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Q9BT22 (ALG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chitobiosyldiphosphodolichol beta-mannosyltransferase

EC=2.4.1.142
Alternative name(s):
Asparagine-linked glycosylation protein 1 homolog
Beta-1,4-mannosyltransferase
GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase
GDP-mannose-dolichol diphosphochitobiose mannosyltransferase
Mannosyltransferase-1
Short name=MT-1
Short name=hMat-1
Gene names
Name:ALG1
Synonyms:HMAT1, HMT1
ORF Names:PSEC0061, UNQ861/PRO1870
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man5 intermediate on the cytoplasmic surface of the ER. Ref.1

Catalytic activity

GDP-mannose + chitobiosyldiphosphodolichol = GDP + beta-1,4-D-mannosylchitobiosyldiphosphodolichol.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein Probable.

Involvement in disease

Congenital disorder of glycosylation 1K (CDG1K) [MIM:608540]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.9

Sequence similarities

Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 33 subfamily.

Sequence caution

The sequence AAQ89432.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Chitobiosyldiphosphodolichol beta-mannosyltransferase
PRO_0000080249

Regions

Topological domain1 – 22Cytoplasmic Potential
Transmembrane3 – 2321Helical; Signal-anchor for type II membrane protein; Potential
Topological domain24 – 464441Lumenal Potential

Amino acid modifications

Modified residue2421Phosphoserine Ref.5

Natural variations

Natural variant1501S → R in CDG1K; impairs activity. Ref.9
Corresponds to variant rs121908340 [ dbSNP | Ensembl ].
VAR_023364
Natural variant2581S → L in CDG1K; impairs activity. Ref.7 Ref.8 Ref.9
Corresponds to variant rs28939378 [ dbSNP | Ensembl ].
VAR_023365
Natural variant2671S → N. Ref.3
Corresponds to variant rs17849848 [ dbSNP | Ensembl ].
VAR_038425
Natural variant3251L → M. Ref.3
Corresponds to variant rs17852920 [ dbSNP | Ensembl ].
VAR_038426
Natural variant3421Q → P in CDG1K; impairs activity. Ref.8
VAR_023366
Natural variant4291D → E No effect on activity. Ref.9
Corresponds to variant rs9745522 [ dbSNP | Ensembl ].
VAR_023367
Natural variant4381R → W.
Corresponds to variant rs16835020 [ dbSNP | Ensembl ].
VAR_049350
Natural variant4551Q → R. Ref.3
Corresponds to variant rs17856919 [ dbSNP | Ensembl ].
VAR_038427

Sequences

Sequence LengthMass (Da)Tools
Q9BT22 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 83F55FD12CFDDBE9

FASTA46452,518
        10         20         30         40         50         60 
MAASCLVLLA LCLLLPLLLL GGWKRWRRGR AARHVVAVVL GDVGRSPRMQ YHALSLAMHG 

        70         80         90        100        110        120 
FSVTLLGFCN SKPHDELLQN NRIQIVGLTE LQSLAVGPRV FQYGVKVVLQ AMYLLWKLMW 

       130        140        150        160        170        180 
REPGAYIFLQ NPPGLPSIAV CWFVGCLCGS KLVIDWHNYG YSIMGLVHGP NHPLVLLAKW 

       190        200        210        220        230        240 
YEKFFGRLSH LNLCVTNAMR EDLADNWHIR AVTVYDKPAS FFKETPLDLQ HRLFMKLGSM 

       250        260        270        280        290        300 
HSPFRARSEP EDPVTERSAF TERDAGSGLV TRLRERPALL VSSTSWTEDE DFSILLAALE 

       310        320        330        340        350        360 
KFEQLTLDGH NLPSLVCVIT GKGPLREYYS RLIHQKHFQH IQVCTPWLEA EDYPLLLGSA 

       370        380        390        400        410        420 
DLGVCLHTSS SGLDLPMKVV DMFGCCLPVC AVNFKCLHEL VKHEENGLVF EDSEELAAQL 

       430        440        450        460 
QMLFSNFPDP AGKLNQFRKN LRESQQLRWD ESWVQTVLPL VMDT 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1."
Takahashi T., Honda R., Nishikawa Y.
Glycobiology 10:321-327(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Fetal brain.
[2]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Teratocarcinoma.
[3]"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], VARIANTS ASN-267; MET-325 AND ARG-455.
Tissue: Brain.
[4]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-464.
[5]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"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].
[7]"Deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase causes congenital disorder of glycosylation type Ik."
Schwarz M., Thiel C., Luebbehusen J., Dorland B., de Koning T., von Figura K., Lehle L., Koerner C.
Am. J. Hum. Genet. 74:472-481(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CDG1K LEU-258.
[8]"Congenital disorder of glycosylation type Ik (CDG-Ik): a defect of mannosyltransferase I."
Kranz C., Denecke J., Lehle L., Sohlbach K., Jeske S., Meinhardt F., Rossi R., Gudowius S., Marquardt T.
Am. J. Hum. Genet. 74:545-551(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CDG1K LEU-258 AND PRO-342.
[9]"Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik."
Grubenmann C.E., Frank C.G., Huelsmeier A.J., Schollen E., Matthijs G., Mayatepek E., Berger E.G., Aebi M., Hennet T.
Hum. Mol. Genet. 13:535-542(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CDG1K ARG-150 AND LEU-258, VARIANT GLU-429.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB019038 mRNA. Translation: BAA90748.1.
AK075373 mRNA. Translation: BAC11576.1.
BC004402 mRNA. Translation: AAH04402.1.
BC031095 mRNA. Translation: AAH31095.1.
AY359073 mRNA. Translation: AAQ89432.1. Different initiation.
CCDSCCDS10528.1.
RefSeqNP_061982.3. NM_019109.4.
UniGeneHs.592086.

3D structure databases

ProteinModelPortalQ9BT22.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121033. 4 interactions.
IntActQ9BT22. 1 interaction.
STRING9606.ENSP00000262374.

Protein family/group databases

CAZyGT33. Glycosyltransferase Family 33.

PTM databases

PhosphoSiteQ9BT22.

Polymorphism databases

DMDM73921663.

Proteomic databases

MaxQBQ9BT22.
PaxDbQ9BT22.
PRIDEQ9BT22.

Protocols and materials databases

DNASU56052.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262374; ENSP00000262374; ENSG00000033011.
GeneID56052.
KEGGhsa:56052.
UCSCuc002cyj.3. human.

Organism-specific databases

CTD56052.
GeneCardsGC16P005121.
H-InvDBHIX0009871.
HIX0009901.
HIX0021452.
HIX0030817.
HIX0030848.
HIX0031467.
HIX0036459.
HGNCHGNC:18294. ALG1.
HPAHPA060392.
MIM605907. gene.
608540. phenotype.
neXtProtNX_Q9BT22.
Orphanet79327. ALG1-CDG.
PharmGKBPA134979319.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0438.
HOGENOMHOG000216716.
HOVERGENHBG055036.
InParanoidQ9BT22.
KOK03842.
OMAIVGYKET.
OrthoDBEOG70W3DB.
PhylomeDBQ9BT22.
TreeFamTF314121.

Enzyme and pathway databases

BRENDA2.4.1.142. 2681.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9BT22.
BgeeQ9BT22.
CleanExHS_ALG1.
GenevestigatorQ9BT22.

Family and domain databases

InterProIPR026051. ALG1-like.
[Graphical view]
PANTHERPTHR13036. PTHR13036. 1 hit.
ProtoNetSearch...

Other

GeneWikiALG1.
GenomeRNAi56052.
NextBio61475.
PROQ9BT22.
SOURCESearch...

Entry information

Entry nameALG1_HUMAN
AccessionPrimary (citable) accession number: Q9BT22
Secondary accession number(s): Q6UVZ9, Q8N5Y4, Q9P2Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: July 9, 2014
This is version 120 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 16

Human chromosome 16: entries, gene names and cross-references to MIM