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YPEL5_CHLAE
ID   YPEL5_CHLAE             Reviewed;         121 AA.
AC   Q65Z55;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Protein yippee-like 5;
GN   Name=YPEL5;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15556292; DOI=10.1016/j.gene.2004.06.014;
RA   Hosono K., Sasaki T., Minoshima S., Shimizu N.;
RT   "Identification and characterization of a novel gene family YPEL in a wide
RT   spectrum of eukaryotic species.";
RL   Gene 340:31-43(2004).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20580816; DOI=10.1016/j.ygeno.2010.05.003;
RA   Hosono K., Noda S., Shimizu A., Nakanishi N., Ohtsubo M., Shimizu N.,
RA   Minoshima S.;
RT   "YPEL5 protein of the YPEL gene family is involved in the cell cycle
RT   progression by interacting with two distinct proteins RanBPM and RanBP10.";
RL   Genomics 96:102-111(2010).
CC   -!- FUNCTION: Component of the CTLH E3 ubiquitin-protein ligase complex
CC       that selectively accepts ubiquitin from UBE2H and mediates
CC       ubiquitination and subsequent proteasomal degradation of the
CC       transcription factor HBP1 (By similarity). Required for normal cell
CC       proliferation (PubMed:20580816). {ECO:0000250|UniProtKB:P62699,
CC       ECO:0000269|PubMed:20580816}.
CC   -!- SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9
CC       and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog
CC       RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA,
CC       RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9
CC       and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and
CC       YPEL5 have ancillary roles. Interacts with RANBP9 and RANBP10.
CC       {ECO:0000250|UniProtKB:P62699}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20580816}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:20580816}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000269|PubMed:20580816}. Midbody {ECO:0000269|PubMed:20580816}.
CC       Note=Deteted in nucleus and at the centrosome during interphase. During
CC       mitosis, detected on the mitotic spindle, at spindle poles and at the
CC       midbody. {ECO:0000269|PubMed:20580816}.
CC   -!- SIMILARITY: Belongs to the yippee family. {ECO:0000305}.
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DR   EMBL; AB160981; BAD51390.1; -; mRNA.
DR   AlphaFoldDB; Q65Z55; -.
DR   SMR; Q65Z55; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR   GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR   InterPro; IPR034751; Yippee.
DR   InterPro; IPR004910; Yippee/Mis18/Cereblon.
DR   InterPro; IPR039058; Yippee_fam.
DR   PANTHER; PTHR13848; PTHR13848; 1.
DR   Pfam; PF03226; Yippee-Mis18; 1.
DR   PROSITE; PS51792; YIPPEE; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Metal-binding; Nucleus; Phosphoprotein; Zinc.
FT   CHAIN           1..121
FT                   /note="Protein yippee-like 5"
FT                   /id="PRO_0000212395"
FT   DOMAIN          13..110
FT                   /note="Yippee"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   MOD_RES         118
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62700"
SQ   SEQUENCE   121 AA;  13842 MW;  ADCF8C4C3B154EAB CRC64;
     MGRIFLDHIG GTRLFSCANC DTILTNRSEL ISTRFTGATG RAFLFNKVVN LQYSEVQDRV
     MLTGRHMVRD VSCKNCNSKL GWIYEFATED SQRYKEGRVI LERALVRESE GFEEHVPSDN
     S
 
 
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