UniProtKB - P11498 (PYC_HUMAN)
Protein
Pyruvate carboxylase, mitochondrial
Gene
PC
Organism
Homo sapiens (Human)
Status
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
- EC:6.4.1.1
Cofactori
Protein has several cofactor binding sites:: gluconeogenesis Pathwayi
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 152 | ATPBy similarity | 1 | |
Binding sitei | 236 | ATPBy similarity | 1 | |
Binding sitei | 271 | ATPBy similarity | 1 | |
Active sitei | 328 | By similarity | 1 | |
Metal bindingi | 572 | Manganese1 Publication | 1 | |
Binding sitei | 644 | Substrate | 1 | |
Metal bindingi | 741 | Manganese; via carbamate group1 Publication | 1 | |
Metal bindingi | 771 | Manganese; via tele nitrogen1 Publication | 1 | |
Metal bindingi | 773 | Manganese; via tele nitrogen1 Publication | 1 | |
Binding sitei | 908 | Substrate | 1 |
GO - Molecular functioni
- ATP binding Source: ProtInc
- biotin binding Source: ProtInc
- identical protein binding Source: IntAct
- metal ion binding Source: UniProtKB-KW
- pyruvate carboxylase activity Source: GO_Central
GO - Biological processi
- biotin metabolic process Source: Reactome
- gluconeogenesis Source: GO_Central
- 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: GO_Central
- viral RNA genome packaging Source: AgBase
Keywordsi
Molecular function | Ligase, Multifunctional enzyme |
Biological process | Gluconeogenesis, Lipid biosynthesis, Lipid metabolism |
Ligand | ATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding, Pyruvate |
Enzyme and pathway databases
BioCyci | MetaCyc:HS10697-MONOMER |
BRENDAi | 6.4.1.1, 2681 |
PathwayCommonsi | P11498 |
Reactomei | R-HSA-196780, Biotin transport and metabolism R-HSA-3371599, Defective HLCS causes multiple carboxylase deficiency R-HSA-70263, Gluconeogenesis |
SABIO-RKi | P11498 |
SIGNORi | P11498 |
UniPathwayi | UPA00138 |
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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:8636, PC |
MIMi | 608786, gene |
neXtProti | NX_P11498 |
VEuPathDBi | HostDB:ENSG00000173599.13 |
Subcellular locationi
Mitochondrion
Cytosol
- cytosol Source: Reactome
Mitochondrion
- mitochondrial matrix Source: Reactome
- mitochondrion Source: HPA
Other locations
- cytoplasm Source: AgBase
Keywords - Cellular componenti
MitochondrionPathology & Biotechi
Involvement in diseasei
Pyruvate carboxylase deficiency (PC deficiency)
The disease is caused by variants 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.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_015199 | 145 | V → A in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs28940591EnsemblClinVar. | 1 | |
Natural variantiVAR_058957 | 156 | R → Q in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs119103241EnsemblClinVar. | 1 | |
Natural variantiVAR_058958 | 270 | R → W in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs1258494752Ensembl. | 1 | |
Natural variantiVAR_058959 | 304 | Y → C in PC deficiency. 1 Publication | 1 | |
Natural variantiVAR_015200 | 451 | R → C in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs113994143EnsemblClinVar. | 1 | |
Natural variantiVAR_058960 | 583 | R → L in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs119103242EnsemblClinVar. | 1 | |
Natural variantiVAR_008095 | 610 | A → T in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs28940589EnsemblClinVar. | 1 | |
Natural variantiVAR_058961 | 631 | R → Q in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs113994145EnsemblClinVar. | 1 | |
Natural variantiVAR_008096 | 743 | M → I in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs28940590EnsemblClinVar. | 1 | |
Natural variantiVAR_058962 | 1131 – 1133 | Missing in PC deficiency. 1 Publication | 3 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1077 | F → A or E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer. 1 Publication | 1 |
Keywords - Diseasei
Disease variantOrganism-specific databases
DisGeNETi | 5091 |
GeneReviewsi | PC |
MalaCardsi | PC |
MIMi | 266150, phenotype |
OpenTargetsi | ENSG00000173599 |
Orphaneti | 353320, Pyruvate carboxylase deficiency, benign type 353308, Pyruvate carboxylase deficiency, infantile type 353314, Pyruvate carboxylase deficiency, severe neonatal type |
PharmGKBi | PA32975 |
Miscellaneous databases
Pharosi | P11498, Tbio |
Chemistry databases
DrugBanki | DB07497, 5-(hexahydro-2-oxo-1H-thieno[3,4-D]imidazol-6-yl)pentanal DB00121, Biotin DB00119, Pyruvic acid |
Genetic variation databases
BioMutai | PC |
DMDMi | 1709947 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 20 | MitochondrionSequence analysisAdd BLAST | 20 | |
ChainiPRO_0000002840 | 21 – 1178 | Pyruvate carboxylase, mitochondrialAdd BLAST | 1158 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 35 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 39 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 79 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 79 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 148 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 152 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 241 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 297 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 319 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 434 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 442 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 589 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 661 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 717 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 741 | N6-carboxylysine1 Publication | 1 | |
Modified residuei | 748 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 892 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 969 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 992 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1003 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 1061 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1090 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1124 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1144 | N6-biotinyllysinePROSITE-ProRule annotation2 Publications | 1 |
Post-translational modificationi
Acetylation of Lys-748 might play a role in catalytic activity regulation.By similarity
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
EPDi | P11498 |
jPOSTi | P11498 |
MassIVEi | P11498 |
MaxQBi | P11498 |
PaxDbi | P11498 |
PeptideAtlasi | P11498 |
PRIDEi | P11498 |
ProteomicsDBi | 4659 52785 [P11498-1] |
PTM databases
iPTMneti | P11498 |
PhosphoSitePlusi | P11498 |
SwissPalmi | P11498 |
Expressioni
Gene expression databases
Bgeei | ENSG00000173599, Expressed in right lobe of liver and 177 other tissues |
ExpressionAtlasi | P11498, baseline and differential |
Genevisiblei | P11498, HS |
Organism-specific databases
HPAi | ENSG00000173599, Tissue enhanced (adipose tissue, liver) |
Interactioni
Subunit structurei
Binary interactionsi
Hide detailsP11498
With | #Exp. | IntAct |
---|---|---|
itself | 3 | EBI-2211322,EBI-2211322 |
Non-structural protein 5A (PRO_0000278740) from Hepatitis C virus genotype 1b (isolate HC-J1). | 7 | EBI-2211322,EBI-8803426 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 111124, 108 interactors |
DIPi | DIP-46372N |
IntActi | P11498, 35 interactors |
MINTi | P11498 |
STRINGi | 9606.ENSP00000377532 |
Miscellaneous databases
RNActi | P11498, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P11498 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P11498 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 36 – 486 | Biotin carboxylationAdd BLAST | 451 | |
Domaini | 156 – 353 | ATP-graspPROSITE-ProRule annotationAdd BLAST | 198 | |
Domaini | 563 – 832 | Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST | 270 | |
Domaini | 1109 – 1178 | Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST | 70 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 571 – 575 | Substrate binding | 5 |
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | KOG0369, Eukaryota |
GeneTreei | ENSGT00900000141164 |
HOGENOMi | CLU_000395_0_1_1 |
InParanoidi | P11498 |
PhylomeDBi | P11498 |
TreeFami | TF300535 |
Family and domain databases
Gene3Di | 3.20.20.70, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR011761, ATP-grasp 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 IPR016185, PreATP-grasp_dom_sf IPR000891, PYR_CT IPR005930, Pyruv_COase IPR011054, Rudment_hybrid_motif IPR011053, Single_hybrid_motif |
Pfami | View protein in Pfam PF02785, 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 |
PIRSFi | PIRSF001594, Pyruv_carbox, 1 hit |
SMARTi | View protein in SMART SM00878, Biotin_carb_C, 1 hit |
SUPFAMi | SSF51230, SSF51230, 1 hit SSF51246, SSF51246, 1 hit SSF52440, SSF52440, 1 hit |
TIGRFAMsi | TIGR01235, pyruv_carbox, 1 hit |
PROSITEi | View protein in PROSITE PS50975, ATP_GRASP, 1 hit PS50979, BC, 1 hit PS00188, BIOTIN, 1 hit PS50968, BIOTINYL_LIPOYL, 1 hit PS50991, PYR_CT, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All
Isoform 1 (identifier: P11498-1) [UniParc]FASTAAdd to basket
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A494C016 | A0A494C016_HUMAN | Pyruvate carboxylase, mitochondrial | PC | 631 | Annotation score: | ||
E9PRE7 | E9PRE7_HUMAN | Pyruvate carboxylase, mitochondrial | PC | 489 | Annotation score: | ||
A0A494C101 | A0A494C101_HUMAN | Pyruvate carboxylase, mitochondrial | PC | 483 | Annotation score: | ||
A0A494C0T2 | A0A494C0T2_HUMAN | Pyruvate carboxylase, mitochondrial | PC | 531 | Annotation score: | ||
A0A494BZT5 | A0A494BZT5_HUMAN | Pyruvate carboxylase, mitochondrial | PC | 68 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 225 – 226 | LA → WP in AAB31500 (PubMed:8048912).Curated | 2 | |
Sequence conflicti | 352 | A → S in AAA82937 (Ref. 3) Curated | 1 | |
Sequence conflicti | 385 – 386 | RS → PT in AAB31500 (PubMed:8048912).Curated | 2 | |
Sequence conflicti | 486 – 487 | EL → DV in AAB31500 (PubMed:8048912).Curated | 2 | |
Sequence conflicti | 638 | P → R in AAB31500 (PubMed:8048912).Curated | 1 | |
Sequence conflicti | 729 | E → A in AAB31500 (PubMed:8048912).Curated | 1 | |
Sequence conflicti | 774 – 775 | DT → AP in AAB31500 (PubMed:8048912).Curated | 2 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_048416 | 76 | H → L. Corresponds to variant dbSNP:rs7104156EnsemblClinVar. | 1 | |
Natural variantiVAR_015199 | 145 | V → A in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs28940591EnsemblClinVar. | 1 | |
Natural variantiVAR_058957 | 156 | R → Q in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs119103241EnsemblClinVar. | 1 | |
Natural variantiVAR_058958 | 270 | R → W in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs1258494752Ensembl. | 1 | |
Natural variantiVAR_058959 | 304 | Y → C in PC deficiency. 1 Publication | 1 | |
Natural variantiVAR_015200 | 451 | R → C in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs113994143EnsemblClinVar. | 1 | |
Natural variantiVAR_058960 | 583 | R → L in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs119103242EnsemblClinVar. | 1 | |
Natural variantiVAR_008095 | 610 | A → T in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs28940589EnsemblClinVar. | 1 | |
Natural variantiVAR_058961 | 631 | R → Q in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs113994145EnsemblClinVar. | 1 | |
Natural variantiVAR_008096 | 743 | M → I in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs28940590EnsemblClinVar. | 1 | |
Natural variantiVAR_058962 | 1131 – 1133 | Missing in PC deficiency. 1 Publication | 3 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_056358 | 457 – 529 | TNIAF…TDPVV → VRRHQAQPLAAALGRPCGQE ARRPQAAVTAPTGPGSPTLV RVPPAARVLSSRLGGPSQTT PETSTEVSPTILL in isoform 2. 1 PublicationAdd BLAST | 73 | |
Alternative sequenceiVSP_056359 | 530 – 1178 | Missing in isoform 2. 1 PublicationAdd BLAST | 649 |
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_005274031.4 [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] |
Genome annotation databases
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
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_005274031.4 [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] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
SMRi | P11498 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 111124, 108 interactors |
DIPi | DIP-46372N |
IntActi | P11498, 35 interactors |
MINTi | P11498 |
STRINGi | 9606.ENSP00000377532 |
Chemistry databases
DrugBanki | DB07497, 5-(hexahydro-2-oxo-1H-thieno[3,4-D]imidazol-6-yl)pentanal DB00121, Biotin DB00119, Pyruvic acid |
PTM databases
iPTMneti | P11498 |
PhosphoSitePlusi | P11498 |
SwissPalmi | P11498 |
Genetic variation databases
BioMutai | PC |
DMDMi | 1709947 |
Proteomic databases
EPDi | P11498 |
jPOSTi | P11498 |
MassIVEi | P11498 |
MaxQBi | P11498 |
PaxDbi | P11498 |
PeptideAtlasi | P11498 |
PRIDEi | P11498 |
ProteomicsDBi | 4659 52785 [P11498-1] |
Protocols and materials databases
Antibodypediai | 30264, 354 antibodies |
Genome annotation databases
Organism-specific databases
CTDi | 5091 |
DisGeNETi | 5091 |
GeneCardsi | PC |
GeneReviewsi | PC |
HGNCi | HGNC:8636, PC |
HPAi | ENSG00000173599, Tissue enhanced (adipose tissue, liver) |
MalaCardsi | PC |
MIMi | 266150, phenotype 608786, gene |
neXtProti | NX_P11498 |
OpenTargetsi | ENSG00000173599 |
Orphaneti | 353320, Pyruvate carboxylase deficiency, benign type 353308, Pyruvate carboxylase deficiency, infantile type 353314, Pyruvate carboxylase deficiency, severe neonatal type |
PharmGKBi | PA32975 |
VEuPathDBi | HostDB:ENSG00000173599.13 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0369, Eukaryota |
GeneTreei | ENSGT00900000141164 |
HOGENOMi | CLU_000395_0_1_1 |
InParanoidi | P11498 |
PhylomeDBi | P11498 |
TreeFami | TF300535 |
Enzyme and pathway databases
UniPathwayi | UPA00138 |
BioCyci | MetaCyc:HS10697-MONOMER |
BRENDAi | 6.4.1.1, 2681 |
PathwayCommonsi | P11498 |
Reactomei | R-HSA-196780, Biotin transport and metabolism R-HSA-3371599, Defective HLCS causes multiple carboxylase deficiency R-HSA-70263, Gluconeogenesis |
SABIO-RKi | P11498 |
SIGNORi | P11498 |
Miscellaneous databases
BioGRID-ORCSi | 5091, 253 hits in 996 CRISPR screens |
ChiTaRSi | PC, human |
EvolutionaryTracei | P11498 |
GenomeRNAii | 5091 |
Pharosi | P11498, Tbio |
PROi | PR:P11498 |
RNActi | P11498, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000173599, Expressed in right lobe of liver and 177 other tissues |
ExpressionAtlasi | P11498, baseline and differential |
Genevisiblei | P11498, HS |
Family and domain databases
Gene3Di | 3.20.20.70, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR011761, ATP-grasp 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 IPR016185, PreATP-grasp_dom_sf IPR000891, PYR_CT IPR005930, Pyruv_COase IPR011054, Rudment_hybrid_motif IPR011053, Single_hybrid_motif |
Pfami | View protein in Pfam PF02785, 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 |
PIRSFi | PIRSF001594, Pyruv_carbox, 1 hit |
SMARTi | View protein in SMART SM00878, Biotin_carb_C, 1 hit |
SUPFAMi | SSF51230, SSF51230, 1 hit SSF51246, SSF51246, 1 hit SSF52440, SSF52440, 1 hit |
TIGRFAMsi | TIGR01235, pyruv_carbox, 1 hit |
PROSITEi | View protein in PROSITE PS50975, ATP_GRASP, 1 hit PS50979, BC, 1 hit PS00188, BIOTIN, 1 hit PS50968, BIOTINYL_LIPOYL, 1 hit PS50991, PYR_CT, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PYC_HUMAN | |
Accessioni | P11498Primary (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: | April 7, 2021 | |
This is version 228 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references