Descriptions

TRIB1 controls the levels of C/EBPs involved in the differentiation of myeloid cells and adipocytes by recruiting the proteins to COP1 ubiquitin ligase. TRIB1 recognizes a conserved stretch within a transactivation domain of C/EBP proteins, and suggests a model by which TRIB1 acts as a dynamic adapter for recruiting C/EBPs to COP1. TRIB1 contains a pseudokinase domain and this pseudokinase interacts with the COP1-binding motif and prevents the recruitment of COP1 ubiquitin ligase.

Autoinhibitory domains (AIDs)

Target domain

326-331 (COP1-binding motif)

Relief mechanism

PTM

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q28283

Entry ID Method Resolution Chain Position Source
AF-Q28283-F1 Predicted AlphaFoldDB

2 variants for Q28283

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3339485468 117 T>A No EVA
rs3340982793 120 I>L No EVA

No associated diseases with Q28283

1 regional properties for Q28283

Type Name Position InterPro Accession
domain Protein kinase domain 61 - 308 IPR000719

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cytoplasm, cytoskeleton
  • May associate with the cytoskeleton
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

2 GO annotations of molecular function

Name Definition
mitogen-activated protein kinase kinase binding Binding to a mitogen-activated protein kinase kinase, a protein that can phosphorylate a MAP kinase.
protein kinase inhibitor activity Binds to and stops, prevents or reduces the activity of a protein kinase.

2 GO annotations of biological process

Name Definition
positive regulation of proteasomal ubiquitin-dependent protein catabolic process Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
regulation of MAP kinase activity Any process that modulates the frequency, rate or extent of MAP kinase activity.

10 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5GLH2 TRIB2 Tribbles homolog 2 Bos taurus (Bovine) SS
Q0VCE3 TRIB3 Tribbles homolog 3 Bos taurus (Bovine) SS
Q92519 TRIB2 Tribbles homolog 2 Homo sapiens (Human) SS
Q96RU7 TRIB3 Tribbles homolog 3 Homo sapiens (Human) PR
Q96RU8 TRIB1 Tribbles homolog 1 Homo sapiens (Human) EV
Q8K4K3 Trib2 Tribbles homolog 2 Mus musculus (Mouse) SS
Q8K4K4 Trib1 Tribbles homolog 1 Mus musculus (Mouse) SS
Q8K4K2 Trib3 Tribbles homolog 3 Mus musculus (Mouse) SS
Q9WTQ6 Trib3 Tribbles homolog 3 Rattus norvegicus (Rat) SS
G5EED4 nipi-3 Protein nipi-3 Caenorhabditis elegans PR
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 DFSVSNSGYG AKEVSDQLVP DVNMEENLDP FFN