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P05165

- PCCA_HUMAN

UniProt

P05165 - PCCA_HUMAN

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Protein

Propionyl-CoA carboxylase alpha chain, mitochondrial

Gene
PCCA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Biotin.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei177 – 1771ATP By similarity
Binding sitei261 – 2611ATP By similarity
Binding sitei296 – 2961ATP By similarity
Active sitei353 – 3531 By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. biotin binding Source: ProtInc
  3. biotin carboxylase activity Source: InterPro
  4. enzyme binding Source: UniProtKB
  5. metal ion binding Source: InterPro
  6. 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
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Biotin, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000175198-MONOMER.
RETL1328306-WGS:GSTH-2235-MONOMER.
ReactomeiREACT_11153. Biotin transport and metabolism.
REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
REACT_993. Propionyl-CoA catabolism.
SABIO-RKP05165.
UniPathwayiUPA00945; UER00908.

Names & Taxonomyi

Protein namesi
Recommended name:
Propionyl-CoA carboxylase alpha chain, mitochondrial (EC:6.4.1.3)
Short name:
PCCase subunit alpha
Alternative name(s):
Propanoyl-CoA:carbon dioxide ligase subunit alpha
Gene namesi
Name:PCCA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:8653. PCCA.

Subcellular locationi

Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrial matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

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.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751A → P in PA-1. 1 Publication
VAR_009087
Natural varianti77 – 771R → W in PA-1. 2 Publications
VAR_009088
Natural varianti138 – 1381A → T in PA-1. 1 Publication
VAR_009089
Natural varianti164 – 1641I → T in PA-1. 1 Publication
VAR_009090
Natural varianti197 – 1971G → E in PA-1. 1 Publication
VAR_023843
Natural varianti229 – 2291M → K in PA-1. 1 Publication
VAR_009091
Natural varianti297 – 2971Q → R in PA-1. 1 Publication
VAR_009092
Natural varianti368 – 3681D → G in PA-1. 1 Publication
VAR_009093
Natural varianti373 – 3731M → K in PA-1; unstable protein. 1 Publication
VAR_009094
Natural varianti379 – 3791G → V in PA-1. 1 Publication
VAR_009095
Natural varianti398 – 3981C → R in PA-1. 1 Publication
VAR_023844
Natural varianti399 – 3991R → Q in PA-1. 1 Publication
VAR_009096
Natural varianti423 – 4231P → L in PA-1. 1 Publication
VAR_009097
Natural varianti532 – 5321Missing in PA-1. 1 Publication
VAR_023845
Natural varianti559 – 5591W → L in PA-1. 1 Publication
Corresponds to variant rs118169528 [ dbSNP | Ensembl ].
VAR_009099
Natural varianti631 – 6311G → R in PA-1. 1 Publication
VAR_009100
Natural varianti668 – 6681G → R in PA-1. 1 Publication
VAR_009101
Natural varianti712 – 7121Missing in PA-1. 1 Publication
VAR_009102

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi606054. phenotype.
Orphaneti35. Propionic acidemia.
PharmGKBiPA32992.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252Mitochondrion1 PublicationAdd
BLAST
Chaini53 – 728676Propionyl-CoA carboxylase alpha chain, mitochondrialPRO_0000002837Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651N6-acetyllysine; alternate By similarity
Modified residuei65 – 651N6-succinyllysine; alternate By similarity
Modified residuei119 – 1191N6-succinyllysine By similarity
Modified residuei150 – 1501N6-acetyllysine; alternate By similarity
Modified residuei150 – 1501N6-succinyllysine; alternate By similarity
Modified residuei200 – 2001N6-acetyllysine; alternate By similarity
Modified residuei200 – 2001N6-succinyllysine; alternate By similarity
Modified residuei252 – 2521Phosphoserine By similarity
Modified residuei262 – 2621N6-succinyllysine By similarity
Modified residuei328 – 3281N6-acetyllysine; alternate By similarity
Modified residuei328 – 3281N6-succinyllysine; alternate By similarity
Modified residuei385 – 3851N6-succinyllysine By similarity
Modified residuei407 – 4071N6-succinyllysine By similarity
Modified residuei496 – 4961N6-acetyllysine By similarity
Modified residuei502 – 5021N6-succinyllysine By similarity
Modified residuei513 – 5131N6-succinyllysine By similarity
Modified residuei648 – 6481N6-succinyllysine By similarity
Modified residuei694 – 6941N6-biotinyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05165.
PaxDbiP05165.
PRIDEiP05165.

PTM databases

PhosphoSiteiP05165.

Expressioni

Gene expression databases

ArrayExpressiP05165.
BgeeiP05165.
CleanExiHS_PCCA.
GenevestigatoriP05165.

Organism-specific databases

HPAiHPA041716.
HPA047792.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi111128. 5 interactions.
DIPiDIP-57493N.
IntActiP05165. 6 interactions.
STRINGi9606.ENSP00000365462.

Structurei

Secondary structure

1
728
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi199 – 2013
Helixi202 – 21211
Beta strandi214 – 2207
Turni226 – 2283
Beta strandi230 – 2345
Helixi235 – 25218
Beta strandi258 – 2625
Beta strandi265 – 2684
Beta strandi665 – 6673
Beta strandi669 – 6735
Beta strandi688 – 6914

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQYNMR-A176-270[»]
2JKUX-ray1.50A658-728[»]
ProteinModelPortaliP05165.
SMRiP05165. Positions 63-728.

Miscellaneous databases

EvolutionaryTraceiP05165.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 509448Biotin carboxylationAdd
BLAST
Domaini181 – 378198ATP-graspAdd
BLAST
Domaini660 – 72768Biotinyl-bindingAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG4770.
HOGENOMiHOG000008989.
HOVERGENiHBG000555.
KOiK01965.
OMAiHTVVASN.
OrthoDBiEOG7RZ5PH.
PhylomeDBiP05165.
TreeFamiTF354220.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR011761. 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]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEiPS50975. 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]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P05165-1) [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

MAGFWVGTAP LVAAGRRGRW PPQQLMLSAA LRTLKHVLYY SRQCLMVSRN    50
LGSVGYDPNE KTFDKILVAN RGEIACRVIR TCKKMGIKTV AIHSDVDASS 100
VHVKMADEAV CVGPAPTSKS YLNMDAIMEA IKKTRAQAVH PGYGFLSENK 150
EFARCLAAED VVFIGPDTHA IQAMGDKIES KLLAKKAEVN TIPGFDGVVK 200
DAEEAVRIAR EIGYPVMIKA SAGGGGKGMR IAWDDEETRD GFRLSSQEAA 250
SSFGDDRLLI EKFIDNPRHI EIQVLGDKHG NALWLNEREC SIQRRNQKVV 300
EEAPSIFLDA ETRRAMGEQA VALARAVKYS SAGTVEFLVD SKKNFYFLEM 350
NTRLQVEHPV TECITGLDLV QEMIRVAKGY PLRHKQADIR INGWAVECRV 400
YAEDPYKSFG LPSIGRLSQY QEPLHLPGVR VDSGIQPGSD ISIYYDPMIS 450
KLITYGSDRT EALKRMADAL DNYVIRGVTH NIALLREVII NSRFVKGDIS 500
TKFLSDVYPD GFKGHMLTKS EKNQLLAIAS SLFVAFQLRA QHFQENSRMP 550
VIKPDIANWE LSVKLHDKVH TVVASNNGSV FSVEVDGSKL NVTSTWNLAS 600
PLLSVSVDGT QRTVQCLSRE AGGNMSIQFL GTVYKVNILT RLAAELNKFM 650
LEKVTEDTSS VLRSPMPGVV VAVSVKPGDA VAEGQEICVI EAMKMQNSMT 700
AGKTGTVKSV HCQAGDTVGE GDLLVELE 728
Length:728
Mass (Da):80,059
Last modified:October 5, 2010 - v4
Checksum:i065F64186A0B8CCC
GO
Isoform 2 (identifier: P05165-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     36-61: Missing.

Show »
Length:702
Mass (Da):77,048
Checksum:iB75C63581796ED53
GO
Isoform 3 (identifier: P05165-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:681
Mass (Da):75,002
Checksum:iCF5795BE08D8BD5B
GO

Sequence cautioni

The sequence AAA60035.1 differs from that shown. Reason: Frameshift at positions 374, 378, 380 and 395.
The sequence CAA32763.1 differs from that shown. Reason: Frameshift at position 23.
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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751A → P in PA-1. 1 Publication
VAR_009087
Natural varianti77 – 771R → W in PA-1. 2 Publications
VAR_009088
Natural varianti138 – 1381A → T in PA-1. 1 Publication
VAR_009089
Natural varianti164 – 1641I → T in PA-1. 1 Publication
VAR_009090
Natural varianti197 – 1971G → E in PA-1. 1 Publication
VAR_023843
Natural varianti229 – 2291M → K in PA-1. 1 Publication
VAR_009091
Natural varianti297 – 2971Q → R in PA-1. 1 Publication
VAR_009092
Natural varianti368 – 3681D → G in PA-1. 1 Publication
VAR_009093
Natural varianti373 – 3731M → K in PA-1; unstable protein. 1 Publication
VAR_009094
Natural varianti379 – 3791G → V in PA-1. 1 Publication
VAR_009095
Natural varianti398 – 3981C → R in PA-1. 1 Publication
VAR_023844
Natural varianti399 – 3991R → Q in PA-1. 1 Publication
VAR_009096
Natural varianti423 – 4231P → L in PA-1. 1 Publication
VAR_009097
Natural varianti475 – 4751I → V.
Corresponds to variant rs35719359 [ dbSNP | Ensembl ].
VAR_009098
Natural varianti532 – 5321Missing in PA-1. 1 Publication
VAR_023845
Natural varianti551 – 5511V → F.1 Publication
Corresponds to variant rs61749895 [ dbSNP | Ensembl ].
VAR_023846
Natural varianti559 – 5591W → L in PA-1. 1 Publication
Corresponds to variant rs118169528 [ dbSNP | Ensembl ].
VAR_009099
Natural varianti631 – 6311G → R in PA-1. 1 Publication
VAR_009100
Natural varianti668 – 6681G → R in PA-1. 1 Publication
VAR_009101
Natural varianti712 – 7121Missing in PA-1. 1 Publication
VAR_009102

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei36 – 6126Missing in isoform 2. VSP_039857Add
BLAST
Alternative sequencei634 – 68047Missing in isoform 3. VSP_044458Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611K → E in BAG60571. 1 Publication
Sequence conflicti93 – 931H → Y in BAG59350. 1 Publication
Sequence conflicti373 – 3731M → R in AAA60035. 1 Publication
Sequence conflicti378 – 3792KG → RS in AAA60035. 1 Publication
Sequence conflicti558 – 5581N → H in AAA60035. 1 Publication
Sequence conflicti610 – 6101T → A in BAG59350. 1 Publication
Sequence conflicti679 – 6791D → A in AAA36424. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF385926 mRNA. Translation: AAL66189.1.
AY035808
, 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
, AL136526, AL353697, AL356575 Genomic DNA. Translation: CAH70370.2.
AL356575
, AL136526, AL353697, AL355338 Genomic DNA. Translation: CAH72681.2.
AL136526
, AL353697, AL355338, AL356575 Genomic DNA. Translation: CAI39557.2.
AL353697
, 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.
CCDSiCCDS45065.1. [P05165-2]
CCDS53878.1. [P05165-3]
CCDS9496.2. [P05165-1]
PIRiS04613. A27883.
RefSeqiNP_000273.2. NM_000282.3. [P05165-1]
NP_001121164.1. NM_001127692.2. [P05165-2]
NP_001171475.1. NM_001178004.1. [P05165-3]
UniGeneiHs.80741.

Genome annotation databases

EnsembliENST00000376279; ENSP00000365456; ENSG00000175198. [P05165-3]
ENST00000376285; ENSP00000365462; ENSG00000175198. [P05165-1]
ENST00000376286; ENSP00000365463; ENSG00000175198. [P05165-2]
GeneIDi5095.
KEGGihsa:5095.
UCSCiuc001voo.3. human. [P05165-1]
uc010aga.3. human. [P05165-2]
uc010tiz.2. human. [P05165-3]

Polymorphism databases

DMDMi308153661.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF385926 mRNA. Translation: AAL66189.1 .
AY035808
, 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
, AL136526 , AL353697 , AL356575 Genomic DNA. Translation: CAH70370.2 .
AL356575
, AL136526 , AL353697 , AL355338 Genomic DNA. Translation: CAH72681.2 .
AL136526
, AL353697 , AL355338 , AL356575 Genomic DNA. Translation: CAI39557.2 .
AL353697
, 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 .
CCDSi CCDS45065.1. [P05165-2 ]
CCDS53878.1. [P05165-3 ]
CCDS9496.2. [P05165-1 ]
PIRi S04613. A27883.
RefSeqi NP_000273.2. NM_000282.3. [P05165-1 ]
NP_001121164.1. NM_001127692.2. [P05165-2 ]
NP_001171475.1. NM_001178004.1. [P05165-3 ]
UniGenei Hs.80741.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CQY NMR - A 176-270 [» ]
2JKU X-ray 1.50 A 658-728 [» ]
ProteinModelPortali P05165.
SMRi P05165. Positions 63-728.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111128. 5 interactions.
DIPi DIP-57493N.
IntActi P05165. 6 interactions.
STRINGi 9606.ENSP00000365462.

Chemistry

DrugBanki DB00121. Biotin.

PTM databases

PhosphoSitei P05165.

Polymorphism databases

DMDMi 308153661.

Proteomic databases

MaxQBi P05165.
PaxDbi P05165.
PRIDEi P05165.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376279 ; ENSP00000365456 ; ENSG00000175198 . [P05165-3 ]
ENST00000376285 ; ENSP00000365462 ; ENSG00000175198 . [P05165-1 ]
ENST00000376286 ; ENSP00000365463 ; ENSG00000175198 . [P05165-2 ]
GeneIDi 5095.
KEGGi hsa:5095.
UCSCi uc001voo.3. human. [P05165-1 ]
uc010aga.3. human. [P05165-2 ]
uc010tiz.2. human. [P05165-3 ]

Organism-specific databases

CTDi 5095.
GeneCardsi GC13P100741.
GeneReviewsi PCCA.
HGNCi HGNC:8653. PCCA.
HPAi HPA041716.
HPA047792.
MIMi 232000. gene.
606054. phenotype.
neXtProti NX_P05165.
Orphaneti 35. Propionic acidemia.
PharmGKBi PA32992.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4770.
HOGENOMi HOG000008989.
HOVERGENi HBG000555.
KOi K01965.
OMAi HTVVASN.
OrthoDBi EOG7RZ5PH.
PhylomeDBi P05165.
TreeFami TF354220.

Enzyme and pathway databases

UniPathwayi UPA00945 ; UER00908 .
BioCyci MetaCyc:ENSG00000175198-MONOMER.
RETL1328306-WGS:GSTH-2235-MONOMER.
Reactomei REACT_11153. Biotin transport and metabolism.
REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
REACT_993. Propionyl-CoA catabolism.
SABIO-RK P05165.

Miscellaneous databases

ChiTaRSi PCCA. human.
EvolutionaryTracei P05165.
GenomeRNAii 5095.
NextBioi 19656.
PROi P05165.
SOURCEi Search...

Gene expression databases

ArrayExpressi P05165.
Bgeei P05165.
CleanExi HS_PCCA.
Genevestigatori P05165.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProi 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.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
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.
[Graphical view ]
SMARTi SM00878. Biotin_carb_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEi PS50975. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiPCCA_HUMAN
AccessioniPrimary (citable) accession number: P05165
Secondary accession number(s): B4DKY8
, B4DPF9, C9JPQ8, Q15979, Q8WXQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: October 5, 2010
Last modified: September 3, 2014
This is version 172 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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

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