YPEL5_MOUSE
ID YPEL5_MOUSE Reviewed; 121 AA.
AC P62700; Q543T4; 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 119.
DE RecName: Full=Protein yippee-like 5;
GN Name=Ypel5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=Amnion, Bone, Cerebellum, Corpora quadrigemina, Spinal cord, and
RC Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland, and Trophoblast stem cell;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(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 (By similarity). {ECO:0000250|UniProtKB:P62699,
CC ECO:0000250|UniProtKB:Q65Z55}.
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: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; AK010201; BAB26764.1; -; mRNA.
DR EMBL; AK046281; BAC32668.1; -; mRNA.
DR EMBL; AK049096; BAC33540.1; -; mRNA.
DR EMBL; AK049644; BAC33855.1; -; mRNA.
DR EMBL; AK137446; BAE23354.1; -; mRNA.
DR EMBL; AK154461; BAE32602.1; -; mRNA.
DR EMBL; AK167998; BAE39988.1; -; mRNA.
DR EMBL; AK169241; BAE41007.1; -; mRNA.
DR EMBL; AK171010; BAE42181.1; -; mRNA.
DR EMBL; BC025125; AAH25125.1; -; mRNA.
DR EMBL; BC085109; AAH85109.1; -; mRNA.
DR CCDS; CCDS28963.1; -.
DR RefSeq; NP_081442.1; NM_027166.5.
DR RefSeq; XP_006524603.1; XM_006524540.1.
DR RefSeq; XP_006524604.1; XM_006524541.1.
DR RefSeq; XP_006524605.1; XM_006524542.3.
DR AlphaFoldDB; P62700; -.
DR SMR; P62700; -.
DR BioGRID; 238688; 18.
DR IntAct; P62700; 18.
DR STRING; 10090.ENSMUSP00000037764; -.
DR iPTMnet; P62700; -.
DR PhosphoSitePlus; P62700; -.
DR EPD; P62700; -.
DR MaxQB; P62700; -.
DR PaxDb; P62700; -.
DR PeptideAtlas; P62700; -.
DR PRIDE; P62700; -.
DR ProteomicsDB; 299635; -.
DR Antibodypedia; 47369; 147 antibodies from 26 providers.
DR Ensembl; ENSMUST00000045174; ENSMUSP00000037764; ENSMUSG00000039770.
DR Ensembl; ENSMUST00000233210; ENSMUSP00000156501; ENSMUSG00000039770.
DR Ensembl; ENSMUST00000233886; ENSMUSP00000156450; ENSMUSG00000039770.
DR GeneID; 383295; -.
DR KEGG; mmu:383295; -.
DR UCSC; uc008dne.1; mouse.
DR CTD; 51646; -.
DR MGI; MGI:1916937; Ypel5.
DR VEuPathDB; HostDB:ENSMUSG00000039770; -.
DR eggNOG; KOG3399; Eukaryota.
DR GeneTree; ENSGT00940000154800; -.
DR HOGENOM; CLU_043857_1_1_1; -.
DR InParanoid; P62700; -.
DR OMA; WVYEFAT; -.
DR OrthoDB; 1431042at2759; -.
DR PhylomeDB; P62700; -.
DR TreeFam; TF323378; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 383295; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Ypel5; mouse.
DR PRO; PR:P62700; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P62700; protein.
DR Bgee; ENSMUSG00000039770; Expressed in blood and 242 other tissues.
DR ExpressionAtlas; P62700; baseline and differential.
DR Genevisible; P62700; MM.
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; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
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_0000212397"
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:0007744|PubMed:21183079"
SQ SEQUENCE 121 AA; 13842 MW; ADCF8C4C3B154EAB CRC64;
MGRIFLDHIG GTRLFSCANC DTILTNRSEL ISTRFTGATG RAFLFNKVVN LQYSEVQDRV
MLTGRHMVRD VSCKNCNSKL GWIYEFATED SQRYKEGRVI LERALVRESE GFEEHVPSDN
S
