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Protein

Serine/threonine-protein kinase TAO3

Gene

Taok3

Organism
Mus musculus (Mouse)
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) (By similarity).By similarity

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

GO - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase TAO3 (EC:2.7.11.1)
Alternative name(s):
Thousand and one amino acid protein 3
Gene namesi
Name:Taok3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:3041177. Taok3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 898898Serine/threonine-protein kinase TAO3PRO_0000086738Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei324 – 3241Phosphoserine; by ATMCombined sources
Modified residuei343 – 3431PhosphoserineBy similarity
Modified residuei346 – 3461PhosphoserineCombined sources
Modified residuei349 – 3491PhosphoserineCombined sources
Modified residuei357 – 3571PhosphothreonineCombined sources
Modified residuei359 – 3591PhosphoserineCombined sources
Modified residuei442 – 4421PhosphoserineBy similarity
Modified residuei830 – 8301N6-acetyllysineCombined sources

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8BYC6.
MaxQBiQ8BYC6.
PaxDbiQ8BYC6.
PRIDEiQ8BYC6.

PTM databases

iPTMnetiQ8BYC6.
PhosphoSiteiQ8BYC6.

Expressioni

Gene expression databases

BgeeiQ8BYC6.
CleanExiMM_TAOK3.
ExpressionAtlasiQ8BYC6. baseline and differential.
GenevisibleiQ8BYC6. MM.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000090565.

Structurei

3D structure databases

ProteinModelPortaliQ8BYC6.
SMRiQ8BYC6. Positions 8-387.
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 – 871118Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi326 – 3294Poly-Glu

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0577. Eukaryota.
ENOG410Y259. LUCA.
GeneTreeiENSGT00840000129798.
HOGENOMiHOG000236358.
HOVERGENiHBG088996.
InParanoidiQ8BYC6.
KOiK04429.
OMAiENQIEYN.
OrthoDBiEOG74XS5S.
PhylomeDBiQ8BYC6.
TreeFamiTF351444.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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.

Q8BYC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKGALKDPE IADLFFKDDP EELFIDLHEI GHGSFGAVYF ATNAHTNEVV
60 70 80 90 100
AVKKMSYSGK QTHEKWQDIL KEVKFLQQLK HPNTIEYKGC YLKEHTAWLV
110 120 130 140 150
MEYCLGSASD LLEVHKKPLQ EVEIAAITHG ALQGLAYLHF HSLIHRDIKA
160 170 180 190 200
GNILLTEPGQ VKLADFGSAS MASPANSFVG TPYWMAPEVI LAMDEGQYDG
210 220 230 240 250
KVDIWSLGIT CIELAERKPP LFNMNAMSAL YHIAQNDSPT LQSREWTDSF
260 270 280 290 300
RRFVDYCLHK IPQERPAAVE LLRHDFIRRE RPPKVLIDLI QRTKDAVREL
310 320 330 340 350
DNLQYRKMKK ILFQETRNGP LNESQEEEED GEQGSNLNRE VDSLGSIHSI
360 370 380 390 400
PSTSVSTGSR SSSVNSMQEV MDESSSELVM MQEDEGTANS SASTVHKKDH
410 420 430 440 450
VFVRDEAGHG DPRPEPRPTQ SVQSRALHYR NRERFATIKS ASLVTRQIHE
460 470 480 490 500
HEQENELREQ MSGYKRMRRQ HQKQLIALEN KLKAEMDEHR LKLQKEVETH
510 520 530 540 550
ANNSSIELEK LAKKQVATIE KEAKVAAADE KKFQQQILAQ QKKDLTTFLE
560 570 580 590 600
SQKKQYKICK EKIKEEMNED HSTPKKEKQE RISKHKENLQ HTQAEEEAHL
610 620 630 640 650
LTQQRLYYDR 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
KAILKTLKDE QTRKLAILAE QYEQSINEMM ASQALRLDEA QEAECQALRL
810 820 830 840 850
QLQQEMELLN AYQSKIKMQT EAQHERELQK LEQRVSLRRA HLEQKIEEEL
860 870 880 890
AALQKERSER IKTLLERQER ETETFDMESL RMGFGNLVTL DFPKEDYR
Length:898
Mass (Da):105,336
Last modified:October 25, 2005 - v2
Checksum:i2A68F2D48906EC05
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040531 mRNA. Translation: BAC30618.1.
AK042181 mRNA. Translation: BAE20625.1.
CJ197745 mRNA. No translation available.
CK625948 mRNA. No translation available.
CO813561 mRNA. No translation available.
CCDSiCCDS39233.1.
RefSeqiNP_001074777.1. NM_001081308.2.
NP_001186614.1. NM_001199685.1.
NP_899129.2. NM_183306.2.
XP_006530448.1. XM_006530385.2.
XP_011246521.1. XM_011248219.1.
XP_011246522.1. XM_011248220.1.
UniGeneiMm.24343.
Mm.487518.

Genome annotation databases

EnsembliENSMUST00000092889; ENSMUSP00000090565; ENSMUSG00000061288.
ENSMUST00000111978; ENSMUSP00000107609; ENSMUSG00000061288.
ENSMUST00000179276; ENSMUSP00000136750; ENSMUSG00000061288.
GeneIDi330177.
KEGGimmu:330177.
UCSCiuc008zfh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040531 mRNA. Translation: BAC30618.1.
AK042181 mRNA. Translation: BAE20625.1.
CJ197745 mRNA. No translation available.
CK625948 mRNA. No translation available.
CO813561 mRNA. No translation available.
CCDSiCCDS39233.1.
RefSeqiNP_001074777.1. NM_001081308.2.
NP_001186614.1. NM_001199685.1.
NP_899129.2. NM_183306.2.
XP_006530448.1. XM_006530385.2.
XP_011246521.1. XM_011248219.1.
XP_011246522.1. XM_011248220.1.
UniGeneiMm.24343.
Mm.487518.

3D structure databases

ProteinModelPortaliQ8BYC6.
SMRiQ8BYC6. Positions 8-387.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000090565.

PTM databases

iPTMnetiQ8BYC6.
PhosphoSiteiQ8BYC6.

Proteomic databases

EPDiQ8BYC6.
MaxQBiQ8BYC6.
PaxDbiQ8BYC6.
PRIDEiQ8BYC6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000092889; ENSMUSP00000090565; ENSMUSG00000061288.
ENSMUST00000111978; ENSMUSP00000107609; ENSMUSG00000061288.
ENSMUST00000179276; ENSMUSP00000136750; ENSMUSG00000061288.
GeneIDi330177.
KEGGimmu:330177.
UCSCiuc008zfh.2. mouse.

Organism-specific databases

CTDi51347.
MGIiMGI:3041177. Taok3.

Phylogenomic databases

eggNOGiKOG0577. Eukaryota.
ENOG410Y259. LUCA.
GeneTreeiENSGT00840000129798.
HOGENOMiHOG000236358.
HOVERGENiHBG088996.
InParanoidiQ8BYC6.
KOiK04429.
OMAiENQIEYN.
OrthoDBiEOG74XS5S.
PhylomeDBiQ8BYC6.
TreeFamiTF351444.

Miscellaneous databases

NextBioi399217.
PROiQ8BYC6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BYC6.
CleanExiMM_TAOK3.
ExpressionAtlasiQ8BYC6. baseline and differential.
GenevisibleiQ8BYC6. MM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-561 AND 766-898.
    Strain: C57BL/6J.
    Tissue: Thymus.
  2. "Expressed sequence tag analysis of mouse RPE/choroid."
    Ida H., Boylan S., Weigel A., Smit-McBride Z., Chao A., Gao J., Buchoff P., Wistow G., Hjelmeland L.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 556-757.
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 766-898.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-346; SER-349; THR-357 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-830, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTAOK3_MOUSE
AccessioniPrimary (citable) accession number: Q8BYC6
Secondary accession number(s): Q3V3B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: May 11, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.