ID   TRIB2_PONAB             Reviewed;         343 AA.
AC   Q5R669; Q5R487;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Tribbles homolog 2;
DE            Short=TRB-2;
GN   Name=TRIB2 {ECO:0000250|UniProtKB:Q96RU7};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAH93429.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain cortex {ECO:0000312|EMBL:CAH93429.1};
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Interacts with MAPK kinases and regulates activation of MAP
CC       kinases. Does not display kinase activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q28283, ECO:0000250|UniProtKB:Q96RU8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}. Note=May associate with the cytoskeleton. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000305};
CC         IsoId=Q5R669-1; Sequence=Displayed;
CC       Name=2 {ECO:0000305};
CC         IsoId=Q5R669-2; Sequence=VSP_051889, VSP_051890;
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. Tribbles subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR860627; CAH92747.1; -; mRNA.
DR   EMBL; CR861369; CAH93429.1; -; mRNA.
DR   RefSeq; NP_001126602.1; NM_001133130.1. [Q5R669-1]
DR   AlphaFoldDB; Q5R669; -.
DR   SMR; Q5R669; -.
DR   STRING; 9601.ENSPPYP00000014112; -.
DR   Ensembl; ENSPPYT00000046447; ENSPPYP00000032873; ENSPPYG00000038287. [Q5R669-1]
DR   GeneID; 100173599; -.
DR   KEGG; pon:100173599; -.
DR   CTD; 28951; -.
DR   eggNOG; KOG0583; Eukaryota.
DR   GeneTree; ENSGT00950000182986; -.
DR   HOGENOM; CLU_000288_13_1_1; -.
DR   InParanoid; Q5R669; -.
DR   OMA; GHFNVPE; -.
DR   TreeFam; TF329785; -.
DR   Proteomes; UP000001595; Chromosome 2A.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0055106; F:ubiquitin-protein transferase regulator activity; IEA:Ensembl.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0032693; P:negative regulation of interleukin-10 production; IEA:Ensembl.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0043405; P:regulation of MAP kinase activity; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR024104; Tribbles/Ser_Thr_kinase_40.
DR   PANTHER; PTHR22961; PTHR22961; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Protein kinase inhibitor;
KW   Reference proteome.
FT   CHAIN           1..343
FT                   /note="Tribbles homolog 2"
FT                   /id="PRO_0000131865"
FT   DOMAIN          61..308
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          25..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..136
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_051889"
FT   VAR_SEQ         343
FT                   /note="N -> NRAHAPRRLSRYQE (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_051890"
SQ   SEQUENCE   343 AA;  38787 MW;  BF8D1300DACB84FA CRC64;
     MNIHRSTPIT IARYGRSRNK TQDFEELSSI RSAEPSQSFS PNLGSPSPPE TPNLSHCVSC
     IGKYLLLEPL EGDHVFRAVH LHSGEELVCK VFDISCYQES LAPCFCLSAH SNINQITEII
     LGETKAYVFF ERSYGDMHSF VRTCKKLREE EAARLFYQIA SAVAHCHDGG LVLRDLKLRK
     FIFKDEERTR VKLESLEDAY ILRGDDDSLS DKHGCPAYVS PEILNTSGSY SGKAADVWSL
     GVMLYTMLVG RYPFHDIEPS SLFSKIRRGQ FNIPETLSPK AKCLIRSILR REPSERLTSQ
     EILDHPWFST DFSVSNSGYG AKEVSDQLVP DVNMEENLDP FFN