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Protein

Lymphokine-activated killer T-cell-originated protein kinase

Gene

Pbk

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by phosphorylation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631ATPPROSITE-ProRule annotation
Active sitei166 – 1661Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi37 – 459ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • cellular response to UV Source: MGI
  • negative regulation of inflammatory response Source: MGI
  • negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  • negative regulation of protein phosphorylation Source: MGI
  • negative regulation of stress-activated MAPK cascade Source: MGI
  • peptidyl-serine phosphorylation Source: MGI
  • peptidyl-threonine phosphorylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lymphokine-activated killer T-cell-originated protein kinase (EC:2.7.12.2)
Alternative name(s):
PDZ-binding kinase
T-LAK cell-originated protein kinase
Gene namesi
Name:Pbk
Synonyms:Topk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1289156. Pbk.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Lymphokine-activated killer T-cell-originated protein kinasePRO_0000086764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei9 – 91PhosphothreonineBy similarity
Modified residuei23 – 231PhosphothreonineBy similarity
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei58 – 581PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated; in a cell-cycle dependent manner at mitosis.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9JJ78.
MaxQBiQ9JJ78.
PaxDbiQ9JJ78.
PeptideAtlasiQ9JJ78.
PRIDEiQ9JJ78.

PTM databases

iPTMnetiQ9JJ78.
PhosphoSiteiQ9JJ78.

Expressioni

Gene expression databases

BgeeiQ9JJ78.
CleanExiMM_PBK.
ExpressionAtlasiQ9JJ78. baseline and differential.
GenevisibleiQ9JJ78. MM.

Interactioni

Subunit structurei

Interacts with DLG1 and TP53.By similarity

Protein-protein interaction databases

BioGridi206338. 1 interaction.
IntActiQ9JJ78. 1 interaction.
MINTiMINT-1341688.
STRINGi10090.ENSMUSP00000022612.

Structurei

3D structure databases

ProteinModelPortaliQ9JJ78.
SMRiQ9JJ78. Positions 24-321.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 330300Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0192. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00720000108839.
HOGENOMiHOG000294208.
HOVERGENiHBG056011.
InParanoidiQ9JJ78.
KOiK08865.
OMAiRNLHMEN.
OrthoDBiEOG7S4X6F.
PhylomeDBiQ9JJ78.
TreeFamiTF329763.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JJ78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGINNFKTP NKSEKRKSVL CSTPCVNIPA SPFMQKLGFG TGVSVYLMKR
60 70 80 90 100
SPRGLSHSPW AVKKISLLCD DHYRTVYQKR LTDEAKILKN LNHPNIIGYR
110 120 130 140 150
AFTEASDGSL CLAMEYGGEK SLNDLIEERN KDSGSPFPAA VILRVALHMA
160 170 180 190 200
RGLKYLHQEK KLLHGDIKSS NVVIKGDFET IKICDVGVSL PLDENMTVTD
210 220 230 240 250
PEACYIGTEP WKPKEALEEN GIITDKADVF AFGLTLWEMM TLCIPHVNLP
260 270 280 290 300
DDDVDEDATF DESDFDDEAY YAALGTRPSI NMEELDDSYQ KAIELFCVCT
310 320 330
NEDPKDRPSA AHIVEALELD GQCCGLSSKH
Length:330
Mass (Da):36,745
Last modified:October 1, 2000 - v1
Checksum:iD274A4DB44CFEEE0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 1231N → D in BAB23029 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041882 mRNA. Translation: BAA99578.1.
AK003838 mRNA. Translation: BAB23029.1.
AK076121 mRNA. Translation: BAC36199.1.
BC006754 mRNA. Translation: AAH06754.1.
BC020099 mRNA. Translation: AAH20099.1.
CCDSiCCDS27215.1.
RefSeqiNP_075698.1. NM_023209.2.
XP_006519320.1. XM_006519257.2.
UniGeneiMm.24337.

Genome annotation databases

EnsembliENSMUST00000022612; ENSMUSP00000022612; ENSMUSG00000022033.
GeneIDi52033.
KEGGimmu:52033.
UCSCiuc007ujo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041882 mRNA. Translation: BAA99578.1.
AK003838 mRNA. Translation: BAB23029.1.
AK076121 mRNA. Translation: BAC36199.1.
BC006754 mRNA. Translation: AAH06754.1.
BC020099 mRNA. Translation: AAH20099.1.
CCDSiCCDS27215.1.
RefSeqiNP_075698.1. NM_023209.2.
XP_006519320.1. XM_006519257.2.
UniGeneiMm.24337.

3D structure databases

ProteinModelPortaliQ9JJ78.
SMRiQ9JJ78. Positions 24-321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206338. 1 interaction.
IntActiQ9JJ78. 1 interaction.
MINTiMINT-1341688.
STRINGi10090.ENSMUSP00000022612.

PTM databases

iPTMnetiQ9JJ78.
PhosphoSiteiQ9JJ78.

Proteomic databases

EPDiQ9JJ78.
MaxQBiQ9JJ78.
PaxDbiQ9JJ78.
PeptideAtlasiQ9JJ78.
PRIDEiQ9JJ78.

Protocols and materials databases

DNASUi52033.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022612; ENSMUSP00000022612; ENSMUSG00000022033.
GeneIDi52033.
KEGGimmu:52033.
UCSCiuc007ujo.1. mouse.

Organism-specific databases

CTDi55872.
MGIiMGI:1289156. Pbk.

Phylogenomic databases

eggNOGiKOG0192. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00720000108839.
HOGENOMiHOG000294208.
HOVERGENiHBG056011.
InParanoidiQ9JJ78.
KOiK08865.
OMAiRNLHMEN.
OrthoDBiEOG7S4X6F.
PhylomeDBiQ9JJ78.
TreeFamiTF329763.

Miscellaneous databases

PROiQ9JJ78.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJ78.
CleanExiMM_PBK.
ExpressionAtlasiQ9JJ78. baseline and differential.
GenevisibleiQ9JJ78. MM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a novel MAPKK-like protein kinase, lymphokine-activated killer T-cell-originated protein kinase, specifically expressed in the testis and activated lymphoid cells."
    Abe Y., Matsumoto S., Kito K., Ueda N.
    J. Biol. Chem. 275:21525-21531(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetus.
  2. "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].
    Strain: C57BL/6J.
  3. "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].
    Strain: FVB/N.
    Tissue: Mammary gland and Mammary tumor.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiTOPK_MOUSE
AccessioniPrimary (citable) accession number: Q9JJ78
Secondary accession number(s): Q922V2, Q9D184
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 1, 2000
Last modified: July 6, 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. 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.