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Protein

Glycosyltransferase-like protein LARGE1

Gene

LARGE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional glycosyltransferase with both xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1) (PubMed:22223806). Phosphorylated O-mannosyl trisaccharid is required for binding laminin G-like domain-containing extracellular proteins with high affinity and plays a key role in skeletal muscle function and regeneration. LARGE elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure initiated by B3GNT1/B4GAT1 by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide (PubMed:25279699).7 Publications

Cofactori

Mn2+1 PublicationNote: Binds 2 Mn(2+) ions per subunit. The xylosyltransferase part binds one Mn(2+) and the beta-1,3-glucuronyltransferase part binds one Mn2+.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi242 – 2421Manganese 1Curated
Metal bindingi244 – 2441Manganese 1Curated
Metal bindingi563 – 5631Manganese 2Curated
Metal bindingi565 – 5651Manganese 2Curated

GO - Molecular functioni

  • acetylglucosaminyltransferase activity Source: ProtInc
  • glucuronosyltransferase activity Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • transferase activity, transferring glycosyl groups Source: UniProtKB
  • xylosyltransferase activity Source: UniProtKB

GO - Biological processi

  • glycoprotein biosynthetic process Source: UniProtKB
  • glycosphingolipid biosynthetic process Source: UniProtKB
  • muscle cell cellular homeostasis Source: UniProtKB
  • N-acetylglucosamine metabolic process Source: ProtInc
  • protein glycosylation Source: ProtInc
  • protein O-linked mannosylation Source: UniProtKB
  • skeletal muscle organ development Source: UniProtKB
  • skeletal muscle tissue regeneration Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT49. Glycosyltransferase Family 49.
GT8. Glycosyltransferase Family 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycosyltransferase-like protein LARGE1 (EC:2.4.-.-)
Alternative name(s):
Acetylglucosaminyltransferase-like 1A
Including the following 2 domains:
Xylosyltransferase LARGECurated (EC:2.4.2.-1 Publication)
Beta-1,3-glucuronyltransferase LARGECurated (EC:2.4.1.-3 Publications)
Gene namesi
Name:LARGE
Synonyms:KIAA0609, LARGE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:6511. LARGE.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010CytoplasmicSequence Analysis
Transmembranei11 – 3121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini32 – 756725LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • Golgi apparatus Source: UniProtKB
  • integral component of Golgi membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Muscular dystrophy-dystroglycanopathy congenital with mental retardation B6 (MDDGB6)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA congenital muscular dystrophy associated with profound mental retardation, white matter changes and structural brain abnormalities. Skeletal muscle biopsies show reduced immunolabeling of alpha-dystroglycan.

See also OMIM:608840
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti509 – 5091E → K in MDDGB6. 1 Publication
VAR_019811
Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A6 (MDDGA6)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound mental retardation, and death usually in the first years of life. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease.

See also OMIM:613154
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti331 – 3311S → F in MDDGA6. 1 Publication
VAR_065064
Natural varianti495 – 4951W → R in MDDGA6. 1 Publication
VAR_065065

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi242 – 2443DTD → NNN: Loss of function, but does not abolish subcellular location. 1 Publication
Mutagenesisi242 – 2443DTD → NTN: Glucuronyltransferase activity is present while xylosyltransferase activity is abolished. 1 Publication
Mutagenesisi334 – 3363DQD → NNN: Loss of function, but does not abolish subcellular location. 1 Publication
Mutagenesisi563 – 5653DID → NIN: Xylosyltransferase activity is present while glucuronyltransferase activity is abolished. 1 Publication
Mutagenesisi563 – 5653DID → NNN: Loss of function and abolishes subcellular location. 1 Publication

Keywords - Diseasei

Congenital muscular dystrophy, Disease mutation, Dystroglycanopathy, Lissencephaly

Organism-specific databases

MIMi608840. phenotype.
613154. phenotype.
Orphaneti370968. Congenital muscular dystrophy with intellectual disability.
588. Muscle-eye-brain disease.
899. Walker-Warburg syndrome.
PharmGKBiPA30296.

Polymorphism and mutation databases

BioMutaiLARGE.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 756756Glycosyltransferase-like protein LARGE1PRO_0000206060Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi122 – 1221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi272 – 2721N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiO95461.
PRIDEiO95461.

PTM databases

PhosphoSiteiO95461.

Expressioni

Tissue specificityi

Ubiquitous. Highest expression in heart, brain and skeletal muscle.1 Publication

Gene expression databases

BgeeiO95461.
CleanExiHS_LARGE.
ExpressionAtlasiO95461. baseline and differential.
GenevestigatoriO95461.

Organism-specific databases

HPAiHPA028878.

Interactioni

Subunit structurei

Interacts with DAG1 (via the N-terminal domain of alpha-DAG1); the interaction increases binding of DAG1 to laminin (By similarity). Interacts with B3GNT1/B4GAT1 (PubMed:19587235).By similarity1 Publication

Protein-protein interaction databases

BioGridi114649. 2 interactions.
DIPiDIP-48922N.
STRINGi9606.ENSP00000347088.

Structurei

3D structure databases

ProteinModelPortaliO95461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni138 – 413276Xylosyltransferase activity1 PublicationAdd
BLAST
Regioni414 – 756343Glucuronyltransferase activity1 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili53 – 9543Sequence AnalysisAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the glycosyltransferase 49 family.Curated
In the N-terminal section; belongs to the glycosyltransferase 8 family.Curated

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG279004.
GeneTreeiENSGT00530000063165.
HOVERGENiHBG052308.
InParanoidiO95461.
KOiK09668.
OMAiFAALKYM.
OrthoDBiEOG7RJPQV.
PhylomeDBiO95461.
TreeFamiTF319168.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01501. Glyco_transf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95461-1) [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
MLGICRGRRK FLAASLSLLC IPAITWIYLF SGSFEDGKPV SLSPLESQAH
60 70 80 90 100
SPRYTASSQR ERESLEVRMR EVEEENRALR RQLSLAQGRA PSHRRGNHSK
110 120 130 140 150
TYSMEEGTGD SENLRAGIVA GNSSECGQQP VVEKCETIHV AIVCAGYNAS
160 170 180 190 200
RDVVTLVKSV LFHRRNPLHF HLIADSIAEQ ILATLFQTWM VPAVRVDFYN
210 220 230 240 250
ADELKSEVSW IPNKHYSGIY GLMKLVLTKT LPANLERVIV LDTDITFATD
260 270 280 290 300
IAELWAVFHK FKGQQVLGLV ENQSDWYLGN LWKNHRPWPA LGRGYNTGVI
310 320 330 340 350
LLLLDKLRKM KWEQMWRLTA ERELMGMLST SLADQDIFNA VIKQNPFLVY
360 370 380 390 400
QLPCFWNVQL SDHTRSEQCY RDVSDLKVIH WNSPKKLRVK NKHVEFFRNL
410 420 430 440 450
YLTFLEYDGN LLRRELFGCP SEADVNSENL QKQLSELDED DLCYEFRRER
460 470 480 490 500
FTVHRTHLYF LHYEYEPAAD STDVTLVAQL SMDRLQMLEA ICKHWEGPIS
510 520 530 540 550
LALYLSDAEA QQFLRYAQGS EVLMSRHNVG YHIVYKEGQF YPVNLLRNVA
560 570 580 590 600
MKHISTPYMF LSDIDFLPMY GLYEYLRKSV IQLDLANTKK AMIVPAFETL
610 620 630 640 650
RYRLSFPKSK AELLSMLDMG TLFTFRYHVW TKGHAPTNFA KWRTATTPYR
660 670 680 690 700
VEWEADFEPY VVVRRDCPEY DRRFVGFGWN KVAHIMELDV QEYEFIVLPN
710 720 730 740 750
AYMIHMPHAP SFDITKFRSN KQYRICLKTL KEEFQQDMSR RYGFAALKYL

TAENNS
Length:756
Mass (Da):88,066
Last modified:May 1, 1999 - v1
Checksum:iB022E118379AA17C
GO
Isoform 2 (identifier: O95461-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     378-429: Missing.

Note: No experimental confirmation available.

Show »
Length:704
Mass (Da):81,846
Checksum:i9CCD42064004C7FF
GO

Sequence cautioni

The sequence BAA25535.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681R → G.
Corresponds to variant rs470035 [ dbSNP | Ensembl ].
VAR_013685
Natural varianti68 – 681R → P.
Corresponds to variant rs135311 [ dbSNP | Ensembl ].
VAR_013686
Natural varianti331 – 3311S → F in MDDGA6. 1 Publication
VAR_065064
Natural varianti495 – 4951W → R in MDDGA6. 1 Publication
VAR_065065
Natural varianti509 – 5091E → K in MDDGB6. 1 Publication
VAR_019811
Natural varianti665 – 6651R → H.
Corresponds to variant rs1046166 [ dbSNP | Ensembl ].
VAR_013687

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei378 – 42952Missing in isoform 2. 1 PublicationVSP_014536Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007583 mRNA. Translation: CAA07571.1.
AB011181 mRNA. Translation: BAA25535.3. Different initiation.
CR456510 mRNA. Translation: CAG30396.1.
AL008630
, AL008715, AL096754, Z68287, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAI17950.1.
AL008715
, AL008630, AL096754, Z68287, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAI17890.1.
AL096754
, AL008630, AL008715, Z68287, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAI18784.1.
Z68287
, AL008630, AL008715, AL096754, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAI18785.1.
Z69042
, AL008630, AL008715, AL096754, Z68287, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAI18772.1.
Z69943
, AL008630, AL008715, AL096754, Z68287, Z69042, Z70288, Z82173 Genomic DNA. Translation: CAI18788.1.
Z70288
, AL008630, AL008715, AL096754, Z68287, Z69042, Z69943, Z82173 Genomic DNA. Translation: CAI18769.1.
Z82173
, AL008630, AL008715, AL096754, Z68287, Z69042, Z69943, Z70288 Genomic DNA. Translation: CAI18754.1.
Z69943
, AL008630, AL008715, AL096754, Z68287, Z69042, Z70288, Z82173 Genomic DNA. Translation: CAQ06856.1.
AL096754
, AL008630, AL008715, Z68287, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAQ08281.1.
Z68287
, AL008630, AL008715, AL096754, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAQ08801.1.
AL008630
, AL008715, AL096754, Z68287, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAQ09323.1.
AL008715
, AL008630, AL096754, Z68287, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAQ09434.1.
Z82173
, AL008630, AL008715, AL096754, Z68287, Z69042, Z69943, Z70288 Genomic DNA. Translation: CAQ09895.1.
Z69042
, AL008630, AL008715, AL096754, Z68287, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAQ10763.1.
Z70288
, AL008630, AL008715, AL096754, Z68287, Z69042, Z69943, Z82173 Genomic DNA. Translation: CAQ11002.1.
BC117425 mRNA. Translation: AAI17426.1.
BC126404 mRNA. Translation: AAI26405.1.
CCDSiCCDS13912.1. [O95461-1]
PIRiT00256.
RefSeqiNP_004728.1. NM_004737.4. [O95461-1]
NP_598397.1. NM_133642.3. [O95461-1]
XP_005261888.1. XM_005261831.2. [O95461-1]
XP_005261889.1. XM_005261832.2. [O95461-1]
UniGeneiHs.474667.

Genome annotation databases

EnsembliENST00000354992; ENSP00000347088; ENSG00000133424. [O95461-1]
ENST00000397394; ENSP00000380549; ENSG00000133424. [O95461-1]
ENST00000402320; ENSP00000385223; ENSG00000133424. [O95461-2]
GeneIDi9215.
KEGGihsa:9215.
UCSCiuc003and.4. human. [O95461-1]
uc010gwp.3. human. [O95461-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Glycosyltransferase-like protein LARGE1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007583 mRNA. Translation: CAA07571.1.
AB011181 mRNA. Translation: BAA25535.3. Different initiation.
CR456510 mRNA. Translation: CAG30396.1.
AL008630
, AL008715, AL096754, Z68287, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAI17950.1.
AL008715
, AL008630, AL096754, Z68287, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAI17890.1.
AL096754
, AL008630, AL008715, Z68287, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAI18784.1.
Z68287
, AL008630, AL008715, AL096754, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAI18785.1.
Z69042
, AL008630, AL008715, AL096754, Z68287, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAI18772.1.
Z69943
, AL008630, AL008715, AL096754, Z68287, Z69042, Z70288, Z82173 Genomic DNA. Translation: CAI18788.1.
Z70288
, AL008630, AL008715, AL096754, Z68287, Z69042, Z69943, Z82173 Genomic DNA. Translation: CAI18769.1.
Z82173
, AL008630, AL008715, AL096754, Z68287, Z69042, Z69943, Z70288 Genomic DNA. Translation: CAI18754.1.
Z69943
, AL008630, AL008715, AL096754, Z68287, Z69042, Z70288, Z82173 Genomic DNA. Translation: CAQ06856.1.
AL096754
, AL008630, AL008715, Z68287, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAQ08281.1.
Z68287
, AL008630, AL008715, AL096754, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAQ08801.1.
AL008630
, AL008715, AL096754, Z68287, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAQ09323.1.
AL008715
, AL008630, AL096754, Z68287, Z69042, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAQ09434.1.
Z82173
, AL008630, AL008715, AL096754, Z68287, Z69042, Z69943, Z70288 Genomic DNA. Translation: CAQ09895.1.
Z69042
, AL008630, AL008715, AL096754, Z68287, Z69943, Z70288, Z82173 Genomic DNA. Translation: CAQ10763.1.
Z70288
, AL008630, AL008715, AL096754, Z68287, Z69042, Z69943, Z82173 Genomic DNA. Translation: CAQ11002.1.
BC117425 mRNA. Translation: AAI17426.1.
BC126404 mRNA. Translation: AAI26405.1.
CCDSiCCDS13912.1. [O95461-1]
PIRiT00256.
RefSeqiNP_004728.1. NM_004737.4. [O95461-1]
NP_598397.1. NM_133642.3. [O95461-1]
XP_005261888.1. XM_005261831.2. [O95461-1]
XP_005261889.1. XM_005261832.2. [O95461-1]
UniGeneiHs.474667.

3D structure databases

ProteinModelPortaliO95461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114649. 2 interactions.
DIPiDIP-48922N.
STRINGi9606.ENSP00000347088.

Chemistry

BindingDBiO95461.
ChEMBLiCHEMBL2146300.

Protein family/group databases

CAZyiGT49. Glycosyltransferase Family 49.
GT8. Glycosyltransferase Family 8.

PTM databases

PhosphoSiteiO95461.

Polymorphism and mutation databases

BioMutaiLARGE.

Proteomic databases

PaxDbiO95461.
PRIDEiO95461.

Protocols and materials databases

DNASUi9215.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354992; ENSP00000347088; ENSG00000133424. [O95461-1]
ENST00000397394; ENSP00000380549; ENSG00000133424. [O95461-1]
ENST00000402320; ENSP00000385223; ENSG00000133424. [O95461-2]
GeneIDi9215.
KEGGihsa:9215.
UCSCiuc003and.4. human. [O95461-1]
uc010gwp.3. human. [O95461-2]

Organism-specific databases

CTDi9215.
GeneCardsiGC22M033561.
GeneReviewsiLARGE.
HGNCiHGNC:6511. LARGE.
HPAiHPA028878.
MIMi603590. gene.
608840. phenotype.
613154. phenotype.
neXtProtiNX_O95461.
Orphaneti370968. Congenital muscular dystrophy with intellectual disability.
588. Muscle-eye-brain disease.
899. Walker-Warburg syndrome.
PharmGKBiPA30296.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG279004.
GeneTreeiENSGT00530000063165.
HOVERGENiHBG052308.
InParanoidiO95461.
KOiK09668.
OMAiFAALKYM.
OrthoDBiEOG7RJPQV.
PhylomeDBiO95461.
TreeFamiTF319168.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

ChiTaRSiLARGE. human.
GeneWikiiLARGE.
GenomeRNAii9215.
NextBioi34547.
PROiO95461.
SOURCEiSearch...

Gene expression databases

BgeeiO95461.
CleanExiHS_LARGE.
ExpressionAtlasiO95461. baseline and differential.
GenevestigatoriO95461.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01501. Glyco_transf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human LARGE gene from 22q12.3-q13.1 is a new, distinct member of the glycosyltransferase gene family."
    Peyrard M., Seroussi E., Sandberg-Nordqvist A.-C., Xie Y.-G., Han F.-Y., Fransson I., Collins J.E., Dunham I., Kost-Alimova M., Imreh S., Dumanski J.P.
    Proc. Natl. Acad. Sci. U.S.A. 96:598-603(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Lung.
  6. "LARGE2 facilitates the maturation of alpha-dystroglycan more effectively than LARGE."
    Fujimura K., Sawaki H., Sakai T., Hiruma T., Nakanishi N., Sato T., Ohkura T., Narimatsu H.
    Biochem. Biophys. Res. Commun. 329:1162-1171(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  7. "Characterization of the LARGE family of putative glycosyltransferases associated with dystroglycanopathies."
    Grewal P.K., McLaughlan J.M., Moore C.J., Browning C.A., Hewitt J.E.
    Glycobiology 15:912-923(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Localization and functional analysis of the LARGE family of glycosyltransferases: significance for muscular dystrophy."
    Brockington M., Torelli S., Prandini P., Boito C., Dolatshad N.F., Longman C., Brown S.C., Muntoni F.
    Hum. Mol. Genet. 14:657-665(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 242-GLY--GLY-244; 334-GLY--GLY-336 AND 563-GLY--GLY-565.
  9. "Tumor suppressor function of laminin-binding alpha-dystroglycan requires a distinct beta3-N-acetylglucosaminyltransferase."
    Bao X., Kobayashi M., Hatakeyama S., Angata K., Gullberg D., Nakayama J., Fukuda M.N., Fukuda M.
    Proc. Natl. Acad. Sci. U.S.A. 106:12109-12114(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH B3GNT1.
  10. "Like-acetylglucosaminyltransferase (LARGE)-dependent modification of dystroglycan at Thr-317/319 is required for laminin binding and arenavirus infection."
    Hara Y., Kanagawa M., Kunz S., Yoshida-Moriguchi T., Satz J.S., Kobayashi Y.M., Zhu Z., Burden S.J., Oldstone M.B., Campbell K.P.
    Proc. Natl. Acad. Sci. U.S.A. 108:17426-17431(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Dystroglycan function requires xylosyl- and glucuronyltransferase activities of LARGE."
    Inamori K., Yoshida-Moriguchi T., Hara Y., Anderson M.E., Yu L., Campbell K.P.
    Science 335:93-96(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 242-ASP--ASP-244 AND 563-ASP--ASP-565.
  12. "The glucuronyltransferase B4GAT1 is required for initiation of LARGE-mediated alpha-dystroglycan functional glycosylation."
    Willer T., Inamori K.I., Venzke D., Harvey C., Morgensen G., Hara Y., Beltran Valero de Bernabe D., Yu L., Wright K.M., Campbell K.P.
    Elife 3:0-0(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PATHWAY.
  13. "B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of alpha-dystroglycan."
    Praissman J.L., Live D.H., Wang S., Ramiah A., Chinoy Z.S., Boons G.J., Moremen K.W., Wells L.
    Elife 3:0-0(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY.
  14. "Endogenous glucuronyltransferase activity of LARGE or LARGE2 required for functional modification of alpha-dystroglycan in cells and tissues."
    Inamori K., Willer T., Hara Y., Venzke D., Anderson M.E., Clarke N.F., Guicheney P., Bonnemann C.G., Moore S.A., Campbell K.P.
    J. Biol. Chem. 289:28138-28148(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR.
  15. "Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan."
    Longman C., Brockington M., Torelli S., Jimenez-Mallebrera C., Kennedy C., Khalil N., Feng L., Saran R.K., Voit T., Merlini L., Sewry C.A., Brown S.C., Muntoni F.
    Hum. Mol. Genet. 12:2853-2861(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MDDGB6 LYS-509.
  16. Cited for: VARIANT MDDGA6 PHE-331.
  17. Cited for: VARIANT MDDGA6 ARG-495.

Entry informationi

Entry nameiLARGE_HUMAN
AccessioniPrimary (citable) accession number: O95461
Secondary accession number(s): B0QXZ7
, O60348, Q17R80, Q9UGD1, Q9UGE7, Q9UGG3, Q9UGZ8, Q9UH22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: May 1, 1999
Last modified: May 27, 2015
This is version 131 of the entry and version 1 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, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.