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Protein

Serine/threonine-protein kinase TAO3

Gene

TAOK3

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

Functioni

Serine/threonine-protein kinase that acts as a regulator of the p38/MAPK14 stress-activated MAPK cascade and of the MAPK8/JNK cascade. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade. 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. Inhibits basal activity of MAPK8/JNK cascade and diminishes its activation in response epidermal growth factor (EGF).3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531ATPPROSITE-ProRule annotation
Active sitei147 – 1471Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 389ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • MAP kinase kinase kinase activity Source: GO_Central
  • protein kinase inhibitor activity Source: ProtInc
  • protein serine/threonine kinase activity Source: HGNC
  • transferase activity Source: HGNC

GO - Biological processi

  • activation of MAPKK activity Source: GO_Central
  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA repair Source: UniProtKB-KW
  • MAPK cascade Source: HGNC
  • mitotic G2 DNA damage checkpoint Source: UniProtKB
  • negative regulation of JNK cascade Source: HGNC
  • negative regulation of protein kinase activity Source: GOC
  • positive regulation of JNK cascade Source: HGNC
  • positive regulation of JUN kinase activity Source: UniProtKB
  • positive regulation of stress-activated MAPK cascade Source: UniProtKB
  • protein autophosphorylation Source: HGNC
  • protein phosphorylation Source: UniProtKB
  • regulation of apoptotic process Source: GO_Central
  • stress-activated protein kinase signaling cascade Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9H2K8.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase TAO3 (EC:2.7.11.1)
Alternative name(s):
Cutaneous T-cell lymphoma-associated antigen HD-CL-09
Short name:
CTCL-associated antigen HD-CL-09
Dendritic cell-derived protein kinase
JNK/SAPK-inhibitory kinase
Jun kinase-inhibitory kinase
Kinase from chicken homolog A
Short name:
hKFC-A
Thousand and one amino acid protein 3
Gene namesi
Name:TAOK3
Synonyms:DPK, JIK, KDS, MAP3K18
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:18133. TAOK3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi165 – 1651D → A: Loss of serine/threonine-protein kinase activity. 1 Publication
Mutagenesisi181 – 1811T → A: No autophosphorylation and no kinase activity; when associated with F-183. 1 Publication
Mutagenesisi183 – 1831Y → F: No autophosphorylation and no kinase activity; when associated with A-181. 1 Publication
Mutagenesisi324 – 3241S → A: Inhibits activation of the p38/MAPK14 stress-activated MAPK cascade in response to DNA damage. 1 Publication

Organism-specific databases

PharmGKBiPA134975064.

Polymorphism and mutation databases

BioMutaiTAOK3.
DMDMi78099183.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 898898Serine/threonine-protein kinase TAO3PRO_0000086737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei324 – 3241Phosphoserine; by ATM6 Publications
Modified residuei331 – 3311Phosphoserine1 Publication
Modified residuei442 – 4421Phosphoserine1 Publication
Modified residuei830 – 8301N6-acetyllysineBy similarity

Post-translational modificationi

Autophosphorylated. Phosphorylation at Ser-324 by ATM following DNA damage is required for activation of the p38/MAPK14 stress-activated MAPK cascade. Phosphorylated by LRRK2.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H2K8.
PaxDbiQ9H2K8.
PRIDEiQ9H2K8.

PTM databases

PhosphoSiteiQ9H2K8.

Expressioni

Tissue specificityi

Ubiquitously expressed at a low level, and highly expressed in peripheral blood leukocytes (PBLs), thymus, spleen, kidney, skeletal muscle, heart and liver.2 Publications

Gene expression databases

BgeeiQ9H2K8.
CleanExiHS_TAOK3.
ExpressionAtlasiQ9H2K8. baseline and differential.
GenevisibleiQ9H2K8. HS.

Organism-specific databases

HPAiHPA017160.

Interactioni

Subunit structurei

Self-associates. Interacts with ERN1 and TRAF2. Interaction with TRAF2 is facilitated under ER stress conditions, such as treatment with tunicamycin, and may promote TRAF2 phosphorylation.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ERN1O754603EBI-1384100,EBI-371750
TRAF2Q129332EBI-1384100,EBI-355744

Protein-protein interaction databases

BioGridi119490. 7 interactions.
IntActiQ9H2K8. 5 interactions.
MINTiMINT-5005619.
STRINGi9606.ENSP00000376317.

Structurei

3D structure databases

ProteinModelPortaliQ9H2K8.
SMRiQ9H2K8. Positions 8-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 277254Protein kinasePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili452 – 50251Sequence AnalysisAdd
BLAST
Coiled coili548 – 649102Sequence AnalysisAdd
BLAST
Coiled coili754 – 879126Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi343 – 39351Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118848.
HOGENOMiHOG000236358.
HOVERGENiHBG088996.
InParanoidiQ9H2K8.
KOiK04429.
OMAiFRGFVDY.
OrthoDBiEOG74XS5S.
PhylomeDBiQ9H2K8.
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]

Sequencei

Sequence statusi: Complete.

Q9H2K8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKGVLKDPE IADLFYKDDP EELFIGLHEI GHGSFGAVYF ATNAHTSEVV
60 70 80 90 100
AIKKMSYSGK QTHEKWQDIL KEVKFLRQLK HPNTIEYKGC YLKEHTAWLV
110 120 130 140 150
MEYCLGSASD LLEVHKKPLQ EVEIAAITHG ALHGLAYLHS HALIHRDIKA
160 170 180 190 200
GNILLTEPGQ VKLADFGSAS MASPANSFVG TPYWMAPEVI LAMDEGQYDG
210 220 230 240 250
KVDIWSLGIT CIELAERKPP LFNMNAMSAL YHIAQNDSPT LQSNEWTDSF
260 270 280 290 300
RRFVDYCLQK IPQERPTSAE LLRHDFVRRD RPLRVLIDLI QRTKDAVREL
310 320 330 340 350
DNLQYRKMKK ILFQETRNGP LNESQEDEED SEHGTSLNRE MDSLGSNHSI
360 370 380 390 400
PSMSVSTGSQ SSSVNSMQEV MDESSSELVM MHDDESTINS SSSVVHKKDH
410 420 430 440 450
VFIRDEAGHG DPRPEPRPTQ SVQSQALHYR NRERFATIKS ASLVTRQIHE
460 470 480 490 500
HEQENELREQ MSGYKRMRRQ HQKQLIALEN KLKAEMDEHR LKLQKEVETH
510 520 530 540 550
ANNSSIELEK LAKKQVAIIE KEAKVAAADE KKFQQQILAQ QKKDLTTFLE
560 570 580 590 600
SQKKQYKICK EKIKEEMNED HSTPKKEKQE RISKHKENLQ HTQAEEEAHL
610 620 630 640 650
LTQQRLYYDK NCRFFKRKIM IKRHEVEQQN IREELNKKRT QKEMEHAMLI
660 670 680 690 700
RHDESTRELE YRQLHTLQKL RMDLIRLQHQ TELENQLEYN KRRERELHRK
710 720 730 740 750
HVMELRQQPK NLKAMEMQIK KQFQDTCKVQ TKQYKALKNH QLEVTPKNEH
760 770 780 790 800
KTILKTLKDE QTRKLAILAE QYEQSINEMM ASQALRLDEA QEAECQALRL
810 820 830 840 850
QLQQEMELLN AYQSKIKMQT EAQHERELQK LEQRVSLRRA HLEQKIEEEL
860 870 880 890
AALQKERSER IKNLLERQER EIETFDMESL RMGFGNLVTL DFPKEDYR
Length:898
Mass (Da):105,406
Last modified:October 25, 2005 - v2
Checksum:iAE7E30745B09763C
GO

Sequence cautioni

The sequence AAN09723.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361A → T in AAG38501 (PubMed:13679851).Curated
Sequence conflicti173 – 1731S → P in AAG38501 (PubMed:13679851).Curated
Sequence conflicti356 – 37823STGSQ…SSSEL → TWNQPEQGNGQPGQQPFHSK HVR in AAF14559 (PubMed:10559204).CuratedAdd
BLAST
Sequence conflicti668 – 6681Q → R in AAG38501 (PubMed:13679851).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201P → T in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041205
Natural varianti47 – 471S → N.3 Publications
Corresponds to variant rs428073 [ dbSNP | Ensembl ].
VAR_023691
Natural varianti392 – 3921S → Y in a lung small cell carcinoma sample; somatic mutation. 1 Publication
VAR_041206
Natural varianti727 – 7271C → Y.1 Publication
Corresponds to variant rs55857273 [ dbSNP | Ensembl ].
VAR_041207

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF179867 mRNA. Translation: AAF14559.1.
AF135158 mRNA. Translation: AAG09131.1.
AF263311 mRNA. Translation: AAG38501.1.
AF181985 mRNA. Translation: AAF25817.1.
BT007185 mRNA. Translation: AAP35849.1.
AC026366 Genomic DNA. No translation available.
BC002756 mRNA. Translation: AAH02756.1.
AL833731 mRNA. Translation: CAH56239.1.
AF328731 mRNA. Translation: AAN09723.1. Different initiation.
CCDSiCCDS9188.1.
RefSeqiNP_057365.3. NM_016281.3.
UniGeneiHs.644420.

Genome annotation databases

EnsembliENST00000392533; ENSP00000376317; ENSG00000135090.
ENST00000419821; ENSP00000416374; ENSG00000135090.
GeneIDi51347.
KEGGihsa:51347.
UCSCiuc001tww.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF179867 mRNA. Translation: AAF14559.1.
AF135158 mRNA. Translation: AAG09131.1.
AF263311 mRNA. Translation: AAG38501.1.
AF181985 mRNA. Translation: AAF25817.1.
BT007185 mRNA. Translation: AAP35849.1.
AC026366 Genomic DNA. No translation available.
BC002756 mRNA. Translation: AAH02756.1.
AL833731 mRNA. Translation: CAH56239.1.
AF328731 mRNA. Translation: AAN09723.1. Different initiation.
CCDSiCCDS9188.1.
RefSeqiNP_057365.3. NM_016281.3.
UniGeneiHs.644420.

3D structure databases

ProteinModelPortaliQ9H2K8.
SMRiQ9H2K8. Positions 8-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119490. 7 interactions.
IntActiQ9H2K8. 5 interactions.
MINTiMINT-5005619.
STRINGi9606.ENSP00000376317.

Chemistry

BindingDBiQ9H2K8.
ChEMBLiCHEMBL5701.
GuidetoPHARMACOLOGYi2235.

PTM databases

PhosphoSiteiQ9H2K8.

Polymorphism and mutation databases

BioMutaiTAOK3.
DMDMi78099183.

Proteomic databases

MaxQBiQ9H2K8.
PaxDbiQ9H2K8.
PRIDEiQ9H2K8.

Protocols and materials databases

DNASUi51347.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392533; ENSP00000376317; ENSG00000135090.
ENST00000419821; ENSP00000416374; ENSG00000135090.
GeneIDi51347.
KEGGihsa:51347.
UCSCiuc001tww.3. human.

Organism-specific databases

CTDi51347.
GeneCardsiGC12M118587.
HGNCiHGNC:18133. TAOK3.
HPAiHPA017160.
neXtProtiNX_Q9H2K8.
PharmGKBiPA134975064.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118848.
HOGENOMiHOG000236358.
HOVERGENiHBG088996.
InParanoidiQ9H2K8.
KOiK04429.
OMAiFRGFVDY.
OrthoDBiEOG74XS5S.
PhylomeDBiQ9H2K8.
TreeFamiTF351444.

Enzyme and pathway databases

SignaLinkiQ9H2K8.

Miscellaneous databases

ChiTaRSiTAOK3. human.
GeneWikiiTAOK3.
GenomeRNAii51347.
NextBioi54794.
PROiQ9H2K8.

Gene expression databases

BgeeiQ9H2K8.
CleanExiHS_TAOK3.
ExpressionAtlasiQ9H2K8. baseline and differential.
GenevisibleiQ9H2K8. HS.

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. "Human JIK, a novel member of the STE20 kinase family that inhibits JNK and is negatively regulated by epidermal growth factor."
    Tassi E., Biesova Z., Di Fiore P.P., Gutkind J.S., Wong W.T.
    J. Biol. Chem. 274:33287-33295(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, MUTAGENESIS OF THR-181 AND TYR-183, FUNCTION.
  2. "Cloning of DPK, a novel dendritic cell-derived protein kinase activating the ERK1/ERK2 and JNK/SAPK pathways."
    Zhang W., Chen T., Wan T., He L., Li N., Yuan Z., Cao X.
    Biochem. Biophys. Res. Commun. 274:872-879(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Dendritic cell.
  3. "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], SELF-ASSOCIATION, TISSUE SPECIFICITY, VARIANT ASN-47, SUBCELLULAR LOCATION.
  4. "KDS and TAO1, two related proteins with kinase domain homology to STE20, differentially relocate in mitogen stimulated T lymphocytes."
    Carter T.G., Benton B., Fruhling D., Monks C.R.F., Windmiller D., Kupfer A., Manfredi J., Johnson G.L., Pleiman C.M.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-47.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Placenta.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-898.
    Tissue: Stomach.
  9. "SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma."
    Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.
    Br. J. Dermatol. 150:252-258(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 304-898.
    Tissue: T-cell lymphoma.
  10. "Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress."
    Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T., Tohyama M.
    J. Biol. Chem. 276:13935-13940(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERN1 AND TRAF2.
  11. "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 AT SER-324, INDUCTION, MUTAGENESIS OF ASP-165 AND SER-324.
  12. "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-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Signal transduction protein array analysis links LRRK2 to Ste20 kinases and PKC zeta that modulate neuronal plasticity."
    Zach S., Felk S., Gillardon F.
    PLoS ONE 5:E13191-E13191(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY LRRK2.
  16. "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-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-20; ASN-47; TYR-392 AND TYR-727.

Entry informationi

Entry nameiTAOK3_HUMAN
AccessioniPrimary (citable) accession number: Q9H2K8
Secondary accession number(s): Q658N1
, Q8IUM4, Q9HC79, Q9NZM9, Q9UHG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: June 24, 2015
This is version 125 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. 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.