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Protein

Pyruvate carboxylase, mitochondrial

Gene

PC

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

Protein has several cofactor binding sites:

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei152ATPBy similarity1
Binding sitei236ATPBy similarity1
Binding sitei271ATPBy similarity1
Active sitei328By similarity1
Metal bindingi572Manganese1 Publication1
Binding sitei644Substrate1
Metal bindingi741Manganese; via carbamate group1 Publication1
Metal bindingi771Manganese; via tele nitrogen1 Publication1
Metal bindingi773Manganese; via tele nitrogen1 Publication1
Binding sitei908Substrate1

GO - Molecular functioni

  • ATP binding Source: ProtInc
  • biotin binding Source: ProtInc
  • biotin carboxylase activity Source: InterPro
  • DNA binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • pyruvate carboxylase activity Source: Reactome

GO - Biological processi

  • biotin metabolic process Source: Reactome
  • gluconeogenesis Source: Reactome
  • lipid metabolic process Source: UniProtKB-KW
  • negative regulation of gene expression Source: AgBase
  • positive regulation by host of viral process Source: AgBase
  • positive regulation by host of viral release from host cell Source: AgBase
  • pyruvate metabolic process Source: InterPro
  • viral RNA genome packaging Source: AgBase
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.
ZFISH:HS10697-MONOMER.
BRENDAi6.4.1.1. 2681.
ReactomeiR-HSA-196780. Biotin transport and metabolism.
R-HSA-3371599. Defective HLCS causes multiple carboxylase deficiency.
R-HSA-70263. Gluconeogenesis.
SABIO-RKP11498.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:8636. PC.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: AgBase
  • cytosol Source: Reactome
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Pyruvate carboxylase deficiency (PC deficiency)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionLeads 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.
See also OMIM:266150
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015199145V → A in PC deficiency; mild. 2 PublicationsCorresponds to variant rs28940591dbSNPEnsembl.1
Natural variantiVAR_058957156R → Q in PC deficiency. 1 PublicationCorresponds to variant rs119103241dbSNPEnsembl.1
Natural variantiVAR_058958270R → W in PC deficiency. 1 Publication1
Natural variantiVAR_058959304Y → C in PC deficiency. 1 Publication1
Natural variantiVAR_015200451R → C in PC deficiency; mild. 2 PublicationsCorresponds to variant rs113994143dbSNPEnsembl.1
Natural variantiVAR_058960583R → L in PC deficiency. 1 PublicationCorresponds to variant rs119103242dbSNPEnsembl.1
Natural variantiVAR_008095610A → T in PC deficiency; mild. 2 PublicationsCorresponds to variant rs28940589dbSNPEnsembl.1
Natural variantiVAR_058961631R → Q in PC deficiency. 1 PublicationCorresponds to variant rs113994145dbSNPEnsembl.1
Natural variantiVAR_008096743M → I in PC deficiency; mild. 2 PublicationsCorresponds to variant rs28940590dbSNPEnsembl.1
Natural variantiVAR_0589621131 – 1133Missing in PC deficiency. 1 Publication3

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1077F → A or E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi5091.
MalaCardsiPC.
MIMi266150. phenotype.
OpenTargetsiENSG00000173599.
Orphaneti353320. Pyruvate carboxylase deficiency, benign type.
353308. Pyruvate carboxylase deficiency, infantile form.
353314. Pyruvate carboxylase deficiency, severe neonatal type.
PharmGKBiPA32975.

Chemistry databases

DrugBankiDB00121. Biotin.
DB00119. Pyruvic acid.

Polymorphism and mutation databases

BioMutaiPC.
DMDMi1709947.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 20MitochondrionSequence analysisAdd BLAST20
ChainiPRO_000000284021 – 1178Pyruvate carboxylase, mitochondrialAdd BLAST1158

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei79N6-acetyllysine; alternateBy similarity1
Modified residuei79N6-succinyllysine; alternateBy similarity1
Modified residuei297N6-acetyllysineBy similarity1
Modified residuei319N6-acetyllysineBy similarity1
Modified residuei434N6-acetyllysineBy similarity1
Modified residuei442N6-succinyllysineBy similarity1
Modified residuei661N6-acetyllysineBy similarity1
Modified residuei741N6-carboxylysine1 Publication1
Modified residuei748N6-acetyllysineBy similarity1
Modified residuei992N6-acetyllysineBy similarity1
Modified residuei1003PhosphothreonineBy similarity1
Modified residuei1061N6-acetyllysineBy similarity1
Modified residuei1090N6-acetyllysineCombined sources1
Modified residuei1124N6-acetyllysineBy similarity1
Modified residuei1144N6-biotinyllysinePROSITE-ProRule annotation2 Publications1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP11498.
MaxQBiP11498.
PaxDbiP11498.
PeptideAtlasiP11498.
PRIDEiP11498.

PTM databases

iPTMnetiP11498.
PhosphoSitePlusiP11498.
SwissPalmiP11498.

Expressioni

Gene expression databases

BgeeiENSG00000173599.
CleanExiHS_PC.
ExpressionAtlasiP11498. baseline and differential.
GenevisibleiP11498. HS.

Organism-specific databases

HPAiCAB033742.
HPA043922.
HPA058765.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111124. 63 interactors.
DIPiDIP-46372N.
IntActiP11498. 16 interactors.
MINTiMINT-3007737.
STRINGi9606.ENSP00000377527.

Structurei

Secondary structure

11178
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi495 – 510Combined sources16
Helixi541 – 559Combined sources19
Beta strandi564 – 567Combined sources4
Turni569 – 571Combined sources3
Helixi572 – 577Combined sources6
Helixi584 – 597Combined sources14
Beta strandi602 – 608Combined sources7
Helixi611 – 617Combined sources7
Helixi623 – 633Combined sources11
Beta strandi635 – 637Combined sources3
Beta strandi639 – 643Combined sources5
Helixi645 – 647Combined sources3
Beta strandi650 – 652Combined sources3
Helixi656 – 669Combined sources14
Beta strandi673 – 677Combined sources5
Helixi683 – 694Combined sources12
Turni695 – 697Combined sources3
Beta strandi698 – 705Combined sources8
Helixi720 – 733Combined sources14
Beta strandi736 – 741Combined sources6
Helixi749 – 762Combined sources14
Beta strandi768 – 771Combined sources4
Helixi779 – 788Combined sources10
Beta strandi792 – 797Combined sources6
Helixi799 – 801Combined sources3
Helixi810 – 817Combined sources8
Helixi828 – 844Combined sources17
Helixi845 – 848Combined sources4
Helixi850 – 852Combined sources3
Helixi861 – 864Combined sources4
Helixi868 – 875Combined sources8
Helixi876 – 878Combined sources3
Turni879 – 881Combined sources3
Helixi886 – 900Combined sources15
Helixi910 – 923Combined sources14
Helixi928 – 934Combined sources7
Turni935 – 937Combined sources3
Helixi942 – 947Combined sources6
Turni948 – 950Combined sources3
Helixi961 – 968Combined sources8
Beta strandi969 – 971Combined sources3
Helixi978 – 981Combined sources4
Helixi989 – 997Combined sources9
Helixi1004 – 1012Combined sources9
Helixi1014 – 1026Combined sources13
Helixi1035 – 1040Combined sources6
Beta strandi1047 – 1051Combined sources5
Turni1053 – 1055Combined sources3
Beta strandi1057 – 1068Combined sources12
Beta strandi1072 – 1090Combined sources19
Helixi1092 – 1094Combined sources3
Beta strandi1108 – 1110Combined sources3
Beta strandi1118 – 1123Combined sources6
Beta strandi1138 – 1144Combined sources7
Beta strandi1146 – 1149Combined sources4
Beta strandi1164 – 1168Combined sources5
Beta strandi1173 – 1175Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BG3X-ray2.80A/B/C/D482-1178[»]
3BG9X-ray3.00A/B/C/D482-1178[»]
ProteinModelPortaliP11498.
SMRiP11498.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11498.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 486Biotin carboxylationAdd BLAST451
Domaini156 – 353ATP-graspPROSITE-ProRule annotationAdd BLAST198
Domaini563 – 832Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST270
Domaini1109 – 1178Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST70

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni571 – 575Substrate binding5

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.Curated
Contains 1 biotinyl-binding domain.PROSITE-ProRule annotationCurated
Contains 1 pyruvate carboxyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IU5D. Eukaryota.
COG1038. LUCA.
GeneTreeiENSGT00550000074986.
HOGENOMiHOG000282801.
HOVERGENiHBG008340.
InParanoidiP11498.
KOiK01958.
OrthoDBiEOG091G00X2.
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.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
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.
PF00289. Biotin_carb_N. 1 hit.
PF00364. Biotin_lipoyl. 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P11498-1) [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
MLKFRTVHGG LRLLGIRRTS TAPAASPNVR RLEYKPIKKV MVANRGEIAI
60 70 80 90 100
RVFRACTELG IRTVAIYSEQ DTGQMHRQKA DEAYLIGRGL APVQAYLHIP
110 120 130 140 150
DIIKVAKENN VDAVHPGYGF LSERADFAQA CQDAGVRFIG PSPEVVRKMG
160 170 180 190 200
DKVEARAIAI AAGVPVVPGT DAPITSLHEA HEFSNTYGFP IIFKAAYGGG
210 220 230 240 250
GRGMRVVHSY EELEENYTRA YSEALAAFGN GALFVEKFIE KPRHIEVQIL
260 270 280 290 300
GDQYGNILHL YERDCSIQRR HQKVVEIAPA AHLDPQLRTR LTSDSVKLAK
310 320 330 340 350
QVGYENAGTV EFLVDRHGKH YFIEVNSRLQ VEHTVTEEIT DVDLVHAQIH
360 370 380 390 400
VAEGRSLPDL GLRQENIRIN GCAIQCRVTT EDPARSFQPD TGRIEVFRSG
410 420 430 440 450
EGMGIRLDNA SAFQGAVISP HYDSLLVKVI AHGKDHPTAA TKMSRALAEF
460 470 480 490 500
RVRGVKTNIA FLQNVLNNQQ FLAGTVDTQF IDENPELFQL RPAQNRAQKL
510 520 530 540 550
LHYLGHVMVN GPTTPIPVKA SPSPTDPVVP AVPIGPPPAG FRDILLREGP
560 570 580 590 600
EGFARAVRNH PGLLLMDTTF RDAHQSLLAT RVRTHDLKKI APYVAHNFSK
610 620 630 640 650
LFSMENWGGA TFDVAMRFLY ECPWRRLQEL RELIPNIPFQ MLLRGANAVG
660 670 680 690 700
YTNYPDNVVF KFCEVAKENG MDVFRVFDSL NYLPNMLLGM EAAGSAGGVV
710 720 730 740 750
EAAISYTGDV ADPSRTKYSL QYYMGLAEEL VRAGTHILCI KDMAGLLKPT
760 770 780 790 800
ACTMLVSSLR DRFPDLPLHI HTHDTSGAGV AAMLACAQAG ADVVDVAADS
810 820 830 840 850
MSGMTSQPSM GALVACTRGT PLDTEVPMER VFDYSEYWEG ARGLYAAFDC
860 870 880 890 900
TATMKSGNSD VYENEIPGGQ YTNLHFQAHS MGLGSKFKEV KKAYVEANQM
910 920 930 940 950
LGDLIKVTPS SKIVGDLAQF MVQNGLSRAE AEAQAEELSF PRSVVEFLQG
960 970 980 990 1000
YIGVPHGGFP EPFRSKVLKD LPRVEGRPGA SLPPLDLQAL EKELVDRHGE
1010 1020 1030 1040 1050
EVTPEDVLSA AMYPDVFAHF KDFTATFGPL DSLNTRLFLQ GPKIAEEFEV
1060 1070 1080 1090 1100
ELERGKTLHI KALAVSDLNR AGQRQVFFEL NGQLRSILVK DTQAMKEMHF
1110 1120 1130 1140 1150
HPKALKDVKG QIGAPMPGKV IDIKVVAGAK VAKGQPLCVL SAMKMETVVT
1160 1170
SPMEGTVRKV HVTKDMTLEG DDLILEIE
Length:1,178
Mass (Da):129,634
Last modified:October 1, 1996 - v2
Checksum:i381F527553A20095
GO
Isoform 2 (identifier: P11498-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     457-529: TNIAFLQNVL...ASPSPTDPVV → VRRHQAQPLA...STEVSPTILL
     530-1178: Missing.

Note: No experimental confirmation available.
Show »
Length:529
Mass (Da):57,925
Checksum:i35B87A653BF6F9C3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti225 – 226LA → WP in AAB31500 (PubMed:8048912).Curated2
Sequence conflicti352A → S in AAA82937 (Ref. 3) Curated1
Sequence conflicti385 – 386RS → PT in AAB31500 (PubMed:8048912).Curated2
Sequence conflicti486 – 487EL → DV in AAB31500 (PubMed:8048912).Curated2
Sequence conflicti638P → R in AAB31500 (PubMed:8048912).Curated1
Sequence conflicti729E → A in AAB31500 (PubMed:8048912).Curated1
Sequence conflicti774 – 775DT → AP in AAB31500 (PubMed:8048912).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04841676H → L.Corresponds to variant rs7104156dbSNPEnsembl.1
Natural variantiVAR_015199145V → A in PC deficiency; mild. 2 PublicationsCorresponds to variant rs28940591dbSNPEnsembl.1
Natural variantiVAR_058957156R → Q in PC deficiency. 1 PublicationCorresponds to variant rs119103241dbSNPEnsembl.1
Natural variantiVAR_058958270R → W in PC deficiency. 1 Publication1
Natural variantiVAR_058959304Y → C in PC deficiency. 1 Publication1
Natural variantiVAR_015200451R → C in PC deficiency; mild. 2 PublicationsCorresponds to variant rs113994143dbSNPEnsembl.1
Natural variantiVAR_058960583R → L in PC deficiency. 1 PublicationCorresponds to variant rs119103242dbSNPEnsembl.1
Natural variantiVAR_008095610A → T in PC deficiency; mild. 2 PublicationsCorresponds to variant rs28940589dbSNPEnsembl.1
Natural variantiVAR_058961631R → Q in PC deficiency. 1 PublicationCorresponds to variant rs113994145dbSNPEnsembl.1
Natural variantiVAR_008096743M → I in PC deficiency; mild. 2 PublicationsCorresponds to variant rs28940590dbSNPEnsembl.1
Natural variantiVAR_0589621131 – 1133Missing in PC deficiency. 1 Publication3

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056358457 – 529TNIAF…TDPVV → VRRHQAQPLAAALGRPCGQE ARRPQAAVTAPTGPGSPTLV RVPPAARVLSSRLGGPSQTT PETSTEVSPTILL in isoform 2. 1 PublicationAdd BLAST73
Alternative sequenceiVSP_056359530 – 1178Missing in isoform 2. 1 PublicationAdd BLAST649

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04641 mRNA. Translation: AAA99537.1.
S72370 mRNA. Translation: AAB31500.1.
U30891 mRNA. Translation: AAA82937.1.
AK297705 mRNA. Translation: BAG60062.1.
AP000485 Genomic DNA. No translation available.
AP003176 Genomic DNA. No translation available.
BC011617 mRNA. Translation: AAH11617.1.
M26122 mRNA. Translation: AAA36423.1.
K02282 mRNA. Translation: AAA60033.1.
CCDSiCCDS8152.1. [P11498-1]
PIRiG01933. JC2460.
RefSeqiNP_000911.2. NM_000920.3. [P11498-1]
NP_001035806.1. NM_001040716.1. [P11498-1]
NP_071504.2. NM_022172.2. [P11498-1]
XP_005274088.1. XM_005274031.4. [P11498-1]
XP_005274089.1. XM_005274032.4. [P11498-1]
XP_006718641.1. XM_006718578.3. [P11498-1]
XP_011543388.1. XM_011545086.2. [P11498-1]
XP_016873357.1. XM_017017868.1. [P11498-1]
XP_016873358.1. XM_017017869.1. [P11498-1]
XP_016873359.1. XM_017017870.1. [P11498-1]
XP_016873360.1. XM_017017871.1. [P11498-1]
XP_016873361.1. XM_017017872.1. [P11498-1]
UniGeneiHs.89890.

Genome annotation databases

EnsembliENST00000393955; ENSP00000377527; ENSG00000173599. [P11498-1]
ENST00000393958; ENSP00000377530; ENSG00000173599. [P11498-1]
ENST00000393960; ENSP00000377532; ENSG00000173599. [P11498-1]
GeneIDi5091.
KEGGihsa:5091.
UCSCiuc001ojn.2. human. [P11498-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Pyruvate carboxylase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04641 mRNA. Translation: AAA99537.1.
S72370 mRNA. Translation: AAB31500.1.
U30891 mRNA. Translation: AAA82937.1.
AK297705 mRNA. Translation: BAG60062.1.
AP000485 Genomic DNA. No translation available.
AP003176 Genomic DNA. No translation available.
BC011617 mRNA. Translation: AAH11617.1.
M26122 mRNA. Translation: AAA36423.1.
K02282 mRNA. Translation: AAA60033.1.
CCDSiCCDS8152.1. [P11498-1]
PIRiG01933. JC2460.
RefSeqiNP_000911.2. NM_000920.3. [P11498-1]
NP_001035806.1. NM_001040716.1. [P11498-1]
NP_071504.2. NM_022172.2. [P11498-1]
XP_005274088.1. XM_005274031.4. [P11498-1]
XP_005274089.1. XM_005274032.4. [P11498-1]
XP_006718641.1. XM_006718578.3. [P11498-1]
XP_011543388.1. XM_011545086.2. [P11498-1]
XP_016873357.1. XM_017017868.1. [P11498-1]
XP_016873358.1. XM_017017869.1. [P11498-1]
XP_016873359.1. XM_017017870.1. [P11498-1]
XP_016873360.1. XM_017017871.1. [P11498-1]
XP_016873361.1. XM_017017872.1. [P11498-1]
UniGeneiHs.89890.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BG3X-ray2.80A/B/C/D482-1178[»]
3BG9X-ray3.00A/B/C/D482-1178[»]
ProteinModelPortaliP11498.
SMRiP11498.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111124. 63 interactors.
DIPiDIP-46372N.
IntActiP11498. 16 interactors.
MINTiMINT-3007737.
STRINGi9606.ENSP00000377527.

Chemistry databases

DrugBankiDB00121. Biotin.
DB00119. Pyruvic acid.

PTM databases

iPTMnetiP11498.
PhosphoSitePlusiP11498.
SwissPalmiP11498.

Polymorphism and mutation databases

BioMutaiPC.
DMDMi1709947.

Proteomic databases

EPDiP11498.
MaxQBiP11498.
PaxDbiP11498.
PeptideAtlasiP11498.
PRIDEiP11498.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000393955; ENSP00000377527; ENSG00000173599. [P11498-1]
ENST00000393958; ENSP00000377530; ENSG00000173599. [P11498-1]
ENST00000393960; ENSP00000377532; ENSG00000173599. [P11498-1]
GeneIDi5091.
KEGGihsa:5091.
UCSCiuc001ojn.2. human. [P11498-1]

Organism-specific databases

CTDi5091.
DisGeNETi5091.
GeneCardsiPC.
GeneReviewsiPC.
HGNCiHGNC:8636. PC.
HPAiCAB033742.
HPA043922.
HPA058765.
MalaCardsiPC.
MIMi266150. phenotype.
608786. gene.
neXtProtiNX_P11498.
OpenTargetsiENSG00000173599.
Orphaneti353320. Pyruvate carboxylase deficiency, benign type.
353308. Pyruvate carboxylase deficiency, infantile form.
353314. Pyruvate carboxylase deficiency, severe neonatal type.
PharmGKBiPA32975.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IU5D. Eukaryota.
COG1038. LUCA.
GeneTreeiENSGT00550000074986.
HOGENOMiHOG000282801.
HOVERGENiHBG008340.
InParanoidiP11498.
KOiK01958.
OrthoDBiEOG091G00X2.
PhylomeDBiP11498.
TreeFamiTF300535.

Enzyme and pathway databases

UniPathwayiUPA00138.
BioCyciMetaCyc:HS10697-MONOMER.
ZFISH:HS10697-MONOMER.
BRENDAi6.4.1.1. 2681.
ReactomeiR-HSA-196780. Biotin transport and metabolism.
R-HSA-3371599. Defective HLCS causes multiple carboxylase deficiency.
R-HSA-70263. Gluconeogenesis.
SABIO-RKP11498.

Miscellaneous databases

ChiTaRSiPC. human.
EvolutionaryTraceiP11498.
GenomeRNAii5091.
PROiP11498.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000173599.
CleanExiHS_PC.
ExpressionAtlasiP11498. baseline and differential.
GenevisibleiP11498. HS.

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.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
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.
PF00289. Biotin_carb_N. 1 hit.
PF00364. Biotin_lipoyl. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPYC_HUMAN
AccessioniPrimary (citable) accession number: P11498
Secondary accession number(s): B4DN00, Q16705
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 195 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

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 one 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.