Q9BT22 (ALG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Disease	Congenital disorder of glycosylation Disease mutation
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dolichol-linked oligosaccharide biosynthetic process Traceable author statement. Source: Reactome lipopolysaccharide biosynthetic process Traceable author statement Ref.1. Source: ProtInc post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	chitobiosyldiphosphodolichol beta-mannosyltransferase activity Inferred from electronic annotation. Source: EC mannosyltransferase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 464	464	Chitobiosyldiphosphodolichol beta-mannosyltransferase		PRO_0000080249
Regions
	Topological domain	1 – 2	2	Cytoplasmic Potential
	Transmembrane	3 – 23	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	24 – 464	441	Lumenal Potential
Amino acid modifications
	Modified residue	242	1	Phosphoserine Ref.5
Natural variations
	Natural variant	150	1	S → R in CDG1K; impairs activity. Ref.9		VAR_023364
	Natural variant	258	1	S → L in CDG1K; impairs activity. Ref.7 Ref.8 Ref.9 Corresponds to variant rs28939378 [ dbSNP | Ensembl ].		VAR_023365
	Natural variant	267	1	S → N. Ref.3 Corresponds to variant rs17849848 [ dbSNP | Ensembl ].		VAR_038425
	Natural variant	325	1	L → M. Ref.3 Corresponds to variant rs17852920 [ dbSNP | Ensembl ].		VAR_038426
	Natural variant	342	1	Q → P in CDG1K; impairs activity. Ref.8		VAR_023366
	Natural variant	429	1	D → E No effect on activity. Ref.9 Corresponds to variant rs9745522 [ dbSNP | Ensembl ].		VAR_023367
	Natural variant	438	1	R → W. Corresponds to variant rs16835020 [ dbSNP | Ensembl ].		VAR_049350
	Natural variant	455	1	Q → R. Ref.3 Corresponds to variant rs17856919 [ dbSNP | Ensembl ].		VAR_038427

Sequences

	Sequence		Length	Mass (Da)
	Q9BT22 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: 83F55FD12CFDDBE9	FASTA	464	52,518
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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

GeneReviews

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.
IPI	IPI00549761.
RefSeq	NP_061982.3. NM_019109.4.
UniGene	Hs.592086.
3D structure databases
ProteinModelPortal	Q9BT22.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BT22. 1 interaction.
STRING	9606.ENSP00000262374.
Protein family/group databases
CAZy	GT33. Glycosyltransferase Family 33.
PTM databases
PhosphoSite	Q9BT22.
Polymorphism databases
DMDM	73921663.
Proteomic databases
PaxDb	Q9BT22.
PRIDE	Q9BT22.
Protocols and materials databases
DNASU	56052.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262374; ENSP00000262374; ENSG00000033011.
GeneID	56052.
KEGG	hsa:56052.
UCSC	uc002cyj.3. human.
Organism-specific databases
CTD	56052.
GeneCards	GC16P005121.
H-InvDB	HIX0009871. HIX0009901. HIX0021452. HIX0030817. HIX0030848. HIX0031467. HIX0036459.
HGNC	HGNC:18294. ALG1.
MIM	605907. gene. 608540. phenotype.
neXtProt	NX_Q9BT22.
Orphanet	79327. ALG1-CDG syndrome.
PharmGKB	PA134979319.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0438.
HOGENOM	HOG000216716.
HOVERGEN	HBG055036.
InParanoid	Q9BT22.
KO	K03842.
OMA	AIAVCWF.
OrthoDB	EOG49078X.
PhylomeDB	Q9BT22.
Enzyme and pathway databases
BRENDA	2.4.1.142. 2681.
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q9BT22.
Bgee	Q9BT22.
CleanEx	HS_ALG1.
Genevestigator	Q9BT22.
GermOnline	ENSG00000033011. Homo sapiens.
Family and domain databases
InterPro	IPR026051. ALG1-like. [Graphical view]
PANTHER	PTHR13036. PTHR13036. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	56052.
NextBio	61475.
SOURCE	Search...

Entry information

Entry name

ALG1_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.