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UBE2F_RAT
ID   UBE2F_RAT               Reviewed;         185 AA.
AC   Q5U203;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=NEDD8-conjugating enzyme UBE2F;
DE            EC=2.3.2.32 {ECO:0000250|UniProtKB:Q969M7};
DE   AltName: Full=NEDD8 carrier protein UBE2F;
DE   AltName: Full=NEDD8 protein ligase UBE2F;
DE   AltName: Full=RING-type E3 NEDD8 transferase UBE2F;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2 F;
GN   Name=Ube2f;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Ovary;
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).
CC   -!- FUNCTION: Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1
CC       E1 complex and catalyzes its covalent attachment to other proteins. The
CC       specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1,
CC       suggests that the RBX2-UBE2F complex neddylates specific target
CC       proteins, such as CUL5. {ECO:0000250|UniProtKB:Q969M7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine
CC         + [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine +
CC         N(6)-[NEDD8-protein]-yl-[cullin]-L-lysine.; EC=2.3.2.32;
CC         Evidence={ECO:0000250|UniProtKB:Q969M7};
CC   -!- PATHWAY: Protein modification; protein neddylation.
CC   -!- SUBUNIT: Interacts with UBA3 and RBX2. Interacts (N-terminally
CC       acetylated form) with (via DCUN1 domain) DCUN1D1, DCUN1D2, DCUN1D3,
CC       DCUN1D4 and DCUN1D5 (By similarity). {ECO:0000250|UniProtKB:Q969M7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5U203-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5U203-2; Sequence=VSP_037303;
CC   -!- PTM: The acetylation of Met-1 increases affinity for DCUN1D3 by about 2
CC       orders of magnitude and is crucial for NEDD8 transfer to cullins.
CC       {ECO:0000250|UniProtKB:Q969M7}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UBE2F
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; DY311915; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC086355; AAH86355.1; -; mRNA.
DR   RefSeq; NP_001008382.1; NM_001008381.1. [Q5U203-2]
DR   RefSeq; XP_006245484.1; XM_006245422.3. [Q5U203-1]
DR   RefSeq; XP_006245485.1; XM_006245423.3. [Q5U203-1]
DR   RefSeq; XP_006245487.1; XM_006245425.3. [Q5U203-1]
DR   RefSeq; XP_006245489.1; XM_006245427.3. [Q5U203-1]
DR   RefSeq; XP_017452028.1; XM_017596539.1. [Q5U203-1]
DR   AlphaFoldDB; Q5U203; -.
DR   SMR; Q5U203; -.
DR   STRING; 10116.ENSRNOP00000027050; -.
DR   iPTMnet; Q5U203; -.
DR   PhosphoSitePlus; Q5U203; -.
DR   SwissPalm; Q5U203; -.
DR   PaxDb; Q5U203; -.
DR   Ensembl; ENSRNOT00000027050; ENSRNOP00000027050; ENSRNOG00000019953. [Q5U203-1]
DR   Ensembl; ENSRNOT00000042082; ENSRNOP00000040354; ENSRNOG00000019953. [Q5U203-2]
DR   GeneID; 363284; -.
DR   KEGG; rno:363284; -.
DR   UCSC; RGD:1307608; rat. [Q5U203-1]
DR   CTD; 140739; -.
DR   RGD; 1307608; Ube2f.
DR   eggNOG; KOG0420; Eukaryota.
DR   GeneTree; ENSGT00940000154349; -.
DR   HOGENOM; CLU_030988_6_4_1; -.
DR   InParanoid; Q5U203; -.
DR   OMA; YNMAPPK; -.
DR   OrthoDB; 1302735at2759; -.
DR   PhylomeDB; Q5U203; -.
DR   TreeFam; TF101125; -.
DR   Reactome; R-RNO-8951664; Neddylation.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00885; -.
DR   PRO; PR:Q5U203; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000019953; Expressed in duodenum and 20 other tissues.
DR   Genevisible; Q5U203; RN.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061654; F:NEDD8 conjugating enzyme activity; ISS:UniProtKB.
DR   GO; GO:0019788; F:NEDD8 transferase activity; ISO:RGD.
DR   GO; GO:0045116; P:protein neddylation; ISS:UniProtKB.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; ATP-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..185
FT                   /note="NEDD8-conjugating enzyme UBE2F"
FT                   /id="PRO_0000374072"
FT   DOMAIN          32..185
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        116
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q969M7"
FT   VAR_SEQ         50..72
FT                   /note="CTCKVHFPDPNKLHCFQLTVSPD -> Y (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_037303"
FT   CONFLICT        181
FT                   /note="K -> Q (in Ref. 1; DY311915)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   185 AA;  21080 MW;  6F1DF65197DBF7A1 CRC64;
     MLTLASKLKR DDGLKGSRAS ASTSDSTRRV SVRDKLLVKE VAELEANLPC TCKVHFPDPN
     KLHCFQLTVS PDEGYYQGGK FQFETEVPDA YNMVPPKVKC LTKIWHPNIT ETGEICLSLL
     REHSIDGTGW APTRTLKDVV WGLNSLFTDL LNFDDPLNIE AAEHHLRDKE DFRDKVDEYI
     KRYAR
 
 
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