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Q14397

- GCKR_HUMAN

UniProt

Q14397 - GCKR_HUMAN

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Protein
Glucokinase regulatory protein
Gene
GCKR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Inhibits glucokinase (GCK) by forming an inactive complex with this enzyme. The affinity of GCKR for GCK is modulated by fructose metabolites: GCKR with bound fructose 6-phosphate has increased affinity for GCK, while GCKR with bound fructose 1-phosphate has strongly decreased affinity for GCK and does not inhibit GCK activity.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei153 – 1531Fructose 1-phosphate
Binding sitei348 – 3481Fructose 1-phosphate
Binding sitei514 – 5141Fructose 1-phosphate/Fructose 6-phosphate

GO - Molecular functioni

  1. carbohydrate binding Source: Ensembl
  2. enzyme inhibitor activity Source: Ensembl
  3. fructose-6-phosphate binding Source: UniProtKB
  4. protein binding Source: IntAct

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cellular glucose homeostasis Source: Ensembl
  3. glucose transport Source: Reactome
  4. hexose transport Source: Reactome
  5. negative regulation of glucokinase activity Source: UniProtKB
  6. positive regulation of glucokinase activity Source: Ensembl
  7. protein import into nucleus, translocation Source: BHF-UCL
  8. regulation of glucose transport Source: Reactome
  9. response to fructose Source: BHF-UCL
  10. small molecule metabolic process Source: Reactome
  11. transmembrane transport Source: Reactome
  12. triglyceride homeostasis Source: BHF-UCL
  13. urate metabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

ReactomeiREACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucokinase regulatory protein
Short name:
GKRP
Short name:
Glucokinase regulator
Gene namesi
Name:GCKR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:4196. GCKR.

Subcellular locationi

Cytoplasm. Nucleus
Note: Under low glucose concentrations, GKRP associates with GCK and the inactive complex is recruited to the hepatocyte nucleus.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. mitochondrion Source: Ensembl
  4. nucleoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi326 – 3272KK → TT: No effect on inhibition of glucokinase. 1 Publication
Mutagenesisi413 – 4131D → A: Impairs inhibition of glucokinase. 2 Publications
Mutagenesisi450 – 4512KK → TT: Impairs inhibition of glucokinase. 1 Publication
Mutagenesisi463 – 4653LLF → ALA: Abolishes interaction with GCK. Abolishes inhibition of GCK. 2 Publications

Organism-specific databases

MIMi613463. phenotype.
PharmGKBiPA28611.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 625625Glucokinase regulatory protein
PRO_0000214826Add
BLAST

Proteomic databases

PaxDbiQ14397.
PRIDEiQ14397.

PTM databases

PhosphoSiteiQ14397.

Expressioni

Tissue specificityi

Found in liver and pancreas. Not detected in muscle, brain, heart, thymus, intestine, uterus, adipose tissue, kidney, adrenal, lung or spleen.2 Publications

Gene expression databases

ArrayExpressiQ14397.
BgeeiQ14397.
CleanExiHS_GCKR.
GenevestigatoriQ14397.

Organism-specific databases

HPAiCAB034098.
HPA045855.
HPA057478.

Interactioni

Subunit structurei

Interacts (fructose 6-phosphate bound form) with GCK.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GCKP355572EBI-709948,EBI-709928

Protein-protein interaction databases

BioGridi108916. 4 interactions.
IntActiQ14397. 2 interactions.
STRINGi9606.ENSP00000264717.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 43
Helixi5 – 73
Helixi23 – 264
Helixi30 – 323
Helixi36 – 383
Helixi41 – 433
Helixi46 – 5813
Helixi59 – 613
Helixi77 – 9418
Beta strandi100 – 1078
Helixi108 – 12720
Beta strandi134 – 1385
Helixi143 – 1464
Helixi150 – 1545
Helixi156 – 16712
Beta strandi171 – 1788
Helixi185 – 19511
Turni198 – 2003
Beta strandi201 – 2066
Helixi211 – 2133
Beta strandi222 – 2243
Helixi226 – 23712
Turni238 – 2403
Beta strandi243 – 2453
Turni258 – 2603
Helixi261 – 28323
Helixi289 – 30719
Helixi310 – 32516
Beta strandi330 – 3356
Helixi337 – 35317
Beta strandi359 – 3668
Turni369 – 3713
Helixi375 – 3773
Turni378 – 3803
Helixi383 – 3853
Helixi389 – 3957
Helixi397 – 3993
Beta strandi405 – 4117
Helixi416 – 42712
Beta strandi433 – 4408
Helixi447 – 4526
Beta strandi457 – 4615
Turni467 – 4693
Helixi470 – 49526
Turni496 – 4983
Helixi513 – 52715
Helixi531 – 54313
Helixi550 – 5534
Helixi557 – 5648
Helixi570 – 58011
Helixi584 – 5929
Beta strandi594 – 5963
Helixi597 – 6059

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BB9X-ray1.47A1-625[»]
4BBAX-ray1.92A1-625[»]
4LY9X-ray2.35A/B1-625[»]
4MQUX-ray2.22A/B1-625[»]
4MROX-ray2.20A/B1-625[»]
4MSUX-ray2.50A/B1-625[»]
ProteinModelPortaliQ14397.
SMRiQ14397. Positions 6-605.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini90 – 286197SIS 1
Add
BLAST
Domaini320 – 499180SIS 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni109 – 1102Fructose 1-phosphate/Fructose 6-phosphate binding
Regioni179 – 1813Fructose 1-phosphate/Fructose 6-phosphate binding
Regioni199 – 2002Important for interaction with GCK By similarity
Regioni463 – 4653Essential for interaction with GCK

Domaini

Fructose 1-phosphate and fructose 6-phosphate compete for the same binding site.

Sequence similaritiesi

Belongs to the GCKR family.
Contains 2 SIS domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2103.
HOGENOMiHOG000031501.
HOVERGENiHBG005818.
InParanoidiQ14397.
OrthoDBiEOG7HXCRC.
PhylomeDBiQ14397.
TreeFamiTF329177.

Family and domain databases

InterProiIPR005486. Glucokinase_regulatory_CS.
IPR001347. SIS.
[Graphical view]
PROSITEiPS01272. GCKR. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14397-1) [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

MPGTKRFQHV IETPEPGKWE LSGYEAAVPI TEKSNPLTQD LDKADAENIV    50
RLLGQCDAEI FQEEGQALST YQRLYSESIL TTMVQVAGKV QEVLKEPDGG 100
LVVLSGGGTS GRMAFLMSVS FNQLMKGLGQ KPLYTYLIAG GDRSVVASRE 150
GTEDSALHGI EELKKVAAGK KRVIVIGISV GLSAPFVAGQ MDCCMNNTAV 200
FLPVLVGFNP VSMARNDPIE DWSSTFRQVA ERMQKMQEKQ KAFVLNPAIG 250
PEGLSGSSRM KGGSATKILL ETLLLAAHKT VDQGIAASQR CLLEILRTFE 300
RAHQVTYSQS PKIATLMKSV STSLEKKGHV YLVGWQTLGI IAIMDGVECI 350
HTFGADFRDV RGFLIGDHSD MFNQKAELTN QGPQFTFSQE DFLTSILPSL 400
TEIDTVVFIF TLDDNLTEVQ TIVEQVKEKT NHIQALAHST VGQTLPIPLK 450
KLFPSIISIT WPLLFFEYEG NFIQKFQREL STKWVLNTVS TGAHVLLGKI 500
LQNHMLDLRI SNSKLFWRAL AMLQRFSGQS KARCIESLLR AIHFPQPLSD 550
DIRAAPISCH VQVAHEKEQV IPIALLSLLF RCSITEAQAH LAAAPSVCEA 600
VRSALAGPGQ KRTADPLEIL EPDVQ 625
Length:625
Mass (Da):68,685
Last modified:April 5, 2011 - v6
Checksum:iDE750462AC603C80
GO
Isoform 2 (identifier: Q14397-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     144-150: SVVASRE → WLPGRRE
     151-625: Missing.

Note: No experimental confirmation available.

Show »
Length:150
Mass (Da):16,477
Checksum:iB958AFB4A930F3B1
GO

Polymorphismi

Genetic variations in GCKR define the fasting plasma glucose levels quantitative trait locus 5 (FGQTL5) [MIMi:613463]. The normal fasting plasma glucose level is defined as less than 100 mg glucose per deciliter plasma (5.55 mmol per liter). Higher fasting plasma glucose levels predict type 2 diabetes in young adults and increases the risk of mortality.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771E → G.1 Publication
Corresponds to variant rs8179206 [ dbSNP | Ensembl ].
VAR_018849
Natural varianti256 – 2561G → S.1 Publication
Corresponds to variant rs8179212 [ dbSNP | Ensembl ].
VAR_018850
Natural varianti446 – 4461P → L Associated with high triglyceride levels and low fasting plasma glucose levels; associated with a reduced risk for type 2 diabetes; the mutant protein is less efficiently regulated by physiological concentrations of fructose-6 phosphate. 5 Publications
Corresponds to variant rs1260326 [ dbSNP | Ensembl ].
VAR_008906
Natural varianti540 – 5401R → Q.1 Publication
Corresponds to variant rs8179249 [ dbSNP | Ensembl ].
VAR_018851

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei144 – 1507SVVASRE → WLPGRRE in isoform 2.
VSP_054853
Alternative sequencei151 – 625475Missing in isoform 2.
VSP_054854Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511P → V in CAB61828. 1 Publication
Sequence conflicti393 – 3931L → P in CAA88367. 1 Publication
Sequence conflicti560 – 5601H → R in CAA88367. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z48475 mRNA. Translation: CAA88367.1.
Y09593 Genomic DNA. Translation: CAA70779.2.
Y09592 Genomic DNA. Translation: CAB61828.1.
AY320034 Genomic DNA. Translation: AAP72013.1.
AK298448 mRNA. Translation: BAG60664.1.
AC074117 Genomic DNA. Translation: AAY14850.1.
BC130481 mRNA. Translation: AAI30482.1.
BC130483 mRNA. Translation: AAI30484.1.
CCDSiCCDS1757.1. [Q14397-1]
PIRiS52485.
RefSeqiNP_001477.2. NM_001486.3.
UniGeneiHs.89771.

Genome annotation databases

EnsembliENST00000264717; ENSP00000264717; ENSG00000084734.
ENST00000417872; ENSP00000398303; ENSG00000084734.
GeneIDi2646.
KEGGihsa:2646.
UCSCiuc002rky.3. human. [Q14397-1]

Polymorphism databases

DMDMi327478611.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z48475 mRNA. Translation: CAA88367.1 .
Y09593 Genomic DNA. Translation: CAA70779.2 .
Y09592 Genomic DNA. Translation: CAB61828.1 .
AY320034 Genomic DNA. Translation: AAP72013.1 .
AK298448 mRNA. Translation: BAG60664.1 .
AC074117 Genomic DNA. Translation: AAY14850.1 .
BC130481 mRNA. Translation: AAI30482.1 .
BC130483 mRNA. Translation: AAI30484.1 .
CCDSi CCDS1757.1. [Q14397-1 ]
PIRi S52485.
RefSeqi NP_001477.2. NM_001486.3.
UniGenei Hs.89771.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BB9 X-ray 1.47 A 1-625 [» ]
4BBA X-ray 1.92 A 1-625 [» ]
4LY9 X-ray 2.35 A/B 1-625 [» ]
4MQU X-ray 2.22 A/B 1-625 [» ]
4MRO X-ray 2.20 A/B 1-625 [» ]
4MSU X-ray 2.50 A/B 1-625 [» ]
ProteinModelPortali Q14397.
SMRi Q14397. Positions 6-605.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108916. 4 interactions.
IntActi Q14397. 2 interactions.
STRINGi 9606.ENSP00000264717.

Chemistry

ChEMBLi CHEMBL1075152.

PTM databases

PhosphoSitei Q14397.

Polymorphism databases

DMDMi 327478611.

Proteomic databases

PaxDbi Q14397.
PRIDEi Q14397.

Protocols and materials databases

DNASUi 2646.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264717 ; ENSP00000264717 ; ENSG00000084734 .
ENST00000417872 ; ENSP00000398303 ; ENSG00000084734 .
GeneIDi 2646.
KEGGi hsa:2646.
UCSCi uc002rky.3. human. [Q14397-1 ]

Organism-specific databases

CTDi 2646.
GeneCardsi GC02P027720.
H-InvDB HIX0030026.
HGNCi HGNC:4196. GCKR.
HPAi CAB034098.
HPA045855.
HPA057478.
MIMi 600842. gene.
613463. phenotype.
neXtProti NX_Q14397.
PharmGKBi PA28611.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2103.
HOGENOMi HOG000031501.
HOVERGENi HBG005818.
InParanoidi Q14397.
OrthoDBi EOG7HXCRC.
PhylomeDBi Q14397.
TreeFami TF329177.

Enzyme and pathway databases

Reactomei REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.

Miscellaneous databases

GenomeRNAii 2646.
NextBioi 10442.
PROi Q14397.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14397.
Bgeei Q14397.
CleanExi HS_GCKR.
Genevestigatori Q14397.

Family and domain databases

InterProi IPR005486. Glucokinase_regulatory_CS.
IPR001347. SIS.
[Graphical view ]
PROSITEi PS01272. GCKR. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human glucokinase regulatory protein (GCKR): cDNA and genomic cloning, complete primary structure, and chromosomal localization."
    Warner J.P., Leek J.P., Intody S., Markham A.F., Bonthron D.T.
    Mamm. Genome 6:532-536(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Hepatoblastoma.
  2. Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION TO 393 AND 560, TISSUE SPECIFICITY.
  3. NIEHS SNPs program
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-77; SER-256; LEU-446 AND GLN-540.
  4. "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: Liver.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-446.
  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].
  7. "Glucokinase regulatory protein is essential for the proper subcellular localisation of liver glucokinase."
    de la Iglesia N., Veiga-da-Cunha M., Van Schaftingen E., Guinovart J.J., Ferrer J.C.
    FEBS Lett. 456:332-338(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT.
  8. "The common P446L polymorphism in GCKR inversely modulates fasting glucose and triglyceride levels and reduces type 2 diabetes risk in the DESIR prospective general French population."
    Vaxillaire M., Cavalcanti-Proenca C., Dechaume A., Tichet J., Marre M., Balkau B., Froguel P.
    Diabetes 57:2253-2257(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN FGQTL5, VARIANT LEU-446, ASSOCIATION WITH LOWER RISK FOR DIABETES TYPE 2.
  9. "The P446L variant in GCKR associated with fasting plasma glucose and triglyceride levels exerts its effect through increased glucokinase activity in liver."
    Beer N.L., Tribble N.D., McCulloch L.J., Roos C., Johnson P.R., Orho-Melander M., Gloyn A.L.
    Hum. Mol. Genet. 18:4081-4088(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT LEU-446.
  10. "Molecular basis for the role of glucokinase regulatory protein as the allosteric switch for glucokinase."
    Choi J.M., Seo M.H., Kyeong H.H., Kim E., Kim H.S.
    Proc. Natl. Acad. Sci. U.S.A. 110:10171-10176(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GCK, MUTAGENESIS OF ASP-413 AND 463-LEU--PHE-465.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-1-PHOSPHATE, FUNCTION, INTERACTION WITH GCK, MUTAGENESIS OF 326-LYS-LYS-327 AND 450-LYS-LYS-451.
  12. Cited for: VARIANT LEU-446, INVOLVEMENT IN FGQTL5, ASSOCIATION WITH HIGH PLASMA TRIGLYCERIDE LEVELS.

Entry informationi

Entry nameiGCKR_HUMAN
AccessioniPrimary (citable) accession number: Q14397
Secondary accession number(s): A1L4C2
, B4DPQ2, Q53RY6, Q99522
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 5, 2011
Last modified: September 3, 2014
This is version 115 of the entry and version 6 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi