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Q7L7X3

- TAOK1_HUMAN

UniProt

Q7L7X3 - TAOK1_HUMAN

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Protein

Serine/threonine-protein kinase TAO1

Gene

TAOK1

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

Functioni

Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Serine/threonine-protein kinase activity is inhibited by SPRED1.

Sites

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

Regions

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

GO - Molecular functioni

  1. ATP binding Source: HGNC
  2. kinase activity Source: HGNC
  3. protein kinase activity Source: HGNC
  4. protein serine/threonine kinase activity Source: UniProtKB
  5. transferase activity Source: HGNC

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. DNA repair Source: UniProtKB-KW
  3. execution phase of apoptosis Source: UniProtKB
  4. G2 DNA damage checkpoint Source: UniProtKB
  5. mitotic cell cycle Source: Reactome
  6. positive regulation of JNK cascade Source: UniProtKB
  7. positive regulation of stress-activated MAPK cascade Source: UniProtKB
  8. protein phosphorylation Source: HGNC
  9. regulation of cytoskeleton organization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. Mitotic Prometaphase.
SignaLinkiQ7L7X3.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase TAO1 (EC:2.7.11.1)
Alternative name(s):
Kinase from chicken homolog B
Short name:
hKFC-B
MARK Kinase
Short name:
MARKK
Prostate-derived sterile 20-like kinase 2
Short name:
PSK-2
Short name:
PSK2
Short name:
Prostate-derived STE20-like kinase 2
Thousand and one amino acid protein kinase 1
Short name:
TAOK1
Short name:
hTAOK1
Gene namesi
Name:TAOK1
Synonyms:KIAA1361, MAP3K16, MARKK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:29259. TAOK1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571K → A: Abolishes kinase activity, ability to activate the MAPK8/JNK cascade and cleavage by caspase-3 (CASP3). 1 Publication
Mutagenesisi169 – 1691D → A: Loss of serine/threonine-protein kinase activity. 1 Publication
Mutagenesisi376 – 3761D → N: Does not abolish cleavage by caspase-3 (CASP3). 1 Publication
Mutagenesisi643 – 6431T → A: Abolishes phosphorylation by ATM; when associated with A-785 and A-990. 1 Publication
Mutagenesisi785 – 7851T → A: Abolishes phosphorylation by ATM; when associated with A-643 and A-990. 1 Publication
Mutagenesisi990 – 9901S → A: Abolishes phosphorylation by ATM; when associated with A-643 and A-785. 1 Publication

Organism-specific databases

PharmGKBiPA134872946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10011001Serine/threonine-protein kinase TAO1PRO_0000086728Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine2 Publications
Modified residuei421 – 4211Phosphoserine7 Publications
Modified residuei445 – 4451Phosphoserine1 Publication
Modified residuei669 – 6691Phosphothreonine1 Publication
Modified residuei965 – 9651Phosphoserine1 Publication

Post-translational modificationi

Proteolytically processed by caspase-3 (CASP3).1 Publication
Autophosphorylated (By similarity). Phosphorylated by ATM in response to DNA damage. Phosphorylated by LRRK2.By similarity9 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ7L7X3.
PaxDbiQ7L7X3.
PeptideAtlasiQ7L7X3.
PRIDEiQ7L7X3.

PTM databases

PhosphoSiteiQ7L7X3.

Expressioni

Tissue specificityi

Highly expressed in the testis, and to a lower extent also expressed in brain, placenta, colon and skeletal muscle.2 Publications

Inductioni

In response to DNA damage.1 Publication

Gene expression databases

BgeeiQ7L7X3.
CleanExiHS_TAOK1.
ExpressionAtlasiQ7L7X3. baseline and differential.
GenevestigatoriQ7L7X3.

Organism-specific databases

HPAiHPA007669.

Interactioni

Subunit structurei

Self-associates. Interacts with MAP2K3 (By similarity). Interacts with SPRED1 and TESK1. Interacts with MAP3K7.By similarity1 Publication

Protein-protein interaction databases

BioGridi121607. 11 interactions.
DIPiDIP-39709N.
IntActiQ7L7X3. 9 interactions.
MINTiMINT-5006389.
STRINGi9606.ENSP00000261716.

Structurei

3D structure databases

ProteinModelPortaliQ7L7X3.
SMRiQ7L7X3. 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 coili458 – 651194Sequence AnalysisAdd
BLAST
Coiled coili754 – 877124Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi330 – 3345Poly-Glu
Compositional biasi347 – 37933Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118848.
HOGENOMiHOG000236358.
HOVERGENiHBG088996.
InParanoidiQ7L7X3.
KOiK04429.
OMAiAGPHWGH.
OrthoDBiEOG74XS5S.
PhylomeDBiQ7L7X3.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q7L7X3-1) [UniParc]FASTAAdd to Basket

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
MPSTNRAGSL KDPEIAELFF KEDPEKLFTD LREIGHGSFG AVYFARDVRT
60 70 80 90 100
NEVVAIKKMS YSGKQSTEKW QDIIKEVKFL QRIKHPNSIE YKGCYLREHT
110 120 130 140 150
AWLVMEYCLG SASDLLEVHK KPLQEVEIAA ITHGALQGLA YLHSHTMIHR
160 170 180 190 200
DIKAGNILLT EPGQVKLADF GSASMASPAN SFVGTPYWMA PEVILAMDEG
210 220 230 240 250
QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN ESPTLQSNEW
260 270 280 290 300
SDYFRNFVDS CLQKIPQDRP TSEELLKHIF VLRERPETVL IDLIQRTKDA
310 320 330 340 350
VRELDNLQYR KMKKLLFQEA HNGPAVEAQE EEEEQDHGVG RTGTVNSVGS
360 370 380 390 400
NQSIPSMSIS ASSQSSSVNS LPDVSDDKSE LDMMEGDHTV MSNSSVIHLK
410 420 430 440 450
PEEENYREEG DPRTRASDPQ SPPQVSRHKS HYRNREHFAT IRTASLVTRQ
460 470 480 490 500
MQEHEQDSEL REQMSGYKRM RRQHQKQLMT LENKLKAEMD EHRLRLDKDL
510 520 530 540 550
ETQRNNFAAE MEKLIKKHQA AMEKEAKVMS NEEKKFQQHI QAQQKKELNS
560 570 580 590 600
FLESQKREYK LRKEQLKEEL NENQSTPKKE KQEWLSKQKE NIQHFQAEEE
610 620 630 640 650
ANLLRRQRQY LELECRRFKR RMLLGRHNLE QDLVREELNK RQTQKDLEHA
660 670 680 690 700
MLLRQHESMQ ELEFRHLNTI QKMRCELIRL QHQTELTNQL EYNKRREREL
710 720 730 740 750
RRKHVMEVRQ QPKSLKSKEL QIKKQFQDTC KIQTRQYKAL RNHLLETTPK
760 770 780 790 800
SEHKAVLKRL KEEQTRKLAI LAEQYDHSIN EMLSTQALRL DEAQEAECQV
810 820 830 840 850
LKMQLQQELE LLNAYQSKIK MQAEAQHDRE LRELEQRVSL RRALLEQKIE
860 870 880 890 900
EEMLALQNER TERIRSLLER QAREIEAFDS ESMRLGFSNM VLSNLSPEAF
910 920 930 940 950
SHSYPGASGW SHNPTGGPGP HWGHPMGGPP QAWGHPMQGG PQPWGHPSGP
960 970 980 990 1000
MQGVPRGSSM GVRNSPQALR RTASGGRTEQ GMSRSTSVTS QISNGSHMSY

T
Length:1,001
Mass (Da):116,070
Last modified:July 5, 2004 - v1
Checksum:i82941DEAEADC7651
GO
Isoform 2 (identifier: Q7L7X3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: Missing.
     569-572: ELNE → VLMS
     573-1001: Missing.

Note: No experimental confirmation available.

Show »
Length:398
Mass (Da):46,163
Checksum:iB2744BCA14C7E63F
GO
Isoform 3 (identifier: Q7L7X3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     569-716: Missing.

Note: No experimental confirmation available.

Show »
Length:853
Mass (Da):97,526
Checksum:i15DE595D707B9E34
GO

Sequence cautioni

The sequence BAA92599.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511S → T in BAB14901. (PubMed:14702039)Curated
Sequence conflicti257 – 2571F → S in AAG38502. (PubMed:13679851)Curated
Sequence conflicti860 – 8601R → C in AAG38502. (PubMed:13679851)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti855 – 8551A → T.1 Publication
Corresponds to variant rs34151057 [ dbSNP | Ensembl ].
VAR_041204

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 174174Missing in isoform 2. 1 PublicationVSP_015964Add
BLAST
Alternative sequencei569 – 716148Missing in isoform 3. 1 PublicationVSP_043706Add
BLAST
Alternative sequencei569 – 5724ELNE → VLMS in isoform 2. 1 PublicationVSP_015965
Alternative sequencei573 – 1001429Missing in isoform 2. 1 PublicationVSP_015966Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF263312 mRNA. Translation: AAG38502.1.
AY049015 mRNA. Translation: AAL12217.1.
CQ834802 mRNA. Translation: CAH05616.1.
AB037782 mRNA. Translation: BAA92599.1. Different initiation.
AK024376 mRNA. Translation: BAB14901.1.
AC068025 Genomic DNA. No translation available.
AC068588 Genomic DNA. No translation available.
AC090698 Genomic DNA. No translation available.
CH471159 Genomic DNA. Translation: EAW51188.1.
BC133039 mRNA. Translation: AAI33040.1.
BC144067 mRNA. Translation: AAI44068.1.
CCDSiCCDS32601.1. [Q7L7X3-1]
CCDS56024.1. [Q7L7X3-3]
RefSeqiNP_065842.1. NM_020791.2. [Q7L7X3-1]
NP_079418.1. NM_025142.1. [Q7L7X3-3]
UniGeneiHs.597434.
Hs.735869.

Genome annotation databases

EnsembliENST00000261716; ENSP00000261716; ENSG00000160551. [Q7L7X3-1]
ENST00000536202; ENSP00000438819; ENSG00000160551. [Q7L7X3-3]
GeneIDi57551.
KEGGihsa:57551.
UCSCiuc002hdz.2. human. [Q7L7X3-1]
uc002heb.1. human. [Q7L7X3-2]
uc010wbe.2. human. [Q7L7X3-3]

Polymorphism databases

DMDMi74759012.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF263312 mRNA. Translation: AAG38502.1 .
AY049015 mRNA. Translation: AAL12217.1 .
CQ834802 mRNA. Translation: CAH05616.1 .
AB037782 mRNA. Translation: BAA92599.1 . Different initiation.
AK024376 mRNA. Translation: BAB14901.1 .
AC068025 Genomic DNA. No translation available.
AC068588 Genomic DNA. No translation available.
AC090698 Genomic DNA. No translation available.
CH471159 Genomic DNA. Translation: EAW51188.1 .
BC133039 mRNA. Translation: AAI33040.1 .
BC144067 mRNA. Translation: AAI44068.1 .
CCDSi CCDS32601.1. [Q7L7X3-1 ]
CCDS56024.1. [Q7L7X3-3 ]
RefSeqi NP_065842.1. NM_020791.2. [Q7L7X3-1 ]
NP_079418.1. NM_025142.1. [Q7L7X3-3 ]
UniGenei Hs.597434.
Hs.735869.

3D structure databases

ProteinModelPortali Q7L7X3.
SMRi Q7L7X3. Positions 12-320.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121607. 11 interactions.
DIPi DIP-39709N.
IntActi Q7L7X3. 9 interactions.
MINTi MINT-5006389.
STRINGi 9606.ENSP00000261716.

Chemistry

BindingDBi Q7L7X3.
ChEMBLi CHEMBL5261.
GuidetoPHARMACOLOGYi 2233.

PTM databases

PhosphoSitei Q7L7X3.

Polymorphism databases

DMDMi 74759012.

Proteomic databases

MaxQBi Q7L7X3.
PaxDbi Q7L7X3.
PeptideAtlasi Q7L7X3.
PRIDEi Q7L7X3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261716 ; ENSP00000261716 ; ENSG00000160551 . [Q7L7X3-1 ]
ENST00000536202 ; ENSP00000438819 ; ENSG00000160551 . [Q7L7X3-3 ]
GeneIDi 57551.
KEGGi hsa:57551.
UCSCi uc002hdz.2. human. [Q7L7X3-1 ]
uc002heb.1. human. [Q7L7X3-2 ]
uc010wbe.2. human. [Q7L7X3-3 ]

Organism-specific databases

CTDi 57551.
GeneCardsi GC17P027717.
HGNCi HGNC:29259. TAOK1.
HPAi HPA007669.
MIMi 610266. gene.
neXtProti NX_Q7L7X3.
PharmGKBi PA134872946.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118848.
HOGENOMi HOG000236358.
HOVERGENi HBG088996.
InParanoidi Q7L7X3.
KOi K04429.
OMAi AGPHWGH.
OrthoDBi EOG74XS5S.
PhylomeDBi Q7L7X3.
TreeFami TF351444.

Enzyme and pathway databases

Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. Mitotic Prometaphase.
SignaLinki Q7L7X3.

Miscellaneous databases

ChiTaRSi TAOK1. human.
GeneWikii TAOK1.
GenomeRNAii 57551.
NextBioi 64014.
PROi Q7L7X3.
SOURCEi Search...

Gene expression databases

Bgeei Q7L7X3.
CleanExi HS_TAOK1.
ExpressionAtlasi Q7L7X3. baseline and differential.
Genevestigatori Q7L7X3.

Family and domain databases

InterProi IPR011009. 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 ]
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. "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 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  2. "Characterization of human TAO1."
    Jenkins S.G., D'Andrea R.J., Gamble J.R., Vadas M.A.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [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 AND 3).
    Tissue: Brain.
  9. "Isolation of TAO1, a protein kinase that activates MEKs in stress-activated protein kinase cascades."
    Hutchison M., Berman K.S., Cobb M.H.
    J. Biol. Chem. 273:28625-28632(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  10. "TAO (thousand-and-one amino acid) protein kinases mediate signaling from carbachol to p38 mitogen-activated protein kinase and ternary complex factors."
    Chen Z., Raman M., Chen L., Lee S.F., Gilman A.G., Cobb M.H.
    J. Biol. Chem. 278:22278-22283(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Prostate-derived sterile 20-like kinase 2 (PSK2) regulates apoptotic morphology via C-Jun N-terminal kinase and Rho kinase-1."
    Zihni C., Mitsopoulos C., Tavares I.A., Ridley A.J., Morris J.D.
    J. Biol. Chem. 281:7317-7323(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF LYS-57 AND ASP-376.
  12. "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: INTERACTION WITH MAP3K7.
  13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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, MUTAGENESIS OF ASP-169; THR-643; THR-785 AND SER-990.
  15. "A functional genomic screen identifies a role for TAO1 kinase in spindle-checkpoint signalling."
    Draviam V.M., Stegmeier F., Nalepa G., Sowa M.E., Chen J., Liang A., Hannon G.J., Sorger P.K., Harper J.W., Elledge S.J.
    Nat. Cell Biol. 9:556-564(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE ROLE IN SPINDLE CHECKPOINT.
  16. "Human TAO kinase 1 induces apoptosis in SH-SY5Y cells."
    Wu M.F., Wang S.G.
    Cell Biol. Int. 32:151-156(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-965, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  18. "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-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-421 AND THR-669, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  23. "Re-examination of siRNA specificity questions role of PICH and Tao1 in the spindle checkpoint and identifies Mad2 as a sensitive target for small RNAs."
    Hubner N.C., Wang L.H., Kaulich M., Descombes P., Poser I., Nigg E.A.
    Chromosoma 119:149-165(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF ROLE IN SPINDLE CHECKPOINT.
  24. "Re-evaluating the role of Tao1 in the spindle checkpoint."
    Westhorpe F.G., Diez M.A., Gurden M.D., Tighe A., Taylor S.S.
    Chromosoma 119:371-379(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF ROLE IN SPINDLE CHECKPOINT.
  25. "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.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "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: VARIANT [LARGE SCALE ANALYSIS] THR-855.

Entry informationi

Entry nameiTAOK1_HUMAN
AccessioniPrimary (citable) accession number: Q7L7X3
Secondary accession number(s): A2RUT8
, B7ZLV6, Q96L75, Q9H2K7, Q9H7S5, Q9P2I6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 111 of the entry and version 1 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 17
    Human chromosome 17: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3