CSN2_RAT
ID CSN2_RAT Reviewed; 443 AA.
AC P61203; Q6P731;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=COP9 signalosome complex subunit 2;
DE Short=SGN2;
DE Short=Signalosome subunit 2;
DE AltName: Full=Alien homolog;
DE AltName: Full=JAB1-containing signalosome subunit 2;
DE AltName: Full=Thyroid receptor-interacting protein 15;
DE Short=TR-interacting protein 15;
DE Short=TRIP-15;
GN Name=Cops2; Synonyms=Csn2, Trip15;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12524175; DOI=10.1016/s0165-3806(02)00574-6;
RA Akiyama H., Sugiyama A., Uzawa K., Fujisawa N., Tashiro Y., Tahiro F.;
RT "Implication of Trip15/CSN2 in early stage of neuronal differentiation of
RT P19 embryonal carcinoma cells.";
RL Brain Res. Dev. Brain Res. 140:45-56(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12606288; DOI=10.1016/s0012-1606(02)00023-4;
RA Tenbaum S.P., Juenemann S., Schlitt T., Bernal J., Renkawitz R., Munoz A.,
RA Baniahmad A.;
RT "Alien/CSN2 gene expression is regulated by thyroid hormone in rat brain.";
RL Dev. Biol. 254:149-160(2003).
RN [4]
RP INTERACTION WITH NIF3L1, AND REGION.
RX PubMed=12522100; DOI=10.1074/jbc.m209856200;
RA Akiyama H., Fujisawa N., Tashiro Y., Takanabe N., Sugiyama A., Tashiro F.;
RT "The role of transcriptional corepressor Nif3l1 in early stage of neural
RT differentiation via cooperation with Trip15/CSN2.";
RL J. Biol. Chem. 278:10752-10762(2003).
CC -!- FUNCTION: Essential component of the COP9 signalosome complex (CSN), a
CC complex involved in various cellular and developmental processes. The
CC CSN complex is an essential regulator of the ubiquitin (Ubl)
CC conjugation pathway by mediating the deneddylation of the cullin
CC subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl
CC ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The
CC complex is also involved in phosphorylation of p53/TP53, c-jun/JUN,
CC IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association
CC with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN
CC promotes and protects degradation by the Ubl system, respectively.
CC Involved in early stage of neuronal differentiation via its interaction
CC with NIF3L1. {ECO:0000250|UniProtKB:P61202,
CC ECO:0000269|PubMed:12524175}.
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2,
CC COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9.
CC In the complex, it probably interacts directly with COPS1, COPS4,
CC COPS5, COPS6 and COPS7 (COPS7A or COPS7B). Specifically interacts with
CC the ligand binding domain of the thyroid receptor (TR). Does not
CC require the presence of thyroid hormone for its interaction. Interacts
CC with CUL1 and CUL2. Interacts with IRF8/ICSBP1 and with nuclear
CC receptors NR2F1 and NR0B1 (By similarity). Interacts with NIF3L1
CC (PubMed:12522100). {ECO:0000250|UniProtKB:P61201,
CC ECO:0000250|UniProtKB:P61202, ECO:0000269|PubMed:12522100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12606288}. Nucleus
CC {ECO:0000269|PubMed:12524175, ECO:0000269|PubMed:12606288}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61203-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61203-2; Sequence=VSP_011886, VSP_011887;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12606288}.
CC -!- INDUCTION: Regulated by thyroid hormone and TR.
CC {ECO:0000269|PubMed:12606288}.
CC -!- PTM: Phosphorylated by CK2 and PKD kinases. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CSN2 family. {ECO:0000305}.
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DR EMBL; AB081072; BAC15575.1; -; mRNA.
DR EMBL; BC061864; AAH61864.1; -; mRNA.
DR RefSeq; NP_695209.1; NM_153297.1. [P61203-1]
DR RefSeq; XP_008760368.1; XM_008762146.2. [P61203-2]
DR AlphaFoldDB; P61203; -.
DR SMR; P61203; -.
DR BioGRID; 251749; 1.
DR STRING; 10116.ENSRNOP00000012287; -.
DR iPTMnet; P61203; -.
DR PhosphoSitePlus; P61203; -.
DR jPOST; P61203; -.
DR PaxDb; P61203; -.
DR PeptideAtlas; P61203; -.
DR PRIDE; P61203; -.
DR Ensembl; ENSRNOT00000084154; ENSRNOP00000075473; ENSRNOG00000008744. [P61203-1]
DR GeneID; 261736; -.
DR KEGG; rno:261736; -.
DR UCSC; RGD:628791; rat. [P61203-1]
DR CTD; 9318; -.
DR RGD; 628791; Cops2.
DR eggNOG; KOG1464; Eukaryota.
DR GeneTree; ENSGT00530000063301; -.
DR InParanoid; P61203; -.
DR OMA; RNYQEAG; -.
DR OrthoDB; 1108845at2759; -.
DR PhylomeDB; P61203; -.
DR Reactome; R-RNO-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-RNO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-9013422; RHOBTB1 GTPase cycle.
DR PRO; PR:P61203; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000008744; Expressed in quadriceps femoris and 20 other tissues.
DR Genevisible; P61203; RN.
DR GO; GO:0008180; C:COP9 signalosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0001833; P:inner cell mass cell proliferation; ISO:RGD.
DR GO; GO:1903507; P:negative regulation of nucleic acid-templated transcription; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; IDA:RGD.
DR GO; GO:0000338; P:protein deneddylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD.
DR GO; GO:0001834; P:trophectodermal cell proliferation; IEA:Ensembl.
DR InterPro; IPR037750; COPS2.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10678:SF3; PTHR10678:SF3; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Signalosome.
FT CHAIN 1..443
FT /note="COP9 signalosome complex subunit 2"
FT /id="PRO_0000120970"
FT DOMAIN 254..416
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..275
FT /note="Mediates interaction with NIF3L1"
FT /evidence="ECO:0000269|PubMed:12522100"
FT VAR_SEQ 124
FT /note="Q -> QNSDFLCQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011886"
FT VAR_SEQ 191..238
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011887"
SQ SEQUENCE 443 AA; 51597 MW; 1DB6FA774C13BC59 CRC64;
MSDMEDDFMC DDEEDYDLEY SEDSNSEPNV DLENQYYNSK ALKEDDPKAA LSSFQKVLEL
EGEKGEWGFK ALKQMIKINF KLTNFPEMMN RYKQLLTYIR SAVTRNYSEK SINSILDYIS
TSKQMDLLQE FYETTLEALK DAKNDRLWFK TNTKLGKLYL EREEYGKLQK ILRQLHQSCQ
TDDGEDDLKK GTQLLEIYAL EIQMYTAQKN NKKLKALYEQ SLHIKSAIPH PLIMGVIREC
GGKMHLREGE FEKAHTDFFE AFKNYDESGS PRRTTCLKYL VLANMLMKSG INPFDSQEAK
PYKNDPEILA MTNLVSAYQN NDITEFEKIL KTNHSNIMDD PFIREHIEEL LRNIRTQVLI
KLIKPYTRIH IPFISKELNI DVADVESLLV QCILDNTIHG RIDQVNQLLE LDHQKRGGAR
YTALDKWTNQ LNSLNQAVVS KLA
