GLCTK_MOUSE
ID GLCTK_MOUSE Reviewed; 523 AA.
AC Q8QZY2; Q7TNX6; Q8BQL0; Q8C717; Q8C7I3; Q8CI81; Q8K0R7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Glycerate kinase;
DE EC=2.7.1.31;
GN Name=Glyctk;
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] (ISOFORM 1).
RC TISSUE=Kidney;
RA Zan Q., Guo J.H., Yu L.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Liver;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Kidney, and Liver;
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 TISSUE SPECIFICITY.
RX PubMed=16753811; DOI=10.1080/10425170500476665;
RA Guo J.-H., Hexige S., Chen L., Zhou G.-J., Wang X., Jiang J.-M.,
RA Kong Y.-H., Ji G.-Q., Wu C.-Q., Zhao S.-Y., Yu L.;
RT "Isolation and characterization of the human D-glyceric acidemia related
RT glycerate kinase gene GLYCTK1 and its alternatively splicing variant
RT GLYCTK2.";
RL DNA Seq. 17:1-7(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, 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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + ATP = (2R)-3-phosphoglycerate + ADP + H(+);
CC Xref=Rhea:RHEA:23516, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216;
CC EC=2.7.1.31; Evidence={ECO:0000250|UniProtKB:Q8IVS8};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IVS8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8QZY2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8QZY2-2; Sequence=VSP_025366;
CC -!- TISSUE SPECIFICITY: Expressed in the hippocampus, callus, brain,
CC cerebellum, renal cortex interstitial cells, epithelium of interlobular
CC bile duct and skeletal muscle. {ECO:0000269|PubMed:16753811}.
CC -!- SIMILARITY: Belongs to the glycerate kinase type-2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36136.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP97704.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF455785; AAP97704.1; ALT_FRAME; mRNA.
DR EMBL; AK049425; BAC33747.1; -; mRNA.
DR EMBL; AK050182; BAC34112.1; -; mRNA.
DR EMBL; AK052709; BAC35110.1; -; mRNA.
DR EMBL; BC025834; AAH25834.1; -; mRNA.
DR EMBL; BC025935; AAH25935.1; -; mRNA.
DR EMBL; BC030732; AAH30732.1; -; mRNA.
DR EMBL; BC033063; AAH33063.1; -; mRNA.
DR EMBL; BC036136; AAH36136.1; ALT_INIT; mRNA.
DR CCDS; CCDS23469.1; -. [Q8QZY2-1]
DR RefSeq; NP_001034675.1; NM_001039586.1.
DR RefSeq; NP_777271.3; NM_174846.4.
DR RefSeq; XP_006511778.1; XM_006511715.3.
DR RefSeq; XP_011241181.1; XM_011242879.2.
DR RefSeq; XP_011241182.1; XM_011242880.2.
DR AlphaFoldDB; Q8QZY2; -.
DR SMR; Q8QZY2; -.
DR STRING; 10090.ENSMUSP00000047761; -.
DR iPTMnet; Q8QZY2; -.
DR PhosphoSitePlus; Q8QZY2; -.
DR SwissPalm; Q8QZY2; -.
DR jPOST; Q8QZY2; -.
DR MaxQB; Q8QZY2; -.
DR PaxDb; Q8QZY2; -.
DR PRIDE; Q8QZY2; -.
DR ProteomicsDB; 263364; -. [Q8QZY2-1]
DR ProteomicsDB; 263365; -. [Q8QZY2-2]
DR DNASU; 235582; -.
DR GeneID; 235582; -.
DR KEGG; mmu:235582; -.
DR UCSC; uc009riz.1; mouse. [Q8QZY2-1]
DR CTD; 132158; -.
DR MGI; MGI:2444085; Glyctk.
DR eggNOG; KOG3935; Eukaryota.
DR InParanoid; Q8QZY2; -.
DR OrthoDB; 1371490at2759; -.
DR PhylomeDB; Q8QZY2; -.
DR TreeFam; TF313770; -.
DR Reactome; R-MMU-70350; Fructose catabolism.
DR BioGRID-ORCS; 235582; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Glyctk; mouse.
DR PRO; PR:Q8QZY2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8QZY2; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008887; F:glycerate kinase activity; ISS:UniProtKB.
DR GO; GO:0006001; P:fructose catabolic process; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR Gene3D; 3.40.1480.10; -; 1.
DR Gene3D; 3.40.50.10180; -; 1.
DR InterPro; IPR037035; GK-like_C_sf.
DR InterPro; IPR038614; GK_N_sf.
DR InterPro; IPR007835; MOFRL.
DR InterPro; IPR025286; MOFRL_assoc_dom.
DR InterPro; IPR039760; MOFRL_protein.
DR PANTHER; PTHR12227; PTHR12227; 1.
DR Pfam; PF13660; DUF4147; 1.
DR Pfam; PF05161; MOFRL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..523
FT /note="Glycerate kinase"
FT /id="PRO_0000287194"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVS8"
FT MOD_RES 200
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 1..127
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025366"
FT CONFLICT 136
FT /note="V -> I (in Ref. 2; BAC33747/BAC34112/BAC35110)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="F -> Y (in Ref. 1; AAP97704)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="Q -> H (in Ref. 2; BAC33747)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="A -> T (in Ref. 2; BAC33747/BAC34112/BAC35110)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="Q -> R (in Ref. 2; BAC34112)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="A -> V (in Ref. 2; BAC33747/BAC34112/BAC35110)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="T -> A (in Ref. 2; BAC33747/BAC34112/BAC35110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 55293 MW; 8EECD09476764FF2 CRC64;
MAAALQVLPC LLRAPSRPLL WGPPVARMTS GMALAEQARQ LFDSAVGAVQ PGPMLQRTLS
LDPSGRQLKV RDRTFQLREN LYLVGFGKAV LGMAAAAEEL LAQHLVQGVI SVPKGIRAAM
EHAGKKEMLL KPHSRVQVFE GAEDNLPDRD ALRAALTIQQ LAEGLTADDL LLVLISGGGS
ALLPAPIPPV TLEEKQMLTK LLAARGATIQ ELNTIRKALS QLKGGGLAQA AYPAQVISLI
LSDVIGDPLE VIASGPTVAS AHSVQDCLHI LNHYGLRAAL PRSVKTVLSR ADSDPHGPHT
CGHVLNVIIG SNSLALAEAQ RQAEVLGYHA MVLSTAMQGD VKRVARFYGL LARVAAAHLT
PSLAERPLEE EAELHQLAAE LQLPDLQLEE ALEAVAKAKG PVCLLAGGEP TVQLQGSGKG
GRNQELALHV GVELGRQPLG PIDVLFLSGG TDGQDGPTKV AGAWVMSDLI SQASAESLDI
ATSLTNNDSY TFFCRFRGGT HLLHTGLTGT NVMDVHLLIL HPQ
