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Q16774

- KGUA_HUMAN

UniProt

Q16774 - KGUA_HUMAN

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Protein
Guanylate kinase
Gene
GUK1, GMK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Essential for recycling GMP and indirectly, cGMP.

Catalytic activityi

ATP + GMP = ADP + GDP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei44 – 441 By similarity
Active sitei137 – 1371 By similarity
Active sitei148 – 1481 By similarity
Binding sitei171 – 1711ATP By similarity
Binding sitei172 – 1721ATP; via carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 188ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. guanylate kinase activity Source: UniProtKB

GO - Biological processi

  1. ATP metabolic process Source: Ensembl
  2. GDP biosynthetic process Source: Ensembl
  3. GDP-mannose metabolic process Source: Ensembl
  4. GMP metabolic process Source: Ensembl
  5. dATP metabolic process Source: Ensembl
  6. dGDP biosynthetic process Source: Ensembl
  7. dGMP metabolic process Source: Ensembl
  8. drug metabolic process Source: Reactome
  9. glycoprotein transport Source: Ensembl
  10. nucleobase-containing small molecule interconversion Source: Reactome
  11. nucleobase-containing small molecule metabolic process Source: Reactome
  12. purine nucleotide metabolic process Source: UniProtKB
  13. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS07104-MONOMER.
ReactomeiREACT_121388. Abacavir metabolism.
REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKQ16774.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate kinase (EC:2.7.4.8)
Alternative name(s):
GMP kinase
Gene namesi
Name:GUK1
Synonyms:GMK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:4693. GUK1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29072.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 197196Guanylate kinase
PRO_0000170651Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ16774.
PaxDbiQ16774.
PRIDEiQ16774.

PTM databases

PhosphoSiteiQ16774.

Expressioni

Gene expression databases

ArrayExpressiQ16774.
BgeeiQ16774.
CleanExiHS_GUK1.
GenevestigatoriQ16774.

Organism-specific databases

HPAiHPA028118.
HPA048587.

Interactioni

Subunit structurei

Monomer By similarity.

Protein-protein interaction databases

BioGridi109242. 3 interactions.
IntActiQ16774. 2 interactions.
STRINGi9606.ENSP00000317659.

Structurei

3D structure databases

ProteinModelPortaliQ16774.
SMRiQ16774. Positions 5-193.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 186183Guanylate kinase-like
Add
BLAST

Sequence similaritiesi

Belongs to the guanylate kinase family.

Phylogenomic databases

eggNOGiCOG0194.
HOGENOMiHOG000037640.
HOVERGENiHBG003344.
KOiK00942.
OrthoDBiEOG7J1814.
PhylomeDBiQ16774.
TreeFamiTF314473.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03263. guanyl_kin. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16774-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSGPRPVVLS GPSGAGKSTL LKRLLQEHSG IFGFSVSHTT RNPRPGEENG    50
KDYYFVTREV MQRDIAAGDF IEHAEFSGNL YGTSKVAVQA VQAMNRICVL 100
DVDLQGVRNI KATDLRPIYI SVQPPSLHVL EQRLRQRNTE TEESLVKRLA 150
AAQADMESSK EPGLFDVVII NDSLDQAYAE LKEALSEEIK KAQRTGA 197
Length:197
Mass (Da):21,726
Last modified:January 23, 2007 - v2
Checksum:iC49573212A0DA825
GO
Isoform 2 (identifier: Q16774-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLRRPLAGLAAAALGRAPPDGM

Show »
Length:218
Mass (Da):23,782
Checksum:i6972858284006BB2
GO
Isoform 3 (identifier: Q16774-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:241
Mass (Da):26,596
Checksum:i418604D9B391F864
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MLRRPLAGLAAAALGRAPPD GM in isoform 2 and isoform 3.
VSP_043778
Alternative sequencei159 – 19739SKEPG…QRTGA → RNQESSKDRRLRLAVCSRHP GPIQDQGSSIEPPPWQAIRQ LCALGQHVEWRRCCPCGWNI LG in isoform 3.
VSP_047372Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1568.1. [Q16774-1]
CCDS53481.1. [Q16774-2]
CCDS55689.1. [Q16774-3]
PIRiS68864.
RefSeqiNP_000849.1. NM_000858.5. [Q16774-1]
NP_001152862.1. NM_001159390.1. [Q16774-2]
NP_001152863.1. NM_001159391.1. [Q16774-1]
NP_001229768.1. NM_001242839.1. [Q16774-1]
NP_001229769.1. NM_001242840.1. [Q16774-3]
UniGeneiHs.376933.

Genome annotation databases

EnsembliENST00000312726; 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]
GeneIDi2987.
KEGGihsa:2987.
UCSCiuc001hsh.3. human. [Q16774-1]
uc001hsi.3. human. [Q16774-2]

Polymorphism databases

DMDMi2497498.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1568.1. [Q16774-1 ]
CCDS53481.1. [Q16774-2 ]
CCDS55689.1. [Q16774-3 ]
PIRi S68864.
RefSeqi NP_000849.1. NM_000858.5. [Q16774-1 ]
NP_001152862.1. NM_001159390.1. [Q16774-2 ]
NP_001152863.1. NM_001159391.1. [Q16774-1 ]
NP_001229768.1. NM_001242839.1. [Q16774-1 ]
NP_001229769.1. NM_001242840.1. [Q16774-3 ]
UniGenei Hs.376933.

3D structure databases

ProteinModelPortali Q16774.
SMRi Q16774. Positions 5-193.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109242. 3 interactions.
IntActi Q16774. 2 interactions.
STRINGi 9606.ENSP00000317659.

Chemistry

ChEMBLi CHEMBL4989.

PTM databases

PhosphoSitei Q16774.

Polymorphism databases

DMDMi 2497498.

Proteomic databases

MaxQBi Q16774.
PaxDbi Q16774.
PRIDEi Q16774.

Protocols and materials databases

DNASUi 2987.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000312726 ; 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 ]
GeneIDi 2987.
KEGGi hsa:2987.
UCSCi uc001hsh.3. human. [Q16774-1 ]
uc001hsi.3. human. [Q16774-2 ]

Organism-specific databases

CTDi 2987.
GeneCardsi GC01P228327.
HGNCi HGNC:4693. GUK1.
HPAi HPA028118.
HPA048587.
MIMi 139270. gene.
neXtProti NX_Q16774.
PharmGKBi PA29072.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0194.
HOGENOMi HOG000037640.
HOVERGENi HBG003344.
KOi K00942.
OrthoDBi EOG7J1814.
PhylomeDBi Q16774.
TreeFami TF314473.

Enzyme and pathway databases

BioCyci MetaCyc:HS07104-MONOMER.
Reactomei REACT_121388. Abacavir metabolism.
REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RK Q16774.

Miscellaneous databases

ChiTaRSi GUK1. human.
GeneWikii GUK1.
GenomeRNAii 2987.
NextBioi 11844.
PROi Q16774.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16774.
Bgeei Q16774.
CleanExi HS_GUK1.
Genevestigatori Q16774.

Family and domain databases

Gene3Di 3.40.50.300. 3 hits.
InterProi IPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00625. Guanylate_kin. 1 hit.
[Graphical view ]
SMARTi SM00072. GuKc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR03263. guanyl_kin. 1 hit.
PROSITEi PS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKGUA_HUMAN
AccessioniPrimary (citable) accession number: Q16774
Secondary accession number(s): B1ANH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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