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JMJD8_MOUSE
ID   JMJD8_MOUSE             Reviewed;         271 AA.
AC   Q3TA59; Q3U1Q1; Q91XD9; Q9D0L5;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 3.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=JmjC domain-containing protein 8 {ECO:0000305};
DE   AltName: Full=Jumonji domain-containing protein 8;
DE   Flags: Precursor;
GN   Name=Jmjd8 {ECO:0000312|MGI:MGI:1919356};
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=C57BL/6J, and NOD; TISSUE=Spleen;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-271.
RC   STRAIN=FVB/N; TISSUE=Kidney;
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   [4]
RP   INDUCTION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=27199445; DOI=10.1161/atvbaha.116.307695;
RA   Boeckel J.N., Derlet A., Glaser S.F., Luczak A., Lucas T., Heumueller A.W.,
RA   Krueger M., Zehendner C.M., Kaluza D., Doddaballapur A., Ohtani K.,
RA   Treguer K., Dimmeler S.;
RT   "JMJD8 Regulates Angiogenic Sprouting and Cellular Metabolism by
RT   Interacting With Pyruvate Kinase M2 in Endothelial Cells.";
RL   Arterioscler. Thromb. Vasc. Biol. 36:1425-1433(2016).
CC   -!- FUNCTION: Functions as a positive regulator of TNF-induced NF-kappaB
CC       signaling (By similarity). Regulates angiogenesis and cellular
CC       metabolism through interaction with PKM (PubMed:27199445).
CC       {ECO:0000250|UniProtKB:Q96S16, ECO:0000269|PubMed:27199445}.
CC   -!- SUBUNIT: Oligomer. Dimer. Interacts with PKM; regulates angiogenesis
CC       and metabolism. {ECO:0000250|UniProtKB:Q96S16}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:Q96S16}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q96S16}.
CC   -!- INDUCTION: Up-regulated upon endothelial differentiation.
CC       {ECO:0000269|PubMed:27199445}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q96S16}.
CC   -!- DISRUPTION PHENOTYPE: Homozygote knockout Jmjd8 show no obvious
CC       phenotype. However, the number of capillaries in muscle tissue is
CC       significantly reduced. {ECO:0000269|PubMed:27199445}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH10800.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAE42811.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK011308; BAB27534.1; -; mRNA.
DR   EMBL; AK148079; BAE28331.1; -; mRNA.
DR   EMBL; AK155810; BAE33443.1; -; mRNA.
DR   EMBL; AK172073; BAE42811.1; ALT_FRAME; mRNA.
DR   EMBL; AC159277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC010800; AAH10800.1; ALT_INIT; mRNA.
DR   RefSeq; NP_082377.2; NM_028101.4.
DR   AlphaFoldDB; Q3TA59; -.
DR   SMR; Q3TA59; -.
DR   STRING; 10090.ENSMUSP00000122744; -.
DR   GlyGen; Q3TA59; 3 sites.
DR   PhosphoSitePlus; Q3TA59; -.
DR   EPD; Q3TA59; -.
DR   PaxDb; Q3TA59; -.
DR   PRIDE; Q3TA59; -.
DR   ProteomicsDB; 301699; -.
DR   Antibodypedia; 22813; 102 antibodies from 22 providers.
DR   DNASU; 72106; -.
DR   Ensembl; ENSMUST00000026832; ENSMUSP00000026832; ENSMUSG00000025736.
DR   GeneID; 72106; -.
DR   KEGG; mmu:72106; -.
DR   UCSC; uc008bce.2; mouse.
DR   CTD; 339123; -.
DR   MGI; MGI:1919356; Jmjd8.
DR   VEuPathDB; HostDB:ENSMUSG00000025736; -.
DR   eggNOG; KOG2131; Eukaryota.
DR   GeneTree; ENSGT00390000015438; -.
DR   InParanoid; Q3TA59; -.
DR   OMA; KCNIERH; -.
DR   OrthoDB; 1029368at2759; -.
DR   PhylomeDB; Q3TA59; -.
DR   TreeFam; TF313408; -.
DR   BioGRID-ORCS; 72106; 2 hits in 74 CRISPR screens.
DR   ChiTaRS; Jmjd8; mouse.
DR   PRO; PR:Q3TA59; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q3TA59; protein.
DR   Bgee; ENSMUSG00000025736; Expressed in embryonic brain and 238 other tissues.
DR   ExpressionAtlas; Q3TA59; baseline and differential.
DR   Genevisible; Q3TA59; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR   GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISS:UniProtKB.
DR   GO; GO:0006110; P:regulation of glycolytic process; ISS:UniProtKB.
DR   GO; GO:1903302; P:regulation of pyruvate kinase activity; ISS:UniProtKB.
DR   InterPro; IPR041667; Cupin_8.
DR   InterPro; IPR003347; JmjC_dom.
DR   Pfam; PF13621; Cupin_8; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Endoplasmic reticulum; Glycoprotein; Reference proteome; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..271
FT                   /note="JmjC domain-containing protein 8"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000344532"
FT   DOMAIN          138..271
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        69
FT                   /note="F -> L (in Ref. 1; BAB27534)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   271 AA;  30666 MW;  ECCF2223658DF49E CRC64;
     MFMAAAGRRG LLLLFVLWMM VTVILPASGE GGWKQNGLGI AAAVMEEERC TVERRAHITY
     SEFMQHYAFL KPVILQGLTD NSKFRALCSR ENLLASFGDN IVRLSTANTY SYQKVDLPFQ
     EYVEQLLQPQ DPASLGNDTL YFFGDNNFTE WASLFQHYSP PPFRLLGTTP AYSFGIAGAG
     SGVPFHWHGP GFSEVIYGRK RWFLYPPEKT PEFHPNKTTL AWLLEIYPSL ALSARPLECT
     IQAGEVLYFP DRWWHATLNL DTSVFISTFL G
 
 
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