Q8K4K4 (TRIB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tribbles homolog 1
Short name=TRB-1

Gene names

Name:	Trib1
Synonyms:	Trb1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Protein existence	Evidence 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 diversity	Alternative splicing
Molecular function	Protein kinase inhibitor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JNK cascade Inferred from electronic annotation. Source: Compara negative regulation of lipopolysaccharide-mediated signaling pathway Inferred from electronic annotation. Source: Compara 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: Compara negative regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara 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 response to lipopolysaccharide Inferred from mutant phenotype PubMed 17724128. Source: BHF-UCL
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	protein 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 ligase 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 372	372	Tribbles homolog 1		PRO_0000131860
Regions
	Domain	1 – 338	338	Protein kinase
Natural variations
	Alternative sequence	219 – 372	154	Missing in isoform 2.		VSP_051888
Experimental info
	Sequence conflict	224	1	E → G in AAM45478. Ref.1
	Sequence conflict	278	1	L → W in AAM45478. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 6, 2005. Version 2. Checksum: AD29BB4E640B4B62	FASTA	372	41,281
	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
	Isoform 2 [UniParc]. Checksum: F3A5AFE16E3450A8	FASTA	218	23,907
	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 EAARLFKQIV SAVAHCHQSA IVLGDLKLRK FVFSTEER

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00227737. IPI00469450.
RefSeq	NP_653132.1. NM_144549.4.
UniGene	Mm.40298.
3D structure databases
ProteinModelPortal	Q8K4K4.
SMR	Q8K4K4. Positions 110-370.
ModBase	Search...
PTM databases
PhosphoSite	Q8K4K4.
Proteomic databases
PRIDE	Q8K4K4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000067543; ENSMUSP00000068834; ENSMUSG00000032501. ENSMUST00000118228; ENSMUSP00000112828; ENSMUSG00000032501.
GeneID	211770.
KEGG	mmu:211770.
UCSC	uc007vxw.1. mouse.
Organism-specific databases
CTD	10221.
MGI	MGI:2443397. Trib1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00700000104008.
HOGENOM	HOG000231872.
HOVERGEN	HBG067729.
InParanoid	Q8K4K4.
KO	K08814.
OMA	AHCHQSA.
OrthoDB	EOG40P476.
Gene expression databases
Bgee	Q8K4K4.
CleanEx	MM_TRIB1.
Genevestigator	Q8K4K4.
GermOnline	ENSMUSG00000032501. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR024104. Tribbles/Ser_Thr_kinase_40. IPR024105. Tribbles_TRB1. [Graphical view]
PANTHER	PTHR22961. PTHR22961. 1 hit. PTHR22961:SF5. PTHR22961:SF5. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS50011. PROTEIN_KINASE_DOM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	373352.
SOURCE	Search...

Entry information

Entry name

TRIB1_MOUSE

Accession

Primary (citable) accession number: Q8K4K4
Secondary accession number(s): Q8BFS7 , Q8BJR9, Q8BZX3, Q91W04

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	May 29, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program