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Q92519 (TRIB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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
Synonyms:TRB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.

Tissue specificity

Highly expressed in peripheral blood leukocytes. Ref.7

Domain

The protein kinase domain is predicted to be catalytically inactive.

Miscellaneous

Antibodies against TRIB2 are present in sera from patients with autoimmune uveitis.

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
   Coding sequence diversityPolymorphism
   Molecular functionProtein kinase inhibitor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of fat cell differentiation

Inferred from sequence or structural similarity PubMed 17576771. Source: BHF-UCL

negative regulation of interleukin-10 biosynthetic process

Inferred from mutant phenotype PubMed 18643775. Source: BHF-UCL

negative regulation of protein kinase activity

Non-traceable author statement PubMed 12791994. Source: BHF-UCL

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity 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

   Molecular_functionprotein kinase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

transcription factor binding

Inferred from sequence or structural similarity PubMed 17576771. Source: BHF-UCL

transferase activity, transferring phosphorus-containing groups

Inferred from electronic annotation. Source: InterPro

ubiquitin protein ligase binding

Inferred from sequence or structural similarity PubMed 20410507. Source: BHF-UCL

ubiquitin-protein transferase regulator activity

Inferred from sequence or structural similarity PubMed 20410507. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343Tribbles homolog 2
PRO_0000131863

Regions

Domain61 – 308248Protein kinase

Natural variations

Natural variant41H → R. Ref.9
Corresponds to variant rs55813198 [ dbSNP | Ensembl ].
VAR_042371

Sequences

Sequence LengthMass (Da)Tools
Q92519 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: BF8B7366DACB84FA

FASTA34338,801
        10         20         30         40         50         60 
MNIHRSTPIT IARYGRSRNK TQDFEELSSI RSAEPSQSFS PNLGSPSPPE TPNLSHCVSC 

        70         80         90        100        110        120 
IGKYLLLEPL EGDHVFRAVH LHSGEELVCK VFDISCYQES LAPCFCLSAH SNINQITEII 

       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 DFSVSNSAYG AKEVSDQLVP DVNMEENLDP FFN 

« Hide

References

« Hide 'large scale' references
[1]"The cloning of a cDNA for putative serine/threonine kinase expressed in human osteoblast."
Ohno I., Hashimoto J., Takaoka K., Ochi T., Okubo K., Matsubara K.
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cancellous bone.
[2]Shan Y.X., Yu L.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Uterus.
[7]"Human tribbles, a protein family controlling mitogen-activated protein kinase cascades."
Kiss-Toth E., Bagstaff S.M., Sung H.Y., Jozsa V., Dempsey C., Caunt J.C., Oxley K.M., Wyllie D.H., Polgar T., Harte M., O'Neill L.A.J., Qwarnstrom E.E., Dower S.K.
J. Biol. Chem. 279:42703-42708(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Identification of tribbles homolog 2 as an autoantigen in autoimmune uveitis by phage display."
Zhang Y., Davis J.L., Li W.
Mol. Immunol. 42:1275-1281(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOANTIBODIES.
[9]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D87119 mRNA. Translation: BAA13250.1.
AY245544 mRNA. Translation: AAO89231.1.
AK313237 mRNA. Translation: BAG36048.1.
AC009486 Genomic DNA. Translation: AAY15015.1.
CH471053 Genomic DNA. Translation: EAX00907.1.
CH471053 Genomic DNA. Translation: EAX00908.1.
CH471053 Genomic DNA. Translation: EAX00909.1.
BC002637 mRNA. Translation: AAH02637.1.
CCDSCCDS1683.1.
RefSeqNP_067675.1. NM_021643.3.
UniGeneHs.467751.

3D structure databases

ProteinModelPortalQ92519.
SMRQ92519. Positions 61-336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118779. 8 interactions.
IntActQ92519. 3 interactions.
MINTMINT-2812905.
STRING9606.ENSP00000155926.

PTM databases

PhosphoSiteQ92519.

Polymorphism databases

DMDM74762638.

Proteomic databases

PaxDbQ92519.
PRIDEQ92519.

Protocols and materials databases

DNASU28951.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000155926; ENSP00000155926; ENSG00000071575.
GeneID28951.
KEGGhsa:28951.
UCSCuc002rbv.4. human.

Organism-specific databases

CTD28951.
GeneCardsGC02P012856.
HGNCHGNC:30809. TRIB2.
HPAHPA001305.
MIM609462. gene.
neXtProtNX_Q92519.
PharmGKBPA128394647.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000231872.
HOVERGENHBG067729.
InParanoidQ92519.
KOK08814.
OMAHCHDNGL.
PhylomeDBQ92519.
TreeFamTF329785.

Enzyme and pathway databases

SignaLinkQ92519.

Gene expression databases

ArrayExpressQ92519.
BgeeQ92519.
CleanExHS_TRIB2.
GenevestigatorQ92519.

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

GeneWikiTRIB2.
GenomeRNAi28951.
NextBio51761.
PROQ92519.
SOURCESearch...

Entry information

Entry nameTRIB2_HUMAN
AccessionPrimary (citable) accession number: Q92519
Secondary accession number(s): B2R851, D6W510
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM