位置:首页 > 蛋白库 > GLPK_MOUSE
GLPK_MOUSE
ID   GLPK_MOUSE              Reviewed;         559 AA.
AC   Q64516; B1ASZ1; Q8C2M1; Q8C8X0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Glycerol kinase;
DE            Short=GK;
DE            Short=Glycerokinase;
DE            EC=2.7.1.30 {ECO:0000269|PubMed:8884278};
DE   AltName: Full=ATP:glycerol 3-phosphotransferase;
GN   Name=Gk; Synonyms=Gyk {ECO:0000303|PubMed:8884278};
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] (ISOFORM 1).
RC   STRAIN=BALB/cJ;
RX   PubMed=8884278; DOI=10.1006/geno.1996.0500;
RA   Huq A.H., Lovell R.S., Sampson M.J., Decker W.K., Dinulos M.B.,
RA   Disteche C.M., Craigen W.J.;
RT   "Isolation, mapping, and functional expression of the mouse X chromosome
RT   glycerol kinase gene.";
RL   Genomics 36:530-534(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Retina, and Thymus;
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Liver;
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: Key enzyme in the regulation of glycerol uptake and
CC       metabolism. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate;
CC         Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
CC         EC=2.7.1.30; Evidence={ECO:0000269|PubMed:8884278};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21645;
CC         Evidence={ECO:0000269|PubMed:8884278};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC       {ECO:0000269|PubMed:8884278}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Bound to the mitochondrial
CC       surface or cytoplasmic. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=3;
CC         IsoId=Q64516-3; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q64516-2; Sequence=VSP_034650;
CC       Name=1;
CC         IsoId=Q64516-1; Sequence=VSP_034650, VSP_034651;
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U48403; AAC52824.1; -; mRNA.
DR   EMBL; AK044308; BAC31861.1; -; mRNA.
DR   EMBL; AK088373; BAC40312.1; -; mRNA.
DR   EMBL; AL645567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL672056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC003767; AAH03767.1; -; mRNA.
DR   CCDS; CCDS41050.1; -. [Q64516-2]
DR   CCDS; CCDS53126.1; -. [Q64516-1]
DR   CCDS; CCDS81149.1; -. [Q64516-3]
DR   RefSeq; NP_001281069.1; NM_001294140.1. [Q64516-3]
DR   RefSeq; NP_032220.1; NM_008194.3. [Q64516-1]
DR   RefSeq; NP_997609.1; NM_212444.2. [Q64516-2]
DR   AlphaFoldDB; Q64516; -.
DR   SMR; Q64516; -.
DR   BioGRID; 200130; 3.
DR   IntAct; Q64516; 3.
DR   MINT; Q64516; -.
DR   STRING; 10090.ENSMUSP00000119564; -.
DR   iPTMnet; Q64516; -.
DR   PhosphoSitePlus; Q64516; -.
DR   SwissPalm; Q64516; -.
DR   jPOST; Q64516; -.
DR   MaxQB; Q64516; -.
DR   PaxDb; Q64516; -.
DR   PeptideAtlas; Q64516; -.
DR   PRIDE; Q64516; -.
DR   ProteomicsDB; 267454; -. [Q64516-3]
DR   ProteomicsDB; 267455; -. [Q64516-2]
DR   ProteomicsDB; 267456; -. [Q64516-1]
DR   DNASU; 14933; -.
DR   Ensembl; ENSMUST00000026039; ENSMUSP00000026039; ENSMUSG00000025059. [Q64516-1]
DR   Ensembl; ENSMUST00000113978; ENSMUSP00000109611; ENSMUSG00000025059. [Q64516-3]
DR   Ensembl; ENSMUST00000156390; ENSMUSP00000119564; ENSMUSG00000025059. [Q64516-2]
DR   GeneID; 14933; -.
DR   KEGG; mmu:14933; -.
DR   UCSC; uc009trv.1; mouse. [Q64516-2]
DR   UCSC; uc009trw.1; mouse. [Q64516-1]
DR   UCSC; uc009trx.1; mouse. [Q64516-3]
DR   CTD; 2710; -.
DR   MGI; MGI:106594; Gk.
DR   VEuPathDB; HostDB:ENSMUSG00000025059; -.
DR   eggNOG; KOG2517; Eukaryota.
DR   GeneTree; ENSGT01000000214434; -.
DR   HOGENOM; CLU_009281_2_2_1; -.
DR   InParanoid; Q64516; -.
DR   OMA; FMLMNIG; -.
DR   OrthoDB; 519426at2759; -.
DR   PhylomeDB; Q64516; -.
DR   TreeFam; TF321504; -.
DR   Reactome; R-MMU-75109; Triglyceride biosynthesis.
DR   UniPathway; UPA00618; UER00672.
DR   BioGRID-ORCS; 14933; 5 hits in 41 CRISPR screens.
DR   ChiTaRS; Gk; mouse.
DR   PRO; PR:Q64516; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q64516; protein.
DR   Bgee; ENSMUSG00000025059; Expressed in proximal tubule and 264 other tissues.
DR   ExpressionAtlas; Q64516; baseline and differential.
DR   Genevisible; Q64516; MM.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004370; F:glycerol kinase activity; IDA:MGI.
DR   GO; GO:0042393; F:histone binding; ISO:MGI.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006071; P:glycerol metabolic process; IMP:MGI.
DR   GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; ISO:MGI.
DR   GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR   GO; GO:0019217; P:regulation of fatty acid metabolic process; IMP:MGI.
DR   GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR   GO; GO:0006641; P:triglyceride metabolic process; ISO:MGI.
DR   CDD; cd07792; FGGY_GK1-3_metazoa; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR042018; GK1-3_metazoa.
DR   InterPro; IPR005999; Glycerol_kin.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Glycerol metabolism; Kinase;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..559
FT                   /note="Glycerol kinase"
FT                   /id="PRO_0000059538"
FT   BINDING         20
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         433..437
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         245..250
FT                   /note="Missing (in isoform 1 and isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:8884278"
FT                   /id="VSP_034650"
FT   VAR_SEQ         528..556
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:8884278"
FT                   /id="VSP_034651"
FT   CONFLICT        55
FT                   /note="Q -> R (in Ref. 2; BAC31861)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   559 AA;  61227 MW;  09A58CB47AB5CD41 CRC64;
     MAAAKKAVLG PLVGAVDQGT SSTRFLVFNS KTAELLSHHQ VEIKQEFPRE GWVEQDPKEI
     LQSVYECIEK TCEKLGQLNI DISNIKAIGV SNQRETTVVW DKVTGEPLYN AVVWLDLRTQ
     STVENLSKRI PGNNNFVKSK TGLPLSTYFS AVKLRWLLDN VKKVQEAVEE NRALFGTIDS
     WLIWSLTGGI HGGVHCTDVT NASRTMLFNI HSLEWDKELC EFFGIPMEIL PNVRSSSEIY
     GLMKISHSLK AGALEGVPIS GCLGDQSAAL VGQMCFQDGQ AKNTYGTGCF LLCNTGHKCV
     FSEHGLLTTV AYKLGRDKPV YYALEGSVAI AGAVIRWLRD NLGIIKSSEE IEKLAKEVGT
     SYGCYFVPAF SGLYAPYWEP SARGIICGLT QFTNKCHIAF AALEAVCFQT REILDAMNRD
     CGIPLSHLQV DGGMTSNKIL MQLQADILYI PVVKPSMPET TALGAAMAAG AAEGVGVWSL
     EPEDLSAVTM ERFEPQINAE ESEIRYSTWK KAVMKSIGWV TTQSPESGDP SIFCSLPLGF
     FIVSSMVMLI GARYISGIP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024