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Protein

Serine/threonine-protein kinase TAO2

Gene

Taok2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase involved in different processes such as membrane blebbing and apoptotic bodies formation DNA damage response and MAPK14/p38 MAPK stress-activated MAPK cascade. Phosphorylates itself, MBP, activated MAPK8, MAP2K3, MAP2K6 and tubulins. Activates the MAPK14/p38 MAPK signaling pathway through the specific activation and phosphorylation of the upstream MAP2K3 and MAP2K6 kinases. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. May affect microtubule organization and stability. May play a role in the osmotic stress-MAPK8 pathway. Prevents MAP3K7-mediated activation of CHUK, and thus NF-kappa-B activation. 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/p38 MAPK activation.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Moderately inhibited by staurosporine, a broad-range protein kinase inhibitor.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571ATPPROSITE-ProRule annotation
Binding sitei106 – 1061Staurosporine inhibitor1 Publication
Binding sitei108 – 1081Staurosporine inhibitor1 Publication
Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation
Binding sitei155 – 1551Staurosporine inhibitor; via carbonyl oxygen1 Publication

Regions

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

GO - Molecular functioni

  • ATP binding Source: RGD
  • MAP kinase kinase kinase activity Source: RGD
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase TAO2 (EC:2.7.11.1)
Alternative name(s):
Thousand and one amino acid protein 2
Gene namesi
Name:Taok2
Synonyms:Tao2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621590. Taok2.

Subcellular locationi

Isoform 2 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei967 – 98721HelicalSequence analysisAdd
BLAST
Transmembranei989 – 100921HelicalSequence analysisAdd
BLAST
Transmembranei1014 – 103421HelicalSequence analysisAdd
BLAST
Transmembranei1040 – 106021HelicalSequence analysisAdd
BLAST
Transmembranei1170 – 119021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571K → A: Loss of activity. Loss of MAPK14 phosphorylation and of PCDH8 internalization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12351235Serine/threonine-protein kinase TAO2PRO_0000086735Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei181 – 1811Phosphoserine1 Publication
Modified residuei416 – 4161PhosphoserineBy similarity
Modified residuei658 – 6581PhosphoserineBy similarity
Modified residuei777 – 7771PhosphoserineBy similarity
Modified residuei825 – 8251PhosphoserineBy similarity
Modified residuei827 – 8271PhosphoserineBy similarity
Isoform 2 (identifier: Q9JLS3-2)
Modified residuei1038 – 10381Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylated. Phosphorylated by ATM (By similarity).By similarity
Isoform 2: Phosphorylated on Ser-1038 by MAPK14. This phosphorylation is required PCDH8 for endocytosis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9JLS3.
PRIDEiQ9JLS3.

PTM databases

iPTMnetiQ9JLS3.
PhosphoSiteiQ9JLS3.

Interactioni

Subunit structurei

Self-associates. Interacts with MAP2K3 and MAP2K6. Interacts with tubulins. Interacts with MAP3K7 and interfers with MAP3K7-binding to CHUK and thus prevents NF-kappa-B activation (By similarity). Isoform 2 interacts with PCDH8; this complex may also include CDH2.By similarity3 Publications

Protein-protein interaction databases

IntActiQ9JLS3. 1 interaction.
STRINGi10116.ENSRNOP00000061854.

Structurei

Secondary structure

1
1235
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 186Combined sources
Helixi24 – 274Combined sources
Beta strandi28 – 369Combined sources
Beta strandi38 – 4710Combined sources
Turni48 – 514Combined sources
Beta strandi52 – 6110Combined sources
Helixi66 – 8217Combined sources
Beta strandi91 – 977Combined sources
Beta strandi100 – 1067Combined sources
Beta strandi109 – 1113Combined sources
Helixi112 – 1198Combined sources
Helixi125 – 14420Combined sources
Helixi154 – 1563Combined sources
Beta strandi157 – 1604Combined sources
Turni161 – 1633Combined sources
Beta strandi164 – 1674Combined sources
Beta strandi174 – 1796Combined sources
Helixi186 – 1883Combined sources
Helixi191 – 1955Combined sources
Turni196 – 1994Combined sources
Helixi205 – 22016Combined sources
Turni224 – 2274Combined sources
Helixi230 – 23910Combined sources
Helixi252 – 26110Combined sources
Helixi266 – 2683Combined sources
Helixi272 – 2754Combined sources
Helixi279 – 2824Combined sources
Helixi289 – 30315Combined sources
Beta strandi304 – 3063Combined sources
Helixi307 – 3093Combined sources
Helixi311 – 3199Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U5QX-ray2.10A/B1-320[»]
1U5RX-ray2.10A/B1-320[»]
2GCDX-ray2.55A/B12-320[»]
ProteinModelPortaliQ9JLS3.
SMRiQ9JLS3. Positions 12-320.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JLS3.

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 coili488 – 52336Sequence analysisAdd
BLAST
Coiled coili576 – 60328Sequence analysisAdd
BLAST
Coiled coili683 – 71533Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi330 – 3367Poly-Glu
Compositional biasi347 – 37024Ser-richAdd
BLAST
Compositional biasi378 – 40831Glu-richAdd
BLAST
Compositional biasi450 – 4556Poly-Ser
Compositional biasi791 – 7944Poly-Glu
Compositional biasi900 – 9089Poly-Glu
Compositional biasi945 – 1062118Leu-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0577. Eukaryota.
ENOG410Y259. LUCA.
HOGENOMiHOG000236358.
HOVERGENiHBG088996.
InParanoidiQ9JLS3.
KOiK04429.
PhylomeDBiQ9JLS3.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JLS3-1) [UniParc]FASTAAdd to basket

Also known as: TAO2-alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPAGGRAGSL KDPDVAELFF KDDPEKLFSD LREIGHGSFG AVYFARDVRN
60 70 80 90 100
SEVVAIKKMS YSGKQSNEKW QDIIKEVRFL QKLRHPNTIQ YRGCYLREHT
110 120 130 140 150
AWLVMEYCLG SASDLLEVHK KPLQEVEIAA VTHGALQGLA YLHSHNMIHR
160 170 180 190 200
DVKAGNILLS EPGLVKLGDF GSASIMAPAN SFVGTPYWMA PEVILAMDEG
210 220 230 240 250
QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN ESPALQSGHW
260 270 280 290 300
SEYFRNFVDS CLQKIPQDRP TSEVLLKHRF VLRERPPTVI MDLIQRTKDA
310 320 330 340 350
VRELDNLQYR KMKKILFQEA PNGPGAEAPE EEEEAEPYMH RAGTLTSLES
360 370 380 390 400
SHSVPSMSIS ASSQSSSVNS LADASDNEEE EEEEEEEEEE EEEEGPESRE
410 420 430 440 450
MAMMQEGEHT VTSHSSIIHR LPGSDNLYDD PYQPEMTPGP LQPPAAPPTS
460 470 480 490 500
TSSSSARRRA YCRNRDHFAT IRTASLVSRQ IQEHEQDSAL REQLSGYKRM
510 520 530 540 550
RRQHQKQLLA LESRLRGERE EHSGRLQREL EAQRAGFGTE AEKLARRHQA
560 570 580 590 600
IGEKEARAAQ AEERKFQQHI LGQQKKELAA LLEAQKRTYK LRKEQLKEEL
610 620 630 640 650
QENPSTPKRE KAEWLLRQKE QLQQCQAEEE AGLLRRQRQY FELQCRQYKR
660 670 680 690 700
KMLLARHSLD QDLLREDLNK KQTQKDLECA LLLRQHEATR ELELRQLQAV
710 720 730 740 750
QRTRAELTRL QHQTELGNQL EYNKRREQEL RQKHAAQVRQ QPKSLKVRAG
760 770 780 790 800
QLPMGLPATG ALGPLSTGTL SEEQPCSSGQ EAILGQRMLG EEEEAVPERM
810 820 830 840 850
ILGKEGTTLE PEEQRILGEE MGTFSSSPQK HRSLVNEEDW DISKEMKESR
860 870 880 890 900
VPSLASQERN IIGQEEAGAW NLWEKEHGNL VDMEFKLGWV QGPVLTPVPE
910 920 930 940 950
EEEEEEEEGG APIGTPRDPG DGCPSPDIPP EPPPSHLRQY PASQLPGFLS
960 970 980 990 1000
HGLLTGLSFA VGSSSGLLPL LLLLLLPLLA AQGGGGLQAA LLALEVGLVG
1010 1020 1030 1040 1050
LGASYLFLCT ALHLPPSLFL LLAQGTALGA VLSLSWRRGL MGVPLGLGAA
1060 1070 1080 1090 1100
WLLAWPSLAL PLAAMAAGGK WVRQQGPQMR RGISRLWLRV LLRLSPMVFR
1110 1120 1130 1140 1150
ALQGCAAVGD RGLFALYPKT NKNGFRSRLP VPWPRQGNPR TTQHPLALLA
1160 1170 1180 1190 1200
RVWALCKGWN WRLARASHRL ASCLPPWAVH ILASWGLLKG ERPSRIPRLL
1210 1220 1230
PRSQRRLGLS ASRQLPPGTV AGRRSQTRRA LPPWR
Length:1,235
Mass (Da):138,751
Last modified:October 1, 2000 - v1
Checksum:i426960D0812518AD
GO
Isoform 2 (identifier: Q9JLS3-2) [UniParc]FASTAAdd to basket

Also known as: TAO2-beta

The sequence of this isoform differs from the canonical sequence as follows:
     333-333: E → ELTPCSQ
     747-1050: VRAGQLPMGL...MGVPLGLGAA → SKELQIKKQF...ILNGSSHFYS
     1051-1235: Missing.

Show »
Length:1,056
Mass (Da):119,965
Checksum:iE6BCAD23F13A189A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti434 – 4341P → L in BAF64457 (PubMed:17988630).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei333 – 3331E → ELTPCSQ in isoform 2. 1 PublicationVSP_040545
Alternative sequencei747 – 1050304VRAGQ…GLGAA → SKELQIKKQFQETCKIQTRQ YKALRAHLLETTPKAQHKSL VKRLKEEQTRKLAILAEQYD QSISEMLSSQALRLDETQEA EFQALRQRSNRNWSSLMLTR ARSKIRTESQHERELRELEQ RVALRRALLEQRVEEELLAL QTGRSERIRSLLERQAREIE AFDAESMRLGFSSMALGGIP AEAAAQGYPAPPPAPAWPSR PVPRSGAHWSHGPPPPGMPP PAWRXPALLAPPGPPNWLGP PTQSGTPSGGALLLLRNSPQ PLKRAASGGSSGENVGPPAA VPGPLSRSTSVASHILNGSS HFYS in isoform 2. 1 PublicationVSP_040546Add
BLAST
Alternative sequencei1051 – 1235185Missing in isoform 2. 1 PublicationVSP_040547Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF140556 mRNA. Translation: AAD39480.2.
AB290408 mRNA. Translation: BAF64457.1.
RefSeqiNP_073193.1. NM_022702.1. [Q9JLS3-1]
UniGeneiRn.9575.

Genome annotation databases

GeneIDi64666.
KEGGirno:64666.
UCSCiRGD:621590. rat. [Q9JLS3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF140556 mRNA. Translation: AAD39480.2.
AB290408 mRNA. Translation: BAF64457.1.
RefSeqiNP_073193.1. NM_022702.1. [Q9JLS3-1]
UniGeneiRn.9575.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U5QX-ray2.10A/B1-320[»]
1U5RX-ray2.10A/B1-320[»]
2GCDX-ray2.55A/B12-320[»]
ProteinModelPortaliQ9JLS3.
SMRiQ9JLS3. Positions 12-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JLS3. 1 interaction.
STRINGi10116.ENSRNOP00000061854.

PTM databases

iPTMnetiQ9JLS3.
PhosphoSiteiQ9JLS3.

Proteomic databases

PaxDbiQ9JLS3.
PRIDEiQ9JLS3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64666.
KEGGirno:64666.
UCSCiRGD:621590. rat. [Q9JLS3-1]

Organism-specific databases

CTDi9344.
RGDi621590. Taok2.

Phylogenomic databases

eggNOGiKOG0577. Eukaryota.
ENOG410Y259. LUCA.
HOGENOMiHOG000236358.
HOVERGENiHBG088996.
InParanoidiQ9JLS3.
KOiK04429.
PhylomeDBiQ9JLS3.

Miscellaneous databases

EvolutionaryTraceiQ9JLS3.
PROiQ9JLS3.

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

  1. "Isolation of the protein kinase TAO2 and identification of its mitogen-activated protein kinase/extracellular signal-regulated kinase kinase binding domain."
    Chen Z., Hutchison M., Cobb M.H.
    J. Biol. Chem. 274:28803-28807(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MAP2K3 AND MAP2K6.
    Tissue: Brain.
  2. "Activity-induced protocadherin arcadlin regulates dendritic spine number by triggering N-cadherin endocytosis via TAO2beta and p38 MAP kinases."
    Yasuda S., Tanaka H., Sugiura H., Okamura K., Sakaguchi T., Tran U., Takemiya T., Mizoguchi A., Yagita Y., Sakurai T., De Robertis E.M., Yamagata K.
    Neuron 56:456-471(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH PCDH8, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-57, PHOSPHORYLATION AT SER-1038 (ISOFORM 2).
  3. "Crystal structure of the TAO2 kinase domain: activation and specificity of a Ste20p MAP3K."
    Zhou T., Raman M., Gao Y., Earnest S., Chen Z., Machius M., Cobb M.H., Goldsmith E.J.
    Structure 12:1891-1900(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-320, PHOSPHORYLATION AT SER-181.
  4. "Crystal structure of the MAP3K TAO2 kinase domain bound by an inhibitor staurosporine."
    Zhou T.J., Sun L.G., Gao Y., Goldsmith E.J.
    Acta Biochim. Biophys. Sin. 38:385-392(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-320 IN COMPLEX WITH STAUROSPORINE, ENZYME REGULATION.

Entry informationi

Entry nameiTAOK2_RAT
AccessioniPrimary (citable) accession number: Q9JLS3
Secondary accession number(s): A6BM05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.