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P05166

- PCCB_HUMAN

UniProt

P05166 - PCCB_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP05166.
CleanExiHS_PCCB.
ExpressionAtlasiP05166. baseline and differential.
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. 9 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.
GeneTreeiENSGT00530000063337.
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) [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

        10         20         30         40         50
MAAALRVAAV GARLSVLASG LRAAVRSLCS QATSVNERIE NKRRTALLGG
60 70 80 90 100
GQRRIDAQHK RGKLTARERI SLLLDPGSFV ESDMFVEHRC ADFGMAADKN
110 120 130 140 150
KFPGDSVVTG RGRINGRLVY VFSQDFTVFG GSLSGAHAQK ICKIMDQAIT
160 170 180 190 200
VGAPVIGLND SGGARIQEGV ESLAGYADIF LRNVTASGVI PQISLIMGPC
210 220 230 240 250
AGGAVYSPAL TDFTFMVKDT SYLFITGPDV VKSVTNEDVT QEELGGAKTH
260 270 280 290 300
TTMSGVAHRA FENDVDALCN LRDFFNYLPL SSQDPAPVRE CHDPSDRLVP
310 320 330 340 350
ELDTIVPLES TKAYNMVDII HSVVDEREFF EIMPNYAKNI IVGFARMNGR
360 370 380 390 400
TVGIVGNQPK VASGCLDINS SVKGARFVRF CDAFNIPLIT FVDVPGFLPG
410 420 430 440 450
TAQEYGGIIR HGAKLLYAFA EATVPKVTVI TRKAYGGAYD VMSSKHLCGD
460 470 480 490 500
TNYAWPTAEI AVMGAKGAVE IIFKGHENVE AAQAEYIEKF ANPFPAAVRG
510 520 530
FVDDIIQPSS TRARICCDLD VLASKKVQRP WRKHANIPL
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. 9 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.
GeneTreei ENSGT00530000063337.
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

Bgeei P05166.
CleanExi HS_PCCB.
ExpressionAtlasi P05166. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 150 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