GLCTK_HUMAN
ID GLCTK_HUMAN Reviewed; 523 AA.
AC Q8IVS8; Q0P630; Q2EZ43; Q6Y2K6; Q7Z6G5; Q86YR8; Q8TED2; Q8WTY2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Glycerate kinase;
DE EC=2.7.1.31 {ECO:0000269|PubMed:16753811, ECO:0000269|PubMed:20949620};
DE AltName: Full=HBeAg-binding protein 4;
GN Name=GLYCTK; Synonyms=HBEBP4; ORFNames=LP5910;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR
RP LOCATION(ISOFORMS 1 AND 2), CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Lung;
RA Guo J.H.;
RT "Cloning of HCG9886S gene and identification of a novel domain.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
RA Zhang J.-K., Cheng J., Lan X.-Y., Guo J., Zhang L.-Y.;
RT "Screening and cloning of HBeAg binding protein 4.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Lung, and Skin;
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 [7]
RP KINETIC PARAMETERS, CATALYTIC ACTIVITY, VARIANT D-GA CYS-493, AND
RP CHARACTERIZATION OF VARIANT D-GA CYS-493.
RX PubMed=20949620; DOI=10.1002/humu.21375;
RA Sass J.O., Fischer K., Wang R., Christensen E., Scholl-Burgi S., Chang R.,
RA Kapelari K., Walter M.;
RT "D-glyceric aciduria is caused by genetic deficiency of D-glycerate kinase
RT (GLYCTK).";
RL Hum. Mutat. 31:1280-1285(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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:0000269|PubMed:16753811,
CC ECO:0000269|PubMed:20949620};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for D-glycerate {ECO:0000269|PubMed:20949620};
CC -!- INTERACTION:
CC Q8IVS8; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-748515, EBI-10173507;
CC Q8IVS8; Q8N9V6-2: ANKRD53; NbExp=3; IntAct=EBI-748515, EBI-13345447;
CC Q8IVS8; Q96C12: ARMC5; NbExp=3; IntAct=EBI-748515, EBI-6425121;
CC Q8IVS8; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-748515, EBI-12811889;
CC Q8IVS8; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-748515, EBI-11976299;
CC Q8IVS8; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-748515, EBI-739580;
CC Q8IVS8; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-748515, EBI-739624;
CC Q8IVS8; Q86UW9: DTX2; NbExp=6; IntAct=EBI-748515, EBI-740376;
CC Q8IVS8; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-748515, EBI-2349927;
CC Q8IVS8; Q9Y5P6: GMPPB; NbExp=5; IntAct=EBI-748515, EBI-750945;
CC Q8IVS8; Q08379: GOLGA2; NbExp=6; IntAct=EBI-748515, EBI-618309;
CC Q8IVS8; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-748515, EBI-8638439;
CC Q8IVS8; Q53G59: KLHL12; NbExp=3; IntAct=EBI-748515, EBI-740929;
CC Q8IVS8; P13646: KRT13; NbExp=3; IntAct=EBI-748515, EBI-1223876;
CC Q8IVS8; P19012: KRT15; NbExp=3; IntAct=EBI-748515, EBI-739566;
CC Q8IVS8; P08727: KRT19; NbExp=3; IntAct=EBI-748515, EBI-742756;
CC Q8IVS8; O76011: KRT34; NbExp=3; IntAct=EBI-748515, EBI-1047093;
CC Q8IVS8; O95678: KRT75; NbExp=3; IntAct=EBI-748515, EBI-2949715;
CC Q8IVS8; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-748515, EBI-1048945;
CC Q8IVS8; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-748515, EBI-11962084;
CC Q8IVS8; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-748515, EBI-741037;
CC Q8IVS8; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-748515, EBI-716006;
CC Q8IVS8; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-748515, EBI-10174029;
CC Q8IVS8; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-748515, EBI-8487781;
CC Q8IVS8; Q9NYP9: MIS18A; NbExp=4; IntAct=EBI-748515, EBI-1104552;
CC Q8IVS8; Q6PF18: MORN3; NbExp=3; IntAct=EBI-748515, EBI-9675802;
CC Q8IVS8; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-748515, EBI-10271199;
CC Q8IVS8; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-748515, EBI-17490746;
CC Q8IVS8; P49902: NT5C2; NbExp=3; IntAct=EBI-748515, EBI-742084;
CC Q8IVS8; Q99471: PFDN5; NbExp=3; IntAct=EBI-748515, EBI-357275;
CC Q8IVS8; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-748515, EBI-79165;
CC Q8IVS8; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-748515, EBI-2876622;
CC Q8IVS8; P01189: POMC; NbExp=3; IntAct=EBI-748515, EBI-12219503;
CC Q8IVS8; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-748515, EBI-3957793;
CC Q8IVS8; Q08623: PUDP; NbExp=3; IntAct=EBI-748515, EBI-12807240;
CC Q8IVS8; Q9BYM8: RBCK1; NbExp=3; IntAct=EBI-748515, EBI-2340624;
CC Q8IVS8; Q93062: RBPMS; NbExp=3; IntAct=EBI-748515, EBI-740322;
CC Q8IVS8; Q04864: REL; NbExp=3; IntAct=EBI-748515, EBI-307352;
CC Q8IVS8; Q04864-2: REL; NbExp=3; IntAct=EBI-748515, EBI-10829018;
CC Q8IVS8; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-748515, EBI-3957636;
CC Q8IVS8; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-748515, EBI-748601;
CC Q8IVS8; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-748515, EBI-12275818;
CC Q8IVS8; Q96H20: SNF8; NbExp=5; IntAct=EBI-748515, EBI-747719;
CC Q8IVS8; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-748515, EBI-11959123;
CC Q8IVS8; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-748515, EBI-5235340;
CC Q8IVS8; P14373: TRIM27; NbExp=3; IntAct=EBI-748515, EBI-719493;
CC Q8IVS8; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-748515, EBI-5235829;
CC Q8IVS8; Q15645: TRIP13; NbExp=9; IntAct=EBI-748515, EBI-358993;
CC Q8IVS8; Q9UGJ1: TUBGCP4; NbExp=3; IntAct=EBI-748515, EBI-1052544;
CC Q8IVS8; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-748515, EBI-12068150;
CC Q8IVS8; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-748515, EBI-11419867;
CC Q8IVS8; O60844: ZG16; NbExp=3; IntAct=EBI-748515, EBI-746479;
CC Q8IVS8; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-748515, EBI-11962760;
CC Q8IVS8; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-748515, EBI-4395669;
CC Q8IVS8; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-748515, EBI-4395732;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:16753811}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Mitochondrion
CC {ECO:0000269|PubMed:16753811}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=Glycerate kinase 1 {ECO:0000303|PubMed:16753811},
CC GLYCTK1 {ECO:0000303|PubMed:16753811};
CC IsoId=Q8IVS8-1; Sequence=Displayed;
CC Name=2; Synonyms=Glycerate kinase 2 {ECO:0000303|PubMed:16753811},
CC GLYCTK2 {ECO:0000303|PubMed:16753811};
CC IsoId=Q8IVS8-2; Sequence=VSP_025360, VSP_025362;
CC Name=3;
CC IsoId=Q8IVS8-3; Sequence=VSP_025358;
CC Name=4;
CC IsoId=Q8IVS8-4; Sequence=VSP_025363, VSP_025365;
CC Name=5;
CC IsoId=Q8IVS8-5; Sequence=VSP_025357, VSP_025364, VSP_025365;
CC Name=6;
CC IsoId=Q8IVS8-6; Sequence=VSP_025356;
CC Name=7;
CC IsoId=Q8IVS8-7; Sequence=VSP_025359, VSP_025361;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16753811}.
CC -!- DISEASE: D-glyceric aciduria (D-GA) [MIM:220120]: A rare metabolic
CC disease characterized by chronic metabolic acidosis and a highly
CC variable clinical phenotype. Clinical features range from an
CC encephalopathic presentation with seizures, microcephaly, severe
CC intellectual disability and early death, to milder manifestations with
CC only speech delay or even normal development.
CC {ECO:0000269|PubMed:20949620}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycerate kinase type-2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36862.1; Type=Frameshift; Evidence={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; AY295075; AAP51132.1; -; mRNA.
DR EMBL; AF448855; AAP41923.1; -; mRNA.
DR EMBL; AY172690; AAO17719.1; -; mRNA.
DR EMBL; AY189286; AAO86730.1; -; mRNA.
DR EMBL; AK074215; BAB85018.1; -; mRNA.
DR EMBL; AY134474; AAM95456.1; -; mRNA.
DR EMBL; DQ352863; ABD22985.1; -; mRNA.
DR EMBL; BC021896; AAH21896.1; -; mRNA.
DR EMBL; BC036862; AAH36862.1; ALT_FRAME; mRNA.
DR EMBL; BC042151; AAH42151.1; -; mRNA.
DR CCDS; CCDS2852.1; -. [Q8IVS8-1]
DR CCDS; CCDS46841.1; -. [Q8IVS8-2]
DR RefSeq; NP_001138423.1; NM_001144951.1. [Q8IVS8-2]
DR RefSeq; NP_660305.2; NM_145262.3. [Q8IVS8-1]
DR AlphaFoldDB; Q8IVS8; -.
DR SMR; Q8IVS8; -.
DR BioGRID; 126307; 60.
DR IntAct; Q8IVS8; 58.
DR MINT; Q8IVS8; -.
DR STRING; 9606.ENSP00000389175; -.
DR iPTMnet; Q8IVS8; -.
DR PhosphoSitePlus; Q8IVS8; -.
DR BioMuta; GLYCTK; -.
DR DMDM; 74728080; -.
DR jPOST; Q8IVS8; -.
DR MassIVE; Q8IVS8; -.
DR MaxQB; Q8IVS8; -.
DR PaxDb; Q8IVS8; -.
DR PeptideAtlas; Q8IVS8; -.
DR PRIDE; Q8IVS8; -.
DR ProteomicsDB; 70758; -. [Q8IVS8-1]
DR ProteomicsDB; 70759; -. [Q8IVS8-2]
DR ProteomicsDB; 70760; -. [Q8IVS8-3]
DR ProteomicsDB; 70761; -. [Q8IVS8-4]
DR ProteomicsDB; 70762; -. [Q8IVS8-5]
DR ProteomicsDB; 70763; -. [Q8IVS8-6]
DR ProteomicsDB; 70764; -. [Q8IVS8-7]
DR Antibodypedia; 1847; 275 antibodies from 30 providers.
DR DNASU; 132158; -.
DR Ensembl; ENST00000305690.12; ENSP00000301965.9; ENSG00000168237.18. [Q8IVS8-2]
DR Ensembl; ENST00000436784.7; ENSP00000389175.2; ENSG00000168237.18. [Q8IVS8-1]
DR Ensembl; ENST00000473032.5; ENSP00000418951.1; ENSG00000168237.18. [Q8IVS8-7]
DR Ensembl; ENST00000477382.1; ENSP00000419008.1; ENSG00000168237.18. [Q8IVS8-2]
DR GeneID; 132158; -.
DR KEGG; hsa:132158; -.
DR MANE-Select; ENST00000436784.7; ENSP00000389175.2; NM_145262.4; NP_660305.2.
DR UCSC; uc003ddo.4; human. [Q8IVS8-1]
DR CTD; 132158; -.
DR DisGeNET; 132158; -.
DR GeneCards; GLYCTK; -.
DR HGNC; HGNC:24247; GLYCTK.
DR HPA; ENSG00000168237; Tissue enriched (liver).
DR MalaCards; GLYCTK; -.
DR MIM; 220120; phenotype.
DR MIM; 610516; gene.
DR neXtProt; NX_Q8IVS8; -.
DR OpenTargets; ENSG00000168237; -.
DR Orphanet; 941; D-glyceric aciduria.
DR PharmGKB; PA162389865; -.
DR VEuPathDB; HostDB:ENSG00000168237; -.
DR eggNOG; KOG3935; Eukaryota.
DR GeneTree; ENSGT00390000014365; -.
DR HOGENOM; CLU_112512_0_0_1; -.
DR InParanoid; Q8IVS8; -.
DR OMA; GKAAWRM; -.
DR OrthoDB; 1371490at2759; -.
DR PhylomeDB; Q8IVS8; -.
DR TreeFam; TF313770; -.
DR BRENDA; 2.7.1.31; 2681.
DR PathwayCommons; Q8IVS8; -.
DR Reactome; R-HSA-70350; Fructose catabolism.
DR SABIO-RK; Q8IVS8; -.
DR SignaLink; Q8IVS8; -.
DR BioGRID-ORCS; 132158; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; GLYCTK; human.
DR GenomeRNAi; 132158; -.
DR Pharos; Q8IVS8; Tbio.
DR PRO; PR:Q8IVS8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8IVS8; protein.
DR Bgee; ENSG00000168237; Expressed in right lobe of liver and 108 other tissues.
DR ExpressionAtlas; Q8IVS8; baseline and differential.
DR Genevisible; Q8IVS8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008887; F:glycerate kinase activity; IDA:UniProtKB.
DR GO; GO:0061624; P:fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate; TAS:Reactome.
DR GO; GO:0006468; P:protein phosphorylation; IDA: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 Alternative splicing; ATP-binding; Cytoplasm; Disease variant; Kinase;
KW Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..523
FT /note="Glycerate kinase"
FT /id="PRO_0000287192"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..336
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15498874, ECO:0000303|Ref.5"
FT /id="VSP_025356"
FT VAR_SEQ 1..127
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025357"
FT VAR_SEQ 119..184
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025358"
FT VAR_SEQ 178..205
FT /note="GGSALLPAPIPPVTLEEKQTLTRLLAAR -> WGTPAAHRDDRYQCHGHPPL
FT VPAASVMA (in isoform 7)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025359"
FT VAR_SEQ 179..234
FT /note="GSALLPAPIPPVTLEEKQTLTRLLAARGATIQELNTIRKALSQLKGGGLAQA
FT AYPA -> EPHPVRCGGGPCGGDCQWPHRGQFPQCARLPAYPQSLRPPCSPATFCEDCA
FT VSGRL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16753811"
FT /id="VSP_025360"
FT VAR_SEQ 206..523
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025361"
FT VAR_SEQ 235..523
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16753811"
FT /id="VSP_025362"
FT VAR_SEQ 340..367
FT /note="DVKSMAQFYGLLAHVARTRLTPSMAGAS -> WGTPAAHRDDRYQCHGHPPL
FT VPAASVMA (in isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_025363"
FT VAR_SEQ 340..367
FT /note="DVKSMAQFYGLLAHVARTRLTPSMAGAS -> WGTPAAHRDDRYQCHGHPPI
FT VPAASVMA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025364"
FT VAR_SEQ 368..523
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.5"
FT /id="VSP_025365"
FT VARIANT 27
FT /note="R -> C (in dbSNP:rs34502608)"
FT /id="VAR_061205"
FT VARIANT 170
FT /note="L -> V (in dbSNP:rs35130772)"
FT /id="VAR_032285"
FT VARIANT 394
FT /note="T -> I (in dbSNP:rs9813489)"
FT /id="VAR_032286"
FT VARIANT 493
FT /note="F -> C (in D-GA; the mutant protein is not expressed
FT and has no enzymatic activity; dbSNP:rs121909448)"
FT /evidence="ECO:0000269|PubMed:20949620"
FT /id="VAR_065909"
FT CONFLICT 144
FT /note="D -> Y (in Ref. 1; AAP51132)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="V -> E (in Ref. 4; BAB85018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 55253 MW; CCBEC88E8850FC11 CRC64;
MAAALQVLPR LARAPLHPLL WRGSVARLAS SMALAEQARQ LFESAVGAVL PGPMLHRALS
LDPGGRQLKV RDRNFQLRQN LYLVGFGKAV LGMAAAAEEL LGQHLVQGVI SVPKGIRAAM
ERAGKQEMLL KPHSRVQVFE GAEDNLPDRD ALRAALAIQQ LAEGLTADDL LLVLISGGGS
ALLPAPIPPV TLEEKQTLTR LLAARGATIQ ELNTIRKALS QLKGGGLAQA AYPAQVVSLI
LSDVVGDPVE VIASGPTVAS SHNVQDCLHI LNRYGLRAAL PRSVKTVLSR ADSDPHGPHT
CGHVLNVIIG SNVLALAEAQ RQAEALGYQA VVLSAAMQGD VKSMAQFYGL LAHVARTRLT
PSMAGASVEE DAQLHELAAE LQIPDLQLEE ALETMAWGRG PVCLLAGGEP TVQLQGSGRG
GRNQELALRV GAELRRWPLG PIDVLFLSGG TDGQDGPTEA AGAWVTPELA SQAAAEGLDI
ATFLAHNDSH TFFCCLQGGA HLLHTGMTGT NVMDTHLLFL RPR
