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Q9JJ78 (TOPK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Pbk
Synonyms:Topk
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by phosphorylation By similarity.

Subunit structure

Interacts with DLG1 and TP53 By similarity.

Post-translational modification

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

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase kinase subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Lymphokine-activated killer T-cell-originated protein kinase
PRO_0000086764

Regions

Domain31 – 330300Protein kinase
Nucleotide binding37 – 459ATP By similarity

Sites

Active site1661Proton acceptor By similarity
Binding site631ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue91Phosphothreonine By similarity
Modified residue231Phosphothreonine By similarity
Modified residue311Phosphoserine By similarity
Modified residue581Phosphoserine By similarity
Modified residue1991Phosphothreonine By similarity

Experimental info

Sequence conflict1231N → D in BAB23029. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9JJ78 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D274A4DB44CFEEE0

FASTA33036,745
        10         20         30         40         50         60 
MEGINNFKTP NKSEKRKSVL CSTPCVNIPA SPFMQKLGFG TGVSVYLMKR SPRGLSHSPW 

        70         80         90        100        110        120 
AVKKISLLCD DHYRTVYQKR LTDEAKILKN LNHPNIIGYR AFTEASDGSL CLAMEYGGEK 

       130        140        150        160        170        180 
SLNDLIEERN KDSGSPFPAA VILRVALHMA RGLKYLHQEK KLLHGDIKSS NVVIKGDFET 

       190        200        210        220        230        240 
IKICDVGVSL PLDENMTVTD PEACYIGTEP WKPKEALEEN GIITDKADVF AFGLTLWEMM 

       250        260        270        280        290        300 
TLCIPHVNLP DDDVDEDATF DESDFDDEAY YAALGTRPSI NMEELDDSYQ KAIELFCVCT 

       310        320        330 
NEDPKDRPSA AHIVEALELD GQCCGLSSKH

« Hide

References

« Hide 'large scale' references
[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: 10781613] [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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland and Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00467350.
RefSeqNP_075698.1. NM_023209.2.
UniGeneMm.24337.

3D structure databases

ProteinModelPortalQ9JJ78.
SMRQ9JJ78. Positions 29-319.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1341688.
STRINGQ9JJ78.

PTM databases

PhosphoSiteQ9JJ78.

Proteomic databases

PRIDEQ9JJ78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022612; ENSMUSP00000022612; ENSMUSG00000022033.
GeneID52033.
KEGGmmu:52033.
UCSCuc007ujo.1. mouse.

Organism-specific databases

CTD55872.
MGIMGI:1289156. Pbk.

Phylogenomic databases

eggNOGroNOG13721.
GeneTreeENSGT00600000084514.
HOGENOMHBG315301.
HOVERGENHBG056011.
InParanoidQ9JJ78.
OMAGVSVYLM.
OrthoDBEOG49ZXPN.
PhylomeDBQ9JJ78.

Gene expression databases

ArrayExpressQ9JJ78.
BgeeQ9JJ78.
CleanExMM_PBK.
GenevestigatorQ9JJ78.
GermOnlineENSMUSG00000022033. Mus musculus.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
KOK08865.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio308402.
SOURCESearch...

Entry information

Entry nameTOPK_MOUSE
AccessionPrimary (citable) accession number: Q9JJ78
Secondary accession number(s): Q922V2, Q9D184
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 1, 2000
Last modified: November 16, 2011
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents