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P11498

- PYC_HUMAN

UniProt

P11498 - PYC_HUMAN

Protein

Pyruvate carboxylase, mitochondrial

Gene

PC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    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 – 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. protein binding Source: IntAct
    7. 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

    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

    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 – 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 Publications

    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

    1
    1178
    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.
    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
    Domaini1110 – 117768Biotinyl-bindingAdd
    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.Curated
    Contains 1 carboxyltransferase domain.Curated

    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]

    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

    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
    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.
    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:
    EMBL
    GenBank
    DDBJ
    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.
    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

    EnsembliENST00000355677; ENSP00000347900; ENSG00000173599.
    ENST00000393955; ENSP00000377527; ENSG00000173599.
    ENST00000393958; ENSP00000377530; ENSG00000173599.
    ENST00000393960; ENSP00000377532; ENSG00000173599.
    GeneIDi5091.
    KEGGihsa:5091.
    UCSCiuc001ojn.1. human.

    Polymorphism databases

    DMDMi1709947.

    Keywords - Coding sequence diversityi

    Alternative splicing, 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 .
    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.
    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...
    MobiDBi 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 ENST00000355677 ; ENSP00000347900 ; ENSG00000173599 .
    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-RK 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

    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: October 1, 2014
    This is version 171 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

    Dasty 3