS LADASDNEEE EEEEEEEEEE EEGPEAREMA 400
MMQEGEHTVT SHSSIIHRLP GSDNLYDDPY QPEITPSPLQ PPAAPAPTST 450
TSSARRRAYC RNRDHFATIR TASLVSRQIQ EHEQDSALRE QLSGYKRMRR 500
QHQKQLLALE SRLRGEREEH SARLQRELEA QRAGFGAEAE KLARRHQAIG 550
EKEARAAQAE ERKFQQHILG QQKKELAALL EAQKRTYKLR KEQLKEELQE 600
NPSTPKREKA EWLLRQKEQL QQCQAEEEAG LLRRQRQYFE LQCRQYKRKM 650
LLARHSLDQD LLREDLNKKQ TQKDLECALL LRQHEATREL ELRQLQAVQR 700
TRAELTRLQH QTELGNQLEY NKRREQELRQ KHAAQVRQQP KSLKVRAGQR 750
PPGLPLPIPG ALGPPNTGTP IEQQPCSPGQ EAVLDQRMLG EEEEAVGERR 800
ILGKEGATLE PKQQRILGEE SGAPSPSPQK HGSLVDEEVW GLPEEIEELR 850
VPSLVPQERS IVGQEEAGTW SLWGKEDESL LDEEFELGWV QGPALTPVPE 900
EEEEEEEGAP IGTPRDPGDG CPSPDIPPEP PPTHLRPCPA SQLPGLLSHG 950
LLAGLSFAVG SSSGLLPLLL LLLLPLLAAQ GGGGLQAALL ALEVGLVGLG 1000
ASYLLLCTAL HLPSSLFLLL AQGTALGAVL GLSWRRGLMG VPLGLGAAWL 1050
LAWPGLALPL VAMAAGGRWV RQQGPRVRRG ISRLWLRVLL RLSPMAFRAL 1100
QGCGAVGDRG LFALYPKTNK DGFRSRLPVP GPRRRNPRTT QHPLALLARV 1150
WVLCKGWNWR LARASQGLAS HLPPWAIHTL ASWGLLRGER PTRIPRLLPR 1200
SQRQLGPPAS RQPLPGTLAG RRSRTRQSRA LPPWR 1235
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 1011. Contains a phosphoserine at position 1031 (By similarity).

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 173173Missing in isoform 3.
VSP_015967Add
BLAST
Alternative sequencei174 – 21845SIMAP…TCIEL → MMGTSQGHVARKSRNWGLNP SRLSSIPLSSTPCHLSPSSL SPFSV in isoform 3.
VSP_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.
VSP_015969Add
BLAST
Alternative sequencei745 – 857113Missing in isoform 4.
VSP_044894Add
BLAST
Alternative sequencei1050 – 1235186Missing in isoform 2.
VSP_015970Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1891M → T in AAI51222. 1 Publication
Sequence conflicti189 – 1891M → T in AAI42664. 1 Publication
Sequence conflicti1211 – 12111R → H in AAD45616. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi116242813.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS10662.1. [Q9UL54-2 ]
CCDS10663.1. [Q9UL54-1 ]
CCDS58448.1. [Q9UL54-4 ]
PIRi T46444.
RefSeqi NP_001238972.1. NM_001252043.1. [Q9UL54-4 ]
NP_004774.1. NM_004783.3. [Q9UL54-2 ]
NP_057235.2. NM_016151.3. [Q9UL54-1 ]
UniGenei Hs.291623.

3D structure databases

ProteinModelPortali Q9UL54.
SMRi Q9UL54. Positions 12-320.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114750. 7 interactions.
IntActi Q9UL54. 4 interactions.
STRINGi 9606.ENSP00000310094.

Chemistry

BindingDBi Q9UL54.
ChEMBLi CHEMBL1075195.
GuidetoPHARMACOLOGYi 2234.

PTM databases

PhosphoSitei Q9UL54.

Polymorphism databases

DMDMi 116242813.

Proteomic databases

MaxQBi Q9UL54.
PaxDbi Q9UL54.
PRIDEi Q9UL54.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000279394 ; ENSP00000279394 ; ENSG00000149930 . [Q9UL54-2 ]
ENST00000308893 ; ENSP00000310094 ; ENSG00000149930 . [Q9UL54-1 ]
ENST00000416441 ; ENSP00000393048 ; ENSG00000149930 . [Q9UL54-3 ]
ENST00000543033 ; ENSP00000440336 ; ENSG00000149930 . [Q9UL54-4 ]
GeneIDi 9344.
KEGGi hsa:9344.
UCSCi uc002dva.2. human. [Q9UL54-1 ]
uc002dvc.2. human. [Q9UL54-2 ]
uc002dvd.2. human. [Q9UL54-3 ]
uc021tgf.1. human.

Organism-specific databases

CTDi 9344.
GeneCardsi GC16P029985.
HGNCi HGNC:16835. TAOK2.
HPAi HPA010650.
MIMi 613199. gene.
neXtProti NX_Q9UL54.
PharmGKBi PA134907964.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG094024.
InParanoidi Q9UL54.
KOi K04429.
OMAi WGKEDES.
OrthoDBi EOG74XS5S.
PhylomeDBi Q9UL54.
TreeFami TF351444.

Enzyme and pathway databases

SignaLinki Q9UL54.

Miscellaneous databases

GeneWikii TAOK2.
GenomeRNAii 9344.
NextBioi 34999.
PROi Q9UL54.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UL54.
Bgeei Q9UL54.
CleanExi HS_TAOK2.
Genevestigatori Q9UL54.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

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; SER-181 AND SER-486, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1011 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Arsenic trioxide-dependent activation of thousand-and-one amino acid kinase 2 and transforming growth factor-beta-activated kinase 1."
    McNeer J.L., Goussetis D.J., Sassano A., Dolniak B., Kroczynska B., Glaser H., Altman J.K., Platanias L.C.
    Mol. Pharmacol. 77:828-835(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825 AND SER-827, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: July 9, 2014
This is version 122 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

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