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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

Protein has several cofactor binding sites:
  • biotinNote: Biotin.
  • Mn2+Note: Binds 1 Mn(2+) ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei152 – 1521ATPBy similarity
Binding sitei236 – 2361ATPBy similarity
Binding sitei271 – 2711ATPBy similarity
Active sitei328 – 3281By similarity
Metal bindingi572 – 5721Manganese1 Publication
Binding sitei644 – 6441Substrate
Metal bindingi741 – 7411Manganese; via carbamate group1 Publication
Metal bindingi771 – 7711Manganese; via tele nitrogen1 Publication
Metal bindingi773 – 7731Manganese; via tele nitrogen1 Publication
Binding sitei908 – 9081Substrate

GO - Molecular functioni

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

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-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
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. 1 Publication
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 – 2020MitochondrionSequence AnalysisAdd
BLAST
Chaini21 – 11781158Pyruvate carboxylase, mitochondrialPRO_0000002840Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791N6-acetyllysine; alternateBy similarity
Modified residuei79 – 791N6-succinyllysine; alternateBy similarity
Modified residuei297 – 2971N6-acetyllysineBy similarity
Modified residuei319 – 3191N6-acetyllysineBy similarity
Modified residuei434 – 4341N6-acetyllysineBy similarity
Modified residuei442 – 4421N6-succinyllysineBy similarity
Modified residuei661 – 6611N6-acetyllysineBy similarity
Modified residuei741 – 7411N6-carboxylysine1 Publication
Modified residuei748 – 7481N6-acetyllysineBy similarity
Modified residuei992 – 9921N6-acetyllysineBy similarity
Modified residuei1061 – 10611N6-acetyllysineBy similarity
Modified residuei1090 – 10901N6-acetyllysine1 Publication
Modified residuei1124 – 11241N6-acetyllysineBy similarity
Modified residuei1144 – 11441N6-biotinyllysine2 PublicationsPROSITE-ProRule annotation

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP11498.
PaxDbiP11498.
PeptideAtlasiP11498.
PRIDEiP11498.

PTM databases

PhosphoSiteiP11498.

Expressioni

Gene expression databases

BgeeiP11498.
CleanExiHS_PC.
ExpressionAtlasiP11498. baseline and differential.
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. 28 interactions.
DIPiDIP-46372N.
IntActiP11498. 4 interactions.
MINTiMINT-3007737.
STRINGi9606.ENSP00000377527.

Structurei

Secondary structure

1
1178
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi495 – 51016Combined sources
Helixi541 – 55919Combined sources
Beta strandi564 – 5674Combined sources
Turni569 – 5713Combined sources
Helixi572 – 5776Combined sources
Helixi584 – 59714Combined sources
Beta strandi602 – 6087Combined sources
Helixi611 – 6177Combined sources
Helixi623 – 63311Combined sources
Beta strandi635 – 6373Combined sources
Beta strandi639 – 6435Combined sources
Helixi645 – 6473Combined sources
Beta strandi650 – 6523Combined sources
Helixi656 – 66914Combined sources
Beta strandi673 – 6775Combined sources
Helixi683 – 69412Combined sources
Turni695 – 6973Combined sources
Beta strandi698 – 7058Combined sources
Helixi720 – 73314Combined sources
Beta strandi736 – 7416Combined sources
Helixi749 – 76214Combined sources
Beta strandi768 – 7714Combined sources
Helixi779 – 78810Combined sources
Beta strandi792 – 7976Combined sources
Helixi799 – 8013Combined sources
Helixi810 – 8178Combined sources
Helixi828 – 84417Combined sources
Helixi845 – 8484Combined sources
Helixi850 – 8523Combined sources
Helixi861 – 8644Combined sources
Helixi868 – 8758Combined sources
Helixi876 – 8783Combined sources
Turni879 – 8813Combined sources
Helixi886 – 90015Combined sources
Helixi910 – 92314Combined sources
Helixi928 – 9347Combined sources
Turni935 – 9373Combined sources
Helixi942 – 9476Combined sources
Turni948 – 9503Combined sources
Helixi961 – 9688Combined sources
Beta strandi969 – 9713Combined sources
Helixi978 – 9814Combined sources
Helixi989 – 9979Combined sources
Helixi1004 – 10129Combined sources
Helixi1014 – 102613Combined sources
Helixi1035 – 10406Combined sources
Beta strandi1047 – 10515Combined sources
Turni1053 – 10553Combined sources
Beta strandi1057 – 106812Combined sources
Beta strandi1072 – 109019Combined sources
Helixi1092 – 10943Combined sources
Beta strandi1108 – 11103Combined sources
Beta strandi1118 – 11236Combined sources
Beta strandi1138 – 11447Combined sources
Beta strandi1146 – 11494Combined sources
Beta strandi1164 – 11685Combined sources
Beta strandi1173 – 11753Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11498.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 486451Biotin carboxylationAdd
BLAST
Domaini156 – 353198ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini563 – 832270CarboxyltransferaseAdd
BLAST
Domaini1109 – 117870Biotinyl-bindingPROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1038.
GeneTreeiENSGT00550000074986.
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]

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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti225 – 2262LA → WP in AAB31500. (PubMed:8048912)Curated
Sequence conflicti352 – 3521A → S in AAA82937. 1 PublicationCurated
Sequence conflicti385 – 3862RS → PT in AAB31500. (PubMed:8048912)Curated
Sequence conflicti486 – 4872EL → DV in AAB31500. (PubMed:8048912)Curated
Sequence conflicti638 – 6381P → R in AAB31500. (PubMed:8048912)Curated
Sequence conflicti729 – 7291E → A in AAB31500. (PubMed:8048912)Curated
Sequence conflicti774 – 7752DT → AP in AAB31500. (PubMed:8048912)Curated

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. 1 Publication
VAR_058962

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei457 – 52973TNIAF…TDPVV → VRRHQAQPLAAALGRPCGQE ARRPQAAVTAPTGPGSPTLV RVPPAARVLSSRLGGPSQTT PETSTEVSPTILL in isoform 2. 1 PublicationVSP_056358Add
BLAST
Alternative sequencei530 – 1178649Missing in isoform 2. 1 PublicationVSP_056359Add
BLAST

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_005274031.2. [P11498-1]
XP_005274089.1. XM_005274032.2. [P11498-1]
XP_006718640.1. XM_006718577.1. [P11498-1]
XP_006718641.1. XM_006718578.1. [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.1. human. [P11498-1]

Polymorphism databases

DMDMi1709947.

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 .
CCDSi CCDS8152.1. [P11498-1 ]
PIRi G01933. JC2460.
RefSeqi NP_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_005274031.2. [P11498-1 ]
XP_005274089.1. XM_005274032.2. [P11498-1 ]
XP_006718640.1. XM_006718577.1. [P11498-1 ]
XP_006718641.1. XM_006718578.1. [P11498-1 ]
UniGenei Hs.89890.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111124. 28 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 . [P11498-1 ]
ENST00000393958 ; ENSP00000377530 ; ENSG00000173599 . [P11498-1 ]
ENST00000393960 ; ENSP00000377532 ; ENSG00000173599 . [P11498-1 ]
GeneIDi 5091.
KEGGi hsa:5091.
UCSCi uc001ojn.1. human. [P11498-1 ]

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.
GeneTreei ENSGT00550000074986.
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-RK P11498.

Miscellaneous databases

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

Gene expression databases

Bgeei P11498.
CleanExi HS_PC.
ExpressionAtlasi P11498. baseline and differential.
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] (ISOFORM 1), BIOTINYLATION AT LYS-1144.
    Tissue: Kidney and Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 1).
    Tissue: Kidney and Liver.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lung.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  7. "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 (ISOFORM 1).
  8. "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 (ISOFORM 1), BIOTINYLATION AT LYS-1144.
  9. "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].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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.
  12. Cited for: VARIANTS PC DEFICIENCY THR-610 AND ILE-743.
  13. "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.
  14. "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): B4DN00, Q16705
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 173 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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