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CSN6_PIG
ID   CSN6_PIG                Reviewed;         323 AA.
AC   A7TX81;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=COP9 signalosome complex subunit 6;
DE            Short=SGN6;
DE            Short=Signalosome subunit 6;
GN   Name=COPS6;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=17976214; DOI=10.1111/j.1365-2052.2007.01665.x;
RA   Wu X., Li K., Yerle M., Pan Y.C.;
RT   "Chromosomal assignments of the porcine COPS2, COPS4, COPS5, COPS6, USP6
RT   and USP10 genes involved in the ubiquitin-proteasome system.";
RL   Anim. Genet. 38:665-666(2007).
CC   -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a complex
CC       involved in various cellular and developmental processes (By
CC       similarity). The CSN complex is an essential regulator of the ubiquitin
CC       (Ubl) 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 (By
CC       similarity). The complex is also involved in phosphorylation of
CC       p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via
CC       its association with CK2 and PKD kinases (By similarity). CSN-dependent
CC       phosphorylation of TP53 and JUN promotes and protects degradation by
CC       the Ubl system, respectively (By similarity). Has some glucocorticoid
CC       receptor-responsive activity (By similarity). Stabilizes COP1 through
CC       reducing COP1 auto-ubiquitination and decelerating COP1 turnover rate,
CC       hence regulates the ubiquitination of COP1 targets, including SFN (By
CC       similarity). {ECO:0000250|UniProtKB:Q7L5N1}.
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       (By similarity). In the complex, it probably interacts directly with
CC       COPS2, COPS4, COPS5, COPS7 (COPS7A or COPS7B) and COPS9 (By
CC       similarity). Interacts with the translation initiation factor EIF3S6
CC       (By similarity). Interacts weakly with RBX1 (By similarity). Directly
CC       interacts with COP1 and 14-3-3 protein sigma/SFN (By similarity).
CC       Interacts with ERCC6 (By similarity). {ECO:0000250|UniProtKB:Q7L5N1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L5N1}. Nucleus
CC       {ECO:0000250|UniProtKB:Q7L5N1}.
CC   -!- SIMILARITY: Belongs to the peptidase M67A family. CSN6 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Although related to the peptidase M67A family, it lacks the
CC       JAMM motif that probably constitutes the catalytic center and therefore
CC       it probably does not have a protease activity. {ECO:0000305}.
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DR   EMBL; EF468513; ABR13017.1; -; mRNA.
DR   RefSeq; NP_001098769.1; NM_001105299.1.
DR   AlphaFoldDB; A7TX81; -.
DR   SMR; A7TX81; -.
DR   IntAct; A7TX81; 1.
DR   PeptideAtlas; A7TX81; -.
DR   PRIDE; A7TX81; -.
DR   Ensembl; ENSSSCT00000067140; ENSSSCP00000071445; ENSSSCG00000034893.
DR   Ensembl; ENSSSCT00005003209; ENSSSCP00005001853; ENSSSCG00005002152.
DR   Ensembl; ENSSSCT00015076247; ENSSSCP00015030623; ENSSSCG00015056935.
DR   Ensembl; ENSSSCT00025014430; ENSSSCP00025005580; ENSSSCG00025010993.
DR   Ensembl; ENSSSCT00030004911; ENSSSCP00030001950; ENSSSCG00030003769.
DR   Ensembl; ENSSSCT00035047917; ENSSSCP00035019165; ENSSSCG00035036150.
DR   Ensembl; ENSSSCT00040047888; ENSSSCP00040020018; ENSSSCG00040035470.
DR   Ensembl; ENSSSCT00045029379; ENSSSCP00045020356; ENSSSCG00045017261.
DR   Ensembl; ENSSSCT00050046096; ENSSSCP00050018974; ENSSSCG00050034350.
DR   Ensembl; ENSSSCT00055055755; ENSSSCP00055044504; ENSSSCG00055028153.
DR   Ensembl; ENSSSCT00055055899; ENSSSCP00055044630; ENSSSCG00055028153.
DR   Ensembl; ENSSSCT00060060661; ENSSSCP00060025986; ENSSSCG00060044722.
DR   Ensembl; ENSSSCT00065067566; ENSSSCP00065029387; ENSSSCG00065049347.
DR   Ensembl; ENSSSCT00065067595; ENSSSCP00065029405; ENSSSCG00065049347.
DR   Ensembl; ENSSSCT00070030098; ENSSSCP00070025101; ENSSSCG00070015310.
DR   GeneID; 100125954; -.
DR   KEGG; ssc:100125954; -.
DR   CTD; 10980; -.
DR   VGNC; VGNC:102553; COPS6.
DR   GeneTree; ENSGT00950000183073; -.
DR   InParanoid; A7TX81; -.
DR   OrthoDB; 1455324at2759; -.
DR   Proteomes; UP000008227; Chromosome 3.
DR   Proteomes; UP000314985; Chromosome 3.
DR   Bgee; ENSSSCG00000034893; Expressed in forelimb bud and 41 other tissues.
DR   ExpressionAtlas; A7TX81; baseline and differential.
DR   GO; GO:0008180; C:COP9 signalosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0000338; P:protein deneddylation; IEA:InterPro.
DR   CDD; cd08063; MPN_CSN6; 1.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR033859; MPN_CSN6.
DR   InterPro; IPR024969; Rpn11/EIF3F_C.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF13012; MitMem_reg; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Reference proteome; Signalosome.
FT   CHAIN           1..323
FT                   /note="COP9 signalosome complex subunit 6"
FT                   /id="PRO_0000331508"
FT   DOMAIN          37..170
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   323 AA;  35865 MW;  416487A3249A8F26 CRC64;
     MAAAAAANGT GGSSGMEVDA AVVPSVMASG VTGSVSVALH PLVILNISDH WIRMRSQEGR
     PMQVIGALIG KQEGRNIEVM NSFELLSHTV EEKIIIDKEY YYTKEEQFKQ VFKELEFLGW
     YTTGGPPDPS DIHVHKQVCE IIESPLFLKL NPMTKHTDLP VSVFESVIDI INGEATMLFA
     ELTYTLATEE AERIGVDHVA RMTATGSGEN STVAEHLIAQ HSAIKMLHSR VKLILEYVKA
     SEAGEVPFNH EILREAYALC HCLPVLSTDK FKTDFYDQCN DVGLMAYLGT ITKTCNTMNQ
     FVNKFNVLYD RQGIGRRMRG LFF
 
 
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