YPEL5_HUMAN
ID YPEL5_HUMAN Reviewed; 121 AA.
AC P62699; D6W568; Q65Z97; Q8R174; Q9D6M1; Q9UMX7; Q9Y3C9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein yippee-like 5;
GN Name=YPEL5; ORFNames=CGI-127;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Luo W.Q., Chen J.H., Hu S.N., Zhou Y., Huang X.W., Zhou H.J., Yuan J.G.,
RA Qiang B.Q.;
RT "Isolating a new human cDNA.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-101.
RC TISSUE=Intestine;
RX PubMed=11240639; DOI=10.1046/j.1365-2583.2001.00239.x;
RA Roxstroem-Lindquist K., Faye I.;
RT "The Drosophila gene Yippee reveals a novel family of putative zinc binding
RT proteins highly conserved among eukaryotes.";
RL Insect Mol. Biol. 10:77-86(2001).
RN [8]
RP INTERACTION WITH RANBP9 AND RANBP10.
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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION, IDENTIFICATION IN THE CTLH COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=29911972; DOI=10.7554/elife.35528;
RA Lampert F., Stafa D., Goga A., Soste M.V., Gilberto S., Olieric N.,
RA Picotti P., Stoffel M., Peter M.;
RT "The multi-subunit GID/CTLH E3 ligase promotes proliferation and targets
RT the transcription factor Hbp1 for degradation.";
RL Elife 7:0-0(2018).
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 (PubMed:29911972). Required for normal cell
CC proliferation (By similarity). {ECO:0000250|UniProtKB:Q65Z55,
CC ECO:0000269|PubMed:29911972}.
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 (PubMed:29911972). Within this
CC complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8,
CC WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4,
CC MKLN1, ARMC8 and YPEL5 have ancillary roles (PubMed:29911972).
CC Interacts with RANBP9 and RANBP10 (PubMed:20580816).
CC {ECO:0000269|PubMed:20580816, ECO:0000269|PubMed:29911972}.
CC -!- INTERACTION:
CC P62699; Q9GZU7: CTDSP1; NbExp=3; IntAct=EBI-11721624, EBI-751587;
CC P62699; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-11721624, EBI-742054;
CC P62699; O15499: GSC2; NbExp=3; IntAct=EBI-11721624, EBI-19954058;
CC P62699; O60336: MAPKBP1; NbExp=3; IntAct=EBI-11721624, EBI-947402;
CC P62699; Q99471: PFDN5; NbExp=3; IntAct=EBI-11721624, EBI-357275;
CC P62699; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-11721624, EBI-2876622;
CC P62699; P25786: PSMA1; NbExp=3; IntAct=EBI-11721624, EBI-359352;
CC P62699; Q92529: SHC3; NbExp=3; IntAct=EBI-11721624, EBI-79084;
CC P62699; O00463: TRAF5; NbExp=3; IntAct=EBI-11721624, EBI-523498;
CC P62699; Q8N720: ZNF655; NbExp=3; IntAct=EBI-11721624, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q65Z55}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q65Z55}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q65Z55}. Midbody {ECO:0000250|UniProtKB:Q65Z55}.
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:0000250|UniProtKB:Q65Z55}.
CC -!- SIMILARITY: Belongs to the yippee family. {ECO:0000305}.
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DR EMBL; AB098739; BAD51380.1; -; mRNA.
DR EMBL; AF151885; AAD34122.1; -; mRNA.
DR EMBL; AF135161; AAF43785.1; -; mRNA.
DR EMBL; AC016907; AAY14780.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00500.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00501.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00504.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00505.1; -; Genomic_DNA.
DR EMBL; BC000836; AAH00836.1; -; mRNA.
DR EMBL; BC047237; AAH47237.1; -; mRNA.
DR EMBL; AF172940; AAD47882.1; -; mRNA.
DR CCDS; CCDS1771.1; -.
DR PIR; T50836; T50836.
DR RefSeq; NP_001120871.1; NM_001127399.1.
DR RefSeq; NP_001120872.1; NM_001127400.1.
DR RefSeq; NP_001120873.1; NM_001127401.1.
DR RefSeq; NP_057145.1; NM_016061.2.
DR RefSeq; XP_016859807.1; XM_017004318.1.
DR RefSeq; XP_016859808.1; XM_017004319.1.
DR RefSeq; XP_016859809.1; XM_017004320.1.
DR RefSeq; XP_016859810.1; XM_017004321.1.
DR RefSeq; XP_016859811.1; XM_017004322.1.
DR AlphaFoldDB; P62699; -.
DR SMR; P62699; -.
DR BioGRID; 119655; 108.
DR IntAct; P62699; 32.
DR MINT; P62699; -.
DR STRING; 9606.ENSP00000368835; -.
DR iPTMnet; P62699; -.
DR PhosphoSitePlus; P62699; -.
DR BioMuta; YPEL5; -.
DR DMDM; 50428911; -.
DR EPD; P62699; -.
DR jPOST; P62699; -.
DR MassIVE; P62699; -.
DR MaxQB; P62699; -.
DR PaxDb; P62699; -.
DR PeptideAtlas; P62699; -.
DR PRIDE; P62699; -.
DR ProteomicsDB; 57416; -.
DR Antibodypedia; 47369; 147 antibodies from 26 providers.
DR DNASU; 51646; -.
DR Ensembl; ENST00000261353.9; ENSP00000261353.4; ENSG00000119801.13.
DR Ensembl; ENST00000379519.7; ENSP00000368834.3; ENSG00000119801.13.
DR Ensembl; ENST00000379520.7; ENSP00000368835.3; ENSG00000119801.13.
DR Ensembl; ENST00000402003.7; ENSP00000383974.3; ENSG00000119801.13.
DR Ensembl; ENST00000402708.5; ENSP00000385278.1; ENSG00000119801.13.
DR GeneID; 51646; -.
DR KEGG; hsa:51646; -.
DR MANE-Select; ENST00000261353.9; ENSP00000261353.4; NM_016061.3; NP_057145.1.
DR UCSC; uc002rmz.5; human.
DR CTD; 51646; -.
DR DisGeNET; 51646; -.
DR GeneCards; YPEL5; -.
DR HGNC; HGNC:18329; YPEL5.
DR HPA; ENSG00000119801; Tissue enriched (bone).
DR MIM; 609726; gene.
DR neXtProt; NX_P62699; -.
DR OpenTargets; ENSG00000119801; -.
DR PharmGKB; PA134863727; -.
DR VEuPathDB; HostDB:ENSG00000119801; -.
DR eggNOG; KOG3399; Eukaryota.
DR GeneTree; ENSGT00940000154800; -.
DR HOGENOM; CLU_043857_1_1_1; -.
DR InParanoid; P62699; -.
DR OMA; WVYEFAT; -.
DR OrthoDB; 1431042at2759; -.
DR PhylomeDB; P62699; -.
DR TreeFam; TF323378; -.
DR PathwayCommons; P62699; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P62699; -.
DR BioGRID-ORCS; 51646; 531 hits in 1039 CRISPR screens.
DR ChiTaRS; YPEL5; human.
DR GenomeRNAi; 51646; -.
DR Pharos; P62699; Tbio.
DR PRO; PR:P62699; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P62699; protein.
DR Bgee; ENSG00000119801; Expressed in secondary oocyte and 206 other tissues.
DR Genevisible; P62699; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; ISS: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 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..121
FT /note="Protein yippee-like 5"
FT /id="PRO_0000212396"
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
