Full text data of ILVBL
ILVBL
(AHAS)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Acetolactate synthase-like protein; 2.2.1.- (IlvB-like protein)
Acetolactate synthase-like protein; 2.2.1.- (IlvB-like protein)
UniProt
A1L0T0
ID ILVBL_HUMAN Reviewed; 632 AA.
AC A1L0T0; O43341; Q96F08; Q99651; Q9BWN5; Q9UEB2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JAN-2008, sequence version 2.
DT 22-JAN-2014, entry version 64.
DE RecName: Full=Acetolactate synthase-like protein;
DE EC=2.2.1.-;
DE AltName: Full=IlvB-like protein;
GN Name=ILVBL; Synonyms=AHAS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=8954801; DOI=10.1006/geno.1996.0615;
RA Joutel A., Ducros A., Alamowitch S., Cruaud C., Domenga V.,
RA Marechal E., Vahedi K., Chabriat H., Bousser M.G.,
RA Tournier-Lasserve E.;
RT "A human homolog of bacterial acetolactate synthase genes maps within
RT the CADASIL critical region.";
RL Genomics 38:192-198(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-374.
RC TISSUE=Pancreas, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, with highest
CC expression in heart, pancreas and placenta.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18916.1; Type=Erroneous gene model prediction;
CC Sequence=AAH00109.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
CC Sequence=AAI26914.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAI26914.1; Type=Miscellaneous discrepancy; Note=Sequence of unknown origin at the C-terminus;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U61263; AAC50934.1; -; mRNA.
DR EMBL; AC003956; AAB94632.1; -; Genomic_DNA.
DR EMBL; AC004794; AAC18916.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471106; EAW84464.1; -; Genomic_DNA.
DR EMBL; BC000109; AAH00109.1; ALT_SEQ; mRNA.
DR EMBL; BC011722; AAH11722.1; -; mRNA.
DR EMBL; BC011761; AAH11761.1; -; mRNA.
DR EMBL; BC126913; AAI26914.1; ALT_SEQ; mRNA.
DR RefSeq; NP_006835.2; NM_006844.4.
DR RefSeq; XP_005259774.1; XM_005259717.1.
DR UniGene; Hs.78880; -.
DR ProteinModelPortal; A1L0T0; -.
DR SMR; A1L0T0; 54-620.
DR IntAct; A1L0T0; 8.
DR MINT; MINT-1417151; -.
DR STRING; 9606.ENSP00000263383; -.
DR PhosphoSite; A1L0T0; -.
DR PaxDb; A1L0T0; -.
DR PeptideAtlas; A1L0T0; -.
DR PRIDE; A1L0T0; -.
DR DNASU; 10994; -.
DR Ensembl; ENST00000263383; ENSP00000263383; ENSG00000105135.
DR GeneID; 10994; -.
DR KEGG; hsa:10994; -.
DR UCSC; uc002nam.3; human.
DR CTD; 10994; -.
DR GeneCards; GC19M015225; -.
DR HGNC; HGNC:6041; ILVBL.
DR MIM; 605770; gene.
DR neXtProt; NX_A1L0T0; -.
DR PharmGKB; PA29857; -.
DR eggNOG; COG0028; -.
DR HOGENOM; HOG000010642; -.
DR HOVERGEN; HBG108004; -.
DR InParanoid; A1L0T0; -.
DR KO; K11259; -.
DR OMA; FMVQKEM; -.
DR OrthoDB; EOG75B84X; -.
DR PhylomeDB; A1L0T0; -.
DR GenomeRNAi; 10994; -.
DR NextBio; 41779; -.
DR PRO; PR:A1L0T0; -.
DR ArrayExpress; A1L0T0; -.
DR Bgee; A1L0T0; -.
DR CleanEx; HS_ILVBL; -.
DR Genevestigator; A1L0T0; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:GOC.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Magnesium; Membrane; Metal-binding; Polymorphism;
KW Reference proteome; Thiamine pyrophosphate; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 632 Acetolactate synthase-like protein.
FT /FTId=PRO_0000314825.
FT TRANSMEM 13 33 Helical; (Potential).
FT REGION 470 550 Thiamine pyrophosphate binding (By
FT similarity).
FT METAL 521 521 Magnesium (By similarity).
FT METAL 547 547 Magnesium (By similarity).
FT BINDING 98 98 Thiamine pyrophosphate (By similarity).
FT VARIANT 374 374 N -> D (in dbSNP:rs17856373).
FT /FTId=VAR_038064.
FT VARIANT 510 510 R -> Q (in dbSNP:rs35548653).
FT /FTId=VAR_061901.
SQ SEQUENCE 632 AA; 67868 MW; 893F539FC5F1B2EC CRC64;
METPAAAAPA GSLFPSFLLL ACGTLVAALL GAAHRLGLFY QLLHKVDKAS VRHGGENVAA
VLRAHGVRFI FTLVGGHISP LLVACEKLGI RVVDTRHEVT AVFAADAMAR LSGTVGVAAV
TAGPGLTNTV TAVKNAQMAQ SPILLLGGAA STLLQNRGAL QAVDQLSLFR PLCKFCVSVR
RVRDIVPTLR AAMAAAQSGT PGPVFVELPV DVLYPYFMVQ KEMVPAKPPK GLVGRVVSWY
LENYLANLFA GAWEPQPEGP LPLDIPQASP QQVQRCVEIL SRAKRPLMVL GSQALLTPTS
ADKLRAAVET LGVPCFLGGM ARGLLGRNHP LHIRENRSAA LKKADVIVLA GTVCDFRLSY
GRVLSHSSKI IIVNRNREEM LLNSDIFWKP QEAVQGDVGS FVLKLVEGLQ GQTWAPDWVE
ELREADRQKE QTFREKAAMP VAQHLNPVQV LQLVEETLPD NSILVVDGGD FVGTAAHLVQ
PRGPLRWLDP GAFGTLGVGA GFALGAKLCR PDAEVWCLFG DGAFGYSLIE FDTFVRHKIP
VMALVGNDAG WTQISREQVP SLGSNVACGL AYTDYHKAAM GLGARGLLLS RENEDQVVKV
LHDAQQQCRD GHPVVVNILI GRTDFRDGSI AV
//
ID ILVBL_HUMAN Reviewed; 632 AA.
AC A1L0T0; O43341; Q96F08; Q99651; Q9BWN5; Q9UEB2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JAN-2008, sequence version 2.
DT 22-JAN-2014, entry version 64.
DE RecName: Full=Acetolactate synthase-like protein;
DE EC=2.2.1.-;
DE AltName: Full=IlvB-like protein;
GN Name=ILVBL; Synonyms=AHAS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=8954801; DOI=10.1006/geno.1996.0615;
RA Joutel A., Ducros A., Alamowitch S., Cruaud C., Domenga V.,
RA Marechal E., Vahedi K., Chabriat H., Bousser M.G.,
RA Tournier-Lasserve E.;
RT "A human homolog of bacterial acetolactate synthase genes maps within
RT the CADASIL critical region.";
RL Genomics 38:192-198(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-374.
RC TISSUE=Pancreas, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, with highest
CC expression in heart, pancreas and placenta.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18916.1; Type=Erroneous gene model prediction;
CC Sequence=AAH00109.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
CC Sequence=AAI26914.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAI26914.1; Type=Miscellaneous discrepancy; Note=Sequence of unknown origin at the C-terminus;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U61263; AAC50934.1; -; mRNA.
DR EMBL; AC003956; AAB94632.1; -; Genomic_DNA.
DR EMBL; AC004794; AAC18916.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471106; EAW84464.1; -; Genomic_DNA.
DR EMBL; BC000109; AAH00109.1; ALT_SEQ; mRNA.
DR EMBL; BC011722; AAH11722.1; -; mRNA.
DR EMBL; BC011761; AAH11761.1; -; mRNA.
DR EMBL; BC126913; AAI26914.1; ALT_SEQ; mRNA.
DR RefSeq; NP_006835.2; NM_006844.4.
DR RefSeq; XP_005259774.1; XM_005259717.1.
DR UniGene; Hs.78880; -.
DR ProteinModelPortal; A1L0T0; -.
DR SMR; A1L0T0; 54-620.
DR IntAct; A1L0T0; 8.
DR MINT; MINT-1417151; -.
DR STRING; 9606.ENSP00000263383; -.
DR PhosphoSite; A1L0T0; -.
DR PaxDb; A1L0T0; -.
DR PeptideAtlas; A1L0T0; -.
DR PRIDE; A1L0T0; -.
DR DNASU; 10994; -.
DR Ensembl; ENST00000263383; ENSP00000263383; ENSG00000105135.
DR GeneID; 10994; -.
DR KEGG; hsa:10994; -.
DR UCSC; uc002nam.3; human.
DR CTD; 10994; -.
DR GeneCards; GC19M015225; -.
DR HGNC; HGNC:6041; ILVBL.
DR MIM; 605770; gene.
DR neXtProt; NX_A1L0T0; -.
DR PharmGKB; PA29857; -.
DR eggNOG; COG0028; -.
DR HOGENOM; HOG000010642; -.
DR HOVERGEN; HBG108004; -.
DR InParanoid; A1L0T0; -.
DR KO; K11259; -.
DR OMA; FMVQKEM; -.
DR OrthoDB; EOG75B84X; -.
DR PhylomeDB; A1L0T0; -.
DR GenomeRNAi; 10994; -.
DR NextBio; 41779; -.
DR PRO; PR:A1L0T0; -.
DR ArrayExpress; A1L0T0; -.
DR Bgee; A1L0T0; -.
DR CleanEx; HS_ILVBL; -.
DR Genevestigator; A1L0T0; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:GOC.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Magnesium; Membrane; Metal-binding; Polymorphism;
KW Reference proteome; Thiamine pyrophosphate; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 632 Acetolactate synthase-like protein.
FT /FTId=PRO_0000314825.
FT TRANSMEM 13 33 Helical; (Potential).
FT REGION 470 550 Thiamine pyrophosphate binding (By
FT similarity).
FT METAL 521 521 Magnesium (By similarity).
FT METAL 547 547 Magnesium (By similarity).
FT BINDING 98 98 Thiamine pyrophosphate (By similarity).
FT VARIANT 374 374 N -> D (in dbSNP:rs17856373).
FT /FTId=VAR_038064.
FT VARIANT 510 510 R -> Q (in dbSNP:rs35548653).
FT /FTId=VAR_061901.
SQ SEQUENCE 632 AA; 67868 MW; 893F539FC5F1B2EC CRC64;
METPAAAAPA GSLFPSFLLL ACGTLVAALL GAAHRLGLFY QLLHKVDKAS VRHGGENVAA
VLRAHGVRFI FTLVGGHISP LLVACEKLGI RVVDTRHEVT AVFAADAMAR LSGTVGVAAV
TAGPGLTNTV TAVKNAQMAQ SPILLLGGAA STLLQNRGAL QAVDQLSLFR PLCKFCVSVR
RVRDIVPTLR AAMAAAQSGT PGPVFVELPV DVLYPYFMVQ KEMVPAKPPK GLVGRVVSWY
LENYLANLFA GAWEPQPEGP LPLDIPQASP QQVQRCVEIL SRAKRPLMVL GSQALLTPTS
ADKLRAAVET LGVPCFLGGM ARGLLGRNHP LHIRENRSAA LKKADVIVLA GTVCDFRLSY
GRVLSHSSKI IIVNRNREEM LLNSDIFWKP QEAVQGDVGS FVLKLVEGLQ GQTWAPDWVE
ELREADRQKE QTFREKAAMP VAQHLNPVQV LQLVEETLPD NSILVVDGGD FVGTAAHLVQ
PRGPLRWLDP GAFGTLGVGA GFALGAKLCR PDAEVWCLFG DGAFGYSLIE FDTFVRHKIP
VMALVGNDAG WTQISREQVP SLGSNVACGL AYTDYHKAAM GLGARGLLLS RENEDQVVKV
LHDAQQQCRD GHPVVVNILI GRTDFRDGSI AV
//
MIM
605770
*RECORD*
*FIELD* NO
605770
*FIELD* TI
*605770 ILVB-LIKE; ILVBL
;;ACETOLACTATE SYNTHASE, BACTERIAL, HOMOLOG OF; AHAS
*FIELD* TX
read moreUsing a fragment isolated from a cosmid containing D19S841 at 19p13.1 to
screen a human fetal brain cDNA library, Joutel et al. (1996) cloned a
novel cDNA, which they called 209L8, encoding a deduced 632-amino acid
protein that shows high homology with several bacterial, plant, and
yeast enzymes that have in common the use of thiamine pyrophosphate as a
cofactor. The highest degree of similarity was found with 2 bacterial
enzymes, the B isozyme of the large catalytic subunit of E. coli
acetohydroxy-acid synthase (AHAS) and the oxalyl-coA decarboxylase of O.
formigenes. Northern blot analysis detected an abundant 2.4-kb
transcript in all tissues tested, with highest expression in heart,
pancreas, and placenta.
Joutel et al. (1996) found that the ILVBL gene contains 15 coding exons.
They excluded the gene as a candidate for CADASIL (125310), which had
been mapped to the same region of chromosome 19.
*FIELD* RF
1. Joutel, A.; Ducros, A.; Alamowitch, S.; Cruaud, C.; Domenga, V.;
Marechal, E.; Vahedi, K.; Chabriat, H.; Bousser, M. G.; Tournier-Lasserve,
E.: A human homolog of bacterial acetolactate synthase genes maps
within the CADASIL critical region. Genomics 38: 192-198, 1996.
*FIELD* CD
Carol A. Bocchini: 3/26/2001
*FIELD* ED
mcapotos: 03/26/2001
carol: 3/26/2001
*RECORD*
*FIELD* NO
605770
*FIELD* TI
*605770 ILVB-LIKE; ILVBL
;;ACETOLACTATE SYNTHASE, BACTERIAL, HOMOLOG OF; AHAS
*FIELD* TX
read moreUsing a fragment isolated from a cosmid containing D19S841 at 19p13.1 to
screen a human fetal brain cDNA library, Joutel et al. (1996) cloned a
novel cDNA, which they called 209L8, encoding a deduced 632-amino acid
protein that shows high homology with several bacterial, plant, and
yeast enzymes that have in common the use of thiamine pyrophosphate as a
cofactor. The highest degree of similarity was found with 2 bacterial
enzymes, the B isozyme of the large catalytic subunit of E. coli
acetohydroxy-acid synthase (AHAS) and the oxalyl-coA decarboxylase of O.
formigenes. Northern blot analysis detected an abundant 2.4-kb
transcript in all tissues tested, with highest expression in heart,
pancreas, and placenta.
Joutel et al. (1996) found that the ILVBL gene contains 15 coding exons.
They excluded the gene as a candidate for CADASIL (125310), which had
been mapped to the same region of chromosome 19.
*FIELD* RF
1. Joutel, A.; Ducros, A.; Alamowitch, S.; Cruaud, C.; Domenga, V.;
Marechal, E.; Vahedi, K.; Chabriat, H.; Bousser, M. G.; Tournier-Lasserve,
E.: A human homolog of bacterial acetolactate synthase genes maps
within the CADASIL critical region. Genomics 38: 192-198, 1996.
*FIELD* CD
Carol A. Bocchini: 3/26/2001
*FIELD* ED
mcapotos: 03/26/2001
carol: 3/26/2001