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Biotin--protein ligase (EC 6.3.4.-) (Biotin apo-protein ligase) [Includes: Biotin--[methylmalonyl-CoA-carboxytransferase] ligase (EC 6.3.4.9); Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase (EC 6.3.4.10) (Holocarboxylase synthetase) (HCS); Biotin--[methylcrotonoyl-CoA-carboxylase] ligase (EC 6.3.4.11); Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)]

 BPL1_HUMAN              Reviewed;         726 AA.
P50747; B2RAH1; D3DSG6; Q99451;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 169.
RecName: Full=Biotin--protein ligase;
EC=6.3.4.-;
AltName: Full=Biotin apo-protein ligase;
Includes:
RecName: Full=Biotin--[methylmalonyl-CoA-carboxytransferase] ligase;
EC=6.3.4.9;
Includes:
RecName: Full=Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase;
EC=6.3.4.10;
AltName: Full=Holocarboxylase synthetase;
Short=HCS;
Includes:
RecName: Full=Biotin--[methylcrotonoyl-CoA-carboxylase] ligase;
EC=6.3.4.11;
Includes:
RecName: Full=Biotin--[acetyl-CoA-carboxylase] ligase;
EC=6.3.4.15;
Name=HLCS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HLCS DEFICIENCY PRO-237.
TISSUE=Liver;
PubMed=7842009; DOI=10.1038/ng1094-122;
Suzuki Y., Aoki Y., Ishida Y., Chiba Y., Iwamatsu A., Kishino T.,
Niikawa N., Matsubara Y., Narisawa K.;
"Isolation and characterization of mutations in the human
holocarboxylase synthetase cDNA.";
Nat. Genet. 8:122-128(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Bone marrow;
PubMed=9037601; DOI=10.1101/gr.7.1.47;
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.;
"Gene identification in 1.6-Mb region of the Down syndrome region on
chromosome 21.";
Genome Res. 7:47-58(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Shibuya K., Kudoh J., Minoshima S., Kawasaki K., Nakatoh E.,
Shintani A., Asakawa S., Shimizu N.;
"Genomic sequencing of 1.2-Mb region on human chromosome 21q22.2.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[4]
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, AND CHARACTERIZATION OF
VARIANTS HLCS DEFICIENCY ASP-42; SER-360; CYS-456; SER-470; GLY-547
AND TYR-634.
PubMed=11735028; DOI=10.1007/s004390100603;
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., Shimizu N., Narisawa K., Matsubara Y., Suzuki Y.;
"Structure of human holocarboxylase synthetase gene and mutation
spectrum of holocarboxylase synthetase deficiency.";
Hum. Genet. 109:526-534(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thalamus, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
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., 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.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-92.
TISSUE=Brain;
PubMed=9503011; DOI=10.1006/geno.1997.5146;
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.;
"Transcriptional map of the 2.5-Mb CBR-ERG region of chromosome 21
involved in Down syndrome.";
Genomics 48:12-23(1998).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
VARIANT HLCS DEFICIENCY PRO-237.
PubMed=8541348; DOI=10.1016/0925-4439(95)00082-8;
Aoki Y., Suzuki Y., Sakamoto O., Li X., Takahashi K., Ohtake A.,
Sakuta R., Ohura T., Miyabayashi S., Narisawa K.;
"Molecular analysis of holocarboxylase synthetase deficiency: a
missense mutation and a single base deletion are predominant in
Japanese patients.";
Biochim. Biophys. Acta 1272:168-174(1995).
[15]
VARIANTS HLCS DEFICIENCY ARG-216; ASP-363; TRP-508; GLU-518; MET-550
AND ASN-571.
PubMed=8817339; DOI=10.1093/hmg/5.7.1011;
Dupuis L., Leon-Del-Rio A., Leclerc D., Campeau E., Sweetman L.,
Saudubray J.-M., Herman G., Gibson K.M., Gravel R.A.;
"Clustering of mutations in the biotin-binding region of
holocarboxylase synthetase in biotin-responsive multiple carboxylase
deficiency.";
Hum. Mol. Genet. 5:1011-1016(1996).
[16]
VARIANTS HLCS DEFICIENCY PRO-237 AND MET-550.
PubMed=9396568; DOI=10.1203/00006450-199712000-00021;
Aoki Y., Suzuki Y., Li X., Sakamoto O., Chikaoka H., Takita S.,
Narisawa K.;
"Characterization of mutant holocarboxylase synthetase (HCS): a Km for
biotin was not elevated in a patient with HCS deficiency.";
Pediatr. Res. 42:849-854(1997).
[17]
VARIANTS HLCS DEFICIENCY GLU-333; ILE-462; ASN-571; SER-581 AND
THR-610 DEL.
PubMed=10190325; DOI=10.1007/s004390050927;
Aoki Y., Li X., Sakamoto O., Hiratsuka M., Akaishi H., Xu L.,
Briones P., Suormala T., Baumgartner E.R., Suzuki Y., Narisawa K.;
"Identification and characterization of mutations in patients with
holocarboxylase synthetase deficiency.";
Hum. Genet. 104:143-148(1999).
[18]
BIOPHYSICOCHEMICAL PROPERTIES, VARIANTS HLCS DEFICIENCY PRO-183;
ARG-216; PRO-237; GLU-333; ASP-363; SER-581 AND THR-610 DEL, AND
CHARACTERIZATION OF VARIANTS HLCS DEFICIENCY PRO-183; ARG-216;
PRO-237; GLU-333; ASP-363; SER-581 AND THR-610 DEL.
PubMed=10590022; DOI=10.1203/00006450-199912000-00006;
Sakamoto O., Suzuki Y., Li X., Aoki Y., Hiratsuka M., Suormala T.,
Baumgartner E.R., Gibson K.M., Narisawa K.;
"Relationship between kinetic properties of mutant enzyme and
biochemical and clinical responsiveness to biotin in holocarboxylase
synthetase deficiency.";
Pediatr. Res. 46:671-676(1999).
[19]
VARIANTS HLCS DEFICIENCY ARG-216; LYS-511; SER-581 AND ARG-582.
PubMed=12124727; DOI=10.1002/ajmg.10532;
Morrone A., Malvagia S., Donati M.A., Funghini S., Ciani F., Pela I.,
Boneh A., Peters H., Pasquini E., Zammarchi E.;
"Clinical findings and biochemical and molecular analysis of four
patients with holocarboxylase synthetase deficiency.";
Am. J. Med. Genet. 111:10-18(2002).
[20]
VARIANTS HLCS DEFICIENCY TRP-508; MET-550 AND ASN-634.
PubMed=12633764; DOI=10.1016/S0009-9120(02)00432-0;
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.;
"A genomic approach to mutation analysis of holocarboxylase synthetase
gene in three Chinese patients with late-onset holocarboxylase
synthetase deficiency.";
Clin. Biochem. 36:145-149(2003).
[21]
VARIANTS HLCS DEFICIENCY TYR-615 AND GLY-715.
PubMed=16134170; DOI=10.1002/humu.20204;
Suzuki Y., Yang X., Aoki Y., Kure S., Matsubara Y.;
"Mutations in the holocarboxylase synthetase gene HLCS.";
Hum. Mutat. 26:285-290(2005).
[22]
VARIANT [LARGE SCALE ANALYSIS] ASP-42.
PubMed=16959974; DOI=10.1126/science.1133427;
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., 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.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[23]
CHARACTERIZATION OF VARIANT HLCS DEFICIENCY ARG-216.
PubMed=18429047; DOI=10.1002/humu.20766;
Bailey L.M., Ivanov R.A., Jitrapakdee S., Wilson C.J., Wallace J.C.,
Polyak S.W.;
"Reduced half-life of holocarboxylase synthetase from patients with
severe multiple carboxylase deficiency.";
Hum. Mutat. 29:E47-E57(2008).
[24]
VARIANTS HLCS DEFICIENCY ARG-505 AND TRP-508.
PubMed=20095979; DOI=10.1111/j.1399-0004.2009.01357.x;
Tammachote R., Janklat S., Tongkobpetch S., Suphapeetiporn K.,
Shotelersuk V.;
"Holocarboxylase synthetase deficiency: novel clinical and molecular
findings.";
Clin. Genet. 78:88-93(2010).
[25]
VARIANT HLCS DEFICIENCY TRP-241.
PubMed=25690727; DOI=10.1007/8904_2014_367;
De Castro M., Zand D.J., Lichter-Konecki U., Kirmse B.;
"Severe neonatal holocarboxylase synthetase deficiency in west african
siblings.";
JIMD Rep. 20:1-4(2015).
-!- 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].
-!- CATALYTIC ACTIVITY: ATP + biotin + apo-[propionyl-CoA:carbon-
dioxide ligase (ADP-forming)] = AMP + diphosphate + [propionyl-
CoA:carbon-dioxide ligase (ADP-forming)].
-!- CATALYTIC ACTIVITY: ATP + biotin + apo-[3-methylcrotonoyl-
CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [3-
methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)].
-!- CATALYTIC ACTIVITY: ATP + biotin + apo-[acetyl-CoA:carbon-dioxide
ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-
dioxide ligase (ADP-forming)].
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=224 nM for biotin {ECO:0000269|PubMed:10590022};
Vmax=143.9 pmol/min/mg enzyme {ECO:0000269|PubMed:10590022};
-!- SUBUNIT: Monomer.
-!- INTERACTION:
O00763:ACACB; NbExp=4; IntAct=EBI-3915568, EBI-2211739;
Q9NUX5:POT1; NbExp=2; IntAct=EBI-3915568, EBI-752420;
-!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion.
-!- TISSUE SPECIFICITY: Mostly expressed in muscle, placenta, in
lesser extent in the brain, kidney, pancreas, liver and lung.
-!- 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.
{ECO:0000269|PubMed:10190325, ECO:0000269|PubMed:10590022,
ECO:0000269|PubMed:11735028, ECO:0000269|PubMed:12124727,
ECO:0000269|PubMed:12633764, ECO:0000269|PubMed:16134170,
ECO:0000269|PubMed:20095979, ECO:0000269|PubMed:25690727,
ECO:0000269|PubMed:7842009, ECO:0000269|PubMed:8541348,
ECO:0000269|PubMed:8817339, ECO:0000269|PubMed:9396568}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the biotin--protein ligase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AK307940; Type=Frameshift; Positions=169; Evidence={ECO:0000305};
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EMBL; D23672; BAA04902.1; -; mRNA.
EMBL; D87328; BAA13332.1; -; mRNA.
EMBL; AP000697; BAA89434.1; -; Genomic_DNA.
EMBL; AP000703; BAA89434.1; JOINED; Genomic_DNA.
EMBL; AP000701; BAA89434.1; JOINED; Genomic_DNA.
EMBL; AP000698; BAA89434.1; JOINED; Genomic_DNA.
EMBL; AB063285; BAB68550.1; -; Genomic_DNA.
EMBL; AK307940; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK314189; BAG36868.1; -; mRNA.
EMBL; AP001726; BAA95510.1; -; Genomic_DNA.
EMBL; AP001727; BAA95511.1; -; Genomic_DNA.
EMBL; CH471079; EAX09731.1; -; Genomic_DNA.
EMBL; CH471079; EAX09732.1; -; Genomic_DNA.
EMBL; BC060787; AAH60787.1; -; mRNA.
EMBL; AJ001864; CAA05056.1; -; mRNA.
CCDS; CCDS13647.1; -.
PIR; S50833; S50833.
RefSeq; NP_000402.3; NM_000411.6.
RefSeq; NP_001229713.1; NM_001242784.1.
RefSeq; NP_001229714.1; NM_001242785.1.
RefSeq; XP_005261012.1; XM_005260955.3.
RefSeq; XP_005261013.1; XM_005260956.3.
RefSeq; XP_006724057.1; XM_006723994.2.
RefSeq; XP_006724058.1; XM_006723995.1.
RefSeq; XP_011527840.1; XM_011529538.1.
RefSeq; XP_011527841.1; XM_011529539.2.
RefSeq; XP_011527843.1; XM_011529541.2.
RefSeq; XP_016883819.1; XM_017028330.1.
UniGene; Hs.371350; -.
UniGene; Hs.732538; -.
ProteinModelPortal; P50747; -.
SMR; P50747; -.
BioGrid; 109386; 9.
IntAct; P50747; 10.
MINT; MINT-3018588; -.
STRING; 9606.ENSP00000338387; -.
BindingDB; P50747; -.
ChEMBL; CHEMBL2062354; -.
DrugBank; DB00121; Biotin.
iPTMnet; P50747; -.
PhosphoSitePlus; P50747; -.
BioMuta; HLCS; -.
DMDM; 1705499; -.
EPD; P50747; -.
MaxQB; P50747; -.
PaxDb; P50747; -.
PeptideAtlas; P50747; -.
PRIDE; P50747; -.
Ensembl; ENST00000336648; ENSP00000338387; ENSG00000159267.
Ensembl; ENST00000399120; ENSP00000382071; ENSG00000159267.
Ensembl; ENST00000612277; ENSP00000479939; ENSG00000159267.
GeneID; 3141; -.
KEGG; hsa:3141; -.
UCSC; uc002yvs.4; human.
CTD; 3141; -.
DisGeNET; 3141; -.
EuPathDB; HostDB:ENSG00000159267.14; -.
GeneCards; HLCS; -.
HGNC; HGNC:4976; HLCS.
HPA; HPA017379; -.
MalaCards; HLCS; -.
MIM; 253270; phenotype.
MIM; 609018; gene.
neXtProt; NX_P50747; -.
OpenTargets; ENSG00000159267; -.
Orphanet; 79242; Holocarboxylase synthetase deficiency.
PharmGKB; PA29310; -.
eggNOG; KOG1536; Eukaryota.
eggNOG; COG0340; LUCA.
GeneTree; ENSGT00390000002960; -.
HOGENOM; HOG000095254; -.
HOVERGEN; HBG004872; -.
InParanoid; P50747; -.
KO; K01942; -.
OMA; RDPLMQW; -.
OrthoDB; EOG091G0G5R; -.
PhylomeDB; P50747; -.
TreeFam; TF105860; -.
Reactome; R-HSA-196780; Biotin transport and metabolism.
SABIO-RK; P50747; -.
ChiTaRS; HLCS; human.
GenomeRNAi; 3141; -.
PRO; PR:P50747; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000159267; -.
CleanEx; HS_HLCS; -.
ExpressionAtlas; P50747; baseline and differential.
Genevisible; P50747; HS.
GO; GO:0000785; C:chromatin; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005652; C:nuclear lamina; IDA:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0009374; F:biotin binding; IDA:UniProtKB.
GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC.
GO; GO:0004078; F:biotin-[methylcrotonoyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC.
GO; GO:0004079; F:biotin-[methylmalonyl-CoA-carboxytransferase] ligase activity; IEA:UniProtKB-EC.
GO; GO:0004080; F:biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase activity; IDA:UniProtKB.
GO; GO:0018271; F:biotin-protein ligase activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0006768; P:biotin metabolic process; TAS:Reactome.
GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
GO; GO:0071110; P:histone biotinylation; IDA:UniProtKB.
GO; GO:0016570; P:histone modification; IDA:UniProtKB.
GO; GO:0009305; P:protein biotinylation; IDA:UniProtKB.
GO; GO:0070781; P:response to biotin; IDA:UniProtKB.
CDD; cd16442; BPL; 1.
InterPro; IPR019197; Biotin-prot_ligase_N.
InterPro; IPR004408; Biotin_CoA_COase_ligase.
InterPro; IPR003142; BPL_C.
InterPro; IPR004143; BPL_LPL_catalytic.
PANTHER; PTHR12835:SF10; PTHR12835:SF10; 1.
Pfam; PF02237; BPL_C; 1.
Pfam; PF03099; BPL_LplA_LipB; 1.
Pfam; PF09825; BPL_N; 1.
TIGRFAMs; TIGR00121; birA_ligase; 1.
PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Disease mutation; Ligase;
Mitochondrion; Multifunctional enzyme; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 726 Biotin--protein ligase.
/FTId=PRO_0000064979.
DOMAIN 463 652 BPL/LPL catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01067}.
MOD_RES 147 147 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 299 299 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 42 42 E -> D (in HLCS deficiency and a breast
cancer sample; somatic mutation;
conserves enzymatic wild-type activity;
unknown pathological significance;
dbSNP:rs61732504).
{ECO:0000269|PubMed:11735028,
ECO:0000269|PubMed:16959974}.
/FTId=VAR_035800.
VARIANT 183 183 R -> P (in HLCS deficiency; has normal or
low KM values for biotin (non-KM
mutant)). {ECO:0000269|PubMed:10590022}.
/FTId=VAR_046507.
VARIANT 216 216 L -> 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;
dbSNP:rs28934602).
{ECO:0000269|PubMed:10590022,
ECO:0000269|PubMed:12124727,
ECO:0000269|PubMed:18429047,
ECO:0000269|PubMed:8817339}.
/FTId=VAR_021218.
VARIANT 237 237 L -> P (in HLCS deficiency; has normal or
low KM values for biotin (non-KM mutant);
dbSNP:rs119103227).
{ECO:0000269|PubMed:10590022,
ECO:0000269|PubMed:11735028,
ECO:0000269|PubMed:7842009,
ECO:0000269|PubMed:8541348,
ECO:0000269|PubMed:9396568}.
/FTId=VAR_005084.
VARIANT 241 241 G -> W (in HLCS deficiency).
{ECO:0000269|PubMed:25690727}.
/FTId=VAR_073074.
VARIANT 333 333 V -> E (in HLCS deficiency; <10%
activity; has normal or low KM values for
biotin (non-KM mutant)).
{ECO:0000269|PubMed:10190325,
ECO:0000269|PubMed:10590022,
ECO:0000269|PubMed:11735028}.
/FTId=VAR_009196.
VARIANT 360 360 R -> S (in HLCS deficiency; 22% activity;
shows elevated KM values for biotin (KM
mutant) compared with that of the wild-
type form).
{ECO:0000269|PubMed:11735028}.
/FTId=VAR_046508.
VARIANT 363 363 V -> D (in HLCS deficiency; has normal or
low KM values for biotin (non-KM mutant);
dbSNP:rs769499327).
{ECO:0000269|PubMed:10590022,
ECO:0000269|PubMed:8817339}.
/FTId=VAR_046509.
VARIANT 456 456 Y -> C (in HLCS deficiency; 0.2%
activity; dbSNP:rs781603756).
{ECO:0000269|PubMed:11735028}.
/FTId=VAR_046510.
VARIANT 462 462 T -> I (in HLCS deficiency; <10%
activity). {ECO:0000269|PubMed:10190325}.
/FTId=VAR_009197.
VARIANT 470 470 L -> S (in HLCS deficiency; 4.3%
activity). {ECO:0000269|PubMed:11735028}.
/FTId=VAR_046511.
VARIANT 505 505 G -> R (in HLCS deficiency).
{ECO:0000269|PubMed:20095979}.
/FTId=VAR_073075.
VARIANT 508 508 R -> W (in HLCS deficiency;
dbSNP:rs119103229).
{ECO:0000269|PubMed:11735028,
ECO:0000269|PubMed:12633764,
ECO:0000269|PubMed:20095979,
ECO:0000269|PubMed:8817339}.
/FTId=VAR_013009.
VARIANT 511 511 N -> K (in HLCS deficiency).
{ECO:0000269|PubMed:12124727}.
/FTId=VAR_021219.
VARIANT 518 518 G -> E (in HLCS deficiency).
{ECO:0000269|PubMed:8817339}.
/FTId=VAR_046512.
VARIANT 547 547 V -> G (in HLCS deficiency; 3.4%
activity). {ECO:0000269|PubMed:11735028}.
/FTId=VAR_046513.
VARIANT 550 550 V -> M (in HLCS deficiency;
dbSNP:rs119103231).
{ECO:0000269|PubMed:11735028,
ECO:0000269|PubMed:12633764,
ECO:0000269|PubMed:8817339,
ECO:0000269|PubMed:9396568}.
/FTId=VAR_009198.
VARIANT 571 571 D -> N (in HLCS deficiency; almost no
activity; dbSNP:rs119103228).
{ECO:0000269|PubMed:10190325,
ECO:0000269|PubMed:8817339}.
/FTId=VAR_009199.
VARIANT 581 581 G -> S (in HLCS deficiency; <10%
activity; dbSNP:rs119103230).
{ECO:0000269|PubMed:10190325,
ECO:0000269|PubMed:10590022,
ECO:0000269|PubMed:11735028,
ECO:0000269|PubMed:12124727}.
/FTId=VAR_009200.
VARIANT 582 582 G -> R (in HLCS deficiency;
dbSNP:rs376899782).
{ECO:0000269|PubMed:12124727}.
/FTId=VAR_021220.
VARIANT 610 610 Missing (in HLCS deficiency; 14% of
activity; shows elevated KM values for
biotin (KM mutant) compared with that of
the wild-type form).
{ECO:0000269|PubMed:10190325,
ECO:0000269|PubMed:10590022,
ECO:0000269|PubMed:11735028}.
/FTId=VAR_009201.
VARIANT 615 615 D -> Y (in HLCS deficiency).
{ECO:0000269|PubMed:16134170}.
/FTId=VAR_046514.
VARIANT 634 634 D -> N (in HLCS deficiency;
dbSNP:rs149399432).
{ECO:0000269|PubMed:12633764}.
/FTId=VAR_046515.
VARIANT 634 634 D -> Y (in HLCS deficiency; 12%
activity). {ECO:0000269|PubMed:11735028}.
/FTId=VAR_046516.
VARIANT 715 715 D -> G (in HLCS deficiency).
{ECO:0000269|PubMed:16134170}.
/FTId=VAR_046517.
CONFLICT 209 209 P -> T (in Ref. 5; AK307940).
{ECO:0000305}.
CONFLICT 463 463 K -> R (in Ref. 5; BAG36868).
{ECO:0000305}.
CONFLICT 558 558 E -> K (in Ref. 2; BAA13332).
{ECO:0000305}.
SEQUENCE 726 AA; 80760 MW; 855B8E52106D675F CRC64;
MEDRLHMDNG LVPQKIVSVH LQDSTLKEVK DQVSNKQAQI LEPKPEPSLE IKPEQDGMEH
VGRDDPKALG EEPKQRRGSA SGSEPAGDSD RGGGPVEHYH LHLSSCHECL ELENSTIESV
KFASAENIPD LPYDYSSSLE SVADETSPER EGRRVNLTGK APNILLYVGS DSQEALGRFH
EVRSVLADCV DIDSYILYHL LEDSALRDPW TDNCLLLVIA TRESIPEDLY QKFMAYLSQG
GKVLGLSSSF TFGGFQVTSK GALHKTVQNL VFSKADQSEV KLSVLSSGCR YQEGPVRLSP
GRLQGHLENE DKDRMIVHVP FGTRGGEAVL CQVHLELPPS SNIVQTPEDF NLLKSSNFRR
YEVLREILTT LGLSCDMKQV PALTPLYLLS AAEEIRDPLM QWLGKHVDSE GEIKSGQLSL
RFVSSYVSEV EITPSCIPVV TNMEAFSSEH FNLEIYRQNL QTKQLGKVIL FAEVTPTTMR
LLDGLMFQTP QEMGLIVIAA RQTEGKGRGG NVWLSPVGCA LSTLLISIPL RSQLGQRIPF
VQHLMSVAVV EAVRSIPEYQ DINLRVKWPN DIYYSDLMKI GGVLVNSTLM GETFYILIGC
GFNVTNSNPT ICINDLITEY NKQHKAELKP LRADYLIARV VTVLEKLIKE FQDKGPNSVL
PLYYRYWVHS GQQVHLGSAE GPKVSIVGLD DSGFLQVHQE GGEVVTVHPD GNSFDMLRNL
ILPKRR


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