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Protein

Serine/threonine-protein kinase TAO1

Gene

Taok1

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 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.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Enzyme regulationi

Serine/threonine-protein kinase activity is inhibited by SPRED1.1 Publication

Sites

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

Regions

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

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein kinase activator activity Source: RGD
  • protein kinase binding Source: RGD
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • activation of protein kinase activity Source: GOC
  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA repair Source: UniProtKB-KW
  • execution phase of apoptosis Source: UniProtKB
  • G2 DNA damage checkpoint Source: UniProtKB
  • positive regulation of JNK cascade Source: UniProtKB
  • positive regulation of stress-activated MAPK cascade Source: UniProtKB
  • protein phosphorylation Source: RGD
  • 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

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase TAO1 (EC:2.7.11.1)
Alternative name(s):
Thousand and one amino acid protein 1
Gene namesi
Name:Taok1
Synonyms:Tao1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi708455. Taok1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571K → A: Loss of serine/threonine-protein kinase without affecting interaction with SPRED1. 1 Publication
Mutagenesisi169 – 1691D → A: No kinase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10011001Serine/threonine-protein kinase TAO1PRO_0000086730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei421 – 4211PhosphoserineBy similarity
Modified residuei445 – 4451PhosphoserineBy similarity
Modified residuei669 – 6691PhosphothreonineBy similarity
Modified residuei965 – 9651PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO88664.
PRIDEiO88664.

PTM databases

iPTMnetiO88664.
PhosphoSiteiO88664.

Interactioni

Subunit structurei

Self-associates. Interacts with MAP2K3. Interacts with MAP3K7 (By similarity). Interacts with SPRED1 and TESK1.By similarity3 Publications

GO - Molecular functioni

  • protein kinase binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021368.

Structurei

3D structure databases

ProteinModelPortaliO88664.
SMRiO88664. 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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0577. Eukaryota.
ENOG410Y259. LUCA.
HOGENOMiHOG000236358.
HOVERGENiHBG088996.
InParanoidiO88664.
KOiK04429.
PhylomeDBiO88664.

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.

O88664-1 [UniParc]FASTAAdd to basket

« 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 TSEELLKHMF VLRERPETVL IDLIQRTKDA
310 320 330 340 350
VRELDNLQYR KMKKLLFQEA HNGPAVEAQE EEEEQDHGGG RTGTVNSVGS
360 370 380 390 400
NQSIPSMSIS ASSQSSSVNS LPDASDDKSE LDMMEGDHTV MSNSSVIHLK
410 420 430 440 450
PEEENYQEEG DPRTRASAPQ SPPQVSRHKS HYRNREHFAT IRTASLVTRQ
460 470 480 490 500
MQEHEQDSEL REQMSGYKRM RRQHQKQLMT LENKLKAEMD EHRLRLDKDL
510 520 530 540 550
ETQRNNFAAE MEKLIKKHQA SMEKEAKVMA 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
SHSYPGASSW SHNPTGGSGP HWGHPMGGTP QAWGHPMQGG PQPWGHPSGP
960 970 980 990 1000
MQGVPRGSSI GVRNSPQALR RTASGGRTEQ GMSRSTSVTS QISNGSHMSY

T
Length:1,001
Mass (Da):115,952
Last modified:November 1, 1998 - v1
Checksum:i85511B62DBD62FCC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084205 mRNA. Translation: AAC71014.1.
PIRiT17365.
RefSeqiNP_775449.1. NM_173327.1.
UniGeneiRn.30050.

Genome annotation databases

GeneIDi286993.
KEGGirno:286993.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084205 mRNA. Translation: AAC71014.1.
PIRiT17365.
RefSeqiNP_775449.1. NM_173327.1.
UniGeneiRn.30050.

3D structure databases

ProteinModelPortaliO88664.
SMRiO88664. Positions 12-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021368.

PTM databases

iPTMnetiO88664.
PhosphoSiteiO88664.

Proteomic databases

PaxDbiO88664.
PRIDEiO88664.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi286993.
KEGGirno:286993.

Organism-specific databases

CTDi57551.
RGDi708455. Taok1.

Phylogenomic databases

eggNOGiKOG0577. Eukaryota.
ENOG410Y259. LUCA.
HOGENOMiHOG000236358.
HOVERGENiHBG088996.
InParanoidiO88664.
KOiK04429.
PhylomeDBiO88664.

Miscellaneous databases

PROiO88664.

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 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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH MKK3, AUTOPHOSPHORYLATION, MUTAGENESIS OF ASP-169.
  2. "MARKK, a Ste20-like kinase, activates the polarity-inducing kinase MARK/PAR-1."
    Timm T., Li X.Y., Biernat J., Jiao J., Mandelkow E., Vandekerckhove J., Mandelkow E.M.
    EMBO J. 22:5090-5101(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MARK2.
  3. "Signaling from MARK to tau: regulation, cytoskeletal crosstalk, and pathological phosphorylation."
    Timm T., Matenia D., Li X.Y., Griesshaber B., Mandelkow E.M.
    Neurodegener. Dis. 3:207-217(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Spred1 and TESK1--two new interaction partners of the kinase MARKK/TAO1 that link the microtubule and actin cytoskeleton."
    Johne C., Matenia D., Li X.Y., Timm T., Balusamy K., Mandelkow E.M.
    Mol. Biol. Cell 19:1391-1403(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TESK1 AND SPRED1, ENZYME REGULATION, MUTAGENESIS OF LYS-57.

Entry informationi

Entry nameiTAOK1_RAT
AccessioniPrimary (citable) accession number: O88664
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 118 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

Complete proteome, Reference proteome

Documents

  1. 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.