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Q9H553

- ALG2_HUMAN

UniProt

Q9H553 - ALG2_HUMAN

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Protein

Alpha-1,3/1,6-mannosyltransferase ALG2

Gene

ALG2

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

Functioni

Mannosylates Man2GlcNAc(2)-dolichol diphosphate and Man1GlcNAc(2)-dolichol diphosphate to form Man3GlcNAc(2)-dolichol diphosphate.1 Publication

Catalytic activityi

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.

Pathwayi

GO - Molecular functioni

  1. alpha-1,3-mannosyltransferase activity Source: UniProtKB
  2. calcium-dependent protein binding Source: UniProtKB
  3. GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity Source: UniProtKB-EC
  4. glycolipid 6-alpha-mannosyltransferase activity Source: InterPro
  5. protein anchor Source: UniProtKB
  6. protein heterodimerization activity Source: UniProtKB
  7. protein N-terminus binding Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. dolichol-linked oligosaccharide biosynthetic process Source: UniProtKB
  3. mannosylation Source: GOC
  4. post-translational protein modification Source: Reactome
  5. protein glycosylation in endoplasmic reticulum Source: UniProtKB
  6. protein N-linked glycosylation via asparagine Source: Reactome
  7. response to calcium ion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ALG2
ORF Names:UNQ666/PRO1298
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:23159. ALG2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei85 – 10521HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum membrane Source: Reactome
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Congenital disorder of glycosylation

Organism-specific databases

MIMi607906. phenotype.
Orphaneti79326. ALG2-CDG.
353327. Congenital myasthenic syndromes with glycosylation defect.
PharmGKBiPA134956849.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Alpha-1,3/1,6-mannosyltransferase ALG2PRO_0000080260Add
BLAST

Proteomic databases

MaxQBiQ9H553.
PaxDbiQ9H553.
PRIDEiQ9H553.

PTM databases

PhosphoSiteiQ9H553.

Expressioni

Gene expression databases

BgeeiQ9H553.
CleanExiHS_ALG2.
ExpressionAtlasiQ9H553. baseline and differential.
GenevestigatoriQ9H553.

Organism-specific databases

HPAiHPA041512.
HPA041601.

Interactioni

Protein-protein interaction databases

BioGridi124493. 18 interactions.
STRINGi9606.ENSP00000417764.

Structurei

3D structure databases

ProteinModelPortaliQ9H553.
SMRiQ9H553. Positions 163-407.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0438.
GeneTreeiENSGT00550000075033.
HOGENOMiHOG000177048.
HOVERGENiHBG009445.
InParanoidiQ9H553.
KOiK03843.
OMAiGETGWLR.
OrthoDBiEOG7HTHH4.
PhylomeDBiQ9H553.
TreeFamiTF106000.

Family and domain databases

InterProiIPR027054. ALG2.
IPR001296. Glyco_trans_1.
IPR028098. Glyco_trans_4_N.
[Graphical view]
PANTHERiPTHR12526:SF221. PTHR12526:SF221. 1 hit.
PfamiPF13579. Glyco_trans_4_4. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H553-1) [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
MAEEQGRERD SVPKPSVLFL HPDLGVGGAE RLVLDAALAL QARGCSVKIW
60 70 80 90 100
TAHYDPGHCF AESRELPVRC AGDWLPRGLG WGGRGAAVCA YVRMVFLALY
110 120 130 140 150
VLFLADEEFD VVVCDQVSAC IPVFRLARRR KKILFYCHFP DLLLTKRDSF
160 170 180 190 200
LKRLYRAPID WIEEYTTGMA DCILVNSQFT AAVFKETFKS LSHIDPDVLY
210 220 230 240 250
PSLNVTSFDS VVPEKLDDLV PKGKKFLLLS INRYERKKNL TLALEALVQL
260 270 280 290 300
RGRLTSQDWE RVHLIVAGGY DERVLENVEH YQELKKMVQQ SDLGQYVTFL
310 320 330 340 350
RSFSDKQKIS LLHSCTCVLY TPSNEHFGIV PLEAMYMQCP VIAVNSGGPL
360 370 380 390 400
ESIDHSVTGF LCEPDPVHFS EAIEKFIREP SLKATMGLAG RARVKEKFSP
410
EAFTEQLYRY VTKLLV
Length:416
Mass (Da):47,092
Last modified:March 1, 2001 - v1
Checksum:i778DB1FD069E7F29
GO
Isoform 2 (identifier: Q9H553-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:323
Mass (Da):37,017
Checksum:iC8506E37A7E15848
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti178 – 1781Q → R in BAC11449. (PubMed:12975309)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111S → P.
Corresponds to variant rs11545137 [ dbSNP | Ensembl ].
VAR_049351
Natural varianti367 – 3671V → A.
Corresponds to variant rs35626507 [ dbSNP | Ensembl ].
VAR_049352

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9191Missing in isoform 2. 2 PublicationsVSP_013188Add
BLAST
Alternative sequencei92 – 11625VRMVF…VVCDQ → MPLLKLVHGSPLVFGEKFKL FTL in isoform 2. 2 PublicationsVSP_013189Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6739.1. [Q9H553-1]
RefSeqiNP_149078.1. NM_033087.3. [Q9H553-1]
UniGeneiHs.40919.

Genome annotation databases

EnsembliENST00000319033; ENSP00000326609; ENSG00000119523. [Q9H553-2]
ENST00000476832; ENSP00000417764; ENSG00000119523. [Q9H553-1]
GeneIDi85365.
KEGGihsa:85365.
UCSCiuc004azf.3. human. [Q9H553-1]
uc004azg.3. human. [Q9H553-2]

Polymorphism databases

DMDMi46395991.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS6739.1. [Q9H553-1 ]
RefSeqi NP_149078.1. NM_033087.3. [Q9H553-1 ]
UniGenei Hs.40919.

3D structure databases

ProteinModelPortali Q9H553.
SMRi Q9H553. Positions 163-407.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124493. 18 interactions.
STRINGi 9606.ENSP00000417764.

Protein family/group databases

CAZyi GT4. Glycosyltransferase Family 4.

PTM databases

PhosphoSitei Q9H553.

Polymorphism databases

DMDMi 46395991.

Proteomic databases

MaxQBi Q9H553.
PaxDbi Q9H553.
PRIDEi Q9H553.

Protocols and materials databases

DNASUi 85365.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000319033 ; ENSP00000326609 ; ENSG00000119523 . [Q9H553-2 ]
ENST00000476832 ; ENSP00000417764 ; ENSG00000119523 . [Q9H553-1 ]
GeneIDi 85365.
KEGGi hsa:85365.
UCSCi uc004azf.3. human. [Q9H553-1 ]
uc004azg.3. human. [Q9H553-2 ]

Organism-specific databases

CTDi 85365.
GeneCardsi GC09M101978.
GeneReviewsi ALG2.
H-InvDB HIX0019474.
HGNCi HGNC:23159. ALG2.
HPAi HPA041512.
HPA041601.
MIMi 607905. gene.
607906. phenotype.
neXtProti NX_Q9H553.
Orphaneti 79326. ALG2-CDG.
353327. Congenital myasthenic syndromes with glycosylation defect.
PharmGKBi PA134956849.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0438.
GeneTreei ENSGT00550000075033.
HOGENOMi HOG000177048.
HOVERGENi HBG009445.
InParanoidi Q9H553.
KOi K03843.
OMAi GETGWLR.
OrthoDBi EOG7HTHH4.
PhylomeDBi Q9H553.
TreeFami TF106000.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

ChiTaRSi ALG2. human.
GeneWikii ALG2.
GenomeRNAii 85365.
NextBioi 75895.
PROi Q9H553.
SOURCEi Search...

Gene expression databases

Bgeei Q9H553.
CleanExi HS_ALG2.
ExpressionAtlasi Q9H553. baseline and differential.
Genevestigatori Q9H553.

Family and domain databases

InterProi IPR027054. ALG2.
IPR001296. Glyco_trans_1.
IPR028098. Glyco_trans_4_N.
[Graphical view ]
PANTHERi PTHR12526:SF221. PTHR12526:SF221. 1 hit.
Pfami PF13579. Glyco_trans_4_4. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiALG2_HUMAN
AccessioniPrimary (citable) accession number: Q9H553
Secondary accession number(s): A2A2Y0, Q8NBX2, Q8NC39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 121 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, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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