Full text data of GUK1
GUK1
(GMK)
[Confidence: low (only semi-automatic identification from reviews)]
Guanylate kinase; 2.7.4.8 (GMP kinase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Guanylate kinase; 2.7.4.8 (GMP kinase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q16774
ID KGUA_HUMAN Reviewed; 197 AA.
AC Q16774; B1ANH1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Guanylate kinase;
DE EC=2.7.4.8;
DE AltName: Full=GMP kinase;
GN Name=GUK1; Synonyms=GMK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Hunt D.M.;
RT "Human guanylate kinase (GUK1): cDNA sequence, expression and
RT chromosomal localisation.";
RL FEBS Lett. 385:185-188(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC -!- CATALYTIC ACTIVITY: ATP + GMP = ADP + GDP.
CC -!- SUBUNIT: Monomer (By similarity).
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 Note=Gene prediction based on EST data;
CC -!- MISCELLANEOUS: In addition to phosphorylating GMP, antiviral
CC prodrugs such as acyclovir, ganciclovir, and carbovir and
CC anticancer prodrugs such as the thiopurines are dependent on GMPK
CC for their activation.
CC -!- SIMILARITY: Belongs to the guanylate kinase family.
CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
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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 PIR; S68864; S68864.
DR RefSeq; NP_000849.1; NM_000858.5.
DR RefSeq; NP_001152862.1; NM_001159390.1.
DR RefSeq; NP_001152863.1; NM_001159391.1.
DR RefSeq; NP_001229768.1; NM_001242839.1.
DR RefSeq; NP_001229769.1; NM_001242840.1.
DR UniGene; Hs.376933; -.
DR ProteinModelPortal; Q16774; -.
DR SMR; Q16774; 5-193.
DR IntAct; Q16774; 2.
DR STRING; 9606.ENSP00000317659; -.
DR ChEMBL; CHEMBL4989; -.
DR PhosphoSite; Q16774; -.
DR DMDM; 2497498; -.
DR PaxDb; Q16774; -.
DR PRIDE; Q16774; -.
DR DNASU; 2987; -.
DR Ensembl; ENST00000312726; ENSP00000317659; ENSG00000143774.
DR Ensembl; ENST00000366716; ENSP00000355677; ENSG00000143774.
DR Ensembl; ENST00000366718; ENSP00000355679; ENSG00000143774.
DR Ensembl; ENST00000366726; ENSP00000355687; ENSG00000143774.
DR Ensembl; ENST00000366728; ENSP00000355689; ENSG00000143774.
DR Ensembl; ENST00000366730; ENSP00000355691; ENSG00000143774.
DR Ensembl; ENST00000391865; ENSP00000375738; ENSG00000143774.
DR GeneID; 2987; -.
DR KEGG; hsa:2987; -.
DR UCSC; uc021pkf.1; human.
DR CTD; 2987; -.
DR GeneCards; GC01P228327; -.
DR HGNC; HGNC:4693; GUK1.
DR HPA; HPA048587; -.
DR MIM; 139270; gene.
DR neXtProt; NX_Q16774; -.
DR PharmGKB; PA29072; -.
DR eggNOG; COG0194; -.
DR HOGENOM; HOG000037640; -.
DR HOVERGEN; HBG003344; -.
DR KO; K00942; -.
DR OrthoDB; EOG7J1814; -.
DR PhylomeDB; Q16774; -.
DR BioCyc; MetaCyc:HS07104-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; Q16774; -.
DR ChiTaRS; GUK1; human.
DR GeneWiki; GUK1; -.
DR GenomeRNAi; 2987; -.
DR NextBio; 11844; -.
DR PRO; PR:Q16774; -.
DR ArrayExpress; Q16774; -.
DR Bgee; Q16774; -.
DR CleanEx; HS_GUK1; -.
DR Genevestigator; Q16774; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004385; F:guanylate kinase activity; IDA:UniProtKB.
DR GO; GO:0017144; P:drug metabolic process; TAS:Reactome.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IDA:UniProtKB.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like.
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 Acetylation; Alternative splicing; ATP-binding; Complete proteome;
KW Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 197 Guanylate kinase.
FT /FTId=PRO_0000170651.
FT DOMAIN 4 186 Guanylate kinase-like.
FT NP_BIND 11 18 ATP (By similarity).
FT ACT_SITE 44 44 By similarity.
FT ACT_SITE 137 137 By similarity.
FT ACT_SITE 148 148 By similarity.
FT BINDING 171 171 ATP (By similarity).
FT BINDING 172 172 ATP; via carbonyl oxygen (By similarity).
FT MOD_RES 2 2 N-acetylserine.
FT VAR_SEQ 1 1 M -> MLRRPLAGLAAAALGRAPPDGM (in isoform 2
FT and isoform 3).
FT /FTId=VSP_043778.
FT VAR_SEQ 159 197 SKEPGLFDVVIINDSLDQAYAELKEALSEEIKKAQRTGA
FT -> RNQESSKDRRLRLAVCSRHPGPIQDQGSSIEPPPWQAI
FT RQLCALGQHVEWRRCCPCGWNILG (in isoform 3).
FT /FTId=VSP_047372.
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
//
ID KGUA_HUMAN Reviewed; 197 AA.
AC Q16774; B1ANH1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Guanylate kinase;
DE EC=2.7.4.8;
DE AltName: Full=GMP kinase;
GN Name=GUK1; Synonyms=GMK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Hunt D.M.;
RT "Human guanylate kinase (GUK1): cDNA sequence, expression and
RT chromosomal localisation.";
RL FEBS Lett. 385:185-188(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC -!- CATALYTIC ACTIVITY: ATP + GMP = ADP + GDP.
CC -!- SUBUNIT: Monomer (By similarity).
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 Note=Gene prediction based on EST data;
CC -!- MISCELLANEOUS: In addition to phosphorylating GMP, antiviral
CC prodrugs such as acyclovir, ganciclovir, and carbovir and
CC anticancer prodrugs such as the thiopurines are dependent on GMPK
CC for their activation.
CC -!- SIMILARITY: Belongs to the guanylate kinase family.
CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
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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 PIR; S68864; S68864.
DR RefSeq; NP_000849.1; NM_000858.5.
DR RefSeq; NP_001152862.1; NM_001159390.1.
DR RefSeq; NP_001152863.1; NM_001159391.1.
DR RefSeq; NP_001229768.1; NM_001242839.1.
DR RefSeq; NP_001229769.1; NM_001242840.1.
DR UniGene; Hs.376933; -.
DR ProteinModelPortal; Q16774; -.
DR SMR; Q16774; 5-193.
DR IntAct; Q16774; 2.
DR STRING; 9606.ENSP00000317659; -.
DR ChEMBL; CHEMBL4989; -.
DR PhosphoSite; Q16774; -.
DR DMDM; 2497498; -.
DR PaxDb; Q16774; -.
DR PRIDE; Q16774; -.
DR DNASU; 2987; -.
DR Ensembl; ENST00000312726; ENSP00000317659; ENSG00000143774.
DR Ensembl; ENST00000366716; ENSP00000355677; ENSG00000143774.
DR Ensembl; ENST00000366718; ENSP00000355679; ENSG00000143774.
DR Ensembl; ENST00000366726; ENSP00000355687; ENSG00000143774.
DR Ensembl; ENST00000366728; ENSP00000355689; ENSG00000143774.
DR Ensembl; ENST00000366730; ENSP00000355691; ENSG00000143774.
DR Ensembl; ENST00000391865; ENSP00000375738; ENSG00000143774.
DR GeneID; 2987; -.
DR KEGG; hsa:2987; -.
DR UCSC; uc021pkf.1; human.
DR CTD; 2987; -.
DR GeneCards; GC01P228327; -.
DR HGNC; HGNC:4693; GUK1.
DR HPA; HPA048587; -.
DR MIM; 139270; gene.
DR neXtProt; NX_Q16774; -.
DR PharmGKB; PA29072; -.
DR eggNOG; COG0194; -.
DR HOGENOM; HOG000037640; -.
DR HOVERGEN; HBG003344; -.
DR KO; K00942; -.
DR OrthoDB; EOG7J1814; -.
DR PhylomeDB; Q16774; -.
DR BioCyc; MetaCyc:HS07104-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; Q16774; -.
DR ChiTaRS; GUK1; human.
DR GeneWiki; GUK1; -.
DR GenomeRNAi; 2987; -.
DR NextBio; 11844; -.
DR PRO; PR:Q16774; -.
DR ArrayExpress; Q16774; -.
DR Bgee; Q16774; -.
DR CleanEx; HS_GUK1; -.
DR Genevestigator; Q16774; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004385; F:guanylate kinase activity; IDA:UniProtKB.
DR GO; GO:0017144; P:drug metabolic process; TAS:Reactome.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IDA:UniProtKB.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like.
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 Acetylation; Alternative splicing; ATP-binding; Complete proteome;
KW Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 197 Guanylate kinase.
FT /FTId=PRO_0000170651.
FT DOMAIN 4 186 Guanylate kinase-like.
FT NP_BIND 11 18 ATP (By similarity).
FT ACT_SITE 44 44 By similarity.
FT ACT_SITE 137 137 By similarity.
FT ACT_SITE 148 148 By similarity.
FT BINDING 171 171 ATP (By similarity).
FT BINDING 172 172 ATP; via carbonyl oxygen (By similarity).
FT MOD_RES 2 2 N-acetylserine.
FT VAR_SEQ 1 1 M -> MLRRPLAGLAAAALGRAPPDGM (in isoform 2
FT and isoform 3).
FT /FTId=VSP_043778.
FT VAR_SEQ 159 197 SKEPGLFDVVIINDSLDQAYAELKEALSEEIKKAQRTGA
FT -> RNQESSKDRRLRLAVCSRHPGPIQDQGSSIEPPPWQAI
FT RQLCALGQHVEWRRCCPCGWNILG (in isoform 3).
FT /FTId=VSP_047372.
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
//
MIM
139270
*RECORD*
*FIELD* NO
139270
*FIELD* TI
*139270 GUANYLATE KINASE 1; GUK1
;;GMP KINASE; GMK;;
ATP:GMP PHOSPHOTRANSFERASE
*FIELD* TX
read more
DESCRIPTION
Guanylate kinase (EC 2.7.4.8) catalyzes the phosphorylation of either
GMP to GDP or dGMP to dGDP and is an essential enzyme in nucleotide
metabolism pathways (summary by Brady et al., 1996).
CLONING
Brady et al. (1996) cloned human and mouse cDNAs of GUK1. They reported
that the human gene predicts a protein of 197 amino acids with a
molecular mass of 21.7 kD. They found that the 1-kb GUK1 transcript was
ubiquitously expressed.
GENE FUNCTION
Brady et al. (1996) stated that the guanylate kinases are targets for
cancer chemotherapy and are inhibited by the antitumor drug
6-thioguanine. They published a computer model of GUK1 tertiary
structure designed to be used in the development of chemotherapy drugs.
MAPPING
From cell hybridization studies, Meera Khan et al. (1974) concluded that
the GUK1 gene may be on chromosome 1. Meera Khan (1977) stated that the
genetic independence of GUK1 and GUK2 (139280) has not been established;
it might be a situation like that of fumarate hydratase in which
cytosolic and mitochondrial forms are encoded by the same gene.
Dallapiccola et al. (1980) found increased red cell GUK in a patient
with a duplication of 1q31-q43.
By fluorescence in situ hybridization, Fitzgibbon et al. (1996) mapped
the GUK1 gene to 1q32-q41.
*FIELD* RF
1. Brady, W. A.; Kokoris, M. S.; Fitzgibbon, M.; Black, M. E.: Cloning,
characterization, and modeling of mouse and human guanylate kinases. J.
Biol. Chem. 271: 16734-16740, 1996.
2. Dallapiccola, B.; Lungarotti, M. S.; Falorni, A.; Magnani, M.;
Dacha, M.: Evidence for the assignment of GUK1 gene locus to 1q32-q43
segment from gene dosage effect. Ann. Genet. 23: 83-85, 1980.
3. Fitzgibbon, J.; Katsanis, N.; Wells, D.; Delhanty, J.; Vallins,
W.; Hunt, D. M.: Human guanylate kinase (GUK1): cDNA sequence, expression
and chromosomal localisation. FEBS Lett. 385: 185-188, 1996.
4. Meera Khan, P.: Personal Communication. Leiden, The Netherlands
1977.
5. Meera Khan, P.; Doppert, B. A.; Hagemeijer, A.; Westerveld, A.
: The human loci for phosphopyruvate hydratase and guanylate kinase
are syntenic with the PGD-PGM1 linkage group in man-Chinese hamster
somatic cell hybrids. Cytogenet. Cell Genet. 13: 130-131, 1974.
*FIELD* CN
Jennifer P. Macke - updated: 6/3/1997
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 01/31/2014
psherman: 4/15/1998
alopez: 9/25/1997
dholmes: 9/10/1997
alopez: 9/10/1997
alopez: 9/9/1997
terry: 7/28/1997
warfield: 4/8/1994
carol: 7/22/1993
supermim: 3/16/1992
carol: 11/16/1990
supermim: 3/20/1990
ddp: 10/27/1989
*RECORD*
*FIELD* NO
139270
*FIELD* TI
*139270 GUANYLATE KINASE 1; GUK1
;;GMP KINASE; GMK;;
ATP:GMP PHOSPHOTRANSFERASE
*FIELD* TX
read more
DESCRIPTION
Guanylate kinase (EC 2.7.4.8) catalyzes the phosphorylation of either
GMP to GDP or dGMP to dGDP and is an essential enzyme in nucleotide
metabolism pathways (summary by Brady et al., 1996).
CLONING
Brady et al. (1996) cloned human and mouse cDNAs of GUK1. They reported
that the human gene predicts a protein of 197 amino acids with a
molecular mass of 21.7 kD. They found that the 1-kb GUK1 transcript was
ubiquitously expressed.
GENE FUNCTION
Brady et al. (1996) stated that the guanylate kinases are targets for
cancer chemotherapy and are inhibited by the antitumor drug
6-thioguanine. They published a computer model of GUK1 tertiary
structure designed to be used in the development of chemotherapy drugs.
MAPPING
From cell hybridization studies, Meera Khan et al. (1974) concluded that
the GUK1 gene may be on chromosome 1. Meera Khan (1977) stated that the
genetic independence of GUK1 and GUK2 (139280) has not been established;
it might be a situation like that of fumarate hydratase in which
cytosolic and mitochondrial forms are encoded by the same gene.
Dallapiccola et al. (1980) found increased red cell GUK in a patient
with a duplication of 1q31-q43.
By fluorescence in situ hybridization, Fitzgibbon et al. (1996) mapped
the GUK1 gene to 1q32-q41.
*FIELD* RF
1. Brady, W. A.; Kokoris, M. S.; Fitzgibbon, M.; Black, M. E.: Cloning,
characterization, and modeling of mouse and human guanylate kinases. J.
Biol. Chem. 271: 16734-16740, 1996.
2. Dallapiccola, B.; Lungarotti, M. S.; Falorni, A.; Magnani, M.;
Dacha, M.: Evidence for the assignment of GUK1 gene locus to 1q32-q43
segment from gene dosage effect. Ann. Genet. 23: 83-85, 1980.
3. Fitzgibbon, J.; Katsanis, N.; Wells, D.; Delhanty, J.; Vallins,
W.; Hunt, D. M.: Human guanylate kinase (GUK1): cDNA sequence, expression
and chromosomal localisation. FEBS Lett. 385: 185-188, 1996.
4. Meera Khan, P.: Personal Communication. Leiden, The Netherlands
1977.
5. Meera Khan, P.; Doppert, B. A.; Hagemeijer, A.; Westerveld, A.
: The human loci for phosphopyruvate hydratase and guanylate kinase
are syntenic with the PGD-PGM1 linkage group in man-Chinese hamster
somatic cell hybrids. Cytogenet. Cell Genet. 13: 130-131, 1974.
*FIELD* CN
Jennifer P. Macke - updated: 6/3/1997
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 01/31/2014
psherman: 4/15/1998
alopez: 9/25/1997
dholmes: 9/10/1997
alopez: 9/10/1997
alopez: 9/9/1997
terry: 7/28/1997
warfield: 4/8/1994
carol: 7/22/1993
supermim: 3/16/1992
carol: 11/16/1990
supermim: 3/20/1990
ddp: 10/27/1989