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CSN5B_BRAOL
ID   CSN5B_BRAOL             Reviewed;          78 AA.
AC   P68355;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=COP9 signalosome complex subunit 5b;
DE            Short=Signalosome subunit 5b;
DE            EC=3.4.-.-;
DE   AltName: Full=Jun activation domain-binding homolog 1;
DE   Flags: Fragments;
GN   Name=CSN5B; Synonyms=AJH1;
OS   Brassica oleracea (Wild cabbage).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3712;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-22 AND 52-65, AND COMPOSITION OF THE CSN COMPLEX.
RX   PubMed=9849901; DOI=10.1016/s0014-5793(98)01367-2;
RA   Karniol B., Yahalom A., Kwok S., Tsuge T., Matsui M., Deng X.-W.,
RA   Chamovitz D.A.;
RT   "The Arabidopsis homologue of an eIF3 complex subunit associates with the
RT   COP9 complex.";
RL   FEBS Lett. 439:173-179(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 23-51 AND 66-78, AND COMPONENT OF THE CSN COMPLEX WITH
RP   CSN1; CSN2; CSN3; CSN4; CSN6; CSN7 AND CSN8.
RX   PubMed=10521526; DOI=10.2307/3871091;
RA   Serino G., Tsuge T., Kwok S., Matsui M., Wei N., Deng X.-W.;
RT   "Arabidopsis cop8 and fus4 mutations define the same gene that encodes
RT   subunit 4 of the COP9 signalosome.";
RL   Plant Cell 11:1967-1980(1999).
CC   -!- FUNCTION: Probable protease subunit of the COP9 signalosome complex
CC       (CSN), a complex involved in various cellular and developmental
CC       processes such as photomorphogenesis and auxin and jasmonate responses.
CC       The CSN complex is an essential regulator of the ubiquitin (Ubl)
CC       conjugation pathway by mediating the deneddylation of the cullin
CC       subunits of the SCF-type E3 ligase complexes, leading to decrease the
CC       Ubl ligase activity of SCF. In the complex, it probably acts as the
CC       catalytic center that mediates the cleavage of Nedd8 from cullins. It
CC       however has no metalloprotease activity by itself and requires the
CC       other subunits of the CSN complex. The CSN complex is involved in
CC       repression of photomorphogenesis in darkness by regulating the activity
CC       of COP1-containing Ubl ligase complexes (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Component of the CSN complex, probably composed of CSN1, CSN2,
CC       CSN3, CSN4, CSN5 (CSN5A or CSN5B), CSN6 (CSN6A or CSN6B), CSN7 and
CC       CSN8.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P68355; -.
DR   SMR; P68355; -.
DR   GO; GO:0008180; C:COP9 signalosome; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR   InterPro; IPR037740; CSN5.
DR   PANTHER; PTHR10410:SF33; PTHR10410:SF33; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Metalloprotease; Nucleus; Phytochrome signaling pathway;
KW   Protease; Signalosome.
FT   CHAIN           <1..>78
FT                   /note="COP9 signalosome complex subunit 5b"
FT                   /id="PRO_0000194845"
FT   NON_CONS        22..23
FT                   /evidence="ECO:0000305"
FT   NON_CONS        39..40
FT                   /evidence="ECO:0000305"
FT   NON_CONS        65..66
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         78
SQ   SEQUENCE   78 AA;  9100 MW;  BDD9EC08FC437666 CRC64;
     VEQPDSSSSD GIFYYDEASQ TKKISDDHVS EYQTIPLNKK QYYSLDITYF KSSLDSHLLD
     LLWNKKDILF NSARQSDK
 
 
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