P35558 (PCKGC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
Short name=PEPCK-C
EC=4.1.1.32

Alternative name(s):
Phosphoenolpyruvate carboxylase

Gene names

Name:	PCK1
Synonyms:	PEPCK1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	622 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.
Cofactor	Binds 1 manganese ion per subunit. Ref.11
Enzyme regulation	Enzyme activity is enhanced by acetylation. Ref.10
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Tissue specificity	Major sites of expression are liver, kidney and adipocytes.
Induction	Regulated by cAMP and insulin. Ref.9 Ref.10
Post-translational modification	Acetylation is increased on addition of glucose and appears to regulate the protein stability.
Involvement in disease	Defects in PCK1 are the cause of cytosolic phosphoenolpyruvate carboxykinase deficiency (C-PEPCKD) [MIM:261680]. A 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. Autoposy reveals fatty infiltration of both the liver and kidneys. The disorder is transmitted as an autosomal recessive trait.
Miscellaneous	In eukaryotes there are two isozymes: a cytoplasmic one and a mitochondrial one.
Sequence similarities	Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.

Ontologies

Keywords
Biological process	Gluconeogenesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Manganese Metal-binding Nucleotide-binding
Molecular function	Decarboxylase Lyase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from sequence or structural similarity. Source: BHF-UCL glucose homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL glycerol biosynthetic process from pyruvate Inferred from sequence or structural similarity. Source: BHF-UCL internal protein amino acid acetylation Inferred from direct assay Ref.10. Source: UniProtKB response to insulin stimulus Inferred from direct assay. Source: BHF-UCL
Cellular component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: HPA
Molecular function	GTP binding Inferred from direct assay Ref.11. Source: BHF-UCL carboxylic acid binding Inferred from direct assay Ref.11. Source: BHF-UCL magnesium ion binding Inferred from direct assay Ref.11. Source: BHF-UCL manganese ion binding Inferred from direct assay Ref.11. Source: BHF-UCL phosphoenolpyruvate carboxykinase (GTP) activity Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 622

622

Phosphoenolpyruvate carboxykinase, cytosolic [GTP]

PRO_0000103627

Regions

Nucleotide binding

287 – 292

6

GTP

Nucleotide binding

530 – 533

4

GTP

Region

403 – 405

3

Substrate binding

Sites

Active site

288

1

Metal binding

244

1

Manganese

Metal binding

264

1

Manganese

Metal binding

311

1

Manganese

Binding site

87

1

Substrate

Binding site

237

1

Substrate; via amide nitrogen

Binding site

244

1

Substrate By similarity

Binding site

286

1

Substrate By similarity

Binding site

405

1

GTP

Binding site

436

1

GTP

Amino acid modifications

Modified residue

70

1

N6-acetyllysine Ref.10

Modified residue

71

1

N6-acetyllysine Ref.10

Modified residue

594

1

N6-acetyllysine Ref.10

Natural variations

Natural variant

55

1

R → Q. Ref.3
Corresponds to variant rs28383585 [ dbSNP | Ensembl ].

VAR_021072

Natural variant

60

1

M → T. Ref.3
Corresponds to variant rs28383586 [ dbSNP | Ensembl ].

VAR_021073

Natural variant

138

1

T → I. Ref.3
Corresponds to variant rs28359542 [ dbSNP | Ensembl ].

VAR_021074

Natural variant

184

1

V → L. Ref.1 Ref.2 Ref.4 Ref.6 Ref.7
Corresponds to variant rs707555 [ dbSNP | Ensembl ].

VAR_021075

Natural variant

267

1

I → V. Ref.3 Ref.7
Corresponds to variant rs8192708 [ dbSNP | Ensembl ].

VAR_015575

Natural variant

276

1

E → K. Ref.3
Corresponds to variant rs11552145 [ dbSNP | Ensembl ].

VAR_021076

Natural variant

368

1

V → I. Ref.3
Corresponds to variant rs1804160 [ dbSNP | Ensembl ].

VAR_021077

Natural variant

427

1

P → S. Ref.3
Corresponds to variant rs28359550 [ dbSNP | Ensembl ].

VAR_021078

Natural variant

586

1

E → D. Ref.1
Corresponds to variant rs1042529 [ dbSNP | Ensembl ].

VAR_042444

Experimental info

Mutagenesis

70

1

K → R: Abolishes acetylation and increases protein stability; when associated with R-71 and R-594. Ref.10

Mutagenesis

71

1

K → R: Abolishes acetylation and increases protein stability; when associated with R-70 and R-594. Ref.10

Mutagenesis

594

1

K → R: Abolishes acetylation and increases protein stability; when associated with R-70 and R-71. Ref.10

Sequence conflict

250

1

M → N in AAA02558. Ref.2

Sequence conflict

256

1

K → E in AAA60084. Ref.1

Sequence conflict

291

1

T → S in AAA02558. Ref.2

Sequence conflict

551 – 552

2

KL → NV in AAA60084. Ref.1

Sequence conflict

597

1

E → V in AAA60084. Ref.1

Secondary structure

1

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622

Helix Strand Turn

Details...

Helix

11 – 14

4

Beta strand

15 – 18

4

Helix

20 – 22

3

Helix

25 – 38

14

Beta strand

41 – 45

5

Helix

50 – 62

13

Beta strand

72 – 74

3

Beta strand

76 – 78

3

Beta strand

84 – 86

3

Helix

89 – 91

3

Beta strand

92 – 95

4

Helix

99 – 102

4

Beta strand

107 – 109

3

Helix

119 – 129

11

Turn

131 – 136

6

Beta strand

137 – 150

14

Beta strand

155 – 162

8

Helix

164 – 173

10

Beta strand

174 – 177

4

Helix

178 – 184

7

Beta strand

190 – 195

6

Helix

214 – 216

3

Beta strand

218 – 222

5

Helix

223 – 225

3

Beta strand

227 – 232

6

Helix

236 – 239

4

Helix

242 – 248

7

Helix

249 – 258

10

Beta strand

261 – 264

4

Beta strand

266 – 271

6

Beta strand

277 – 283

7

Helix

290 – 294

5

Beta strand

304 – 311

8

Beta strand

313 – 317

5

Beta strand

321 – 326

6

Beta strand

330 – 335

6

Turn

341 – 343

3

Helix

345 – 350

6

Beta strand

356 – 359

4

Beta strand

361 – 363

3

Beta strand

388 – 391

4

Beta strand

395 – 397

3

Beta strand

405 – 409

5

Helix

410 – 412

3

Turn

418 – 421

4

Beta strand

426 – 434

9

Beta strand

438 – 440

3

Beta strand

443 – 446

4

Helix

450 – 458

9

Beta strand

461 – 463

3

Beta strand

475 – 477

3

Helix

479 – 481

3

Turn

483 – 485

3

Helix

490 – 499

10

Helix

500 – 502

3

Beta strand

510 – 514

5

Beta strand

525 – 527

3

Helix

530 – 533

4

Helix

534 – 544

11

Beta strand

550 – 553

4

Beta strand

556 – 559

4

Helix

574 – 577

4

Helix

582 – 600

19

Helix

601 – 603

3

Helix

606 – 620

15

Sequences

	Sequence		Length	Mass (Da)
	P35558 [UniParc]. Last modified March 7, 2006. Version 3. Checksum: 78D309E0845CC181	FASTA	622	69,195
	10 20 30 40 50 60 MPPQLQNGLN LSAKVVQGSL DSLPQAVREF LENNAELCQP DHIHICDGSE EENGRLLGQM 70 80 90 100 110 120 EEEGILRRLK KYDNCWLALT DPRDVARIES KTVIVTQEQR DTVPIPKTGL SQLGRWMSEE 130 140 150 160 170 180 DFEKAFNARF PGCMKGRTMY VIPFSMGPLG SPLSKIGIEL TDSPYVVASM RIMTRMGTPV 190 200 210 220 230 240 LEAVGDGEFV KCLHSVGCPL PLQKPLVNNW PCNPELTLIA HLPDRREIIS FGSGYGGNSL 250 260 270 280 290 300 LGKKCFALRM ASRLAKEEGW LAEHMLILGI TNPEGEKKYL AAAFPSACGK TNLAMMNPSL 310 320 330 340 350 360 PGWKVECVGD DIAWMKFDAQ GHLRAINPEN GFFGVAPGTS VKTNPNAIKT IQKNTIFTNV 370 380 390 400 410 420 AETSDGGVYW EGIDEPLASG VTITSWKNKE WSSEDGEPCA HPNSRFCTPA SQCPIIDAAW 430 440 450 460 470 480 ESPEGVPIEG IIFGGRRPAG VPLVYEALSW QHGVFVGAAM RSEATAAAEH KGKIIMHDPF 490 500 510 520 530 540 AMRPFFGYNF GKYLAHWLSM AQHPAAKLPK IFHVNWFRKD KEGKFLWPGF GENSRVLEWM 550 560 570 580 590 600 FNRIDGKAST KLTPIGYIPK EDALNLKGLG HINMMELFSI SKEFWEKEVE DIEKYLEDQV 610 620 NADLPCEIER EILALKQRIS QM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8490617] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 8325643] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-184. Tissue: Kidney.
[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: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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. , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], 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: 8547315] [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: 1656199] [Abstract] Cited for: INDUCTION.
[10]	"Regulation of cellular metabolism by protein lysine acetylation." Zhao S., Xu W., Jiang W., Yu W., Lin Y., Zhang T., Yao J., Zhou L., Zeng Y., Li H., Li Y., Shi J., An W., Hancock S.M., He F., Qin L., Chin J., Yang P. , Chen X., Lei Q., Xiong Y., Guan K.L. Science 327:1000-1004(2010) [PubMed: 20167786] [Abstract] Cited for: ACETYLATION AT LYS-70; LYS-71 AND LYS-594, ENZYME REGULATION, MASS SPECTROMETRY, MUTAGENESIS OF LYS-70; LYS-71 AND LYS-594.
[11]	"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: 11851336] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH GTP ANALOG; PEP AND MANGANESE, GTP-BINDING SITE, COFACTOR.
+	Additional computationally mapped references.

Web resources

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L05144 mRNA. Translation: AAA60084.1.
L12760 Genomic DNA. Translation: AAA02558.1.
AY794987 Genomic DNA. Translation: AAV50001.1.
AK290802 mRNA. Translation: BAF83491.1.
AL035541 Genomic DNA. Translation: CAB55863.1.
CH471077 Genomic DNA. Translation: EAW75514.1.
BC023978 mRNA. Translation: AAH23978.1.
U31519 Genomic DNA. Translation: AAA91026.1.

IPI

IPI00292709.

PIR

A45746.

RefSeq

NP_002582.3. NM_002591.3.

UniGene

Hs.1872.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P35558.

SMR

P35558. Positions 10-622.

ModBase

Search...

Protein-protein interaction databases

IntAct

P35558. 1 interaction.

STRING

P35558.

PTM databases

PhosphoSite

P35558.

Polymorphism databases

DMDM

93138710.

Proteomic databases

PRIDE

P35558.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000319441; ENSP00000319814; ENSG00000124253.

GeneID

5105.

KEGG

hsa:5105.

NMPDR

fig|9606.3.peg.20531.

UCSC

uc002xyn.2. human.

Organism-specific databases

CTD

5105.

GeneCards

GC20P056136.

H-InvDB

HIX0015941.

HGNC

HGNC:8724. PCK1.

HPA

CAB017027.
HPA006277.
HPA006507.

MIM

261680. phenotype.
614168. gene.

neXtProt

NX_P35558.

Orphanet

2880. Phosphoenolpyruvate carboxykinase deficiency.

PharmGKB

PA33069.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05504.

GeneTree

ENSGT00390000001912.

HOGENOM

HBG484437.

HOVERGEN

HBG053651.

InParanoid

P35558.

OMA

CPIIDAA.

OrthoDB

EOG47SSD8.

PhylomeDB

P35558.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.

Reactome

REACT_111045. Developmental Biology.
REACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpress

P35558.

Bgee

P35558.

CleanEx

HS_PCK1.

Genevestigator

P35558.

GermOnline

ENSG00000124253. Homo sapiens.

Family and domain databases

InterPro

IPR018091. PEP_carboxykin_GTP_CS.
IPR013035. PEP_carboxykinase_C.
IPR008209. PEP_carboxykinase_GTP.
IPR008210. PEP_carboxykinase_N.
[Graphical view]

Gene3D

G3DSA:3.90.228.20. PEP_carboxykinase_C. 2 hits.
G3DSA:3.40.449.10. PEP_carboxykinase_N. 1 hit.

KO

K01596.

PANTHER

PTHR11561. PEP_carboxykin. 1 hit.

Pfam

PF00821. PEPCK. 1 hit.
[Graphical view]

PIRSF

PIRSF001348. PEP_carboxykinase_GTP. 1 hit.

SUPFAM

SSF68923. PEP_carboxykinase_N. 1 hit.

PROSITE

PS00505. PEPCK_GTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

19702.

SOURCE

Search...

Entry information

Entry name

PCKGC_HUMAN

Accession

Primary (citable) accession number: P35558
Secondary accession number(s): A8K437, Q8TCA3, Q9UJD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	March 7, 2006
Last modified:	January 25, 2012
This is version 132 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.