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YPEL3_MOUSE
ID   YPEL3_MOUSE             Reviewed;         119 AA.
AC   P61237; Q71E85; Q9BSJ4; Q9CQB6; Q9D0U3;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Protein yippee-like 3;
DE   AltName: Full=Small ubiquitinated apoptotic protein;
GN   Name=Ypel3; Synonyms=Suap;
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 [MRNA], FUNCTION, PROBABLE UBIQUITINATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RC   TISSUE=Bone marrow;
RX   PubMed=12566317;
RA   Baker S.J.;
RT   "Small unstable apoptotic protein, an apoptosis-associated protein,
RT   suppresses proliferation of myeloid cells.";
RL   Cancer Res. 63:705-712(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
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).
CC   -!- FUNCTION: Involved in proliferation and apoptosis in myeloid precursor
CC       cells. {ECO:0000269|PubMed:12566317}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Strongly expressed in heart,
CC       brain, testis, lung, spleen, liver, kidney and myeloid cells.
CC       {ECO:0000269|PubMed:12566317, ECO:0000269|PubMed:15556292}.
CC   -!- INDUCTION: Up-regulated after the removal of interleukin 3 and exposure
CC       to granulocyte colony stimulating factor.
CC       {ECO:0000269|PubMed:12566317}.
CC   -!- PTM: Probably ubiquitinated leading to its degradation by the
CC       proteasome.
CC   -!- SIMILARITY: Belongs to the yippee family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH09171.4; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF523353; AAO85716.1; -; mRNA.
DR   EMBL; AB098742; BAD51383.1; -; mRNA.
DR   EMBL; AK002925; BAB22461.1; -; mRNA.
DR   EMBL; AK003371; BAB22745.1; -; mRNA.
DR   EMBL; AK004431; BAB23301.1; -; mRNA.
DR   EMBL; CH466531; EDL17433.1; -; Genomic_DNA.
DR   EMBL; CH466531; EDL17435.1; -; Genomic_DNA.
DR   EMBL; BC009171; AAH09171.4; ALT_INIT; mRNA.
DR   CCDS; CCDS21842.1; -.
DR   RefSeq; NP_079623.1; NM_025347.2.
DR   RefSeq; NP_081151.2; NM_026875.2.
DR   AlphaFoldDB; P61237; -.
DR   BioGRID; 211207; 1.
DR   STRING; 10090.ENSMUSP00000037332; -.
DR   PaxDb; P61237; -.
DR   PRIDE; P61237; -.
DR   ProteomicsDB; 299634; -.
DR   Antibodypedia; 27015; 81 antibodies from 25 providers.
DR   DNASU; 66090; -.
DR   Ensembl; ENSMUST00000038614; ENSMUSP00000037332; ENSMUSG00000042675.
DR   Ensembl; ENSMUST00000106356; ENSMUSP00000101963; ENSMUSG00000042675.
DR   Ensembl; ENSMUST00000106357; ENSMUSP00000101964; ENSMUSG00000042675.
DR   Ensembl; ENSMUST00000170882; ENSMUSP00000128753; ENSMUSG00000042675.
DR   GeneID; 66090; -.
DR   KEGG; mmu:66090; -.
DR   UCSC; uc009jsp.1; mouse.
DR   CTD; 83719; -.
DR   MGI; MGI:1913340; Ypel3.
DR   VEuPathDB; HostDB:ENSMUSG00000042675; -.
DR   eggNOG; KOG3399; Eukaryota.
DR   GeneTree; ENSGT00940000161514; -.
DR   HOGENOM; CLU_043857_5_2_1; -.
DR   InParanoid; P61237; -.
DR   OMA; CCCGQII; -.
DR   OrthoDB; 1431042at2759; -.
DR   PhylomeDB; P61237; -.
DR   TreeFam; TF313936; -.
DR   BioGRID-ORCS; 66090; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Ypel3; mouse.
DR   PRO; PR:P61237; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P61237; protein.
DR   Bgee; ENSMUSG00000042675; Expressed in granulocyte and 256 other tissues.
DR   ExpressionAtlas; P61237; baseline and differential.
DR   Genevisible; P61237; MM.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:2000774; P:positive regulation of cellular senescence; ISO:MGI.
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   Apoptosis; Metal-binding; Nucleus; Reference proteome; Ubl conjugation;
KW   Zinc.
FT   CHAIN           1..119
FT                   /note="Protein yippee-like 3"
FT                   /id="PRO_0000212390"
FT   DOMAIN          19..116
FT                   /note="Yippee"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   CONFLICT        16
FT                   /note="D -> N (in Ref. 1; BAB23301)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        25
FT                   /note="H -> Q (in Ref. 1; BAB23301)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   119 AA;  13608 MW;  A35E852DEB1FFBB4 CRC64;
     MVRISKPKTF QAYLDDCHRR YSCAHCRAHL ANHDDLISKS FQGSQGRAYL FNSVVNVGCG
     PAEERVLLTG LHAVADIHCE NCKTTLGWKY EQAFESSQKY KEGKYIIELN HMIKDNGWD
 
 
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