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Q9H553 (ALG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-1,3/1,6-mannosyltransferase ALG2

EC=2.4.1.132
EC=2.4.1.257
Alternative name(s):
Asparagine-linked glycosylation protein 2 homolog
GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase
GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase
Gene names
Name:ALG2
ORF Names:UNQ666/PRO1298
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mannosylates Man2GlcNAc(2)-dolichol diphosphate and Man1GlcNAc(2)-dolichol diphosphate to form Man3GlcNAc(2)-dolichol diphosphate. Ref.6

Catalytic activity

GDP-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol.

GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = GDP + D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Membrane; Single-pass membrane protein Potential.

Involvement in disease

Congenital disorder of glycosylation 1I (CDG1I) [MIM:607906]: 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.6

Sequence similarities

Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCongenital disorder of glycosylation
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

dolichol-linked oligosaccharide biosynthetic process

Inferred from genetic interaction Ref.6. Source: UniProtKB

mannosylation

Inferred from direct assay Ref.6. Source: GOC

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

protein glycosylation in endoplasmic reticulum

Inferred from genetic interaction Ref.6. Source: UniProtKB

response to calcium ion

Inferred from direct assay PubMed 12445460PubMed 17196169. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11278427PubMed 14999017PubMed 16996505PubMed 17045351PubMed 17196169. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay PubMed 16996505. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 11278427PubMed 17045351PubMed 17196169. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 17196169. Source: UniProtKB

   Molecular_functionGDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

alpha-1,3-mannosyltransferase activity

Inferred from direct assay Ref.6. Source: UniProtKB

calcium-dependent protein binding

Inferred from mutant phenotype PubMed 14999017. Source: UniProtKB

glycolipid 6-alpha-mannosyltransferase activity

Inferred from electronic annotation. Source: InterPro

protein N-terminus binding

Inferred from physical interaction PubMed 12445460. Source: UniProtKB

protein anchor

Inferred from mutant phenotype PubMed 16957052. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 11278427. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H553-1)

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.
Isoform 2 (identifier: Q9H553-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-91: Missing.
     92-116: VRMVFLALYVLFLADEEFDVVVCDQ → MPLLKLVHGSPLVFGEKFKLFTL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Alpha-1,3/1,6-mannosyltransferase ALG2
PRO_0000080260

Regions

Transmembrane85 – 10521Helical; Potential

Natural variations

Alternative sequence1 – 9191Missing in isoform 2.
VSP_013188
Alternative sequence92 – 11625VRMVF…VVCDQ → MPLLKLVHGSPLVFGEKFKL FTL in isoform 2.
VSP_013189
Natural variant111S → P.
Corresponds to variant rs11545137 [ dbSNP | Ensembl ].
VAR_049351
Natural variant3671V → A.
Corresponds to variant rs35626507 [ dbSNP | Ensembl ].
VAR_049352

Experimental info

Sequence conflict1781Q → R in BAC11449. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 778DB1FD069E7F29

FASTA41647,092
        10         20         30         40         50         60 
MAEEQGRERD SVPKPSVLFL HPDLGVGGAE RLVLDAALAL QARGCSVKIW TAHYDPGHCF 

        70         80         90        100        110        120 
AESRELPVRC AGDWLPRGLG WGGRGAAVCA YVRMVFLALY VLFLADEEFD VVVCDQVSAC 

       130        140        150        160        170        180 
IPVFRLARRR KKILFYCHFP DLLLTKRDSF LKRLYRAPID WIEEYTTGMA DCILVNSQFT 

       190        200        210        220        230        240 
AAVFKETFKS LSHIDPDVLY PSLNVTSFDS VVPEKLDDLV PKGKKFLLLS INRYERKKNL 

       250        260        270        280        290        300 
TLALEALVQL RGRLTSQDWE RVHLIVAGGY DERVLENVEH YQELKKMVQQ SDLGQYVTFL 

       310        320        330        340        350        360 
RSFSDKQKIS LLHSCTCVLY TPSNEHFGIV PLEAMYMQCP VIAVNSGGPL ESIDHSVTGF 

       370        380        390        400        410 
LCEPDPVHFS EAIEKFIREP SLKATMGLAG RARVKEKFSP EAFTEQLYRY VTKLLV 

« Hide

Isoform 2 [UniParc].

Checksum: C8506E37A7E15848
Show »

FASTA32337,017

References

« Hide 'large scale' references
[1]"Molecular cloning of the mammalian genes which complement the defect of the yeast alg2 mutation."
Takahashi T., Katoh R., Okutomi S., Suzuki Y., Mori H., Takizawa Y., Nishikawa Y.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"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] (ISOFORM 2).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Placenta.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [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: Embryonic testis carcinoma.
[6]"A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis."
Thiel C., Schwarz M., Peng J., Grzmil M., Hasilik M., Braulke T., Kohlschuetter A., von Figura K., Lehle L., Koerner C.
J. Biol. Chem. 278:22498-22505(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INVOLVEMENT IN CDG1I.
[7]"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].

Web resources

GeneReviews
GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB161356 mRNA. Translation: BAD11905.1.
AY358697 mRNA. Translation: AAQ89060.1.
AK027417 mRNA. Translation: BAB55099.1.
AK074704 mRNA. Translation: BAC11150.1.
AK074988 mRNA. Translation: BAC11337.1.
AK075172 mRNA. Translation: BAC11449.1.
AL137067 Genomic DNA. Translation: CAC07999.1.
BC017876 mRNA. Translation: AAH17876.1.
RefSeqNP_149078.1. NM_033087.3.
UniGeneHs.40919.

3D structure databases

ProteinModelPortalQ9H553.
SMRQ9H553. Positions 163-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124493. 16 interactions.
STRING9606.ENSP00000417764.

Protein family/group databases

CAZyGT4. Glycosyltransferase Family 4.

PTM databases

PhosphoSiteQ9H553.

Polymorphism databases

DMDM46395991.

Proteomic databases

PaxDbQ9H553.
PRIDEQ9H553.

Protocols and materials databases

DNASU85365.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319033; ENSP00000326609; ENSG00000119523. [Q9H553-2]
ENST00000476832; ENSP00000417764; ENSG00000119523. [Q9H553-1]
GeneID85365.
KEGGhsa:85365.
UCSCuc004azf.3. human. [Q9H553-1]
uc004azg.3. human. [Q9H553-2]

Organism-specific databases

CTD85365.
GeneCardsGC09M101978.
H-InvDBHIX0019474.
HGNCHGNC:23159. ALG2.
HPAHPA041512.
HPA041601.
MIM607905. gene.
607906. phenotype.
neXtProtNX_Q9H553.
Orphanet79326. ALG2-CDG.
353327. Congenital myasthenic syndromes with glycosylation defect.
PharmGKBPA134956849.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0438.
HOGENOMHOG000177048.
HOVERGENHBG009445.
InParanoidQ9H553.
KOK03843.
OMAAVCAYVR.
OrthoDBEOG7HTHH4.
PhylomeDBQ9H553.
TreeFamTF106000.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9H553.
BgeeQ9H553.
CleanExHS_ALG2.
GenevestigatorQ9H553.

Family and domain databases

InterProIPR027054. ALG2.
IPR001296. Glyco_trans_1.
[Graphical view]
PANTHERPTHR12526:SF22. PTHR12526:SF22. 1 hit.
PfamPF00534. Glycos_transf_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALG2. human.
GeneWikiALG2.
GenomeRNAi85365.
NextBio75895.
PROQ9H553.
SOURCESearch...

Entry information

Entry nameALG2_HUMAN
AccessionPrimary (citable) accession number: Q9H553
Secondary accession number(s): A2A2Y0, Q8NBX2, Q8NC39
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 115 of the entry and version 1 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 9

Human chromosome 9: entries, gene names and cross-references to MIM