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P50747 (BPL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biotin--protein ligase

EC=6.3.4.-
Alternative name(s):
Biotin apo-protein ligase

Including the following 4 domains:

  1. Biotin--[methylmalonyl-CoA-carboxytransferase] ligase
    EC=6.3.4.9
  2. Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase
    EC=6.3.4.10
    Alternative name(s):
    Holocarboxylase synthetase
    Short name=HCS
  3. Biotin--[methylcrotonoyl-CoA-carboxylase] ligase
    EC=6.3.4.11
  4. Biotin--[acetyl-CoA-carboxylase] ligase
    EC=6.3.4.15
Gene names
Name:HLCS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length726 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase.

Catalytic activity

ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] = AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxytransferase].

ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)].

ATP + biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)].

ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)].

Subunit structure

Monomer.

Subcellular location

Cytoplasm. Mitochondrion.

Tissue specificity

Mostly expressed in muscle, placenta, in lesser extent in the brain, kidney, pancreas, liver and lung.

Involvement in disease

Holocarboxylase synthetase deficiency (HLCS deficiency) [MIM:253270]: A neonatal form of multiple carboxylase deficiency, an autosomal recessive disorder of biotin metabolism, characterized by ketoacidosis, hyperammonemia, excretion of abnormal organic acid metabolites, and dermatitis. In holocarboxylase synthetase deficiency, clinical and biochemical symptoms improve dramatically with administration of biotin.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the biotin--protein ligase family.

Biophysicochemical properties

Kinetic parameters:

KM=224 nM for biotin Ref.15

Vmax=143.9 pmol/min/mg enzyme

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processbiotin metabolic process

Traceable author statement. Source: Reactome

cell proliferation

Inferred from mutant phenotype Ref.20. Source: UniProtKB

histone biotinylation

Inferred from direct assay PubMed 14613969. Source: UniProtKB

histone modification

Inferred from direct assay PubMed 14613969. Source: UniProtKB

protein biotinylation

Inferred from direct assay Ref.1. Source: UniProtKB

response to biotin

Inferred from direct assay PubMed 17904341. Source: UniProtKB

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_componentchromatin

Inferred from direct assay PubMed 14613969. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay PubMed 16780588PubMed 9630604. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear lamina

Inferred from direct assay PubMed 14613969. Source: UniProtKB

nuclear matrix

Inferred from direct assay PubMed 14613969. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

biotin binding

Inferred from direct assay PubMed 14613969. Source: UniProtKB

biotin-[acetyl-CoA-carboxylase] ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

biotin-[methylcrotonoyl-CoA-carboxylase] ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

biotin-[methylmalonyl-CoA-carboxytransferase] ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase activity

Inferred from direct assay Ref.1. Source: UniProtKB

biotin-protein ligase activity

Inferred from direct assay PubMed 9630604. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 19157941. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACACBO007634EBI-3915568,EBI-2211739

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 726726Biotin--protein ligase
PRO_0000064979

Amino acid modifications

Modified residue1471Phosphoserine Ref.9

Natural variations

Natural variant421E → D in HLCS deficiency and a breast cancer sample; somatic mutation; conserves enzymatic wild-type activity; unknown pathological significance. Ref.4 Ref.19
VAR_035800
Natural variant1831R → P in HLCS deficiency; has normal or low KM values for biotin (non-KM mutant). Ref.15
VAR_046507
Natural variant2161L → R in HLCS deficiency; has normal or low KM values for biotin (non-KM mutant); growth of patients' fibroblasts is compromised compared with normal fibroblasts; patients cells are not sensitive to biotin-depletion from the media; growth rates cannot be restored by re-administration of biotin; enzyme activity is severely compromised and cannot be increased by additional biotin; turn-over rate for the mutant protein is double that of wild-type enzyme. Ref.12 Ref.15 Ref.16 Ref.20
Corresponds to variant rs28934602 [ dbSNP | Ensembl ].
VAR_021218
Natural variant2371L → P in HLCS deficiency; has normal or low KM values for biotin (non-KM mutant). Ref.1 Ref.4 Ref.11 Ref.13 Ref.15
VAR_005084
Natural variant3331V → E in HLCS deficiency; <10% activity; has normal or low KM values for biotin (non-KM mutant). Ref.4 Ref.14 Ref.15
VAR_009196
Natural variant3601R → S in HLCS deficiency; 22% activity; shows elevated KM values for biotin (KM mutant) compared with that of the wild-type form. Ref.4
VAR_046508
Natural variant3631V → D in HLCS deficiency; has normal or low KM values for biotin (non-KM mutant). Ref.12 Ref.15
VAR_046509
Natural variant4561Y → C in HLCS deficiency; 0.2% activity. Ref.4
VAR_046510
Natural variant4621T → I in HLCS deficiency; <10% activity. Ref.14
VAR_009197
Natural variant4701L → S in HLCS deficiency; 4.3% activity. Ref.4
VAR_046511
Natural variant5081R → W in HLCS deficiency. Ref.4 Ref.12 Ref.17
VAR_013009
Natural variant5111N → K in HLCS deficiency. Ref.16
VAR_021219
Natural variant5181G → E in HLCS deficiency. Ref.12
VAR_046512
Natural variant5471V → G in HLCS deficiency; 3.4% activity. Ref.4
VAR_046513
Natural variant5501V → M in HLCS deficiency. Ref.4 Ref.12 Ref.13 Ref.17
VAR_009198
Natural variant5711D → N in HLCS deficiency; almost no activity. Ref.12 Ref.14
VAR_009199
Natural variant5811G → S in HLCS deficiency; <10% activity. Ref.4 Ref.14 Ref.15 Ref.16
VAR_009200
Natural variant5821G → R in HLCS deficiency. Ref.16
VAR_021220
Natural variant6101Missing in HLCS deficiency; 14% of activity; shows elevated KM values for biotin (KM mutant) compared with that of the wild-type form. Ref.4 Ref.14 Ref.15
VAR_009201
Natural variant6151D → Y in HLCS deficiency. Ref.18
VAR_046514
Natural variant6341D → N in HLCS deficiency. Ref.17
VAR_046515
Natural variant6341D → Y in HLCS deficiency; 12% activity. Ref.4
VAR_046516
Natural variant7151D → G in HLCS deficiency. Ref.18
VAR_046517

Experimental info

Sequence conflict5581E → K in BAA13332. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P50747 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 855B8E52106D675F

FASTA72680,760
        10         20         30         40         50         60 
MEDRLHMDNG LVPQKIVSVH LQDSTLKEVK DQVSNKQAQI LEPKPEPSLE IKPEQDGMEH 

        70         80         90        100        110        120 
VGRDDPKALG EEPKQRRGSA SGSEPAGDSD RGGGPVEHYH LHLSSCHECL ELENSTIESV 

       130        140        150        160        170        180 
KFASAENIPD LPYDYSSSLE SVADETSPER EGRRVNLTGK APNILLYVGS DSQEALGRFH 

       190        200        210        220        230        240 
EVRSVLADCV DIDSYILYHL LEDSALRDPW TDNCLLLVIA TRESIPEDLY QKFMAYLSQG 

       250        260        270        280        290        300 
GKVLGLSSSF TFGGFQVTSK GALHKTVQNL VFSKADQSEV KLSVLSSGCR YQEGPVRLSP 

       310        320        330        340        350        360 
GRLQGHLENE DKDRMIVHVP FGTRGGEAVL CQVHLELPPS SNIVQTPEDF NLLKSSNFRR 

       370        380        390        400        410        420 
YEVLREILTT LGLSCDMKQV PALTPLYLLS AAEEIRDPLM QWLGKHVDSE GEIKSGQLSL 

       430        440        450        460        470        480 
RFVSSYVSEV EITPSCIPVV TNMEAFSSEH FNLEIYRQNL QTKQLGKVIL FAEVTPTTMR 

       490        500        510        520        530        540 
LLDGLMFQTP QEMGLIVIAA RQTEGKGRGG NVWLSPVGCA LSTLLISIPL RSQLGQRIPF 

       550        560        570        580        590        600 
VQHLMSVAVV EAVRSIPEYQ DINLRVKWPN DIYYSDLMKI GGVLVNSTLM GETFYILIGC 

       610        620        630        640        650        660 
GFNVTNSNPT ICINDLITEY NKQHKAELKP LRADYLIARV VTVLEKLIKE FQDKGPNSVL 

       670        680        690        700        710        720 
PLYYRYWVHS GQQVHLGSAE GPKVSIVGLD DSGFLQVHQE GGEVVTVHPD GNSFDMLRNL 


ILPKRR 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA."
Suzuki Y., Aoki Y., Ishida Y., Chiba Y., Iwamatsu A., Kishino T., Niikawa N., Matsubara Y., Narisawa K.
Nat. Genet. 8:122-128(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HLCS DEFICIENCY PRO-237.
Tissue: Liver.
[2]"Gene identification in the 1.6 Mb of the Down syndrome region on chromosome 21."
Ohira M., Seki N., Nagase T., Suzuki E., Nomura N., Ohara O., Hattori M., Sakaki Y., Eki T., Murakami Y., Saito T., Ichikawa H., Ohki M.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Bone marrow.
[3]"Genomic sequencing of 1.2-Mb region on human chromosome 21q22.2."
Shibuya K., Kudoh J., Minoshima S., Kawasaki K., Nakatoh E., Shintani A., Asakawa S., Shimizu N.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Structure of human holocarboxylase synthetase gene and mutation spectrum of holocarboxylase synthetase deficiency."
Yang X., Aoki Y., Li X., Sakamoto O., Hiratsuka M., Kure S., Taheri S., Christensen E., Inui K., Kubota M., Ohira M., Ohki M., Kudoh J., Kawasaki K., Shibuya K., Shintani A., Asakawa S., Minoshima S. expand/collapse author list , Shimizu N., Narisawa K., Matsubara Y., Suzuki Y.
Hum. Genet. 109:526-534(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HLCS DEFICIENCY ASP-42; PRO-237; GLU-333; SER-360; CYS-456; SER-470; TRP-508; GLY-547; MET-550; SER-581; THR-610 DEL AND TYR-634, CHARACTERIZATION OF VARIANTS HLCS DEFICIENCY ASP-42; SER-360; CYS-456; SER-470; GLY-547 AND TYR-634.
[5]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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 (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].
Tissue: Placenta.
[8]"Transcriptional map of the 2.5-Mb CBR-ERG region of chromosome 21 involved in Down syndrome."
Dahmane N., Ait-Ghezala G., Gosset P., Chamoun Z., Dufresne-Zacharia M.-C., Lopes C., Rabatel N., Gassanova-Maugenre S., Chettouh Z., Abramowski V., Fayet E., Yaspo M.-L., Korn B., Blouin J.-L., Lehrach H., Poustka A., Antonarakis S.E., Sinet P.-M., Creau N., Delabar J.-M.
Genomics 48:12-23(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-92.
Tissue: Brain.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"Molecular analysis of holocarboxylase synthetase deficiency: a missense mutation and a single base deletion are predominant in Japanese patients."
Aoki Y., Suzuki Y., Sakamoto O., Li X., Takahashi K., Ohtake A., Sakuta R., Ohura T., Miyabayashi S., Narisawa K.
Biochim. Biophys. Acta 1272:168-174(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLCS DEFICIENCY PRO-237.
[12]"Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency."
Dupuis L., Leon-Del-Rio A., Leclerc D., Campeau E., Sweetman L., Saudubray J.-M., Herman G., Gibson K.M., Gravel R.A.
Hum. Mol. Genet. 5:1011-1016(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLCS DEFICIENCY ARG-216; ASP-363; TRP-508; GLU-518; MET-550 AND ASN-571.
[13]"Characterization of mutant holocarboxylase synthetase (HCS): a Km for biotin was not elevated in a patient with HCS deficiency."
Aoki Y., Suzuki Y., Li X., Sakamoto O., Chikaoka H., Takita S., Narisawa K.
Pediatr. Res. 42:849-854(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLCS DEFICIENCY PRO-237 AND MET-550.
[14]"Identification and characterization of mutations in patients with holocarboxylase synthetase deficiency."
Aoki Y., Li X., Sakamoto O., Hiratsuka M., Akaishi H., Xu L., Briones P., Suormala T., Baumgartner E.R., Suzuki Y., Narisawa K.
Hum. Genet. 104:143-148(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLCS DEFICIENCY GLU-333; ILE-462; ASN-571; SER-581 AND THR-610 DEL.
[15]"Relationship between kinetic properties of mutant enzyme and biochemical and clinical responsiveness to biotin in holocarboxylase synthetase deficiency."
Sakamoto O., Suzuki Y., Li X., Aoki Y., Hiratsuka M., Suormala T., Baumgartner E.R., Gibson K.M., Narisawa K.
Pediatr. Res. 46:671-676(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, VARIANTS HLCS DEFICIENCY PRO-183; ARG-216; PRO-237; GLU-333; ASP-363; SER-581 AND THR-610 DEL, CHARACTERIZATION OF VARIANTS HLCS DEFICIENCY PRO-183; ARG-216; PRO-237; GLU-333; ASP-363; SER-581 AND THR-610 DEL.
[16]"Clinical findings and biochemical and molecular analysis of four patients with holocarboxylase synthetase deficiency."
Morrone A., Malvagia S., Donati M.A., Funghini S., Ciani F., Pela I., Boneh A., Peters H., Pasquini E., Zammarchi E.
Am. J. Med. Genet. 111:10-18(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLCS DEFICIENCY ARG-216; LYS-511; SER-581 AND ARG-582.
[17]"A genomic approach to mutation analysis of holocarboxylase synthetase gene in three Chinese patients with late-onset holocarboxylase synthetase deficiency."
Tang N.L.S., Hui J., Yong C.K.K., Wong L.T.K., Applegarth D.A., Vallance H.D., Law L.K., Fung S.L.M., Mak T.W.L., Sung Y.M., Cheung K.L., Fok T.F.
Clin. Biochem. 36:145-149(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLCS DEFICIENCY TRP-508; MET-550 AND ASN-634.
[18]"Mutations in the holocarboxylase synthetase gene HLCS."
Suzuki Y., Yang X., Aoki Y., Kure S., Matsubara Y.
Hum. Mutat. 26:285-290(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLCS DEFICIENCY TYR-615 AND GLY-715.
[19]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-42.
[20]"Reduced half-life of holocarboxylase synthetase from patients with severe multiple carboxylase deficiency."
Bailey L.M., Ivanov R.A., Jitrapakdee S., Wilson C.J., Wallace J.C., Polyak S.W.
Hum. Mutat. 29:E47-E57(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT HLCS DEFICIENCY ARG-216.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D23672 mRNA. Translation: BAA04902.1.
D87328 mRNA. Translation: BAA13332.1.
AP000697 expand/collapse EMBL AC list , AP000703, AP000701, AP000698 Genomic DNA. Translation: BAA89434.1.
AB063285 Genomic DNA. Translation: BAB68550.1.
AP001727 Genomic DNA. Translation: BAA95511.1.
AP001726 Genomic DNA. Translation: BAA95510.1.
CH471079 Genomic DNA. Translation: EAX09731.1.
CH471079 Genomic DNA. Translation: EAX09732.1.
BC060787 mRNA. Translation: AAH60787.1.
AJ001864 mRNA. Translation: CAA05056.1.
PIRS50833.
RefSeqNP_000402.3. NM_000411.6.
NP_001229713.1. NM_001242784.1.
NP_001229714.1. NM_001242785.1.
XP_005261012.1. XM_005260955.2.
XP_005261013.1. XM_005260956.2.
UniGeneHs.371350.
Hs.732538.

3D structure databases

ProteinModelPortalP50747.
SMRP50747. Positions 460-707.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109386. 7 interactions.
IntActP50747. 3 interactions.
MINTMINT-3018588.
STRING9606.ENSP00000338387.

Chemistry

ChEMBLCHEMBL2062354.
DrugBankDB00121. Biotin.

PTM databases

PhosphoSiteP50747.

Polymorphism databases

DMDM1705499.

Proteomic databases

PaxDbP50747.
PRIDEP50747.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336648; ENSP00000338387; ENSG00000159267.
ENST00000399120; ENSP00000382071; ENSG00000159267.
ENST00000448340; ENSP00000392923; ENSG00000159267.
GeneID3141.
KEGGhsa:3141.
UCSCuc002yvs.3. human.

Organism-specific databases

CTD3141.
GeneCardsGC21M038123.
HGNCHGNC:4976. HLCS.
HPAHPA017379.
MIM253270. phenotype.
609018. gene.
neXtProtNX_P50747.
Orphanet79242. Holocarboxylase synthetase deficiency.
PharmGKBPA29310.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0340.
HOGENOMHOG000095254.
HOVERGENHBG004872.
InParanoidP50747.
KOK01942.
OMANLQTKQL.
OrthoDBEOG7SV0TT.
PhylomeDBP50747.
TreeFamTF105860.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP50747.
BgeeP50747.
CleanExHS_HLCS.
GenevestigatorP50747.

Family and domain databases

InterProIPR004408. Biotin_CoA_COase_ligase.
IPR003142. BPL_C.
IPR004143. BPL_LipA_LipB.
[Graphical view]
PANTHERPTHR12835. PTHR12835. 1 hit.
PfamPF02237. BPL_C. 1 hit.
PF03099. BPL_LplA_LipB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00121. birA_ligase. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi3141.
NextBio12456.
PROP50747.
SOURCESearch...

Entry information

Entry nameBPL1_HUMAN
AccessionPrimary (citable) accession number: P50747
Secondary accession number(s): D3DSG6, Q99451
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 136 of the entry and version 1 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

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 21

Human chromosome 21: entries, gene names and cross-references to MIM