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A1L0T0 (ILVBL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 69. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetolactate synthase-like protein

EC=2.2.1.-
Alternative name(s):
IlvB-like protein
Gene names
Name:ILVBL
Synonyms:AHAS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length632 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Binds 1 thiamine pyrophosphate per subunit By similarity.

Subcellular location

Membrane; Single-pass membrane protein.

Tissue specificity

Expressed in all tissues tested, with highest expression in heart, pancreas and placenta. Ref.1

Sequence similarities

Belongs to the TPP enzyme family.

Sequence caution

The sequence AAC18916.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAH00109.1 differs from that shown. Reason: Aberrant splicing.

The sequence AAI26914.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAI26914.1 differs from that shown. Reason: Sequence of unknown origin at the C-terminus.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   LigandMagnesium
Metal-binding
Thiamine pyrophosphate
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

thiamine pyrophosphate binding

Inferred from electronic annotation. Source: InterPro

transferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 632632Acetolactate synthase-like protein
PRO_0000314825

Regions

Transmembrane13 – 3321Helical; Potential
Region470 – 55081Thiamine pyrophosphate binding By similarity

Sites

Metal binding5211Magnesium By similarity
Metal binding5471Magnesium By similarity
Binding site981Thiamine pyrophosphate By similarity

Natural variations

Natural variant3741N → D. Ref.4
Corresponds to variant rs17856373 [ dbSNP | Ensembl ].
VAR_038064
Natural variant5101R → Q.
Corresponds to variant rs35548653 [ dbSNP | Ensembl ].
VAR_061901

Sequences

Sequence LengthMass (Da)Tools
A1L0T0 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 893F539FC5F1B2EC

FASTA63267,868
        10         20         30         40         50         60 
METPAAAAPA GSLFPSFLLL ACGTLVAALL GAAHRLGLFY QLLHKVDKAS VRHGGENVAA 

        70         80         90        100        110        120 
VLRAHGVRFI FTLVGGHISP LLVACEKLGI RVVDTRHEVT AVFAADAMAR LSGTVGVAAV 

       130        140        150        160        170        180 
TAGPGLTNTV TAVKNAQMAQ SPILLLGGAA STLLQNRGAL QAVDQLSLFR PLCKFCVSVR 

       190        200        210        220        230        240 
RVRDIVPTLR AAMAAAQSGT PGPVFVELPV DVLYPYFMVQ KEMVPAKPPK GLVGRVVSWY 

       250        260        270        280        290        300 
LENYLANLFA GAWEPQPEGP LPLDIPQASP QQVQRCVEIL SRAKRPLMVL GSQALLTPTS 

       310        320        330        340        350        360 
ADKLRAAVET LGVPCFLGGM ARGLLGRNHP LHIRENRSAA LKKADVIVLA GTVCDFRLSY 

       370        380        390        400        410        420 
GRVLSHSSKI IIVNRNREEM LLNSDIFWKP QEAVQGDVGS FVLKLVEGLQ GQTWAPDWVE 

       430        440        450        460        470        480 
ELREADRQKE QTFREKAAMP VAQHLNPVQV LQLVEETLPD NSILVVDGGD FVGTAAHLVQ 

       490        500        510        520        530        540 
PRGPLRWLDP GAFGTLGVGA GFALGAKLCR PDAEVWCLFG DGAFGYSLIE FDTFVRHKIP 

       550        560        570        580        590        600 
VMALVGNDAG WTQISREQVP SLGSNVACGL AYTDYHKAAM GLGARGLLLS RENEDQVVKV 

       610        620        630 
LHDAQQQCRD GHPVVVNILI GRTDFRDGSI AV 

« Hide

References

« Hide 'large scale' references
[1]"A human homolog of bacterial acetolactate synthase genes maps within the CADASIL critical region."
Joutel A., Ducros A., Alamowitch S., Cruaud C., Domenga V., Marechal E., Vahedi K., Chabriat H., Bousser M.G., Tournier-Lasserve E.
Genomics 38:192-198(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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], VARIANT ASP-374.
Tissue: Pancreas and Placenta.
[5]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U61263 mRNA. Translation: AAC50934.1.
AC003956 Genomic DNA. Translation: AAB94632.1.
AC004794 Genomic DNA. Translation: AAC18916.1. Sequence problems.
CH471106 Genomic DNA. Translation: EAW84464.1.
BC000109 mRNA. Translation: AAH00109.1. Sequence problems.
BC011722 mRNA. Translation: AAH11722.1.
BC011761 mRNA. Translation: AAH11761.1.
BC126913 mRNA. Translation: AAI26914.1. Sequence problems.
CCDSCCDS12325.1.
RefSeqNP_006835.2. NM_006844.4.
XP_005259774.1. XM_005259717.2.
UniGeneHs.78880.

3D structure databases

ProteinModelPortalA1L0T0.
SMRA1L0T0. Positions 54-586.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116190. 20 interactions.
IntActA1L0T0. 8 interactions.
MINTMINT-1417151.
STRING9606.ENSP00000263383.

PTM databases

PhosphoSiteA1L0T0.

Proteomic databases

MaxQBA1L0T0.
PaxDbA1L0T0.
PeptideAtlasA1L0T0.
PRIDEA1L0T0.

Protocols and materials databases

DNASU10994.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263383; ENSP00000263383; ENSG00000105135.
GeneID10994.
KEGGhsa:10994.
UCSCuc002nam.3. human.

Organism-specific databases

CTD10994.
GeneCardsGC19M015225.
HGNCHGNC:6041. ILVBL.
MIM605770. gene.
neXtProtNX_A1L0T0.
PharmGKBPA29857.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0028.
HOGENOMHOG000010642.
HOVERGENHBG108004.
InParanoidA1L0T0.
KOK11259.
OMAHETNFAG.
OrthoDBEOG75B84X.
PhylomeDBA1L0T0.
TreeFamTF354221.

Gene expression databases

ArrayExpressA1L0T0.
BgeeA1L0T0.
CleanExHS_ILVBL.
GenevestigatorA1L0T0.

Family and domain databases

Gene3D3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMSSF52467. SSF52467. 2 hits.
SSF52518. SSF52518. 2 hits.
PROSITEPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi10994.
NextBio41779.
PROA1L0T0.
SOURCESearch...

Entry information

Entry nameILVBL_HUMAN
AccessionPrimary (citable) accession number: A1L0T0
Secondary accession number(s): O43341 expand/collapse secondary AC list , Q96F08, Q99651, Q9BWN5, Q9UEB2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: July 9, 2014
This is version 69 of the entry and version 2 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 19

Human chromosome 19: entries, gene names and cross-references to MIM