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GLPK5_MOUSE
ID   GLPK5_MOUSE             Reviewed;         534 AA.
AC   Q8BX05; Q14B67; Q3TK02; Q3TSE0; Q80VA9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Putative glycerol kinase 5;
DE            Short=GK 5;
DE            Short=Glycerokinase 5;
DE            EC=2.7.1.30;
DE   AltName: Full=ATP:glycerol 3-phosphotransferase 5;
GN   Name=Gk5;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Blastocyst, Egg, and Stomach;
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] (ISOFORMS 2 AND 3).
RC   STRAIN=NMRI; 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   -!- 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;
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BX05-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BX05-2; Sequence=VSP_032125;
CC       Name=3;
CC         IsoId=Q8BX05-3; Sequence=VSP_032124, VSP_032125;
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH50033.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK049275; BAC33651.1; -; mRNA.
DR   EMBL; AK160477; BAE35811.1; -; mRNA.
DR   EMBL; AK162119; BAE36735.1; -; mRNA.
DR   EMBL; AK167217; BAE39343.1; -; mRNA.
DR   EMBL; BC050033; AAH50033.1; ALT_INIT; mRNA.
DR   EMBL; BC116302; AAI16303.1; -; mRNA.
DR   EMBL; BC116303; AAI16304.1; -; mRNA.
DR   CCDS; CCDS52891.1; -. [Q8BX05-2]
DR   CCDS; CCDS90642.1; -. [Q8BX05-1]
DR   RefSeq; NP_796326.1; NM_177352.4. [Q8BX05-2]
DR   RefSeq; XP_006511194.1; XM_006511131.2.
DR   AlphaFoldDB; Q8BX05; -.
DR   SMR; Q8BX05; -.
DR   STRING; 10090.ENSMUSP00000112717; -.
DR   iPTMnet; Q8BX05; -.
DR   PhosphoSitePlus; Q8BX05; -.
DR   REPRODUCTION-2DPAGE; IPI00475236; -.
DR   MaxQB; Q8BX05; -.
DR   PaxDb; Q8BX05; -.
DR   PeptideAtlas; Q8BX05; -.
DR   PRIDE; Q8BX05; -.
DR   ProteomicsDB; 271391; -. [Q8BX05-1]
DR   ProteomicsDB; 271392; -. [Q8BX05-2]
DR   ProteomicsDB; 271393; -. [Q8BX05-3]
DR   Antibodypedia; 35071; 200 antibodies from 26 providers.
DR   DNASU; 235533; -.
DR   Ensembl; ENSMUST00000085217; ENSMUSP00000082313; ENSMUSG00000041440. [Q8BX05-1]
DR   Ensembl; ENSMUST00000122383; ENSMUSP00000112717; ENSMUSG00000041440. [Q8BX05-2]
DR   GeneID; 235533; -.
DR   KEGG; mmu:235533; -.
DR   UCSC; uc009rbz.1; mouse. [Q8BX05-1]
DR   UCSC; uc009rca.1; mouse. [Q8BX05-2]
DR   UCSC; uc012gyo.1; mouse. [Q8BX05-3]
DR   CTD; 256356; -.
DR   MGI; MGI:2443336; Gk5.
DR   VEuPathDB; HostDB:ENSMUSG00000041440; -.
DR   eggNOG; KOG2517; Eukaryota.
DR   GeneTree; ENSGT01000000214434; -.
DR   HOGENOM; CLU_009281_2_3_1; -.
DR   InParanoid; Q8BX05; -.
DR   OMA; CTFLTWN; -.
DR   OrthoDB; 519426at2759; -.
DR   PhylomeDB; Q8BX05; -.
DR   TreeFam; TF321504; -.
DR   UniPathway; UPA00618; UER00672.
DR   BioGRID-ORCS; 235533; 1 hit in 74 CRISPR screens.
DR   ChiTaRS; Gk5; mouse.
DR   PRO; PR:Q8BX05; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8BX05; protein.
DR   Bgee; ENSMUSG00000041440; Expressed in tail skin and 165 other tissues.
DR   ExpressionAtlas; Q8BX05; baseline and differential.
DR   Genevisible; Q8BX05; MM.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004370; F:glycerol kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006071; P:glycerol metabolic process; IBA:GO_Central.
DR   GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR   GO; GO:0006641; P:triglyceride metabolic process; IBA:GO_Central.
DR   CDD; cd07793; FGGY_GK5_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; IPR037444; GK5_FGGY.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Glycerol metabolism; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..534
FT                   /note="Putative glycerol kinase 5"
FT                   /id="PRO_0000323755"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         444..449
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..90
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032124"
FT   VAR_SEQ         515..534
FT                   /note="VNMENWVKAVKRSMNWYNKT -> AF (in isoform 2 and isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_032125"
FT   CONFLICT        45
FT                   /note="A -> P (in Ref. 2; AAH50033)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   534 AA;  59812 MW;  E643A4284E3377FE CRC64;
     MSGQQERAER QREELSASAS PPSRFVLGLD VGSTVIRCHV YDQTARVRGS SAQKVENVYP
     QPGWVEIDPD SLWAQFVAVI KDAVKAAGVQ MNQIVGLGIS TQRATFITWN KKTGHHFHNF
     ISWQDLRAAE LVKSWNNSLI MKLLHGATRV LHFFSRSKVM LTVSRFNFST QHATLRLTWI
     LQNLSEVKRA VEEDNCCFGT IDTWLLYKLT KGSSYATDYS NASTTGFFDP YAMRWSRLIT
     TMVSIPLSIL PPVKDTSYNF GSVDEKIFGV PIPVVALVGD QQSAMFGECC FETGDVKLTM
     GTGTFLDINT GKNLQHVNGG FYPLIGWKIG QELVCLAEGN AGDTGTAIMW AQKLDLFTDA
     AETEKMALSL EDSEGVYFVP SFSGLQAPLN DPCACASFMG LKHSTNKYHL VRAILESIAF
     RNKQLYDMLQ REIQIPVTNI RADGGVCNNA FVMQMTSDLI NEKIDRPAHF DMSCLGAASL
     AGLAVGFWAD KEELQKLRQS EMVFKPQKKW QEYEVNMENW VKAVKRSMNW YNKT
 
 
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