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Protein

Glucokinase regulatory protein

Gene

GCKR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • carbohydrate binding Source: InterPro
  • fructose-6-phosphate binding Source: UniProtKB

GO - Biological processi

  • carbohydrate metabolic process Source: Reactome
  • glucose transport Source: Reactome
  • hexose transport Source: Reactome
  • negative regulation of glucokinase activity Source: UniProtKB
  • protein import into nucleus, translocation Source: BHF-UCL
  • regulation of glucose transport Source: Reactome
  • response to fructose Source: BHF-UCL
  • small molecule metabolic process Source: Reactome
  • transmembrane transport Source: Reactome
  • triglyceride homeostasis Source: BHF-UCL
  • 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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:4196. GCKR.

Subcellular locationi

GO - Cellular componenti

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. 1 Publication
Mutagenesisi450 – 4512KK → TT: Impairs inhibition of glucokinase. 1 Publication
Mutagenesisi463 – 4653LLF → ALA: Abolishes interaction with GCK. Abolishes inhibition of GCK. 1 Publication

Organism-specific databases

MIMi613463. phenotype.
PharmGKBiPA28611.

Polymorphism and mutation databases

BioMutaiGCKR.
DMDMi327478611.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 625625Glucokinase regulatory proteinPRO_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

BgeeiQ14397.
CleanExiHS_GCKR.
ExpressionAtlasiQ14397. baseline and differential.
GenevisibleiQ14397. HS.

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. 3 interactions.
IntActiQ14397. 2 interactions.
STRINGi9606.ENSP00000264717.

Structurei

Secondary structure

1
625
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 43Combined sources
Helixi5 – 73Combined sources
Turni19 – 224Combined sources
Helixi23 – 264Combined sources
Helixi30 – 323Combined sources
Helixi36 – 383Combined sources
Helixi41 – 433Combined sources
Helixi46 – 5813Combined sources
Helixi59 – 613Combined sources
Helixi77 – 9418Combined sources
Beta strandi100 – 1078Combined sources
Helixi108 – 12720Combined sources
Beta strandi134 – 1385Combined sources
Helixi143 – 1464Combined sources
Helixi150 – 1545Combined sources
Helixi156 – 16712Combined sources
Beta strandi171 – 1788Combined sources
Helixi185 – 19511Combined sources
Turni198 – 2003Combined sources
Beta strandi201 – 2066Combined sources
Helixi211 – 2133Combined sources
Beta strandi222 – 2243Combined sources
Helixi226 – 23712Combined sources
Turni238 – 2403Combined sources
Beta strandi243 – 2453Combined sources
Turni258 – 2603Combined sources
Helixi261 – 28323Combined sources
Helixi289 – 30719Combined sources
Helixi310 – 32516Combined sources
Beta strandi330 – 3356Combined sources
Helixi337 – 35317Combined sources
Beta strandi359 – 3668Combined sources
Turni369 – 3713Combined sources
Helixi375 – 3773Combined sources
Turni378 – 3803Combined sources
Helixi383 – 3853Combined sources
Helixi389 – 3957Combined sources
Helixi397 – 3993Combined sources
Beta strandi405 – 4117Combined sources
Helixi416 – 42712Combined sources
Beta strandi433 – 4408Combined sources
Helixi447 – 4526Combined sources
Beta strandi453 – 4553Combined sources
Beta strandi457 – 4615Combined sources
Turni467 – 4693Combined sources
Helixi470 – 49526Combined sources
Turni496 – 4983Combined sources
Helixi513 – 52715Combined sources
Helixi531 – 54313Combined sources
Helixi550 – 5534Combined sources
Helixi557 – 5648Combined sources
Beta strandi567 – 5693Combined sources
Helixi570 – 58011Combined sources
Helixi584 – 5929Combined sources
Beta strandi594 – 5963Combined sources
Helixi597 – 6059Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4OHKX-ray2.80A/B1-625[»]
4OHMX-ray2.40A/B1-625[»]
4OHOX-ray2.58A/B1-625[»]
4OHPX-ray2.40A/B1-625[»]
4OLHX-ray2.40A/B1-625[»]
4OP1X-ray2.39A/B1-625[»]
4OP2X-ray2.24A/B1-625[»]
4OP3X-ray2.82A/B1-625[»]
4PX2X-ray2.15A/B1-625[»]
4PX3X-ray2.43A/B1-625[»]
4PX5X-ray2.20A/B1-625[»]
4PXSX-ray2.60A/B1-625[»]
ProteinModelPortaliQ14397.
SMRiQ14397. Positions 6-605.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini90 – 286197SIS 1PROSITE-ProRule annotationAdd
BLAST
Domaini320 – 499180SIS 2PROSITE-ProRule annotationAdd
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 GCKBy 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.Curated
Contains 2 SIS domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2103.
GeneTreeiENSGT00390000005345.
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. AlignAdd to basket

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

        10         20         30         40         50
MPGTKRFQHV IETPEPGKWE LSGYEAAVPI TEKSNPLTQD LDKADAENIV
60 70 80 90 100
RLLGQCDAEI FQEEGQALST YQRLYSESIL TTMVQVAGKV QEVLKEPDGG
110 120 130 140 150
LVVLSGGGTS GRMAFLMSVS FNQLMKGLGQ KPLYTYLIAG GDRSVVASRE
160 170 180 190 200
GTEDSALHGI EELKKVAAGK KRVIVIGISV GLSAPFVAGQ MDCCMNNTAV
210 220 230 240 250
FLPVLVGFNP VSMARNDPIE DWSSTFRQVA ERMQKMQEKQ KAFVLNPAIG
260 270 280 290 300
PEGLSGSSRM KGGSATKILL ETLLLAAHKT VDQGIAASQR CLLEILRTFE
310 320 330 340 350
RAHQVTYSQS PKIATLMKSV STSLEKKGHV YLVGWQTLGI IAIMDGVECI
360 370 380 390 400
HTFGADFRDV RGFLIGDHSD MFNQKAELTN QGPQFTFSQE DFLTSILPSL
410 420 430 440 450
TEIDTVVFIF TLDDNLTEVQ TIVEQVKEKT NHIQALAHST VGQTLPIPLK
460 470 480 490 500
KLFPSIISIT WPLLFFEYEG NFIQKFQREL STKWVLNTVS TGAHVLLGKI
510 520 530 540 550
LQNHMLDLRI SNSKLFWRAL AMLQRFSGQS KARCIESLLR AIHFPQPLSD
560 570 580 590 600
DIRAAPISCH VQVAHEKEQV IPIALLSLLF RCSITEAQAH LAAAPSVCEA
610 620
VRSALAGPGQ KRTADPLEIL EPDVQ
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511P → V in CAB61828 (PubMed:9570959).Curated
Sequence conflicti393 – 3931L → P in CAA88367 (PubMed:8589523).Curated
Sequence conflicti560 – 5601H → R in CAA88367 (PubMed:8589523).Curated

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. 1 PublicationVSP_054853
Alternative sequencei151 – 625475Missing in isoform 2. 1 PublicationVSP_054854Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000417872; ENSP00000398303; ENSG00000084734. [Q14397-2]
GeneIDi2646.
KEGGihsa:2646.
UCSCiuc002rky.3. human. [Q14397-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4OHKX-ray2.80A/B1-625[»]
4OHMX-ray2.40A/B1-625[»]
4OHOX-ray2.58A/B1-625[»]
4OHPX-ray2.40A/B1-625[»]
4OLHX-ray2.40A/B1-625[»]
4OP1X-ray2.39A/B1-625[»]
4OP2X-ray2.24A/B1-625[»]
4OP3X-ray2.82A/B1-625[»]
4PX2X-ray2.15A/B1-625[»]
4PX3X-ray2.43A/B1-625[»]
4PX5X-ray2.20A/B1-625[»]
4PXSX-ray2.60A/B1-625[»]
ProteinModelPortaliQ14397.
SMRiQ14397. Positions 6-605.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108916. 3 interactions.
IntActiQ14397. 2 interactions.
STRINGi9606.ENSP00000264717.

Chemistry

BindingDBiQ14397.
ChEMBLiCHEMBL1075152.

PTM databases

PhosphoSiteiQ14397.

Polymorphism and mutation databases

BioMutaiGCKR.
DMDMi327478611.

Proteomic databases

PaxDbiQ14397.
PRIDEiQ14397.

Protocols and materials databases

DNASUi2646.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000417872; ENSP00000398303; ENSG00000084734. [Q14397-2]
GeneIDi2646.
KEGGihsa:2646.
UCSCiuc002rky.3. human. [Q14397-1]

Organism-specific databases

CTDi2646.
GeneCardsiGC02P027720.
H-InvDBHIX0030026.
HGNCiHGNC:4196. GCKR.
HPAiCAB034098.
HPA045855.
HPA057478.
MIMi600842. gene.
613463. phenotype.
neXtProtiNX_Q14397.
PharmGKBiPA28611.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2103.
GeneTreeiENSGT00390000005345.
HOGENOMiHOG000031501.
HOVERGENiHBG005818.
InParanoidiQ14397.
OrthoDBiEOG7HXCRC.
PhylomeDBiQ14397.
TreeFamiTF329177.

Enzyme and pathway databases

ReactomeiREACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.

Miscellaneous databases

GenomeRNAii2646.
NextBioi10442.
PROiQ14397.
SOURCEiSearch...

Gene expression databases

BgeeiQ14397.
CleanExiHS_GCKR.
ExpressionAtlasiQ14397. baseline and differential.
GenevisibleiQ14397. HS.

Family and domain databases

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

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: July 22, 2015
This is version 125 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.