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Q16774 (KGUA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanylate kinase

EC=2.7.4.8
Alternative name(s):
GMP kinase
Gene names
Name:GUK1
Synonyms:GMK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length197 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for recycling GMP and indirectly, cGMP.

Catalytic activity

ATP + GMP = ADP + GDP.

Subunit structure

Monomer By similarity.

Miscellaneous

In addition to phosphorylating GMP, antiviral prodrugs such as acyclovir, ganciclovir, and carbovir and anticancer prodrugs such as the thiopurines are dependent on GMPK for their activation.

Sequence similarities

Belongs to the guanylate kinase family.

Contains 1 guanylate kinase-like domain.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP metabolic process

Inferred from electronic annotation. Source: Ensembl

GDP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

GDP-mannose metabolic process

Inferred from electronic annotation. Source: Ensembl

GMP metabolic process

Inferred from electronic annotation. Source: Ensembl

dATP metabolic process

Inferred from electronic annotation. Source: Ensembl

dGDP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

dGMP metabolic process

Inferred from electronic annotation. Source: Ensembl

drug metabolic process

Traceable author statement. Source: Reactome

glycoprotein transport

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule interconversion

Traceable author statement. Source: Reactome

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

purine nucleotide metabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

guanylate kinase activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16774-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q16774-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLRRPLAGLAAAALGRAPPDGM
Isoform 3 (identifier: Q16774-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLRRPLAGLAAAALGRAPPDGM
     159-197: SKEPGLFDVV...EIKKAQRTGA → RNQESSKDRR...CCPCGWNILG
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 197196Guanylate kinase
PRO_0000170651

Regions

Domain4 – 186183Guanylate kinase-like
Nucleotide binding11 – 188ATP By similarity

Sites

Active site441 By similarity
Active site1371 By similarity
Active site1481 By similarity
Binding site1711ATP By similarity
Binding site1721ATP; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.7

Natural variations

Alternative sequence11M → MLRRPLAGLAAAALGRAPPD GM in isoform 2 and isoform 3.
VSP_043778
Alternative sequence159 – 19739SKEPG…QRTGA → RNQESSKDRRLRLAVCSRHP GPIQDQGSSIEPPPWQAIRQ LCALGQHVEWRRCCPCGWNI LG in isoform 3.
VSP_047372

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: C49573212A0DA825

FASTA19721,726
        10         20         30         40         50         60 
MSGPRPVVLS GPSGAGKSTL LKRLLQEHSG IFGFSVSHTT RNPRPGEENG KDYYFVTREV 

        70         80         90        100        110        120 
MQRDIAAGDF IEHAEFSGNL YGTSKVAVQA VQAMNRICVL DVDLQGVRNI KATDLRPIYI 

       130        140        150        160        170        180 
SVQPPSLHVL EQRLRQRNTE TEESLVKRLA AAQADMESSK EPGLFDVVII NDSLDQAYAE 

       190 
LKEALSEEIK KAQRTGA 

« Hide

Isoform 2 [UniParc].

Checksum: 6972858284006BB2
Show »

FASTA21823,782
Isoform 3 [UniParc].

Checksum: 418604D9B391F864
Show »

FASTA24126,596

References

« Hide 'large scale' references
[1]"Human guanylate kinase (GUK1): cDNA sequence, expression and chromosomal localisation."
Fitzgibbon J., Katsanis N., Wells D., Delhanty J., Vallins W., Hunt D.M.
FEBS Lett. 385:185-188(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Retina.
[2]"Cloning, characterization, and modeling of mouse and human guanylate kinases."
Brady W.A., Kokoris M.S., Fitzgibbon M., Black M.E.
J. Biol. Chem. 271:16734-16740(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Ovary.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L76200 mRNA. Translation: AAC37598.1.
U66895 mRNA. Translation: AAC50659.1.
AK303845 mRNA. Translation: BAG64788.1.
AL359510 Genomic DNA. No translation available.
CH471098 Genomic DNA. Translation: EAW69856.1.
BC006249 mRNA. Translation: AAH06249.1.
BC009914 mRNA. Translation: AAH09914.1.
PIRS68864.
RefSeqNP_000849.1. NM_000858.5.
NP_001152862.1. NM_001159390.1.
NP_001152863.1. NM_001159391.1.
NP_001229768.1. NM_001242839.1.
NP_001229769.1. NM_001242840.1.
UniGeneHs.376933.

3D structure databases

ProteinModelPortalQ16774.
SMRQ16774. Positions 5-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109242. 3 interactions.
IntActQ16774. 2 interactions.
STRING9606.ENSP00000317659.

Chemistry

ChEMBLCHEMBL4989.

PTM databases

PhosphoSiteQ16774.

Polymorphism databases

DMDM2497498.

Proteomic databases

PaxDbQ16774.
PRIDEQ16774.

Protocols and materials databases

DNASU2987.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312726; ENSP00000317659; ENSG00000143774. [Q16774-1]
ENST00000366716; ENSP00000355677; ENSG00000143774. [Q16774-1]
ENST00000366718; ENSP00000355679; ENSG00000143774. [Q16774-1]
ENST00000366726; ENSP00000355687; ENSG00000143774. [Q16774-1]
ENST00000366728; ENSP00000355689; ENSG00000143774. [Q16774-3]
ENST00000366730; ENSP00000355691; ENSG00000143774. [Q16774-1]
ENST00000391865; ENSP00000375738; ENSG00000143774. [Q16774-2]
GeneID2987.
KEGGhsa:2987.
UCSCuc001hsh.3. human. [Q16774-1]
uc001hsi.3. human. [Q16774-2]

Organism-specific databases

CTD2987.
GeneCardsGC01P228327.
HGNCHGNC:4693. GUK1.
HPAHPA028118.
HPA048587.
MIM139270. gene.
neXtProtNX_Q16774.
PharmGKBPA29072.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0194.
HOGENOMHOG000037640.
HOVERGENHBG003344.
KOK00942.
OrthoDBEOG7J1814.
PhylomeDBQ16774.
TreeFamTF314473.

Enzyme and pathway databases

BioCycMetaCyc:HS07104-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ16774.

Gene expression databases

ArrayExpressQ16774.
BgeeQ16774.
CleanExHS_GUK1.
GenevestigatorQ16774.

Family and domain databases

Gene3D3.40.50.300. 3 hits.
InterProIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR03263. guanyl_kin. 1 hit.
PROSITEPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGUK1. human.
GeneWikiGUK1.
GenomeRNAi2987.
NextBio11844.
PROQ16774.
SOURCESearch...

Entry information

Entry nameKGUA_HUMAN
AccessionPrimary (citable) accession number: Q16774
Secondary accession number(s): B1ANH1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM