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Q8K4K4 (TRIB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tribbles homolog 1

Short name=TRB-1
Gene names
Name:Trib1
Synonyms:Trb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

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.

Sequence caution

The sequence BAC28245.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC37854.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   Molecular functionProtein kinase inhibitor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of lipopolysaccharide-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 17724128. Source: BHF-UCL

negative regulation of smooth muscle cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

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

positive regulation of ubiquitin-protein transferase activity

Inferred by curator PubMed 20410507. Source: BHF-UCL

regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

response to lipopolysaccharide

Inferred from mutant phenotype PubMed 17724128. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

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 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 transferase regulator activity

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

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q8K4K4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8K4K4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     219-372: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Tribbles homolog 1
PRO_0000131860

Regions

Domain1 – 338338Protein kinase

Natural variations

Alternative sequence219 – 372154Missing in isoform 2.
VSP_051888

Experimental info

Sequence conflict2241E → G in AAM45478. Ref.1
Sequence conflict2781L → W in AAM45478. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: AD29BB4E640B4B62

FASTA37241,281
        10         20         30         40         50         60 
MRVGPVRFAL SGASQPRGPG LLFPAARGTP AKRLLDTDDA GAVAAKCPRL SECSSPPDYL 

        70         80         90        100        110        120 
SPPGSPCSPQ PPPSTQGTGG SCVSSPGPSR IADYLLLPLA EREHVSRALC IHTGRELRCK 

       130        140        150        160        170        180 
EFPIKHYQDK IRPYIQLPSH SNITGIVEVL LGESKAYVFF EKDFGDMHSY VRSRKRLREE 

       190        200        210        220        230        240 
EAARLFKQIV SAVAHCHQSA IVLGDLKLRK FVFSTEERTQ LRLESLEDTH IIKGEDDALS 

       250        260        270        280        290        300 
DKHGCPAYVS PEILNTTGTY SGKAADVWSL GVMLYTLLVG RYPFHDSDPS ALFSKIRRGQ 

       310        320        330        340        350        360 
FCIPEHVSPK ARCLIRSLLR REPSERLTAP QILLHPWFEY VLEPGYVDSE IGTSDQIVPE 

       370 
YQEDSDISSF FC 

« Hide

Isoform 2 [UniParc].

Checksum: F3A5AFE16E3450A8
Show »

FASTA21823,907

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Aorta, Hypothalamus, Lung, Skin 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] (ISOFORM 1).
Strain: FVB/N-3.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF358866 mRNA. Translation: AAM45478.1.
AK028626 mRNA. Translation: BAC26038.1.
AK033358 mRNA. Translation: BAC28245.1. Different initiation.
AK040738 mRNA. Translation: BAC30688.1.
AK041212 mRNA. Translation: BAC30865.1.
AK080228 mRNA. Translation: BAC37854.1. Different initiation.
AK162876 mRNA. Translation: BAE37097.1.
BC006800 mRNA. Translation: AAH06800.1.
CCDSCCDS27499.1. [Q8K4K4-1]
RefSeqNP_653132.1. NM_144549.4. [Q8K4K4-1]
UniGeneMm.40298.

3D structure databases

ProteinModelPortalQ8K4K4.
SMRQ8K4K4. Positions 113-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229263. 3 interactions.
IntActQ8K4K4. 1 interaction.

PTM databases

PhosphoSiteQ8K4K4.

Proteomic databases

PRIDEQ8K4K4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067543; ENSMUSP00000068834; ENSMUSG00000032501. [Q8K4K4-1]
ENSMUST00000118228; ENSMUSP00000112828; ENSMUSG00000032501. [Q8K4K4-2]
GeneID211770.
KEGGmmu:211770.
UCSCuc007vxw.1. mouse. [Q8K4K4-1]

Organism-specific databases

CTD10221.
MGIMGI:2443397. Trib1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000114880.
HOGENOMHOG000231872.
HOVERGENHBG067729.
InParanoidQ8K4K4.
KOK08814.
OMAAHCHQSA.
OrthoDBEOG7RJPR4.
PhylomeDBQ8K4K4.
TreeFamTF329785.

Gene expression databases

BgeeQ8K4K4.
CleanExMM_TRIB1.
GenevestigatorQ8K4K4.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR024105. TRB1.
IPR024104. Tribbles/Ser_Thr_kinase_40.
[Graphical view]
PANTHERPTHR22961. PTHR22961. 1 hit.
PTHR22961:SF10. PTHR22961:SF10. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio373352.
PROQ8K4K4.
SOURCESearch...

Entry information

Entry nameTRIB1_MOUSE
AccessionPrimary (citable) accession number: Q8K4K4
Secondary accession number(s): Q8BFS7 expand/collapse secondary AC list , Q8BJR9, Q8BZX3, Q91W04
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 97 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