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P05165 (PCCA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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 alpha chain, mitochondrial

Short name=PCCase subunit alpha
EC=6.4.1.3
Alternative name(s):
Propanoyl-CoA:carbon dioxide ligase subunit alpha
Gene names
Name:PCCA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length728 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.

Cofactor

Biotin.

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.8.

Involvement in disease

Propionic acidemia type I (PA-1) [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.15 Ref.16 Ref.17 Ref.18

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Sequence caution

The sequence AAA60035.1 differs from that shown. Reason: Frameshift at positions 374, 378, 380 and 395.

The sequence AAH00140.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAK61392.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA32763.1 differs from that shown. Reason: Frameshift at position 23.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   LigandATP-binding
Biotin
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbiotin metabolic process

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

fatty acid beta-oxidation

Traceable author statement. Source: Reactome

short-chain fatty acid catabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

vitamin metabolic process

Traceable author statement. Source: Reactome

water-soluble vitamin metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

mitochondrial matrix

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

biotin binding

Traceable author statement Ref.10. Source: ProtInc

biotin carboxylase activity

Inferred from electronic annotation. Source: InterPro

enzyme binding

Inferred from physical interaction PubMed 19157941. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: InterPro

propionyl-CoA carboxylase activity

Traceable author statement Ref.10. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05165-1)

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: P05165-2)

The sequence of this isoform differs from the canonical sequence as follows:
     36-61: Missing.
Isoform 3 (identifier: P05165-3)

The sequence of this isoform differs from the canonical sequence as follows:
     634-680: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5252Mitochondrion Ref.8
Chain53 – 728676Propionyl-CoA carboxylase alpha chain, mitochondrial
PRO_0000002837

Regions

Domain62 – 509448Biotin carboxylation
Domain181 – 378198ATP-grasp
Domain660 – 72768Biotinyl-binding

Sites

Active site3531 By similarity
Binding site1771ATP By similarity
Binding site2611ATP By similarity
Binding site2961ATP By similarity

Amino acid modifications

Modified residue651N6-acetyllysine; alternate By similarity
Modified residue651N6-succinyllysine; alternate By similarity
Modified residue1191N6-succinyllysine By similarity
Modified residue1501N6-acetyllysine; alternate By similarity
Modified residue1501N6-succinyllysine; alternate By similarity
Modified residue2001N6-acetyllysine; alternate By similarity
Modified residue2001N6-succinyllysine; alternate By similarity
Modified residue2521Phosphoserine By similarity
Modified residue2621N6-succinyllysine By similarity
Modified residue3281N6-acetyllysine; alternate By similarity
Modified residue3281N6-succinyllysine; alternate By similarity
Modified residue3851N6-succinyllysine By similarity
Modified residue4071N6-succinyllysine By similarity
Modified residue4961N6-acetyllysine By similarity
Modified residue5021N6-succinyllysine By similarity
Modified residue5131N6-succinyllysine By similarity
Modified residue6481N6-succinyllysine By similarity
Modified residue6941N6-biotinyllysine By similarity

Natural variations

Alternative sequence36 – 6126Missing in isoform 2.
VSP_039857
Alternative sequence634 – 68047Missing in isoform 3.
VSP_044458
Natural variant751A → P in PA-1. Ref.18
VAR_009087
Natural variant771R → W in PA-1. Ref.15 Ref.17
VAR_009088
Natural variant1381A → T in PA-1. Ref.15
VAR_009089
Natural variant1641I → T in PA-1. Ref.15
VAR_009090
Natural variant1971G → E in PA-1. Ref.17
VAR_023843
Natural variant2291M → K in PA-1. Ref.18
VAR_009091
Natural variant2971Q → R in PA-1. Ref.17
VAR_009092
Natural variant3681D → G in PA-1. Ref.18
VAR_009093
Natural variant3731M → K in PA-1; unstable protein. Ref.15
VAR_009094
Natural variant3791G → V in PA-1. Ref.18
VAR_009095
Natural variant3981C → R in PA-1. Ref.17
VAR_023844
Natural variant3991R → Q in PA-1. Ref.17
VAR_009096
Natural variant4231P → L in PA-1. Ref.17
VAR_009097
Natural variant4751I → V.
Corresponds to variant rs35719359 [ dbSNP | Ensembl ].
VAR_009098
Natural variant5321Missing in PA-1. Ref.16
VAR_023845
Natural variant5511V → F. Ref.16
Corresponds to variant rs61749895 [ dbSNP | Ensembl ].
VAR_023846
Natural variant5591W → L in PA-1. Ref.17
Corresponds to variant rs118169528 [ dbSNP | Ensembl ].
VAR_009099
Natural variant6311G → R in PA-1. Ref.15
VAR_009100
Natural variant6681G → R in PA-1. Ref.18
VAR_009101
Natural variant7121Missing in PA-1. Ref.18
VAR_009102

Experimental info

Sequence conflict611K → E in BAG60571. Ref.2
Sequence conflict931H → Y in BAG59350. Ref.4
Sequence conflict3731M → R in AAA60035. Ref.10
Sequence conflict378 – 3792KG → RS in AAA60035. Ref.10
Sequence conflict5581N → H in AAA60035. Ref.10
Sequence conflict6101T → A in BAG59350. Ref.4
Sequence conflict6791D → A in AAA36424. Ref.11

Secondary structure

..................... 728
Helix Strand Turn

Details...

Sequences

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

Last modified October 5, 2010. Version 4.
Checksum: 065F64186A0B8CCC

FASTA72880,059
        10         20         30         40         50         60 
MAGFWVGTAP LVAAGRRGRW PPQQLMLSAA LRTLKHVLYY SRQCLMVSRN LGSVGYDPNE 

        70         80         90        100        110        120 
KTFDKILVAN RGEIACRVIR TCKKMGIKTV AIHSDVDASS VHVKMADEAV CVGPAPTSKS 

       130        140        150        160        170        180 
YLNMDAIMEA IKKTRAQAVH PGYGFLSENK EFARCLAAED VVFIGPDTHA IQAMGDKIES 

       190        200        210        220        230        240 
KLLAKKAEVN TIPGFDGVVK DAEEAVRIAR EIGYPVMIKA SAGGGGKGMR IAWDDEETRD 

       250        260        270        280        290        300 
GFRLSSQEAA SSFGDDRLLI EKFIDNPRHI EIQVLGDKHG NALWLNEREC SIQRRNQKVV 

       310        320        330        340        350        360 
EEAPSIFLDA ETRRAMGEQA VALARAVKYS SAGTVEFLVD SKKNFYFLEM NTRLQVEHPV 

       370        380        390        400        410        420 
TECITGLDLV QEMIRVAKGY PLRHKQADIR INGWAVECRV YAEDPYKSFG LPSIGRLSQY 

       430        440        450        460        470        480 
QEPLHLPGVR VDSGIQPGSD ISIYYDPMIS KLITYGSDRT EALKRMADAL DNYVIRGVTH 

       490        500        510        520        530        540 
NIALLREVII NSRFVKGDIS TKFLSDVYPD GFKGHMLTKS EKNQLLAIAS SLFVAFQLRA 

       550        560        570        580        590        600 
QHFQENSRMP VIKPDIANWE LSVKLHDKVH TVVASNNGSV FSVEVDGSKL NVTSTWNLAS 

       610        620        630        640        650        660 
PLLSVSVDGT QRTVQCLSRE AGGNMSIQFL GTVYKVNILT RLAAELNKFM LEKVTEDTSS 

       670        680        690        700        710        720 
VLRSPMPGVV VAVSVKPGDA VAEGQEICVI EAMKMQNSMT AGKTGTVKSV HCQAGDTVGE 


GDLLVELE 

« Hide

Isoform 2 [UniParc].

Checksum: B75C63581796ED53
Show »

FASTA70277,048
Isoform 3 [UniParc].

Checksum: CF5795BE08D8BD5B
Show »

FASTA68175,002

References

« Hide 'large scale' references
[1]"Structure of the PCCA gene and distribution of mutations causing propionic acidemia."
Campeau E., Desviat L.R., Leclerc D., Wu X., Perez B., Ugarte M., Gravel R.A.
Mol. Genet. Metab. 74:238-247(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[2]"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] (ISOFORMS 2 AND 3).
Tissue: Kidney and Tongue.
[3]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] OF 9-728 (ISOFORM 1).
Tissue: Placenta.
[6]"Human mitochondrial propionyl-CoA carboxylase: localization of the N-terminus of the pro- and mature alpha chains in the deduced primary sequence of a full-length cDNA."
Lamhonwah A.-M., Mahuran D.J., Gravel R.A.
Nucleic Acids Res. 17:4396-4396(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-728 (ISOFORM 1).
[7]Gravel R.A.
Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[8]"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 53-58, SUBCELLULAR LOCATION.
Tissue: Kidney.
[9]"Cloning of functional alpha propionyl CoA carboxylase and correction of enzyme deficiency in pccA fibroblasts."
Stankovics J., Ledley F.D.
Am. J. Hum. Genet. 52:144-151(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 364-392.
Tissue: Liver.
[10]"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 369-561.
[11]"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 633-728.
[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]"Solution structure of B domain from human propionyl-CoA carboxylase alpha subunit."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 175-270.
[14]"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.
[15]"Genetic heterogeneity in propionic acidemia patients with alpha-subunit defects: identification of five novel mutations, one of them causing instability of the protein."
Richard E., Desviat L.R., Perez B., Perez-Cerda C., Ugarte M.
Biochim. Biophys. Acta 1453:351-358(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PA-1 TRP-77; THR-138; THR-164; LYS-373 AND ARG-631.
[16]"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: VARIANT PHE-551, VARIANT PA-1 LEU-532 DEL.
[17]"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-1 TRP-77; GLU-197; ARG-297; ARG-398; GLN-399; LEU-423 AND LEU-559.
[18]"Coding sequence mutations in the alpha subunit of propionyl-CoA carboxylase in patients with propionic acidemia."
Campeau E., Dupuis L., Leon-Del-Rio A., Gravel R.
Mol. Genet. Metab. 67:11-22(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PA-1 PRO-75; LYS-229; GLY-368; VAL-379; ARG-668 AND CYS-712 DEL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF385926 mRNA. Translation: AAL66189.1.
AY035808 expand/collapse EMBL AC list , AY035786, AY035787, AY035788, AY035789, AY035790, AY035791, AY035792, AY035793, AY035794, AY035795, AY035796, AY035797, AY035798, AY035799, AY035800, AY035801, AY035802, AY035803, AY035804, AY035805, AY035806, AY035807 Genomic DNA. Translation: AAK61392.1. Different initiation.
AK296771 mRNA. Translation: BAG59350.1.
AK298318 mRNA. Translation: BAG60571.1.
AL355338 expand/collapse EMBL AC list , AL136526, AL353697, AL356575 Genomic DNA. Translation: CAH70370.2.
AL356575 expand/collapse EMBL AC list , AL136526, AL353697, AL355338 Genomic DNA. Translation: CAH72681.2.
AL136526 expand/collapse EMBL AC list , AL353697, AL355338, AL356575 Genomic DNA. Translation: CAI39557.2.
AL353697 expand/collapse EMBL AC list , AL136526, AL355338, AL356575 Genomic DNA. Translation: CAI40434.2.
CH471085 Genomic DNA. Translation: EAX09034.1.
BC000140 mRNA. Translation: AAH00140.1. Different initiation.
X14608 mRNA. Translation: CAA32763.1. Frameshift.
S55656 mRNA. Translation: AAB25345.1.
M13572 mRNA. Translation: AAA60035.1. Frameshift.
M26121 mRNA. Translation: AAA36424.1.
CCDSCCDS45065.1. [P05165-2]
CCDS53878.1. [P05165-3]
CCDS9496.2. [P05165-1]
PIRA27883. S04613.
RefSeqNP_000273.2. NM_000282.3. [P05165-1]
NP_001121164.1. NM_001127692.2. [P05165-2]
NP_001171475.1. NM_001178004.1. [P05165-3]
UniGeneHs.80741.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQYNMR-A176-270[»]
2JKUX-ray1.50A658-728[»]
ProteinModelPortalP05165.
SMRP05165. Positions 63-728.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111128. 8 interactions.
DIPDIP-57493N.
IntActP05165. 6 interactions.
STRING9606.ENSP00000365462.

Chemistry

DrugBankDB00121. Biotin.

PTM databases

PhosphoSiteP05165.

Polymorphism databases

DMDM308153661.

Proteomic databases

MaxQBP05165.
PaxDbP05165.
PRIDEP05165.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376279; ENSP00000365456; ENSG00000175198. [P05165-3]
ENST00000376285; ENSP00000365462; ENSG00000175198. [P05165-1]
ENST00000376286; ENSP00000365463; ENSG00000175198. [P05165-2]
GeneID5095.
KEGGhsa:5095.
UCSCuc001voo.3. human. [P05165-1]
uc010aga.3. human. [P05165-2]
uc010tiz.2. human. [P05165-3]

Organism-specific databases

CTD5095.
GeneCardsGC13P100741.
GeneReviewsPCCA.
HGNCHGNC:8653. PCCA.
HPAHPA041716.
HPA047792.
MIM232000. gene.
606054. phenotype.
neXtProtNX_P05165.
Orphanet35. Propionic acidemia.
PharmGKBPA32992.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4770.
HOGENOMHOG000008989.
HOVERGENHBG000555.
KOK01965.
OMAHTVVASN.
OrthoDBEOG7RZ5PH.
PhylomeDBP05165.
TreeFamTF354220.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000175198-MONOMER.
RETL1328306-WGS:GSTH-2235-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP05165.
UniPathwayUPA00945; UER00908.

Gene expression databases

ArrayExpressP05165.
BgeeP05165.
CleanExHS_PCCA.
GenevestigatorP05165.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProIPR011761. 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.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPCCA. human.
EvolutionaryTraceP05165.
GenomeRNAi5095.
NextBio19656.
PROP05165.
SOURCESearch...

Entry information

Entry namePCCA_HUMAN
AccessionPrimary (citable) accession number: P05165
Secondary accession number(s): B4DKY8 expand/collapse secondary AC list , B4DPF9, C9JPQ8, Q15979, Q8WXQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 171 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 13

Human chromosome 13: entries, gene names and cross-references to MIM