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WDR12_BOVIN
ID   WDR12_BOVIN             Reviewed;         423 AA.
AC   Q0VC24; A5PJI2;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Ribosome biogenesis protein WDR12 {ECO:0000255|HAMAP-Rule:MF_03029};
DE   AltName: Full=WD repeat-containing protein 12 {ECO:0000255|HAMAP-Rule:MF_03029};
GN   Name=WDR12 {ECO:0000255|HAMAP-Rule:MF_03029};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon, and Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the PeBoW complex, which is required for
CC       maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S
CC       ribosome. {ECO:0000255|HAMAP-Rule:MF_03029}.
CC   -!- SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and
CC       WDR12. The complex is held together by BOP1, which interacts with PES1
CC       via its N-terminal domain and with WDR12 via a high-affinity
CC       interaction between the seven-bladed beta-propeller domains of the 2
CC       proteins. The PeBoW complex associates with the 66S pre-ribosome.
CC       Interacts (via UBL domain) with MDN1 (via VWFA/MIDAS domain).
CC       {ECO:0000255|HAMAP-Rule:MF_03029}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC       Rule:MF_03029}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03029}.
CC   -!- SIMILARITY: Belongs to the WD repeat WDR12/YTM1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03029}.
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DR   EMBL; BT029892; ABM06142.1; -; mRNA.
DR   EMBL; BC120386; AAI20387.1; -; mRNA.
DR   EMBL; BC142121; AAI42122.1; -; mRNA.
DR   RefSeq; NP_001069375.1; NM_001075907.1.
DR   AlphaFoldDB; Q0VC24; -.
DR   SMR; Q0VC24; -.
DR   STRING; 9913.ENSBTAP00000020499; -.
DR   PaxDb; Q0VC24; -.
DR   PRIDE; Q0VC24; -.
DR   Ensembl; ENSBTAT00000020499; ENSBTAP00000020499; ENSBTAG00000015424.
DR   GeneID; 528209; -.
DR   KEGG; bta:528209; -.
DR   CTD; 55759; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015424; -.
DR   VGNC; VGNC:36882; WDR12.
DR   eggNOG; KOG0313; Eukaryota.
DR   GeneTree; ENSGT00930000150950; -.
DR   HOGENOM; CLU_000288_57_0_1; -.
DR   InParanoid; Q0VC24; -.
DR   OMA; VDCTRTK; -.
DR   OrthoDB; 1540178at2759; -.
DR   TreeFam; TF313023; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000015424; Expressed in conceptus and 108 other tissues.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0070545; C:PeBoW complex; ISS:UniProtKB.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; ISS:UniProtKB.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 1.
DR   HAMAP; MF_03029; WDR12; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR012972; NLE.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR028599; WDR12/Ytm1.
DR   Pfam; PF08154; NLE; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Ribosome biogenesis; rRNA processing; Ubl conjugation; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZL7"
FT   CHAIN           2..423
FT                   /note="Ribosome biogenesis protein WDR12"
FT                   /id="PRO_0000283706"
FT   REPEAT          99..137
FT                   /note="WD 1"
FT   REPEAT          138..180
FT                   /note="WD 2"
FT   REPEAT          187..226
FT                   /note="WD 3"
FT   REPEAT          255..293
FT                   /note="WD 4"
FT   REPEAT          295..334
FT                   /note="WD 5"
FT   REPEAT          340..380
FT                   /note="WD 6"
FT   REPEAT          384..422
FT                   /note="WD 7"
FT   REGION          4..87
FT                   /note="Ubiquitin-like (UBL) domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT   REGION          98..423
FT                   /note="Sufficient for nucleolar localization"
FT                   /evidence="ECO:0000250"
FT   REGION          221..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZL7"
FT   MOD_RES         415
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZL7"
FT   CROSSLNK        239
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZL7"
SQ   SEQUENCE   423 AA;  47709 MW;  F321563DB8F91E00 CRC64;
     MAQLQTRFFT DNKKYAVDDV PFSIPAASEI ADLSNLINKL LEAKNEFHKH VEFDFLIKGQ
     FLRMPLFKHM ELENISSEEV VELEYVEKYT APQPEQCMFH DDWISAIEGT EEWILTGSYD
     KTSRIWSLEG KSIMTIVGHT DVVKDVAWVK KDSLSCLLLS ASMDQTILLW EWNVERNKVK
     ALHCCRGHAG SVDSIAVDST GTKFCSGSWD KMLKIWSTVP TDEEDEMEES TNRPRKKQKT
     EQLGLTRTPI VTLSGHKEAI SSVLWSDAEE ICSASWDHTI KVWDVESGSL KSTLTGNKVF
     NCISYSPLCK RLASGSTDRH IRLWDPRTKD GSLVSLSLTS HTGWVTSVKW SPTHEQQLIS
     GSLDNMVKLW DTRSCKAPLY DLAAHEDKVL SVDWTDSGLL LSGGADNKLY SYRYSPTTSH
     VGA
 
 
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