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RFWD3_AILME
ID   RFWD3_AILME             Reviewed;         773 AA.
AC   D2HWM5;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=E3 ubiquitin-protein ligase RFWD3;
DE            EC=2.3.2.27;
DE   AltName: Full=RING finger and WD repeat domain-containing protein 3;
DE   AltName: Full=RING finger protein 201;
GN   Name=RFWD3; Synonyms=RNF201; ORFNames=PANDA_016934;
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase required for the repair of DNA
CC       interstrand cross-links (ICL) in response to DNA damage. Plays a key
CC       role in RPA-mediated DNA damage signaling and repair. Acts by mediating
CC       ubiquitination of the RPA complex (RPA1, RPA2 and RPA3 subunits) and
CC       RAD51 at stalled replication forks, leading to remove them from DNA
CC       damage sites and promote homologous recombination. Also mediates the
CC       ubiquitination of p53/TP53 in the late response to DNA damage, and acts
CC       as a positive regulator of p53/TP53 stability, thereby regulating the
CC       G1/S DNA damage checkpoint. May act by catalyzing the formation of
CC       short polyubiquitin chains on p53/TP53 that are not targeted to the
CC       proteasome. In response to ionizing radiation, interacts with MDM2 and
CC       enhances p53/TP53 ubiquitination, possibly by restricting MDM2 from
CC       extending polyubiquitin chains on ubiquitinated p53/TP53.
CC       {ECO:0000250|UniProtKB:Q6PCD5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q6PCD5};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q6PCD5}.
CC   -!- SUBUNIT: Interacts with MDM2 and p53/TP53. Binds to the RPA complex via
CC       direct interaction with RPA2. Interacts with RAD51.
CC       {ECO:0000250|UniProtKB:Q6PCD5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6PCD5}. Nucleus,
CC       PML body {ECO:0000250|UniProtKB:Q6PCD5}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q6PCD5}. Note=In undamaged cells, found both in
CC       the cytoplasm and in the nucleus, partially associated with PML nuclear
CC       bodies. In response to replication block, such as that caused by
CC       hydroxyurea treatment, or to DNA damage caused by ionizing radiations
CC       or doxorubicin, recruited to the nucleus, to stalled replication forks
CC       or to sites of DNA repair. This recruitment depends upon RPA2.
CC       {ECO:0000250|UniProtKB:Q6PCD5}.
CC   -!- DOMAIN: The coiled coil domain may be involved in RPA2-binding.
CC       {ECO:0000250|UniProtKB:Q6PCD5}.
CC   -!- PTM: Phosphorylated at Ser-46 and Ser-63 upon DNA damage by ATM or ATR.
CC       ATM phosphorylation occurs at early times upon DNA damage, while ATR is
CC       the major kinase at later times. Phosphorylation by ATM and ATR is
CC       required to stabilize p53/TP53. Part of the phosphorylation depends
CC       upon RPA2 presence. {ECO:0000250|UniProtKB:Q6PCD5}.
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DR   EMBL; GL193557; EFB22419.1; -; Genomic_DNA.
DR   RefSeq; XP_011232989.1; XM_011234687.2.
DR   AlphaFoldDB; D2HWM5; -.
DR   SMR; D2HWM5; -.
DR   STRING; 9646.ENSAMEP00000001391; -.
DR   Ensembl; ENSAMET00000001443; ENSAMEP00000001391; ENSAMEG00000001323.
DR   GeneID; 100478259; -.
DR   KEGG; aml:100478259; -.
DR   CTD; 55159; -.
DR   eggNOG; KOG1645; Eukaryota.
DR   HOGENOM; CLU_021009_1_0_1; -.
DR   InParanoid; D2HWM5; -.
DR   OrthoDB; 1451258at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008912; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR   GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
DR   GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:2000001; P:regulation of DNA damage checkpoint; IEA:Ensembl.
DR   GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR   GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR037381; RFWD3.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR16047; PTHR16047; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; DNA damage; DNA repair; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transferase;
KW   Ubl conjugation pathway; WD repeat; Zinc; Zinc-finger.
FT   CHAIN           1..773
FT                   /note="E3 ubiquitin-protein ligase RFWD3"
FT                   /id="PRO_0000394253"
FT   REPEAT          494..536
FT                   /note="WD 1"
FT   REPEAT          538..576
FT                   /note="WD 2"
FT   REPEAT          582..627
FT                   /note="WD 3"
FT   ZN_FING         287..331
FT                   /note="RING-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          18..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          361..403
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        92..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         47
FT                   /note="Phosphoserine; by ATM and ATR"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PCD5"
FT   MOD_RES         64
FT                   /note="Phosphoserine; by ATM and ATR"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PCD5"
SQ   SEQUENCE   773 AA;  84945 MW;  1336647E0E02ABE5 CRC64;
     MAQEAMEYNV DEQLEHRVAE QPVPAEVVST QGGPPPLQPL PTEVVSSQGA PPLLQPAPAE
     GTSSQVGPHL LQPAAQLSVD LTEEVELLGE DRVENINPGA SEEHRQPSRV NRPIPVSSLD
     SMNSFISGLQ RLHGMLEFLR PPSDHNVGPV RSRRRRGSAS RRSRTVGSQR TDSARSRAPL
     DAYFQVSRTQ PHLPSMSQDS ETRNPVSEDL QVSSSSSSDS ESSAEYEEVV VQAEDTRAVV
     SEEQGGTAAE QEVTCVGGGE TLPKQSPQKT NPLLPSVSKD DEEGDTCTIC FEHWTNAGDH
     RLSALRCGHL FGYKCISKWL KGQARKCPQC NKKAKHSDIV VLYARTLRAL DTSEHERMKS
     SLLKEQMLRK QAELESAQCR LQLQVLTDEC SKLHSRVQDL QKLTVQHRDQ ISQSPSGSQA
     RSLNCLPSSQ NQRKYHFQKT FTVSPTGNCR IMTYCDALSC LVVSQPSPQA SFLPGFGVKM
     LSTANMKSSQ YVPMHGKQIR GLAFSSRSKG LLLSASLDST VKLTSLETNT VVQTYNAGRP
     VWSCCWCLDE SNHIYAGLVN GSILVYDLRN TSSHIQELVP QKARCPLVSL SYIPRAASAA
     FPYGGVLAGT LENASFWELK MGFSHWPHVL PMEPGGCVDF QTESSTRHCL VTYRPDKNHN
     TLRSVLMEMS YKLNDAGEPV CSCRPVQTFL GGPTCKLLTK SAIFQNPEND GSILVCTGDE
     ASNSALLWDA GSGSLLQELQ ADQPVLDICP FEANHSSCLA TLTEKMVHIY RWE
 
 
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