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P05166

- PCCB_HUMAN

UniProt

P05166 - PCCB_HUMAN

Protein

Propionyl-CoA carboxylase beta chain, mitochondrial

Gene

PCCB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA.

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. propionyl-CoA carboxylase activity Source: ProtInc

    GO - Biological processi

    1. biotin metabolic process Source: Reactome
    2. cellular lipid metabolic process Source: Reactome
    3. fatty acid beta-oxidation Source: Reactome
    4. short-chain fatty acid catabolic process Source: Reactome
    5. small molecule metabolic process Source: Reactome
    6. vitamin metabolic process Source: Reactome
    7. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000114054-MONOMER.
    BRENDAi6.4.1.3. 2681.
    ReactomeiREACT_11153. Biotin transport and metabolism.
    REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
    REACT_993. Propionyl-CoA catabolism.
    SABIO-RKP05166.
    UniPathwayiUPA00945; UER00908.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Propionyl-CoA carboxylase beta chain, mitochondrial (EC:6.4.1.3)
    Short name:
    PCCase subunit beta
    Alternative name(s):
    Propanoyl-CoA:carbon dioxide ligase subunit beta
    Gene namesi
    Name:PCCB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:8654. PCCB.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrial matrix Source: Reactome
    3. mitochondrion Source: ProtInc

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Propionic acidemia type II (PA-2) [MIM:606054]: Life-threatening disease characterized by episodic vomiting, lethargy and ketosis, neutropenia, periodic thrombocytopenia, hypogammaglobulinemia, developmental retardation, and intolerance to protein.7 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171L → M in PA-2. 1 Publication
    VAR_009080
    Natural varianti44 – 441R → P in PA-2.
    VAR_000271
    Natural varianti67 – 671R → S in PA-2. 1 Publication
    VAR_023847
    Natural varianti106 – 1061S → R in PA-2.
    VAR_000272
    Natural varianti107 – 1071V → M in PA-2. 1 Publication
    VAR_023848
    Natural varianti112 – 1121G → D in PA-2. 1 Publication
    VAR_023849
    Natural varianti131 – 1311G → R in PA-2.
    VAR_000273
    Natural varianti140 – 1401K → KICK in PA-2.
    VAR_009081
    Natural varianti153 – 1531A → P in PA-2. 1 Publication
    VAR_023850
    Natural varianti165 – 1651R → Q in PA-2; does not affect either heteromeric or homomeric assembly. 1 Publication
    VAR_023851
    Natural varianti165 – 1651R → W in PA-2. 1 Publication
    VAR_000274
    Natural varianti168 – 1681E → K in PA-2; common mutation. 2 Publications
    VAR_000275
    Natural varianti188 – 1881G → R in PA-2. 1 Publication
    VAR_023852
    Natural varianti198 – 1981G → D in PA-2.
    VAR_000276
    Natural varianti205 – 2051V → D in PA-2. 1 Publication
    VAR_009082
    Natural varianti228 – 2281P → L in PA-2.
    VAR_009083
    Natural varianti246 – 2461G → V in PA-2. 1 Publication
    VAR_023853
    Natural varianti341 – 3411Missing in PA-2. 1 Publication
    VAR_023854
    Natural varianti408 – 4081Missing in PA-2. 2 Publications
    VAR_000277
    Natural varianti410 – 4101R → W in PA-2. 3 Publications
    VAR_000278
    Natural varianti428 – 4281T → I in PA-2. 2 Publications
    Corresponds to variant rs28934887 [ dbSNP | Ensembl ].
    VAR_009084
    Natural varianti430 – 4301I → L in PA-2. 1 Publication
    VAR_023855
    Natural varianti435 – 4351Y → C in PA-2. 1 Publication
    VAR_023856
    Natural varianti439 – 4391Y → C in PA-2. 1 Publication
    VAR_023857
    Natural varianti442 – 4421M → T in PA-2. 1 Publication
    VAR_009085
    Natural varianti468 – 4681A → T in PA-2. 1 Publication
    VAR_023858
    Natural varianti497 – 4971A → V in PA-2; common mutation; does not affect either heteromeric or homomeric assembly.
    Corresponds to variant rs142403318 [ dbSNP | Ensembl ].
    VAR_000279
    Natural varianti512 – 5121R → C in PA-2; affects heteromeric and homomeric assembly. 1 Publication
    Corresponds to variant rs186710233 [ dbSNP | Ensembl ].
    VAR_000280
    Natural varianti519 – 5191L → P in PA-2; affects heteromeric and homomeric assembly.
    VAR_000281
    Natural varianti536 – 5361N → D in PA-2; affects heteromeric and homomeric assembly.
    VAR_009086

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi606054. phenotype.
    Orphaneti35. Propionic acidemia.
    PharmGKBiPA32993.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2828Mitochondrion1 PublicationAdd
    BLAST
    Chaini29 – 539511Propionyl-CoA carboxylase beta chain, mitochondrialPRO_0000000293Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei99 – 991N6-acetyllysine; alternateBy similarity
    Modified residuei99 – 991N6-succinyllysine; alternateBy similarity
    Modified residuei248 – 2481N6-succinyllysineBy similarity
    Modified residuei474 – 4741N6-acetyllysine; alternateBy similarity
    Modified residuei474 – 4741N6-succinyllysine; alternateBy similarity
    Modified residuei489 – 4891N6-acetyllysine; alternateBy similarity
    Modified residuei489 – 4891N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP05166.
    PaxDbiP05166.
    PeptideAtlasiP05166.
    PRIDEiP05166.

    PTM databases

    PhosphoSiteiP05166.

    Expressioni

    Gene expression databases

    ArrayExpressiP05166.
    BgeeiP05166.
    CleanExiHS_PCCB.
    GenevestigatoriP05166.

    Organism-specific databases

    HPAiHPA036939.
    HPA036940.

    Interactioni

    Subunit structurei

    Probably a dodecamer composed of six biotin-containing alpha subunits and six beta subunits.

    Protein-protein interaction databases

    BioGridi111129. 8 interactions.
    DIPiDIP-38244N.
    IntActiP05166. 8 interactions.
    MINTiMINT-3004663.
    STRINGi9606.ENSP00000251654.

    Structurei

    3D structure databases

    ProteinModelPortaliP05166.
    SMRiP05166. Positions 37-539.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 531494CarboxyltransferaseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni325 – 35834Acyl-CoA bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the AccD/PCCB family.Curated
    Contains 1 carboxyltransferase domain.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG4799.
    HOGENOMiHOG000218693.
    HOVERGENiHBG003970.
    InParanoidiP05166.
    KOiK01966.
    PhylomeDBiP05166.
    TreeFamiTF314350.

    Family and domain databases

    Gene3Di3.90.226.10. 2 hits.
    InterProiIPR000022. Carboxyl_trans.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    [Graphical view]
    PfamiPF01039. Carboxyl_trans. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 2 hits.
    PROSITEiPS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 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: P05166-1) [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

    MAAALRVAAV GARLSVLASG LRAAVRSLCS QATSVNERIE NKRRTALLGG    50
    GQRRIDAQHK RGKLTARERI SLLLDPGSFV ESDMFVEHRC ADFGMAADKN 100
    KFPGDSVVTG RGRINGRLVY VFSQDFTVFG GSLSGAHAQK ICKIMDQAIT 150
    VGAPVIGLND SGGARIQEGV ESLAGYADIF LRNVTASGVI PQISLIMGPC 200
    AGGAVYSPAL TDFTFMVKDT SYLFITGPDV VKSVTNEDVT QEELGGAKTH 250
    TTMSGVAHRA FENDVDALCN LRDFFNYLPL SSQDPAPVRE CHDPSDRLVP 300
    ELDTIVPLES TKAYNMVDII HSVVDEREFF EIMPNYAKNI IVGFARMNGR 350
    TVGIVGNQPK VASGCLDINS SVKGARFVRF CDAFNIPLIT FVDVPGFLPG 400
    TAQEYGGIIR HGAKLLYAFA EATVPKVTVI TRKAYGGAYD VMSSKHLCGD 450
    TNYAWPTAEI AVMGAKGAVE IIFKGHENVE AAQAEYIEKF ANPFPAAVRG 500
    FVDDIIQPSS TRARICCDLD VLASKKVQRP WRKHANIPL 539
    Length:539
    Mass (Da):58,216
    Last modified:January 23, 2007 - v3
    Checksum:iA2DAAC00312D3C0F
    GO
    Isoform 2 (identifier: P05166-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         124-124: Q → QQIIGWAQWLPLVISALWEAE

    Note: No experimental confirmation available.

    Show »
    Length:559
    Mass (Da):60,521
    Checksum:i07788B2E955626AA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 592QH → HD in AAB28900. (PubMed:8225321)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171L → M in PA-2. 1 Publication
    VAR_009080
    Natural varianti44 – 441R → P in PA-2.
    VAR_000271
    Natural varianti67 – 671R → S in PA-2. 1 Publication
    VAR_023847
    Natural varianti106 – 1061S → R in PA-2.
    VAR_000272
    Natural varianti107 – 1071V → M in PA-2. 1 Publication
    VAR_023848
    Natural varianti112 – 1121G → D in PA-2. 1 Publication
    VAR_023849
    Natural varianti131 – 1311G → R in PA-2.
    VAR_000273
    Natural varianti140 – 1401K → KICK in PA-2.
    VAR_009081
    Natural varianti153 – 1531A → P in PA-2. 1 Publication
    VAR_023850
    Natural varianti165 – 1651R → Q in PA-2; does not affect either heteromeric or homomeric assembly. 1 Publication
    VAR_023851
    Natural varianti165 – 1651R → W in PA-2. 1 Publication
    VAR_000274
    Natural varianti168 – 1681E → K in PA-2; common mutation. 2 Publications
    VAR_000275
    Natural varianti188 – 1881G → R in PA-2. 1 Publication
    VAR_023852
    Natural varianti198 – 1981G → D in PA-2.
    VAR_000276
    Natural varianti205 – 2051V → D in PA-2. 1 Publication
    VAR_009082
    Natural varianti228 – 2281P → L in PA-2.
    VAR_009083
    Natural varianti246 – 2461G → V in PA-2. 1 Publication
    VAR_023853
    Natural varianti287 – 2871P → S.1 Publication
    Corresponds to variant rs2228310 [ dbSNP | Ensembl ].
    VAR_048163
    Natural varianti341 – 3411Missing in PA-2. 1 Publication
    VAR_023854
    Natural varianti408 – 4081Missing in PA-2. 2 Publications
    VAR_000277
    Natural varianti410 – 4101R → W in PA-2. 3 Publications
    VAR_000278
    Natural varianti428 – 4281T → I in PA-2. 2 Publications
    Corresponds to variant rs28934887 [ dbSNP | Ensembl ].
    VAR_009084
    Natural varianti430 – 4301I → L in PA-2. 1 Publication
    VAR_023855
    Natural varianti435 – 4351Y → C in PA-2. 1 Publication
    VAR_023856
    Natural varianti439 – 4391Y → C in PA-2. 1 Publication
    VAR_023857
    Natural varianti442 – 4421M → T in PA-2. 1 Publication
    VAR_009085
    Natural varianti468 – 4681A → T in PA-2. 1 Publication
    VAR_023858
    Natural varianti497 – 4971A → V in PA-2; common mutation; does not affect either heteromeric or homomeric assembly.
    Corresponds to variant rs142403318 [ dbSNP | Ensembl ].
    VAR_000279
    Natural varianti512 – 5121R → C in PA-2; affects heteromeric and homomeric assembly. 1 Publication
    Corresponds to variant rs186710233 [ dbSNP | Ensembl ].
    VAR_000280
    Natural varianti519 – 5191L → P in PA-2; affects heteromeric and homomeric assembly.
    VAR_000281
    Natural varianti536 – 5361N → D in PA-2; affects heteromeric and homomeric assembly.
    VAR_009086

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei124 – 1241Q → QQIIGWAQWLPLVISALWEA E in isoform 2. 1 PublicationVSP_042568

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X73424 mRNA. Translation: CAA51825.1.
    S67325 mRNA. Translation: AAB28900.1.
    AJ006487
    , AJ006488, AJ006489, AJ006490, AJ006491, AJ006492, AJ006493, AJ006494, AJ006495, AJ006496, AJ006497, AJ006498, AJ006499 Genomic DNA. Translation: CAA07066.1.
    AK295312 mRNA. Translation: BAH12030.1.
    AC069524 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79118.1.
    BC013768 mRNA. Translation: AAH13768.1.
    BC053661 mRNA. Translation: AAH53661.1.
    M13573 mRNA. Translation: AAA60036.1.
    M31167 Genomic DNA. Translation: AAA60037.1.
    M31169 Genomic DNA. Translation: AAA60038.1.
    CCDSiCCDS3089.1. [P05166-1]
    CCDS54643.1. [P05166-2]
    PIRiT45009.
    RefSeqiNP_000523.2. NM_000532.4. [P05166-1]
    NP_001171485.1. NM_001178014.1. [P05166-2]
    UniGeneiHs.63788.

    Genome annotation databases

    EnsembliENST00000251654; ENSP00000251654; ENSG00000114054. [P05166-1]
    ENST00000469217; ENSP00000419027; ENSG00000114054. [P05166-2]
    GeneIDi5096.
    KEGGihsa:5096.
    UCSCiuc003eqy.2. human. [P05166-1]
    uc011bmc.2. human. [P05166-2]

    Polymorphism databases

    DMDMi124106304.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X73424 mRNA. Translation: CAA51825.1 .
    S67325 mRNA. Translation: AAB28900.1 .
    AJ006487
    , AJ006488 , AJ006489 , AJ006490 , AJ006491 , AJ006492 , AJ006493 , AJ006494 , AJ006495 , AJ006496 , AJ006497 , AJ006498 , AJ006499 Genomic DNA. Translation: CAA07066.1 .
    AK295312 mRNA. Translation: BAH12030.1 .
    AC069524 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79118.1 .
    BC013768 mRNA. Translation: AAH13768.1 .
    BC053661 mRNA. Translation: AAH53661.1 .
    M13573 mRNA. Translation: AAA60036.1 .
    M31167 Genomic DNA. Translation: AAA60037.1 .
    M31169 Genomic DNA. Translation: AAA60038.1 .
    CCDSi CCDS3089.1. [P05166-1 ]
    CCDS54643.1. [P05166-2 ]
    PIRi T45009.
    RefSeqi NP_000523.2. NM_000532.4. [P05166-1 ]
    NP_001171485.1. NM_001178014.1. [P05166-2 ]
    UniGenei Hs.63788.

    3D structure databases

    ProteinModelPortali P05166.
    SMRi P05166. Positions 37-539.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111129. 8 interactions.
    DIPi DIP-38244N.
    IntActi P05166. 8 interactions.
    MINTi MINT-3004663.
    STRINGi 9606.ENSP00000251654.

    Chemistry

    DrugBanki DB00121. Biotin.
    DB00161. L-Valine.

    PTM databases

    PhosphoSitei P05166.

    Polymorphism databases

    DMDMi 124106304.

    Proteomic databases

    MaxQBi P05166.
    PaxDbi P05166.
    PeptideAtlasi P05166.
    PRIDEi P05166.

    Protocols and materials databases

    DNASUi 5096.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000251654 ; ENSP00000251654 ; ENSG00000114054 . [P05166-1 ]
    ENST00000469217 ; ENSP00000419027 ; ENSG00000114054 . [P05166-2 ]
    GeneIDi 5096.
    KEGGi hsa:5096.
    UCSCi uc003eqy.2. human. [P05166-1 ]
    uc011bmc.2. human. [P05166-2 ]

    Organism-specific databases

    CTDi 5096.
    GeneCardsi GC03P135969.
    GeneReviewsi PCCB.
    HGNCi HGNC:8654. PCCB.
    HPAi HPA036939.
    HPA036940.
    MIMi 232050. gene.
    606054. phenotype.
    neXtProti NX_P05166.
    Orphaneti 35. Propionic acidemia.
    PharmGKBi PA32993.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4799.
    HOGENOMi HOG000218693.
    HOVERGENi HBG003970.
    InParanoidi P05166.
    KOi K01966.
    PhylomeDBi P05166.
    TreeFami TF314350.

    Enzyme and pathway databases

    UniPathwayi UPA00945 ; UER00908 .
    BioCyci MetaCyc:ENSG00000114054-MONOMER.
    BRENDAi 6.4.1.3. 2681.
    Reactomei REACT_11153. Biotin transport and metabolism.
    REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
    REACT_993. Propionyl-CoA catabolism.
    SABIO-RK P05166.

    Miscellaneous databases

    GenomeRNAii 5096.
    NextBioi 19660.
    PROi P05166.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05166.
    Bgeei P05166.
    CleanExi HS_PCCB.
    Genevestigatori P05166.

    Family and domain databases

    Gene3Di 3.90.226.10. 2 hits.
    InterProi IPR000022. Carboxyl_trans.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    [Graphical view ]
    Pfami PF01039. Carboxyl_trans. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52096. SSF52096. 2 hits.
    PROSITEi PS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Correction of the metabolic defect in propionic acidemia fibroblasts by microinjection of a full-length cDNA or RNA transcript encoding the propionyl-CoA carboxylase beta subunit."
      Lamhonwah A.-M., Leclerc D., Loyer M., Clarizio R., Gravel R.A.
      Genomics 19:500-505(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-287.
      Tissue: Fibroblast, Kidney and Liver.
    2. "The molecular defect in propionic acidemia: exon skipping caused by an 8-bp deletion from an intron in the PCCB allele."
      Ohura T., Ogasawara M., Ikeda H., Narisawa K., Tada K.
      Hum. Genet. 92:397-402(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver and Placenta.
    3. "Human propionyl-CoA carboxylase beta subunit gene: exon-intron definition and mutation spectrum in Spanish and Latin American propionic acidemia patients."
      Rodriguez-Pombo P., Hoenicka J., Muro S., Perez B., Perez-Cerda C., Richard E., Desviat L.R., Ugarte M.
      Am. J. Hum. Genet. 63:360-369(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PA-2.
      Tissue: Blood and Skin fibroblast.
    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: Caudate nucleus.
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Pancreas and Skin.
    8. "Isolation of cDNA clones coding for the alpha and beta chains of human propionyl-CoA carboxylase: chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes."
      Lamhonwah A.-M., Barankiewicz T.J., Willard H.F., Mahuran D.J., Quan F., Gravel R.A.
      Proc. Natl. Acad. Sci. U.S.A. 83:4864-4868(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 289-443 (ISOFORM 1).
    9. Cited for: PROTEIN SEQUENCE OF 29-33, SUBCELLULAR LOCATION.
      Tissue: Kidney.
    10. Lamhonwah A.-M.
      Submitted (DEC-1986) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    11. "An unusual insertion/deletion in the gene encoding the beta-subunit of propionyl-CoA carboxylase is a frequent mutation in Caucasian propionic acidemia."
      Tahara T., Kraus J.P., Rosenberg L.E.
      Proc. Natl. Acad. Sci. U.S.A. 87:1372-1376(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 401-433, VARIANT PA-2 ILE-408 DEL.
      Tissue: Skin fibroblast.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Three independent mutations in the same exon of the PCCB gene: differences between Caucasian and Japanese propionic acidaemia."
      Tahara T., Kraus J.P., Ohura T., Rosenberg L.E., Fenton W.A.
      J. Inherit. Metab. Dis. 16:353-360(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PA-2 TRP-410 AND ILE-408 DEL.
    14. "Identification of novel mutations in the PCCB gene in European propionic acidemia patients."
      Muro S., Rodriguez-Pombo P., Perez B., Perez-Cerda C., Desviat L.R., Sperl W., Skladal D., Sass J.O., Ugarte M.
      Hum. Mutat. 14:89-90(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PA-2 MET-17; LYS-168; ASP-205 AND THR-442.
    15. Cited for: REVIEW ON PA VARIANTS.
    16. "Effect of PCCB gene mutations on the heteromeric and homomeric assembly of propionyl-CoA carboxylase."
      Muro S., Perez B., Desviat L.R., Rodriguez-Pombo P., Perez-Cerda C., Clavero S., Ugarte M.
      Mol. Genet. Metab. 74:476-483(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS PA-2 GLN-165; VAL-497; CYS-512; PRO-519 AND ASP-536.
    17. "Unexpectedly high prevalence of the mild form of propionic acidemia in Japan: presence of a common mutation and possible clinical implications."
      Yorifuji T., Kawai M., Muroi J., Mamada M., Kurokawa K., Shigematsu Y., Hirano S., Sakura N., Yoshida I., Kuhara T., Endo F., Mitsubuchi H., Nakahata T.
      Hum. Genet. 111:161-165(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PA-2 ILE-428; LEU-430; CYS-435; CYS-439 AND THR-468.
    18. "Propionic acidemia: identification of twenty-four novel mutations in Europe and North America."
      Perez B., Desviat L.R., Rodriguez-Pombo P., Clavero S., Navarrete R., Perez-Cerda C., Ugarte M.
      Mol. Genet. Metab. 78:59-67(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PA-2 SER-67; MET-107; ASP-112; GLN-165; LYS-168; ARG-188; VAL-246; ILE-341 DEL AND TRP-410.
    19. Cited for: VARIANTS PA-2 PRO-153; TRP-165; TRP-410; ILE-428 AND CYS-512.

    Entry informationi

    Entry nameiPCCB_HUMAN
    AccessioniPrimary (citable) accession number: P05166
    Secondary accession number(s): B7Z2Z4, Q16813, Q96CX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 149 of the entry and version 3 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3