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P11498

- PYC_HUMAN

UniProt

P11498 - PYC_HUMAN

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Protein
Pyruvate carboxylase, mitochondrial
Gene
PC
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.

Catalytic activityi

ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate.

Cofactori

Biotin.
Binds 1 manganese ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei152 – 1521ATP By similarity
Binding sitei236 – 2361ATP By similarity
Binding sitei271 – 2711ATP By similarity
Active sitei328 – 3281 By similarity
Metal bindingi572 – 5721Manganese
Binding sitei644 – 6441Substrate
Metal bindingi741 – 7411Manganese; via carbamate group
Metal bindingi771 – 7711Manganese; via tele nitrogen
Metal bindingi773 – 7731Manganese; via tele nitrogen
Binding sitei908 – 9081Substrate

GO - Molecular functioni

  1. ATP binding Source: ProtInc
  2. DNA binding Source: InterPro
  3. biotin binding Source: ProtInc
  4. biotin carboxylase activity Source: InterPro
  5. metal ion binding Source: UniProtKB-KW
  6. protein binding Source: IntAct
  7. pyruvate carboxylase activity Source: Reactome
Complete GO annotation...

GO - Biological processi

  1. biotin metabolic process Source: Reactome
  2. carbohydrate metabolic process Source: Reactome
  3. gluconeogenesis Source: Reactome
  4. glucose metabolic process Source: Reactome
  5. lipid metabolic process Source: UniProtKB-KW
  6. oxaloacetate metabolic process Source: Ensembl
  7. pyruvate metabolic process Source: Ensembl
  8. small molecule metabolic process Source: Reactome
  9. vitamin metabolic process Source: Reactome
  10. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Gluconeogenesis, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding, Pyruvate

Enzyme and pathway databases

BioCyciMetaCyc:HS10697-MONOMER.
BRENDAi6.4.1.1. 2681.
ReactomeiREACT_11153. Biotin transport and metabolism.
REACT_1520. Gluconeogenesis.
REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
SABIO-RKiP11498.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate carboxylase, mitochondrial (EC:6.4.1.1)
Alternative name(s):
Pyruvic carboxylase
Short name:
PCB
Gene namesi
Name:PC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:8636. PC.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrial inner membrane Source: Ensembl
  3. mitochondrial matrix Source: Reactome
  4. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Pyruvate carboxylase deficiency (PC deficiency) [MIM:266150]: Leads to lactic acidosis, mental retardation and death. It occurs in three forms: mild or type A, severe neonatal or type B, and a very mild lacticacidemia.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti145 – 1451V → A in PC deficiency; mild. 2 Publications
Corresponds to variant rs28940591 [ dbSNP | Ensembl ].
VAR_015199
Natural varianti156 – 1561R → Q in PC deficiency. 1 Publication
VAR_058957
Natural varianti270 – 2701R → W in PC deficiency. 1 Publication
VAR_058958
Natural varianti304 – 3041Y → C in PC deficiency. 1 Publication
VAR_058959
Natural varianti451 – 4511R → C in PC deficiency; mild. 2 Publications
VAR_015200
Natural varianti583 – 5831R → L in PC deficiency. 1 Publication
VAR_058960
Natural varianti610 – 6101A → T in PC deficiency; mild. 2 Publications
Corresponds to variant rs28940589 [ dbSNP | Ensembl ].
VAR_008095
Natural varianti631 – 6311R → Q in PC deficiency. 1 Publication
VAR_058961
Natural varianti743 – 7431M → I in PC deficiency; mild. 2 Publications
Corresponds to variant rs28940590 [ dbSNP | Ensembl ].
VAR_008096
Natural varianti1131 – 11333Missing in PC deficiency.
VAR_058962

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1077 – 10771F → A or E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi266150. phenotype.
Orphaneti353320. Pyruvate carboxylase deficiency, benign type.
353308. Pyruvate carboxylase deficiency, infantile type.
353314. Pyruvate carboxylase deficiency, severe neonatal type.
PharmGKBiPA32975.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2020Mitochondrion Reviewed prediction
Add
BLAST
Chaini21 – 11781158Pyruvate carboxylase, mitochondrial
PRO_0000002840Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791N6-acetyllysine; alternate By similarity
Modified residuei79 – 791N6-succinyllysine; alternate By similarity
Modified residuei297 – 2971N6-acetyllysine By similarity
Modified residuei319 – 3191N6-acetyllysine By similarity
Modified residuei434 – 4341N6-acetyllysine By similarity
Modified residuei442 – 4421N6-succinyllysine By similarity
Modified residuei661 – 6611N6-acetyllysine By similarity
Modified residuei741 – 7411N6-carboxylysine
Modified residuei748 – 7481N6-acetyllysine By similarity
Modified residuei992 – 9921N6-acetyllysine By similarity
Modified residuei1061 – 10611N6-acetyllysine By similarity
Modified residuei1090 – 10901N6-acetyllysine1 Publication
Modified residuei1124 – 11241N6-acetyllysine By similarity
Modified residuei1144 – 11441N6-biotinyllysine

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP11498.
PaxDbiP11498.
PeptideAtlasiP11498.
PRIDEiP11498.

PTM databases

PhosphoSiteiP11498.

Expressioni

Gene expression databases

ArrayExpressiP11498.
BgeeiP11498.
CleanExiHS_PC.
GenevestigatoriP11498.

Organism-specific databases

HPAiCAB033742.
HPA043922.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q034637EBI-2211322,EBI-8803426From a different organism.

Protein-protein interaction databases

BioGridi111124. 19 interactions.
DIPiDIP-46372N.
IntActiP11498. 4 interactions.
MINTiMINT-3007737.
STRINGi9606.ENSP00000377527.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi495 – 51016
Helixi541 – 55919
Beta strandi564 – 5674
Turni569 – 5713
Helixi572 – 5776
Helixi584 – 59714
Beta strandi602 – 6087
Helixi611 – 6177
Helixi623 – 63311
Beta strandi635 – 6373
Beta strandi639 – 6435
Helixi645 – 6473
Beta strandi650 – 6523
Helixi656 – 66914
Beta strandi673 – 6775
Helixi683 – 69412
Turni695 – 6973
Beta strandi698 – 7058
Helixi720 – 73314
Beta strandi736 – 7416
Helixi749 – 76214
Beta strandi768 – 7714
Helixi779 – 78810
Beta strandi792 – 7976
Helixi799 – 8013
Helixi810 – 8178
Helixi828 – 84417
Helixi845 – 8484
Helixi850 – 8523
Helixi861 – 8644
Helixi868 – 8758
Helixi876 – 8783
Turni879 – 8813
Helixi886 – 90015
Helixi910 – 92314
Helixi928 – 9347
Turni935 – 9373
Helixi942 – 9476
Turni948 – 9503
Helixi961 – 9688
Beta strandi969 – 9713
Helixi978 – 9814
Helixi989 – 9979
Helixi1004 – 10129
Helixi1014 – 102613
Helixi1035 – 10406
Beta strandi1047 – 10515
Turni1053 – 10553
Beta strandi1057 – 106812
Beta strandi1072 – 109019
Helixi1092 – 10943
Beta strandi1108 – 11103
Beta strandi1118 – 11236
Beta strandi1138 – 11447
Beta strandi1146 – 11494
Beta strandi1164 – 11685
Beta strandi1173 – 11753

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BG3X-ray2.80A/B/C/D482-1178[»]
3BG9X-ray3.00A/B/C/D482-1178[»]
ProteinModelPortaliP11498.
SMRiP11498. Positions 37-488, 494-1178.

Miscellaneous databases

EvolutionaryTraceiP11498.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 486451Biotin carboxylation
Add
BLAST
Domaini156 – 353198ATP-grasp
Add
BLAST
Domaini563 – 832270Carboxyltransferase
Add
BLAST
Domaini1110 – 117768Biotinyl-binding
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni571 – 5755Substrate binding

Sequence similaritiesi

Contains 1 ATP-grasp domain.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1038.
HOGENOMiHOG000282801.
HOVERGENiHBG008340.
InParanoidiP11498.
KOiK01958.
OMAiHSMENIT.
OrthoDBiEOG7WT40F.
PhylomeDBiP11498.
TreeFamiTF300535.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.20.20.70. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
IPR003379. Carboxylase_cons_dom.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR009057. Homeodomain-like.
IPR016185. PreATP-grasp_dom.
IPR000891. PYR_CT.
IPR005930. Pyruv_COase.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PIRSFiPIRSF001594. Pyruv_carbox. 1 hit.
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01235. pyruv_carbox. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P11498-1 [UniParc]FASTAAdd to Basket

« Hide

MLKFRTVHGG LRLLGIRRTS TAPAASPNVR RLEYKPIKKV MVANRGEIAI     50
RVFRACTELG IRTVAIYSEQ DTGQMHRQKA DEAYLIGRGL APVQAYLHIP 100
DIIKVAKENN VDAVHPGYGF LSERADFAQA CQDAGVRFIG PSPEVVRKMG 150
DKVEARAIAI AAGVPVVPGT DAPITSLHEA HEFSNTYGFP IIFKAAYGGG 200
GRGMRVVHSY EELEENYTRA YSEALAAFGN GALFVEKFIE KPRHIEVQIL 250
GDQYGNILHL YERDCSIQRR HQKVVEIAPA AHLDPQLRTR LTSDSVKLAK 300
QVGYENAGTV EFLVDRHGKH YFIEVNSRLQ VEHTVTEEIT DVDLVHAQIH 350
VAEGRSLPDL GLRQENIRIN GCAIQCRVTT EDPARSFQPD TGRIEVFRSG 400
EGMGIRLDNA SAFQGAVISP HYDSLLVKVI AHGKDHPTAA TKMSRALAEF 450
RVRGVKTNIA FLQNVLNNQQ FLAGTVDTQF IDENPELFQL RPAQNRAQKL 500
LHYLGHVMVN GPTTPIPVKA SPSPTDPVVP AVPIGPPPAG FRDILLREGP 550
EGFARAVRNH PGLLLMDTTF RDAHQSLLAT RVRTHDLKKI APYVAHNFSK 600
LFSMENWGGA TFDVAMRFLY ECPWRRLQEL RELIPNIPFQ MLLRGANAVG 650
YTNYPDNVVF KFCEVAKENG MDVFRVFDSL NYLPNMLLGM EAAGSAGGVV 700
EAAISYTGDV ADPSRTKYSL QYYMGLAEEL VRAGTHILCI KDMAGLLKPT 750
ACTMLVSSLR DRFPDLPLHI HTHDTSGAGV AAMLACAQAG ADVVDVAADS 800
MSGMTSQPSM GALVACTRGT PLDTEVPMER VFDYSEYWEG ARGLYAAFDC 850
TATMKSGNSD VYENEIPGGQ YTNLHFQAHS MGLGSKFKEV KKAYVEANQM 900
LGDLIKVTPS SKIVGDLAQF MVQNGLSRAE AEAQAEELSF PRSVVEFLQG 950
YIGVPHGGFP EPFRSKVLKD LPRVEGRPGA SLPPLDLQAL EKELVDRHGE 1000
EVTPEDVLSA AMYPDVFAHF KDFTATFGPL DSLNTRLFLQ GPKIAEEFEV 1050
ELERGKTLHI KALAVSDLNR AGQRQVFFEL NGQLRSILVK DTQAMKEMHF 1100
HPKALKDVKG QIGAPMPGKV IDIKVVAGAK VAKGQPLCVL SAMKMETVVT 1150
SPMEGTVRKV HVTKDMTLEG DDLILEIE 1178
Length:1,178
Mass (Da):129,634
Last modified:October 1, 1996 - v2
Checksum:i381F527553A20095
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761H → L.
Corresponds to variant rs7104156 [ dbSNP | Ensembl ].
VAR_048416
Natural varianti145 – 1451V → A in PC deficiency; mild. 2 Publications
Corresponds to variant rs28940591 [ dbSNP | Ensembl ].
VAR_015199
Natural varianti156 – 1561R → Q in PC deficiency. 1 Publication
VAR_058957
Natural varianti270 – 2701R → W in PC deficiency. 1 Publication
VAR_058958
Natural varianti304 – 3041Y → C in PC deficiency. 1 Publication
VAR_058959
Natural varianti451 – 4511R → C in PC deficiency; mild. 2 Publications
VAR_015200
Natural varianti583 – 5831R → L in PC deficiency. 1 Publication
VAR_058960
Natural varianti610 – 6101A → T in PC deficiency; mild. 2 Publications
Corresponds to variant rs28940589 [ dbSNP | Ensembl ].
VAR_008095
Natural varianti631 – 6311R → Q in PC deficiency. 1 Publication
VAR_058961
Natural varianti743 – 7431M → I in PC deficiency; mild. 2 Publications
Corresponds to variant rs28940590 [ dbSNP | Ensembl ].
VAR_008096
Natural varianti1131 – 11333Missing in PC deficiency.
VAR_058962

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti225 – 2262LA → WP in AAB31500. 1 Publication
Sequence conflicti352 – 3521A → S in AAA82937. 1 Publication
Sequence conflicti385 – 3862RS → PT in AAB31500. 1 Publication
Sequence conflicti486 – 4872EL → DV in AAB31500. 1 Publication
Sequence conflicti638 – 6381P → R in AAB31500. 1 Publication
Sequence conflicti729 – 7291E → A in AAB31500. 1 Publication
Sequence conflicti774 – 7752DT → AP in AAB31500. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U04641 mRNA. Translation: AAA99537.1.
S72370 mRNA. Translation: AAB31500.1.
U30891 mRNA. Translation: AAA82937.1.
BC011617 mRNA. Translation: AAH11617.1.
M26122 mRNA. Translation: AAA36423.1.
K02282 mRNA. Translation: AAA60033.1.
CCDSiCCDS8152.1.
PIRiG01933. JC2460.
RefSeqiNP_000911.2. NM_000920.3.
NP_001035806.1. NM_001040716.1.
NP_071504.2. NM_022172.2.
XP_005274088.1. XM_005274031.2.
XP_005274089.1. XM_005274032.2.
XP_006718640.1. XM_006718577.1.
XP_006718641.1. XM_006718578.1.
UniGeneiHs.89890.

Genome annotation databases

EnsembliENST00000393955; ENSP00000377527; ENSG00000173599.
ENST00000393958; ENSP00000377530; ENSG00000173599.
ENST00000393960; ENSP00000377532; ENSG00000173599.
GeneIDi5091.
KEGGihsa:5091.
UCSCiuc001ojn.1. human.

Polymorphism databases

DMDMi1709947.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Pyruvate carboxylase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U04641 mRNA. Translation: AAA99537.1 .
S72370 mRNA. Translation: AAB31500.1 .
U30891 mRNA. Translation: AAA82937.1 .
BC011617 mRNA. Translation: AAH11617.1 .
M26122 mRNA. Translation: AAA36423.1 .
K02282 mRNA. Translation: AAA60033.1 .
CCDSi CCDS8152.1.
PIRi G01933. JC2460.
RefSeqi NP_000911.2. NM_000920.3.
NP_001035806.1. NM_001040716.1.
NP_071504.2. NM_022172.2.
XP_005274088.1. XM_005274031.2.
XP_005274089.1. XM_005274032.2.
XP_006718640.1. XM_006718577.1.
XP_006718641.1. XM_006718578.1.
UniGenei Hs.89890.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BG3 X-ray 2.80 A/B/C/D 482-1178 [» ]
3BG9 X-ray 3.00 A/B/C/D 482-1178 [» ]
ProteinModelPortali P11498.
SMRi P11498. Positions 37-488, 494-1178.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111124. 19 interactions.
DIPi DIP-46372N.
IntActi P11498. 4 interactions.
MINTi MINT-3007737.
STRINGi 9606.ENSP00000377527.

Chemistry

DrugBanki DB00121. Biotin.
DB00119. Pyruvic acid.

PTM databases

PhosphoSitei P11498.

Polymorphism databases

DMDMi 1709947.

Proteomic databases

MaxQBi P11498.
PaxDbi P11498.
PeptideAtlasi P11498.
PRIDEi P11498.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000393955 ; ENSP00000377527 ; ENSG00000173599 .
ENST00000393958 ; ENSP00000377530 ; ENSG00000173599 .
ENST00000393960 ; ENSP00000377532 ; ENSG00000173599 .
GeneIDi 5091.
KEGGi hsa:5091.
UCSCi uc001ojn.1. human.

Organism-specific databases

CTDi 5091.
GeneCardsi GC11M066615.
GeneReviewsi PC.
HGNCi HGNC:8636. PC.
HPAi CAB033742.
HPA043922.
MIMi 266150. phenotype.
608786. gene.
neXtProti NX_P11498.
Orphaneti 353320. Pyruvate carboxylase deficiency, benign type.
353308. Pyruvate carboxylase deficiency, infantile type.
353314. Pyruvate carboxylase deficiency, severe neonatal type.
PharmGKBi PA32975.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1038.
HOGENOMi HOG000282801.
HOVERGENi HBG008340.
InParanoidi P11498.
KOi K01958.
OMAi HSMENIT.
OrthoDBi EOG7WT40F.
PhylomeDBi P11498.
TreeFami TF300535.

Enzyme and pathway databases

UniPathwayi UPA00138 .
BioCyci MetaCyc:HS10697-MONOMER.
BRENDAi 6.4.1.1. 2681.
Reactomei REACT_11153. Biotin transport and metabolism.
REACT_1520. Gluconeogenesis.
REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
SABIO-RKi P11498.

Miscellaneous databases

ChiTaRSi PC. human.
EvolutionaryTracei P11498.
GenomeRNAii 5091.
NextBioi 19632.
PROi P11498.
SOURCEi Search...

Gene expression databases

ArrayExpressi P11498.
Bgeei P11498.
CleanExi HS_PC.
Genevestigatori P11498.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
3.20.20.70. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
IPR003379. Carboxylase_cons_dom.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR009057. Homeodomain-like.
IPR016185. PreATP-grasp_dom.
IPR000891. PYR_CT.
IPR005930. Pyruv_COase.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view ]
PIRSFi PIRSF001594. Pyruv_carbox. 1 hit.
SMARTi SM00878. Biotin_carb_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsi TIGR01235. pyruv_carbox. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOTINYLATION AT LYS-1144.
    Tissue: Kidney and Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  3. Walker M.E., Jitrapakdee S., Val D.L., Wallace J.C.
    Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney and Liver.
  4. "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].
    Tissue: Lung.
  5. "Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase."
    Lamhonwah A.-M., Quan F., Gravel R.A.
    Arch. Biochem. Biophys. 254:631-636(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1083-1178.
  6. "Molecular cloning of a cDNA for human pyruvate carboxylase. Structural relationship to other biotin-containing carboxylases and regulation of mRNA content in differentiating preadipocytes."
    Freytag S.O., Collier K.J.
    J. Biol. Chem. 259:12831-12837(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1135-1178, BIOTINYLATION AT LYS-1144.
  7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1090, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction."
    Xiang S., Tong L.
    Nat. Struct. Mol. Biol. 15:295-302(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 481-1178 IN COMPLEX WITH PYRUVATE; MANGANESE AND BIOTIN ANALOG, CARBAMYLATION AT LYS-741, MUTAGENESIS OF PHE-1077, SUBUNIT.
  10. Cited for: VARIANTS PC DEFICIENCY THR-610 AND ILE-743.
  11. "Molecular characterization of pyruvate carboxylase deficiency in two consanguineous families."
    Wexler I.D., Kerr D.S., Du Y., Kaung M.M., Stephenson W., Lusk M.M., Wappner R.S., Higgins J.J.
    Pediatr. Res. 43:579-584(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PC DEFICIENCY ALA-145 AND CYS-451.
  12. "Structural insights on pathogenic effects of novel mutations causing pyruvate carboxylase deficiency."
    Monnot S., Serre V., Chadefaux-Vekemans B., Aupetit J., Romano S., De Lonlay P., Rival J.-M., Munnich A., Steffann J., Bonnefont J.-P.
    Hum. Mutat. 30:734-740(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PC DEFICIENCY ALA-145; GLN-156; TRP-270; CYS-304; CYS-451; LEU-583; THR-610; GLN-631; ILE-743 AND 1131-VAL--LYS-1133 DEL.

Entry informationi

Entry nameiPYC_HUMAN
AccessioniPrimary (citable) accession number: P11498
Secondary accession number(s): Q16705
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 170 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

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

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