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P05166 (PCCB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:PCCB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3.

Subunit structure

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

Subcellular location

Mitochondrion matrix Ref.9.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19

Sequence similarities

Belongs to the AccD/PCCB family.

Contains 1 carboxyltransferase domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05166-1)

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.
Isoform 2 (identifier: P05166-2)

The sequence of this isoform differs from the canonical sequence as follows:
     124-124: Q → QQIIGWAQWLPLVISALWEAE
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Ref.9
Chain29 – 539511Propionyl-CoA carboxylase beta chain, mitochondrial
PRO_0000000293

Regions

Domain38 – 531494Carboxyltransferase
Region325 – 35834Acyl-CoA binding Potential

Amino acid modifications

Modified residue991N6-acetyllysine; alternate By similarity
Modified residue991N6-succinyllysine; alternate By similarity
Modified residue2481N6-succinyllysine By similarity
Modified residue4741N6-acetyllysine; alternate By similarity
Modified residue4741N6-succinyllysine; alternate By similarity
Modified residue4891N6-acetyllysine; alternate By similarity
Modified residue4891N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence1241Q → QQIIGWAQWLPLVISALWEA E in isoform 2.
VSP_042568
Natural variant171L → M in PA-2. Ref.14
VAR_009080
Natural variant441R → P in PA-2.
VAR_000271
Natural variant671R → S in PA-2. Ref.18
VAR_023847
Natural variant1061S → R in PA-2.
VAR_000272
Natural variant1071V → M in PA-2. Ref.18
VAR_023848
Natural variant1121G → D in PA-2. Ref.18
VAR_023849
Natural variant1311G → R in PA-2.
VAR_000273
Natural variant1401K → KICK in PA-2.
VAR_009081
Natural variant1531A → P in PA-2. Ref.19
VAR_023850
Natural variant1651R → Q in PA-2; does not affect either heteromeric or homomeric assembly. Ref.16 Ref.18
VAR_023851
Natural variant1651R → W in PA-2. Ref.19
VAR_000274
Natural variant1681E → K in PA-2; common mutation. Ref.14 Ref.18
VAR_000275
Natural variant1881G → R in PA-2. Ref.18
VAR_023852
Natural variant1981G → D in PA-2.
VAR_000276
Natural variant2051V → D in PA-2. Ref.14
VAR_009082
Natural variant2281P → L in PA-2.
VAR_009083
Natural variant2461G → V in PA-2. Ref.18
VAR_023853
Natural variant2871P → S. Ref.1
Corresponds to variant rs2228310 [ dbSNP | Ensembl ].
VAR_048163
Natural variant3411Missing in PA-2. Ref.18
VAR_023854
Natural variant4081Missing in PA-2. Ref.11 Ref.13
VAR_000277
Natural variant4101R → W in PA-2. Ref.13 Ref.18 Ref.19
VAR_000278
Natural variant4281T → I in PA-2. Ref.17 Ref.19
Corresponds to variant rs28934887 [ dbSNP | Ensembl ].
VAR_009084
Natural variant4301I → L in PA-2. Ref.17
VAR_023855
Natural variant4351Y → C in PA-2. Ref.17
VAR_023856
Natural variant4391Y → C in PA-2. Ref.17
VAR_023857
Natural variant4421M → T in PA-2. Ref.14
VAR_009085
Natural variant4681A → T in PA-2. Ref.17
VAR_023858
Natural variant4971A → V in PA-2; common mutation; does not affect either heteromeric or homomeric assembly. Ref.16
Corresponds to variant rs142403318 [ dbSNP | Ensembl ].
VAR_000279
Natural variant5121R → C in PA-2; affects heteromeric and homomeric assembly. Ref.16 Ref.19
Corresponds to variant rs186710233 [ dbSNP | Ensembl ].
VAR_000280
Natural variant5191L → P in PA-2; affects heteromeric and homomeric assembly. Ref.16
VAR_000281
Natural variant5361N → D in PA-2; affects heteromeric and homomeric assembly. Ref.16
VAR_009086

Experimental info

Sequence conflict58 – 592QH → HD in AAB28900. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A2DAAC00312D3C0F

FASTA53958,216
        10         20         30         40         50         60 
MAAALRVAAV GARLSVLASG LRAAVRSLCS QATSVNERIE NKRRTALLGG GQRRIDAQHK 

        70         80         90        100        110        120 
RGKLTARERI SLLLDPGSFV ESDMFVEHRC ADFGMAADKN KFPGDSVVTG RGRINGRLVY 

       130        140        150        160        170        180 
VFSQDFTVFG GSLSGAHAQK ICKIMDQAIT VGAPVIGLND SGGARIQEGV ESLAGYADIF 

       190        200        210        220        230        240 
LRNVTASGVI PQISLIMGPC AGGAVYSPAL TDFTFMVKDT SYLFITGPDV VKSVTNEDVT 

       250        260        270        280        290        300 
QEELGGAKTH TTMSGVAHRA FENDVDALCN LRDFFNYLPL SSQDPAPVRE CHDPSDRLVP 

       310        320        330        340        350        360 
ELDTIVPLES TKAYNMVDII HSVVDEREFF EIMPNYAKNI IVGFARMNGR TVGIVGNQPK 

       370        380        390        400        410        420 
VASGCLDINS SVKGARFVRF CDAFNIPLIT FVDVPGFLPG TAQEYGGIIR HGAKLLYAFA 

       430        440        450        460        470        480 
EATVPKVTVI TRKAYGGAYD VMSSKHLCGD TNYAWPTAEI AVMGAKGAVE IIFKGHENVE 

       490        500        510        520        530 
AAQAEYIEKF ANPFPAAVRG FVDDIIQPSS TRARICCDLD VLASKKVQRP WRKHANIPL 

« Hide

Isoform 2 [UniParc].

Checksum: 07788B2E955626AA
Show »

FASTA55960,521

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] [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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"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] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS PA-2 PRO-153; TRP-165; TRP-410; ILE-428 AND CYS-512.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73424 mRNA. Translation: CAA51825.1.
S67325 mRNA. Translation: AAB28900.1.
AJ006487 expand/collapse EMBL AC list , 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.
CCDSCCDS3089.1. [P05166-1]
CCDS54643.1. [P05166-2]
PIRT45009.
RefSeqNP_000523.2. NM_000532.4. [P05166-1]
NP_001171485.1. NM_001178014.1. [P05166-2]
UniGeneHs.63788.

3D structure databases

ProteinModelPortalP05166.
SMRP05166. Positions 37-539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111129. 12 interactions.
DIPDIP-38244N.
IntActP05166. 8 interactions.
MINTMINT-3004663.
STRING9606.ENSP00000251654.

Chemistry

DrugBankDB00121. Biotin.
DB00161. L-Valine.

PTM databases

PhosphoSiteP05166.

Polymorphism databases

DMDM124106304.

Proteomic databases

MaxQBP05166.
PaxDbP05166.
PeptideAtlasP05166.
PRIDEP05166.

Protocols and materials databases

DNASU5096.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000251654; ENSP00000251654; ENSG00000114054. [P05166-1]
ENST00000469217; ENSP00000419027; ENSG00000114054. [P05166-2]
GeneID5096.
KEGGhsa:5096.
UCSCuc003eqy.2. human. [P05166-1]
uc011bmc.2. human. [P05166-2]

Organism-specific databases

CTD5096.
GeneCardsGC03P135969.
GeneReviewsPCCB.
HGNCHGNC:8654. PCCB.
HPAHPA036939.
HPA036940.
MIM232050. gene.
606054. phenotype.
neXtProtNX_P05166.
Orphanet35. Propionic acidemia.
PharmGKBPA32993.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4799.
HOGENOMHOG000218693.
HOVERGENHBG003970.
InParanoidP05166.
KOK01966.
PhylomeDBP05166.
TreeFamTF314350.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000114054-MONOMER.
BRENDA6.4.1.3. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP05166.
UniPathwayUPA00945; UER00908.

Gene expression databases

ArrayExpressP05166.
BgeeP05166.
CleanExHS_PCCB.
GenevestigatorP05166.

Family and domain databases

Gene3D3.90.226.10. 2 hits.
InterProIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMSSF52096. SSF52096. 2 hits.
PROSITEPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi5096.
NextBio19660.
PROP05166.
SOURCESearch...

Entry information

Entry namePCCB_HUMAN
AccessionPrimary (citable) accession number: P05166
Secondary accession number(s): B7Z2Z4, Q16813, Q96CX0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM