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Q8K4K3 (TRIB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

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

Names and origin

Protein namesRecommended name:
Tribbles homolog 2

Short name=TRB-2
Gene names
Name:Trib2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Interacts with MAPK kinases and regulates activation of MAP kinases. Does not display kinase activity By similarity. UniProtKB Q28283 UniProtKB Q96RU8

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Note: May associate with the cytoskeleton By similarity.

Domain

The protein kinase domain is predicted to be catalytically inactive.

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Molecular functionProtein kinase inhibitor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of fat cell differentiation

Inferred from mutant phenotype PubMed 17576771. Source: BHF-UCL

negative regulation of interleukin-10 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred by curator PubMed 20410507. Source: BHF-UCL

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 20410507. Source: BHF-UCL

positive regulation of ubiquitin-protein ligase activity

Inferred by curator PubMed 20410507. Source: BHF-UCL

regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein kinase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

transcription factor binding

Inferred from direct assay PubMed 17576771PubMed 20410507. Source: BHF-UCL

transferase activity, transferring phosphorus-containing groups

Inferred from electronic annotation. Source: InterPro

ubiquitin protein ligase binding

Inferred from direct assay PubMed 20410507. Source: BHF-UCL

ubiquitin-protein ligase regulator activity

Inferred from direct assay PubMed 20410507. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343Tribbles homolog 2
PRO_0000131864

Regions

Domain61 – 308248Protein kinase

Experimental info

Sequence conflict2441L → V in AAM45477. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8K4K3 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 9418B7AC19FCC23F

FASTA34338,773
        10         20         30         40         50         60 
MNIHRSTPIT IARYGRSRNK TQDFEELSSI RSAEPSQSFS PNLGSPSPPE TPNLSHCVSC 

        70         80         90        100        110        120 
IGKYLLLEPL EGDHVFRAVH LHSGEELVCK VFEISCYQES LAPCFCLSAH SNINQITEIL 

       130        140        150        160        170        180 
LGETKAYVFF ERSYGDMHSF VRTCKKLREE EAARLFYQIA SAVAHCHDGG LVLRDLKLRK 

       190        200        210        220        230        240 
FIFKDEERTR VKLESLEDAY ILRGDDDSLS DKHGCPAYVS PEILNTSGSY SGKAADVWSL 

       250        260        270        280        290        300 
GVMLYTMLVG RYPFHDIEPS SLFSKIRRGQ FNIPETLSPK AKCLIRSILR REPSERLTSQ 

       310        320        330        340 
EILDHPWFST DFSVSNSGFG AKEACDQLVP DVNMEENLDP FFN 

« Hide

References

« Hide 'large scale' references
[1]"Mammalian homologs of Drosophila tribbles (htrb) control mitogen activated protein kinase signaling."
Kiss-Toth E., Dempsey C., Jozsa V., Caunt J., Oxley K.M., Bagstaff S.M., Wyllie D.H., Harte M., O'Neill L.A.J., Qwarnstrom E.E., Dower S.K.
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Aorta, Cerebellum, Colon, Retina and Vein.
[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: Eye, Kidney and Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF358867 mRNA. Translation: AAM45477.1.
AK044747 mRNA. Translation: BAC32063.1.
AK080064 mRNA. Translation: BAC37820.1.
AK082329 mRNA. Translation: BAC38467.1.
AK144192 mRNA. Translation: BAE25758.1.
BC027159 mRNA. Translation: AAH27159.1.
BC034338 mRNA. Translation: AAH34338.1.
BC037387 mRNA. Translation: AAH37387.1.
RefSeqNP_653134.2. NM_144551.5.
XP_006515117.1. XM_006515054.1.
UniGeneMm.491136.

3D structure databases

ProteinModelPortalQ8K4K3.
SMRQ8K4K3. Positions 61-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229913. 2 interactions.
IntActQ8K4K3. 1 interaction.
STRING10090.ENSMUSP00000020922.

PTM databases

PhosphoSiteQ8K4K3.

Proteomic databases

PRIDEQ8K4K3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020922; ENSMUSP00000020922; ENSMUSG00000020601.
GeneID217410.
KEGGmmu:217410.
UCSCuc007nbq.1. mouse.

Organism-specific databases

CTD28951.
MGIMGI:2145021. Trib2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000114880.
HOGENOMHOG000231872.
HOVERGENHBG067729.
InParanoidQ8K4K3.
KOK08814.
OMAHCHDNGL.
OrthoDBEOG7RJPR4.
PhylomeDBQ8K4K3.
TreeFamTF329785.

Gene expression databases

BgeeQ8K4K3.
CleanExMM_TRIB2.
GenevestigatorQ8K4K3.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR024104. Tribbles/Ser_Thr_kinase_40.
[Graphical view]
PANTHERPTHR22961. PTHR22961. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRIB2. mouse.
NextBio375849.
PROQ8K4K3.
SOURCESearch...

Entry information

Entry nameTRIB2_MOUSE
AccessionPrimary (citable) accession number: Q8K4K3
Secondary accession number(s): Q8K017, Q8R2V8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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