P05166 (PCCB_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 120.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Propionyl-CoA carboxylase beta chain, mitochondrial Short name=PCCase subunit beta EC=6.4.1.3 Alternative name(s): Propanoyl-CoA:carbon dioxide ligase subunit beta | ||
| Gene names |
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| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 539 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA. |
| Pathway | |
| Subunit structure | Probably a dodecamer composed of six biotin-containing alpha subunits and six beta subunits. |
| Subcellular location | |
| Involvement in disease | Defects in PCCB are the cause of propionic acidemia type II (PA-2) [MIM:606054]. PA-2 is a life-threatening disease characterized by episodic vomiting, lethargy and ketosis, neutropenia, periodic thrombocytopenia, hypogammaglobulinemia, developmental retardation, and intolerance to protein. Ref.3 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 |
| Sequence similarities | Belongs to the AccD/PCCB family. Contains 1 carboxyltransferase domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Coding sequence diversity | Polymorphism |
| Disease | Disease mutation |
| Domain | Transit peptide |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| PTM | Acetylation |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | fatty acid beta-oxidation Traceable author statement. Source: Reactome |
| Cellular component | mitochondrial matrix Traceable author statement. Source: Reactome |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW propionyl-CoA carboxylase activityTraceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 28 | 28 | Mitochondrion Ref.6 | ||||||
| Chain | 29 – 539 | 511 | Propionyl-CoA carboxylase beta chain, mitochondrial | PRO_0000000293 | |||||
Regions | |||||||||
| Domain | 38 – 531 | 494 | Carboxyltransferase | ||||||
| Region | 325 – 358 | 34 | Acyl-CoA binding Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 60 | 1 | N6-acetyllysine By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 17 | 1 | L → M in PA-2. Ref.11 | VAR_009080 | |||||
| Natural variant | 44 | 1 | R → P in PA-2. | VAR_000271 | |||||
| Natural variant | 67 | 1 | R → S in PA-2. Ref.15 | VAR_023847 | |||||
| Natural variant | 106 | 1 | S → R in PA-2. | VAR_000272 | |||||
| Natural variant | 107 | 1 | V → M in PA-2. Ref.15 | VAR_023848 | |||||
| Natural variant | 112 | 1 | G → D in PA-2. Ref.15 | VAR_023849 | |||||
| Natural variant | 131 | 1 | G → R in PA-2. | VAR_000273 | |||||
| Natural variant | 140 | 1 | K → KICK in PA-2. | VAR_009081 | |||||
| Natural variant | 153 | 1 | A → P in PA-2. Ref.16 | VAR_023850 | |||||
| Natural variant | 165 | 1 | R → Q in PA-2; does not affect either heteromeric or homomeric assembly. Ref.13 Ref.15 | VAR_023851 | |||||
| Natural variant | 165 | 1 | R → W in PA-2. Ref.16 | VAR_000274 | |||||
| Natural variant | 168 | 1 | E → K in PA-2; common mutation. Ref.11 Ref.15 | VAR_000275 | |||||
| Natural variant | 188 | 1 | G → R in PA-2. Ref.15 | VAR_023852 | |||||
| Natural variant | 198 | 1 | G → D in PA-2. | VAR_000276 | |||||
| Natural variant | 205 | 1 | V → D in PA-2. Ref.11 | VAR_009082 | |||||
| Natural variant | 228 | 1 | P → L in PA-2. | VAR_009083 | |||||
| Natural variant | 246 | 1 | G → V in PA-2. Ref.15 | VAR_023853 | |||||
| Natural variant | 287 | 1 | P → S. Ref.1 Corresponds to variant rs2228310 [ dbSNP | Ensembl ]. | VAR_048163 | |||||
| Natural variant | 341 | 1 | Missing in PA-2. | VAR_023854 | |||||
| Natural variant | 408 | 1 | Missing in PA-2. | VAR_000277 | |||||
| Natural variant | 410 | 1 | R → W in PA-2. Ref.10 Ref.15 Ref.16 | VAR_000278 | |||||
| Natural variant | 428 | 1 | T → I in PA-2. Ref.14 Ref.16 Corresponds to variant rs28934887 [ dbSNP | Ensembl ]. | VAR_009084 | |||||
| Natural variant | 430 | 1 | I → L in PA-2. Ref.14 | VAR_023855 | |||||
| Natural variant | 435 | 1 | Y → C in PA-2. Ref.14 | VAR_023856 | |||||
| Natural variant | 439 | 1 | Y → C in PA-2. Ref.14 | VAR_023857 | |||||
| Natural variant | 442 | 1 | M → T in PA-2. Ref.11 | VAR_009085 | |||||
| Natural variant | 468 | 1 | A → T in PA-2. Ref.14 | VAR_023858 | |||||
| Natural variant | 497 | 1 | A → V in PA-2; common mutation; does not affect either heteromeric or homomeric assembly. Ref.13 | VAR_000279 | |||||
| Natural variant | 512 | 1 | R → C in PA-2; affects heteromeric and homomeric assembly. Ref.13 Ref.16 | VAR_000280 | |||||
| Natural variant | 519 | 1 | L → P in PA-2; affects heteromeric and homomeric assembly. Ref.13 | VAR_000281 | |||||
| Natural variant | 536 | 1 | N → D in PA-2; affects heteromeric and homomeric assembly. Ref.13 | VAR_009086 | |||||
Experimental info | |||||||||
| Sequence conflict | 58 – 59 | 2 | QH → HD in AAB28900. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 8188292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 8225321] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 9683601] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PA-2. Tissue: Blood and Skin fibroblast. |
| [4] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas and Skin. |
| [5] | "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: 3460076] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 289-443. |
| [6] | "Mitochondrial targeting signals and mature peptides of 3-methylcrotonyl-CoA carboxylase." Stadler S.C., Polanetz R., Meier S., Mayerhofer P.U., Herrmann J.M., Anslinger K., Roscher A.A., Roschinger W., Holzinger A. Biochem. Biophys. Res. Commun. 334:939-946(2005) [PubMed: 16023992] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-33, SUBCELLULAR LOCATION. Tissue: Kidney. |
| [7] | Lamhonwah A.-M. Submitted (DEC-1986) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| [8] | "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: 2154743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 401-433, VARIANT PA-2 ILE-408 DEL. Tissue: Skin fibroblast. |
| [9] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [10] | "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: 8411997] [Abstract] Cited for: VARIANTS PA-2 TRP-410 AND ILE-408 DEL. |
| [11] | "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: 10447268] [Abstract] Cited for: VARIANTS PA-2 MET-17; LYS-168; ASP-205 AND THR-442. |
| [12] | "Overview of mutations in the PCCA and PCCB genes causing propionic acidemia." Ugarte M., Perez-Cerda C., Rodriguez-Pombo P., Desviat L.R., Perez B., Richard E., Muro S., Campeau E., Ohura T., Gravel R.A. Hum. Mutat. 14:275-282(1999) [PubMed: 10502773] [Abstract] Cited for: REVIEW ON PA VARIANTS. |
| [13] | "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: 11749052] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS PA-2 GLN-165; VAL-497; CYS-512; PRO-519 AND ASP-536. |
| [14] | "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: 12189489] [Abstract] Cited for: VARIANTS PA-2 ILE-428; LEU-430; CYS-435; CYS-439 AND THR-468. |
| [15] | "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: 12559849] [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. |
| [16] | "Mutation spectrum of the PCCA and PCCB genes in Japanese patients with propionic acidemia." Yang X., Sakamoto O., Matsubara Y., Kure S., Suzuki Y., Aoki Y., Yamaguchi S., Takahashi Y., Nishikubo T., Kawaguchi C., Yoshioka A., Kimura T., Hayasaka K., Kohno Y., Iinuma K., Ohura T. Mol. Genet. Metab. 81:335-342(2004) [PubMed: 15059621] [Abstract] Cited for: VARIANTS PA-2 PRO-153; TRP-165; TRP-410; ILE-428 AND CYS-512. |
| + | Additional computationally mapped references. |
Web resources
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X73424 mRNA. Translation: CAA51825.1. S67325 mRNA. Translation: AAB28900.1. AJ006487 AJ006499 Genomic DNA. Translation: CAA07066.1.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. |
| IPI | IPI00007247. |
| PIR | T45009. |
| RefSeq | NP_000523.2. NM_000532.4. |
| UniGene | Hs.63788. |
3D structure databases | |
| ProteinModelPortal | P05166. |
| SMR | P05166. Positions 37-539. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P05166. 4 interactions. |
| MINT | MINT-3004663. |
| STRING | P05166. |
PTM databases | |
| PhosphoSite | P05166. |
Polymorphism databases | |
| DMDM | 124106304. |
Proteomic databases | |
| PeptideAtlas | P05166. |
| PRIDE | P05166. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000251654; ENSP00000251654; ENSG00000114054. |
| GeneID | 5096. |
| KEGG | hsa:5096. |
| UCSC | uc003eqy.1. human. |
Organism-specific databases | |
| CTD | 5096. |
| GeneCards | GC03P135969. |
| H-InvDB | HIX0020182. |
| HGNC | HGNC:8654. PCCB. |
| HPA | HPA036939. HPA036940. |
| MIM | 232050. gene. 606054. phenotype. |
| neXtProt | NX_P05166. |
| Orphanet | 35. Propionic acidemia. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG13877. |
| HOVERGEN | HBG003970. |
| InParanoid | P05166. |
| OMA | VTGYGMI. |
| PhylomeDB | P05166. |
Enzyme and pathway databases | |
| BRENDA | 6.4.1.3. 2681. |
| Reactome | REACT_22258. Metabolism of lipids and lipoproteins. |
Gene expression databases | |
| ArrayExpress | P05166. |
| Bgee | P05166. |
| CleanEx | HS_PCCB. |
| Genevestigator | P05166. |
| GermOnline | ENSG00000114054. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR000022. Carboxyl_trans. IPR011763. COA_CT_C. IPR011762. COA_CT_N. [Graphical view] |
| KO | K01966. |
| Pfam | PF01039. Carboxyl_trans. 1 hit. [Graphical view] |
| PROSITE | PS50989. COA_CT_CTER. 1 hit. PS50980. COA_CT_NTER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| DrugBank | DB00121. Biotin. DB00161. L-Valine. |
| NextBio | 19660. |
| SOURCE | Search... |
Entry information
| Entry name | PCCB_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P05166 Secondary accession number(s): Q16813, Q96CX0 | ||||||||
| Entry history |
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| Entry status | 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. | ||||||||
Relevant documents
| Human chromosome 3 Human chromosome 3: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with