Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P35558

- PCKGC_HUMAN

UniProt

P35558 - PCKGC_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Phosphoenolpyruvate carboxykinase, cytosolic [GTP]

Gene

PCK1

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

Functioni

Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.

Catalytic activityi

GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.

Cofactori

Binds 1 manganese ion per subunit.1 Publication

Enzyme regulationi

Enzyme activity is enhanced by acetylation.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei87 – 871Substrate
Binding sitei237 – 2371Substrate; via amide nitrogen
Metal bindingi244 – 2441Manganese1 Publication
Binding sitei244 – 2441SubstrateBy similarity
Metal bindingi264 – 2641Manganese; via tele nitrogen1 Publication
Binding sitei286 – 2861SubstrateBy similarity
Active sitei288 – 2881
Metal bindingi311 – 3111Manganese1 Publication
Binding sitei405 – 4051GTP
Binding sitei436 – 4361GTP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi287 – 2926GTP
Nucleotide bindingi530 – 5334GTP

GO - Molecular functioni

  1. carboxylic acid binding Source: BHF-UCL
  2. GDP binding Source: Ensembl
  3. GTP binding Source: BHF-UCL
  4. magnesium ion binding Source: BHF-UCL
  5. manganese ion binding Source: BHF-UCL
  6. phosphoenolpyruvate carboxykinase (GTP) activity Source: BHF-UCL

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. drug metabolic process Source: Reactome
  3. gluconeogenesis Source: BHF-UCL
  4. glucose homeostasis Source: BHF-UCL
  5. glucose metabolic process Source: BHF-UCL
  6. glycerol biosynthetic process from pyruvate Source: BHF-UCL
  7. internal protein amino acid acetylation Source: UniProtKB
  8. oxaloacetate metabolic process Source: Ensembl
  9. response to activity Source: Ensembl
  10. response to insulin Source: BHF-UCL
  11. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Gluconeogenesis

Keywords - Ligandi

GTP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS04751-MONOMER.
ReactomeiREACT_121388. Abacavir metabolism.
REACT_1520. Gluconeogenesis.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SABIO-RKP35558.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (EC:4.1.1.32)
Short name:
PEPCK-C
Gene namesi
Name:PCK1
Synonyms:PEPCK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:8724. PCK1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Cytosolic phosphoenolpyruvate carboxykinase deficiency (C-PEPCKD) [MIM:261680]: Metabolic disorder resulting from impaired gluconeogenesis. It is a rare disease with less than 10 cases reported in the literature. Clinical characteristics include hypotonia, hepatomegaly, failure to thrive, lactic acidosis and hypoglycemia. Autopsy reveals fatty infiltration of both the liver and kidneys. The disorder is transmitted as an autosomal recessive trait.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi70 – 701K → R: Abolishes acetylation and increases protein stability; when associated with R-71 and R-594. 1 Publication
Mutagenesisi71 – 711K → R: Abolishes acetylation and increases protein stability; when associated with R-70 and R-594. 1 Publication
Mutagenesisi594 – 5941K → R: Abolishes acetylation and increases protein stability; when associated with R-70 and R-71. 1 Publication

Organism-specific databases

MIMi261680. phenotype.
Orphaneti79316. Phosphoenolpyruvate carboxykinase 1 deficiency.
PharmGKBiPA33069.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622Phosphoenolpyruvate carboxykinase, cytosolic [GTP]PRO_0000103627Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-acetyllysine; by p300/EP3002 Publications
Modified residuei71 – 711N6-acetyllysine; by p300/EP3002 Publications
Modified residuei594 – 5941N6-acetyllysine; by p300/EP3002 Publications

Post-translational modificationi

Lysine acetylation by p300/EP300 is increased on high glucose conditions and promotes ubiquitination by UBR5, acetylation is enhanced in the presence of BAG6. Deacetylated by SIRT2.2 Publications
Ubiquitination by UBR5 leads to proteasomal degradation.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiP35558.
PaxDbiP35558.
PRIDEiP35558.

PTM databases

PhosphoSiteiP35558.

Expressioni

Tissue specificityi

Major sites of expression are liver, kidney and adipocytes.

Inductioni

Regulated by cAMP and insulin.1 Publication

Gene expression databases

BgeeiP35558.
CleanExiHS_PCK1.
GenevestigatoriP35558.

Organism-specific databases

HPAiCAB017027.
HPA006277.
HPA006507.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi111136. 75 interactions.
IntActiP35558. 1 interaction.
MINTiMINT-3013923.
STRINGi9606.ENSP00000319814.

Structurei

Secondary structure

1
622
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 144
Beta strandi15 – 184
Helixi20 – 223
Helixi25 – 3814
Beta strandi41 – 455
Helixi50 – 6213
Beta strandi65 – 684
Beta strandi72 – 743
Beta strandi76 – 783
Beta strandi84 – 863
Helixi89 – 913
Beta strandi92 – 954
Helixi99 – 1024
Beta strandi107 – 1093
Helixi119 – 12911
Turni131 – 1366
Beta strandi137 – 15014
Beta strandi155 – 1628
Helixi164 – 17310
Beta strandi174 – 1774
Helixi178 – 1847
Beta strandi190 – 1956
Helixi214 – 2163
Beta strandi218 – 2225
Helixi223 – 2253
Beta strandi227 – 2326
Helixi236 – 2394
Helixi242 – 2487
Helixi249 – 25810
Beta strandi261 – 2644
Beta strandi266 – 2716
Beta strandi277 – 2837
Helixi290 – 2945
Beta strandi304 – 3118
Beta strandi313 – 3175
Beta strandi321 – 3266
Beta strandi330 – 3356
Turni341 – 3433
Helixi345 – 3506
Beta strandi356 – 3594
Beta strandi361 – 3633
Beta strandi388 – 3914
Beta strandi395 – 3973
Beta strandi405 – 4095
Helixi410 – 4123
Turni418 – 4214
Beta strandi426 – 4349
Beta strandi438 – 4403
Beta strandi443 – 4464
Helixi450 – 4589
Beta strandi461 – 4633
Beta strandi475 – 4773
Helixi479 – 4813
Turni483 – 4853
Helixi490 – 49910
Helixi500 – 5023
Beta strandi510 – 5145
Beta strandi525 – 5273
Helixi530 – 5334
Helixi534 – 54411
Beta strandi550 – 5534
Beta strandi556 – 5594
Turni561 – 5633
Helixi574 – 5774
Helixi582 – 60019
Helixi601 – 6033
Helixi606 – 62015

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KHBX-ray1.85A1-622[»]
1KHEX-ray2.40A1-622[»]
1KHFX-ray2.02A1-622[»]
1KHGX-ray2.34A1-622[»]
1M51X-ray2.25A1-622[»]
1NHXX-ray2.10A1-622[»]
2GMVX-ray2.30A/B1-622[»]
ProteinModelPortaliP35558.
SMRiP35558. Positions 10-622.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35558.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni403 – 4053Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1274.
GeneTreeiENSGT00390000001912.
HOGENOMiHOG000191700.
HOVERGENiHBG053651.
InParanoidiP35558.
KOiK01596.
OMAiPDHIHIC.
OrthoDBiEOG7KSX81.
PhylomeDBiP35558.
TreeFamiTF314402.

Family and domain databases

Gene3Di3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPiMF_00452. PEPCK_GTP.
InterProiIPR018091. PEP_carboxykin_GTP_CS.
IPR013035. PEP_carboxykinase_C.
IPR008209. PEP_carboxykinase_GTP.
IPR008210. PEP_carboxykinase_N.
[Graphical view]
PANTHERiPTHR11561. PTHR11561. 1 hit.
PfamiPF00821. PEPCK. 1 hit.
[Graphical view]
PIRSFiPIRSF001348. PEP_carboxykinase_GTP. 1 hit.
SUPFAMiSSF68923. SSF68923. 1 hit.
PROSITEiPS00505. PEPCK_GTP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35558-1) [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
MPPQLQNGLN LSAKVVQGSL DSLPQAVREF LENNAELCQP DHIHICDGSE
60 70 80 90 100
EENGRLLGQM EEEGILRRLK KYDNCWLALT DPRDVARIES KTVIVTQEQR
110 120 130 140 150
DTVPIPKTGL SQLGRWMSEE DFEKAFNARF PGCMKGRTMY VIPFSMGPLG
160 170 180 190 200
SPLSKIGIEL TDSPYVVASM RIMTRMGTPV LEAVGDGEFV KCLHSVGCPL
210 220 230 240 250
PLQKPLVNNW PCNPELTLIA HLPDRREIIS FGSGYGGNSL LGKKCFALRM
260 270 280 290 300
ASRLAKEEGW LAEHMLILGI TNPEGEKKYL AAAFPSACGK TNLAMMNPSL
310 320 330 340 350
PGWKVECVGD DIAWMKFDAQ GHLRAINPEN GFFGVAPGTS VKTNPNAIKT
360 370 380 390 400
IQKNTIFTNV AETSDGGVYW EGIDEPLASG VTITSWKNKE WSSEDGEPCA
410 420 430 440 450
HPNSRFCTPA SQCPIIDAAW ESPEGVPIEG IIFGGRRPAG VPLVYEALSW
460 470 480 490 500
QHGVFVGAAM RSEATAAAEH KGKIIMHDPF AMRPFFGYNF GKYLAHWLSM
510 520 530 540 550
AQHPAAKLPK IFHVNWFRKD KEGKFLWPGF GENSRVLEWM FNRIDGKAST
560 570 580 590 600
KLTPIGYIPK EDALNLKGLG HINMMELFSI SKEFWEKEVE DIEKYLEDQV
610 620
NADLPCEIER EILALKQRIS QM
Length:622
Mass (Da):69,195
Last modified:March 7, 2006 - v3
Checksum:i78D309E0845CC181
GO
Isoform 2 (identifier: P35558-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MPP → MTT
     4-320: Missing.

Note: No experimental confirmation available

Show »
Length:305
Mass (Da):34,156
Checksum:i2FDE6275A0F15D6C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti250 – 2501M → N in AAA02558. (PubMed:8325643)Curated
Sequence conflicti256 – 2561K → E in AAA60084. (PubMed:8490617)Curated
Sequence conflicti291 – 2911T → S in AAA02558. (PubMed:8325643)Curated
Sequence conflicti551 – 5522KL → NV in AAA60084. (PubMed:8490617)Curated
Sequence conflicti597 – 5971E → V in AAA60084. (PubMed:8490617)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551R → Q.1 Publication
Corresponds to variant rs28383585 [ dbSNP | Ensembl ].
VAR_021072
Natural varianti60 – 601M → T.1 Publication
Corresponds to variant rs28383586 [ dbSNP | Ensembl ].
VAR_021073
Natural varianti138 – 1381T → I.1 Publication
Corresponds to variant rs28359542 [ dbSNP | Ensembl ].
VAR_021074
Natural varianti184 – 1841V → L.5 Publications
Corresponds to variant rs707555 [ dbSNP | Ensembl ].
VAR_021075
Natural varianti267 – 2671I → V.2 Publications
Corresponds to variant rs8192708 [ dbSNP | Ensembl ].
VAR_015575
Natural varianti276 – 2761E → K.1 Publication
Corresponds to variant rs11552145 [ dbSNP | Ensembl ].
VAR_021076
Natural varianti368 – 3681V → I.1 Publication
Corresponds to variant rs1804160 [ dbSNP | Ensembl ].
VAR_021077
Natural varianti427 – 4271P → S.1 Publication
Corresponds to variant rs28359550 [ dbSNP | Ensembl ].
VAR_021078
Natural varianti586 – 5861E → D.1 Publication
Corresponds to variant rs1042529 [ dbSNP | Ensembl ].
VAR_042444

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 33MPP → MTT in isoform 2. 1 PublicationVSP_057073
Alternative sequencei4 – 320317Missing in isoform 2. 1 PublicationVSP_057074Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L05144 mRNA. Translation: AAA60084.1.
L12760 Genomic DNA. Translation: AAA02558.1.
AY794987 Genomic DNA. Translation: AAV50001.1.
AK290802 mRNA. Translation: BAF83491.1.
AK300072 mRNA. Translation: BAG61876.1.
AL035541 Genomic DNA. Translation: CAB55863.1.
CH471077 Genomic DNA. Translation: EAW75514.1.
BC023978 mRNA. Translation: AAH23978.1.
U31519 Genomic DNA. Translation: AAA91026.1.
CCDSiCCDS13460.1.
PIRiA45746.
RefSeqiNP_002582.3. NM_002591.3.
UniGeneiHs.1872.

Genome annotation databases

EnsembliENST00000319441; ENSP00000319814; ENSG00000124253.
GeneIDi5105.
KEGGihsa:5105.
UCSCiuc002xyn.4. human.

Polymorphism databases

DMDMi93138710.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L05144 mRNA. Translation: AAA60084.1 .
L12760 Genomic DNA. Translation: AAA02558.1 .
AY794987 Genomic DNA. Translation: AAV50001.1 .
AK290802 mRNA. Translation: BAF83491.1 .
AK300072 mRNA. Translation: BAG61876.1 .
AL035541 Genomic DNA. Translation: CAB55863.1 .
CH471077 Genomic DNA. Translation: EAW75514.1 .
BC023978 mRNA. Translation: AAH23978.1 .
U31519 Genomic DNA. Translation: AAA91026.1 .
CCDSi CCDS13460.1.
PIRi A45746.
RefSeqi NP_002582.3. NM_002591.3.
UniGenei Hs.1872.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KHB X-ray 1.85 A 1-622 [» ]
1KHE X-ray 2.40 A 1-622 [» ]
1KHF X-ray 2.02 A 1-622 [» ]
1KHG X-ray 2.34 A 1-622 [» ]
1M51 X-ray 2.25 A 1-622 [» ]
1NHX X-ray 2.10 A 1-622 [» ]
2GMV X-ray 2.30 A/B 1-622 [» ]
ProteinModelPortali P35558.
SMRi P35558. Positions 10-622.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111136. 75 interactions.
IntActi P35558. 1 interaction.
MINTi MINT-3013923.
STRINGi 9606.ENSP00000319814.

Chemistry

BindingDBi P35558.
ChEMBLi CHEMBL2911.

PTM databases

PhosphoSitei P35558.

Polymorphism databases

DMDMi 93138710.

Proteomic databases

MaxQBi P35558.
PaxDbi P35558.
PRIDEi P35558.

Protocols and materials databases

DNASUi 5105.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000319441 ; ENSP00000319814 ; ENSG00000124253 .
GeneIDi 5105.
KEGGi hsa:5105.
UCSCi uc002xyn.4. human.

Organism-specific databases

CTDi 5105.
GeneCardsi GC20P056136.
H-InvDB HIX0015941.
HGNCi HGNC:8724. PCK1.
HPAi CAB017027.
HPA006277.
HPA006507.
MIMi 261680. phenotype.
614168. gene.
neXtProti NX_P35558.
Orphaneti 79316. Phosphoenolpyruvate carboxykinase 1 deficiency.
PharmGKBi PA33069.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1274.
GeneTreei ENSGT00390000001912.
HOGENOMi HOG000191700.
HOVERGENi HBG053651.
InParanoidi P35558.
KOi K01596.
OMAi PDHIHIC.
OrthoDBi EOG7KSX81.
PhylomeDBi P35558.
TreeFami TF314402.

Enzyme and pathway databases

UniPathwayi UPA00138 .
BioCyci MetaCyc:HS04751-MONOMER.
Reactomei REACT_121388. Abacavir metabolism.
REACT_1520. Gluconeogenesis.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SABIO-RK P35558.

Miscellaneous databases

ChiTaRSi PCK1. human.
EvolutionaryTracei P35558.
GeneWikii PCK1.
GenomeRNAii 5105.
NextBioi 19702.
PROi P35558.
SOURCEi Search...

Gene expression databases

Bgeei P35558.
CleanExi HS_PCK1.
Genevestigatori P35558.

Family and domain databases

Gene3Di 3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPi MF_00452. PEPCK_GTP.
InterProi IPR018091. PEP_carboxykin_GTP_CS.
IPR013035. PEP_carboxykinase_C.
IPR008209. PEP_carboxykinase_GTP.
IPR008210. PEP_carboxykinase_N.
[Graphical view ]
PANTHERi PTHR11561. PTHR11561. 1 hit.
Pfami PF00821. PEPCK. 1 hit.
[Graphical view ]
PIRSFi PIRSF001348. PEP_carboxykinase_GTP. 1 hit.
SUPFAMi SSF68923. SSF68923. 1 hit.
PROSITEi PS00505. PEPCK_GTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence and localization of polymorphic human cytosolic phosphoenolpyruvate carboxykinase gene (PCK1) to chromosome 20, band q13.31: PCK1 is not tightly linked to maturity-onset diabetes of the young."
    Stoffel M., Xiang K.S., Espinosa R. III, Cox N.J., le Beau M.M., Bell G.I.
    Hum. Mol. Genet. 2:1-4(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS LEU-184 AND ASP-586.
  2. "Phosphoenolpyruvate carboxykinase (GTP): characterization of the human PCK1 gene and localization distal to MODY on chromosome 20."
    Ting C.-N., Burgess D.L., Chamberlain J.S., Keith T.P., Falls K., Meisler M.H.
    Genomics 16:698-706(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-184.
    Tissue: Liver.
  3. NIEHS SNPs program
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-55; THR-60; ILE-138; VAL-267; LYS-276; ILE-368 AND SER-427.
  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] (ISOFORMS 1 AND 2), VARIANT LEU-184.
    Tissue: Kidney and Pericardium.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-184.
  7. "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), VARIANTS LEU-184 AND VAL-267.
    Tissue: Kidney.
  8. "Structural and functional analysis of the human phosphoenolpyruvate carboxykinase gene promoter."
    O'Brien R.M., Printz R.L., Halmi N., Tiesinga J.J., Granner D.K.
    Biochim. Biophys. Acta 1264:284-288(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74.
  9. "Regulation of phosphoenolpyruvate carboxykinase (GTP) gene transcription."
    Liu J., Hanson R.W.
    Mol. Cell. Biochem. 104:89-100(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. Cited for: ACETYLATION AT LYS-70; LYS-71 AND LYS-594, ENZYME REGULATION, MUTAGENESIS OF LYS-70; LYS-71 AND LYS-594, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase."
    Jiang W., Wang S., Xiao M., Lin Y., Zhou L., Lei Q., Xiong Y., Guan K.L., Zhao S.
    Mol. Cell 43:33-44(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-70; LYS-71 AND LYS-594, DEACETYLATION BY SIRT2, UBIQUITINATION BY UBR5.
  12. "Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site."
    Dunten P., Belunis C., Crowther R., Hollfelder K., Kammlott U., Levin W., Michel H., Ramsey G.B., Swain A., Weber D., Wertheimer S.J.
    J. Mol. Biol. 316:257-264(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH GTP ANALOG; PEP AND MANGANESE, GTP-BINDING SITE, COFACTOR.

Entry informationi

Entry nameiPCKGC_HUMAN
AccessioniPrimary (citable) accession number: P35558
Secondary accession number(s): A8K437
, B4DT64, Q8TCA3, Q9UJD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: March 7, 2006
Last modified: October 29, 2014
This is version 160 of the entry and version 3 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 eukaryotes there are two isozymes: a cytoplasmic one and a mitochondrial one.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3