KGUA_HUMAN
ID KGUA_HUMAN Reviewed; 197 AA.
AC Q16774; B1ANH1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Guanylate kinase;
DE EC=2.7.4.8 {ECO:0000269|PubMed:31201273};
DE AltName: Full=GMP kinase;
DE AltName: Full=Guanylate kinase 1 {ECO:0000312|HGNC:HGNC:4693};
GN Name=GUK1 {ECO:0000303|PubMed:8647247, ECO:0000312|HGNC:HGNC:4693};
GN Synonyms=GMK, GMPK {ECO:0000303|PubMed:31201273};
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] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=8647247; DOI=10.1016/0014-5793(96)00365-1;
RA Fitzgibbon J., Katsanis N., Wells D., Delhanty J., Vallins W., Hunt D.M.;
RT "Human guanylate kinase (GUK1): cDNA sequence, expression and chromosomal
RT localisation.";
RL FEBS Lett. 385:185-188(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8663313; DOI=10.1074/jbc.271.28.16734;
RA Brady W.A., Kokoris M.S., Fitzgibbon M., Black M.E.;
RT "Cloning, characterization, and modeling of mouse and human guanylate
RT kinases.";
RL J. Biol. Chem. 271:16734-16740(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 FUNCTION AS DRUG-METABOLIZING ENZYME.
RX PubMed=197968; DOI=10.1016/0006-2952(77)90071-5;
RA Miller R.L., Adamczyk D.L., Spector T.;
RT "Reassessment of the interactions of guanylate kinase and 6-thioguanosine
RT 5'-phosphate.";
RL Biochem. Pharmacol. 26:1573-1576(1977).
RN [8]
RP FUNCTION AS DRUG-METABOLIZING ENZYME.
RX PubMed=6248551; DOI=10.1016/s0021-9258(20)79686-9;
RA Miller W.H., Miller R.L.;
RT "Phosphorylation of acyclovir (acycloguanosine) monophosphate by GMP
RT kinase.";
RL J. Biol. Chem. 255:7204-7207(1980).
RN [9]
RP FUNCTION AS DRUG-METABOLIZING ENZYME.
RX PubMed=6306664; DOI=10.1073/pnas.80.13.4139;
RA Field A.K., Davies M.E., DeWitt C., Perry H.C., Liou R., Germershausen J.,
RA Karkas J.D., Ashton W.T., Johnston D.B., Tolman R.L.;
RT "9-([2-hydroxy-1-(hydroxymethyl)ethoxy]methyl)guanine: a selective
RT inhibitor of herpes group virus replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4139-4143(1983).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY 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).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP INTERACTION WITH RD3.
RX PubMed=29515371; DOI=10.3389/fnmol.2018.00052;
RA Wimberg H., Janssen-Bienhold U., Koch K.W.;
RT "Control of the Nucleotide Cycle in Photoreceptor Cell Extracts by Retinal
RT Degeneration Protein 3.";
RL Front. Mol. Neurosci. 11:52-52(2018).
RN [15]
RP STRUCTURE BY NMR, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP SER-2; GLY-3; LEU-25; VAL-91; ARG-96; ARG-116; SER-121 AND SER-186, AND
RP SUBUNIT.
RX PubMed=31201273; DOI=10.1074/jbc.ra119.009251;
RA Khan N., Shah P.P., Ban D., Trigo-Mourino P., Carneiro M.G., DeLeeuw L.,
RA Dean W.L., Trent J.O., Beverly L.J., Konrad M., Lee D., Sabo T.M.;
RT "Solution structure and functional investigation of human guanylate kinase
RT reveals allosteric networking and a crucial role for the enzyme in
RT cancer.";
RL J. Biol. Chem. 294:11920-11933(2019).
CC -!- FUNCTION: Catalyzes the phosphorylation of GMP to GDP. Essential enzyme
CC for recycling GMP and indirectly, cyclic GMP (cGMP) (PubMed:31201273).
CC Involved in the cGMP metabolism in photoreceptors (By similarity). It
CC may also have a role in the survival and growth progression of some
CC tumors (PubMed:31201273). In addition to its physiological role, GUK1
CC is essential for convert prodrugs used for the treatment of cancers and
CC viral infections into their pharmacologically active metabolites, most
CC notably acyclovir, ganciclovir, and 6-thioguanine and its closely
CC related analog 6-mercaptopurine (PubMed:197968, PubMed:6248551,
CC PubMed:6306664). {ECO:0000250|UniProtKB:P46195,
CC ECO:0000269|PubMed:197968, ECO:0000269|PubMed:31201273,
CC ECO:0000269|PubMed:6248551, ECO:0000269|PubMed:6306664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GMP = ADP + GDP; Xref=Rhea:RHEA:20780,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:456216; EC=2.7.4.8;
CC Evidence={ECO:0000269|PubMed:31201273};
CC -!- ACTIVITY REGULATION: Up-regulated by RD3.
CC {ECO:0000250|UniProtKB:P46195}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20.7 uM for GMP {ECO:0000269|PubMed:31201273};
CC Note=kcat is 58.5 sec(-1) with GMP as substrate.
CC {ECO:0000269|PubMed:31201273};
CC -!- SUBUNIT: Monomer (PubMed:31201273). Interacts with RD3
CC (PubMed:29515371). {ECO:0000269|PubMed:29515371,
CC ECO:0000269|PubMed:31201273}.
CC -!- SUBCELLULAR LOCATION: Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:Q64520}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q64520}. Note=Colocalizes with RD3 in
CC photoreceptor inner segments and to a lesser extent in the outer
CC plexiform layer. {ECO:0000250|UniProtKB:Q64520}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q16774-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16774-2; Sequence=VSP_043778;
CC Name=3;
CC IsoId=Q16774-3; Sequence=VSP_043778, VSP_047372;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8663313}.
CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
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DR EMBL; L76200; AAC37598.1; -; mRNA.
DR EMBL; U66895; AAC50659.1; -; mRNA.
DR EMBL; AK303845; BAG64788.1; -; mRNA.
DR EMBL; AL359510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471098; EAW69856.1; -; Genomic_DNA.
DR EMBL; BC006249; AAH06249.1; -; mRNA.
DR EMBL; BC009914; AAH09914.1; -; mRNA.
DR CCDS; CCDS1568.1; -. [Q16774-1]
DR CCDS; CCDS53481.1; -. [Q16774-2]
DR CCDS; CCDS55689.1; -. [Q16774-3]
DR PIR; S68864; S68864.
DR RefSeq; NP_000849.1; NM_000858.5. [Q16774-1]
DR RefSeq; NP_001152862.1; NM_001159390.1. [Q16774-2]
DR RefSeq; NP_001152863.1; NM_001159391.1. [Q16774-1]
DR RefSeq; NP_001229768.1; NM_001242839.1. [Q16774-1]
DR RefSeq; NP_001229769.1; NM_001242840.1. [Q16774-3]
DR PDB; 6NUI; NMR; -; A=1-197.
DR PDBsum; 6NUI; -.
DR AlphaFoldDB; Q16774; -.
DR SMR; Q16774; -.
DR BioGRID; 109242; 48.
DR IntAct; Q16774; 8.
DR STRING; 9606.ENSP00000355689; -.
DR ChEMBL; CHEMBL4989; -.
DR DrugBank; DB00787; Acyclovir.
DR DrugBank; DB01972; Guanosine-5'-Monophosphate.
DR DrugBank; DB00577; Valaciclovir.
DR iPTMnet; Q16774; -.
DR MetOSite; Q16774; -.
DR PhosphoSitePlus; Q16774; -.
DR BioMuta; GUK1; -.
DR DMDM; 2497498; -.
DR EPD; Q16774; -.
DR jPOST; Q16774; -.
DR MassIVE; Q16774; -.
DR MaxQB; Q16774; -.
DR PaxDb; Q16774; -.
DR PeptideAtlas; Q16774; -.
DR PRIDE; Q16774; -.
DR ProteomicsDB; 3255; -.
DR ProteomicsDB; 61062; -. [Q16774-1]
DR ProteomicsDB; 61063; -. [Q16774-2]
DR Antibodypedia; 34661; 257 antibodies from 23 providers.
DR DNASU; 2987; -.
DR Ensembl; ENST00000312726.9; ENSP00000317659.4; ENSG00000143774.17. [Q16774-1]
DR Ensembl; ENST00000366716.1; ENSP00000355677.1; ENSG00000143774.17. [Q16774-1]
DR Ensembl; ENST00000366718.5; ENSP00000355679.1; ENSG00000143774.17. [Q16774-1]
DR Ensembl; ENST00000366726.5; ENSP00000355687.1; ENSG00000143774.17. [Q16774-1]
DR Ensembl; ENST00000366728.6; ENSP00000355689.2; ENSG00000143774.17. [Q16774-3]
DR Ensembl; ENST00000366730.5; ENSP00000355691.1; ENSG00000143774.17. [Q16774-1]
DR Ensembl; ENST00000391865.7; ENSP00000375738.3; ENSG00000143774.17. [Q16774-2]
DR GeneID; 2987; -.
DR KEGG; hsa:2987; -.
DR MANE-Select; ENST00000312726.9; ENSP00000317659.4; NM_000858.7; NP_000849.1.
DR UCSC; uc001hsi.4; human. [Q16774-1]
DR CTD; 2987; -.
DR DisGeNET; 2987; -.
DR GeneCards; GUK1; -.
DR HGNC; HGNC:4693; GUK1.
DR HPA; ENSG00000143774; Low tissue specificity.
DR MIM; 139270; gene.
DR neXtProt; NX_Q16774; -.
DR OpenTargets; ENSG00000143774; -.
DR PharmGKB; PA29072; -.
DR VEuPathDB; HostDB:ENSG00000143774; -.
DR eggNOG; KOG0707; Eukaryota.
DR GeneTree; ENSGT00940000155815; -.
DR HOGENOM; CLU_001715_0_2_1; -.
DR InParanoid; Q16774; -.
DR OMA; EWAVVHG; -.
DR PhylomeDB; Q16774; -.
DR TreeFam; TF314473; -.
DR BioCyc; MetaCyc:HS07104-MON; -.
DR BRENDA; 2.7.4.8; 2681.
DR PathwayCommons; Q16774; -.
DR Reactome; R-HSA-2161541; Abacavir metabolism.
DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-HSA-9748787; Azathioprine ADME.
DR SABIO-RK; Q16774; -.
DR SignaLink; Q16774; -.
DR BioGRID-ORCS; 2987; 725 hits in 1055 CRISPR screens.
DR ChiTaRS; GUK1; human.
DR GeneWiki; GUK1; -.
DR GenomeRNAi; 2987; -.
DR Pharos; Q16774; Tbio.
DR PRO; PR:Q16774; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q16774; protein.
DR Bgee; ENSG00000143774; Expressed in right frontal lobe and 210 other tissues.
DR ExpressionAtlas; Q16774; baseline and differential.
DR Genevisible; Q16774; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004385; F:guanylate kinase activity; IDA:UniProtKB.
DR GO; GO:0006185; P:dGDP biosynthetic process; IMP:UniProtKB.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IDA:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR017665; Guanylate_kinase.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00625; Guanylate_kin; 1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03263; guanyl_kin; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..197
FT /note="Guanylate kinase"
FT /id="PRO_0000170651"
FT DOMAIN 4..186
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT ACT_SITE 44
FT /evidence="ECO:0000250|UniProtKB:Q64520"
FT ACT_SITE 137
FT /evidence="ECO:0000250|UniProtKB:Q64520"
FT ACT_SITE 148
FT /evidence="ECO:0000250|UniProtKB:Q64520"
FT BINDING 14..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q64520"
FT BINDING 37..51
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q64520"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q64520"
FT BINDING 171..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q64520"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 1
FT /note="M -> MLRRPLAGLAAAALGRAPPDGM (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043778"
FT VAR_SEQ 159..197
FT /note="SKEPGLFDVVIINDSLDQAYAELKEALSEEIKKAQRTGA -> RNQESSKDR
FT RLRLAVCSRHPGPIQDQGSSIEPPPWQAIRQLCALGQHVEWRRCCPCGWNILG (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047372"
FT MUTAGEN 2
FT /note="S->L: Increases in kcat with GMP as substrate."
FT /evidence="ECO:0000269|PubMed:31201273"
FT MUTAGEN 3
FT /note="G->A: Increases in kcat with GMP as substrate."
FT /evidence="ECO:0000269|PubMed:31201273"
FT MUTAGEN 25
FT /note="L->P: Leads to aggregation. Increases in kcat with
FT GMP as substrate."
FT /evidence="ECO:0000269|PubMed:31201273"
FT MUTAGEN 91
FT /note="V->M: Increases in kcat with GMP as substrate."
FT /evidence="ECO:0000269|PubMed:31201273"
FT MUTAGEN 96
FT /note="R->H: Increases in kcat with GMP as substrate."
FT /evidence="ECO:0000269|PubMed:31201273"
FT MUTAGEN 116
FT /note="R->Q: Increases in kcat with GMP as substrate."
FT /evidence="ECO:0000269|PubMed:31201273"
FT MUTAGEN 121
FT /note="S->F: Increases in kcat with GMP as substrate."
FT /evidence="ECO:0000269|PubMed:31201273"
FT MUTAGEN 186
FT /note="S->Y: Increases in kcat with GMP as substrate."
FT /evidence="ECO:0000269|PubMed:31201273"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:6NUI"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6NUI"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:6NUI"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:6NUI"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6NUI"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6NUI"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6NUI"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:6NUI"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:6NUI"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6NUI"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:6NUI"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:6NUI"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:6NUI"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:6NUI"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:6NUI"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:6NUI"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:6NUI"
FT HELIX 142..158
FT /evidence="ECO:0007829|PDB:6NUI"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:6NUI"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6NUI"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:6NUI"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:6NUI"
SQ SEQUENCE 197 AA; 21726 MW; C49573212A0DA825 CRC64;
MSGPRPVVLS GPSGAGKSTL LKRLLQEHSG IFGFSVSHTT RNPRPGEENG KDYYFVTREV
MQRDIAAGDF IEHAEFSGNL YGTSKVAVQA VQAMNRICVL DVDLQGVRNI KATDLRPIYI
SVQPPSLHVL EQRLRQRNTE TEESLVKRLA AAQADMESSK EPGLFDVVII NDSLDQAYAE
LKEALSEEIK KAQRTGA
