SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q2TAA5

- ALG11_HUMAN

UniProt

Q2TAA5 - ALG11_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase

Gene
ALG11, GT8
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Mannosyltransferase involved in the last steps of the synthesis of Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum. Catalyzes the addition of the 4th and 5th mannose residues to the dolichol-linked oligosaccharide chain.1 Publication

Catalytic activityi

2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = 2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol.1 Publication

GO - Molecular functioni

  1. GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  3. post-translational protein modification Source: Reactome
  4. protein N-linked glycosylation via asparagine Source: Reactome
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.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase (EC:2.4.1.131)
Alternative name(s):
Asparagine-linked glycosylation protein 11 homolog
Glycolipid 2-alpha-mannosyltransferase
Gene namesi
Name:ALG11
Synonyms:GT8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:32456. ALG11.

Subcellular locationi

Endoplasmic reticulum. Endoplasmic reticulum membrane; Multi-pass membrane protein Inferred 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei20 – 4021Helical; Reviewed predictionAdd
BLAST
Transmembranei234 – 25421Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital disorder of glycosylation 1P (CDG1P) [MIM:613661]: 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.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti86 – 861L → S in CDG1P; does not affect subcellular localization; results in the accumulation of under-glycosylated proteins. 1 Publication
VAR_064908
Natural varianti279 – 2791Y → S in CDG1P. 1 Publication
VAR_068070
Natural varianti318 – 3181Q → P in CDG1P. 1 Publication
VAR_068071
Natural varianti381 – 3811L → S in CDG1P. 1 Publication
VAR_068072
Natural varianti398 – 3981E → K in CDG1P. 1 Publication
VAR_068073

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861L → A: Does not affect function. 1 Publication
Mutagenesisi86 – 861L → P: Loss of function. 1 Publication

Keywords - Diseasei

Congenital disorder of glycosylation, Disease mutation

Organism-specific databases

MIMi613661. phenotype.
Orphaneti280071. ALG11-CDG.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferasePRO_0000295616Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi257 – 2571N-linked (GlcNAc...) Reviewed prediction
Glycosylationi273 – 2731N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ2TAA5.
PaxDbiQ2TAA5.
PRIDEiQ2TAA5.

PTM databases

PhosphoSiteiQ2TAA5.

Expressioni

Gene expression databases

BgeeiQ2TAA5.
CleanExiHS_ALG11.
GenevestigatoriQ2TAA5.

Organism-specific databases

HPAiHPA047214.

Interactioni

Protein-protein interaction databases

BioGridi136328. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ2TAA5.
SMRiQ2TAA5. Positions 251-475.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5644.
HOGENOMiHOG000209670.
HOVERGENiHBG057178.
InParanoidiQ2TAA5.
KOiK03844.
OMAiGTVILAH.
PhylomeDBiQ2TAA5.
TreeFamiTF313056.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
[Graphical view]
PfamiPF00534. Glycos_transf_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2TAA5-1 [UniParc]FASTAAdd to Basket

« Hide

MAAGERSWCL CKLLRFFYSL FFPGLIVCGT LCVCLVIVLW GIRLLLQRKK    50
KLVSTSKNGK NQMVIAFFHP YCNAGGGGER VLWCALRALQ KKYPEAVYVV 100
YTGDVNVNGQ QILEGAFRRF NIRLIHPVQF VFLRKRYLVE DSLYPHFTLL 150
GQSLGSIFLG WEALMQCVPD VYIDSMGYAF TLPLFKYIGG CQVGSYVHYP 200
TISTDMLSVV KNQNIGFNNA AFITRNPFLS KVKLIYYYLF AFIYGLVGSC 250
SDVVMVNSSW TLNHILSLWK VGNCTNIVYP PCDVQTFLDI PLHEKKMTPG 300
HLLVSVGQFR PEKNHPLQIR AFAKLLNKKM VESPPSLKLV LIGGCRNKDD 350
ELRVNQLRRL SEDLGVQEYV EFKINIPFDE LKNYLSEATI GLHTMWNEHF 400
GIGVVECMAA GTIILAHNSG GPKLDIVVPH EGDITGFLAE SEEDYAETIA 450
HILSMSAEKR LQIRKSARAS VSRFSDQEFE VTFLSSVEKL FK 492
Length:492
Mass (Da):55,651
Last modified:July 24, 2007 - v2
Checksum:i1B3B0789030777FC
GO

Sequence cautioni

The sequence AAI11023.1 differs from that shown. Reason: Frameshift at position 16.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti86 – 861L → S in CDG1P; does not affect subcellular localization; results in the accumulation of under-glycosylated proteins. 1 Publication
VAR_064908
Natural varianti108 – 1081N → S.
Corresponds to variant rs17480245 [ dbSNP | Ensembl ].
VAR_055902
Natural varianti279 – 2791Y → S in CDG1P. 1 Publication
VAR_068070
Natural varianti318 – 3181Q → P in CDG1P. 1 Publication
VAR_068071
Natural varianti381 – 3811L → S in CDG1P. 1 Publication
VAR_068072
Natural varianti398 – 3981E → K in CDG1P. 1 Publication
VAR_068073

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961A → V in AAI42999. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK296747 mRNA. Translation: BAG59331.1.
AL139082 Genomic DNA. Translation: CAI12890.1.
BC073862 mRNA. Translation: AAH73862.1.
BC010857 mRNA. Translation: AAH10857.3.
BC111022 mRNA. Translation: AAI11023.1. Sequence problems.
BC142998 mRNA. Translation: AAI42999.1.
CCDSiCCDS31977.1.
RefSeqiNP_001004127.2. NM_001004127.2.
UniGeneiHs.512963.
Hs.732220.

Genome annotation databases

EnsembliENST00000521508; ENSP00000430236; ENSG00000253710.
GeneIDi440138.
KEGGihsa:440138.
UCSCiuc001vga.3. human.

Polymorphism databases

DMDMi156631015.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK296747 mRNA. Translation: BAG59331.1 .
AL139082 Genomic DNA. Translation: CAI12890.1 .
BC073862 mRNA. Translation: AAH73862.1 .
BC010857 mRNA. Translation: AAH10857.3 .
BC111022 mRNA. Translation: AAI11023.1 . Sequence problems.
BC142998 mRNA. Translation: AAI42999.1 .
CCDSi CCDS31977.1.
RefSeqi NP_001004127.2. NM_001004127.2.
UniGenei Hs.512963.
Hs.732220.

3D structure databases

ProteinModelPortali Q2TAA5.
SMRi Q2TAA5. Positions 251-475.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 136328. 1 interaction.

Protein family/group databases

CAZyi GT4. Glycosyltransferase Family 4.

PTM databases

PhosphoSitei Q2TAA5.

Polymorphism databases

DMDMi 156631015.

Proteomic databases

MaxQBi Q2TAA5.
PaxDbi Q2TAA5.
PRIDEi Q2TAA5.

Protocols and materials databases

DNASUi 440138.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000521508 ; ENSP00000430236 ; ENSG00000253710 .
GeneIDi 440138.
KEGGi hsa:440138.
UCSCi uc001vga.3. human.

Organism-specific databases

CTDi 440138.
GeneCardsi GC13P052587.
GeneReviewsi ALG11.
H-InvDB HIX0011337.
HGNCi HGNC:32456. ALG11.
HPAi HPA047214.
MIMi 613661. phenotype.
613666. gene.
neXtProti NX_Q2TAA5.
Orphaneti 280071. ALG11-CDG.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5644.
HOGENOMi HOG000209670.
HOVERGENi HBG057178.
InParanoidi Q2TAA5.
KOi K03844.
OMAi GTVILAH.
PhylomeDBi Q2TAA5.
TreeFami TF313056.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi ALG11. human.
GeneWikii ALG11.
GenomeRNAii 440138.
NextBioi 108982.
PROi Q2TAA5.
SOURCEi Search...

Gene expression databases

Bgeei Q2TAA5.
CleanExi HS_ALG11.
Genevestigatori Q2TAA5.

Family and domain databases

InterProi IPR001296. Glyco_trans_1.
[Graphical view ]
Pfami PF00534. Glycos_transf_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Tongue.
  2. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Lung and Skin.
  4. "A severe human metabolic disease caused by deficiency of the endoplasmatic mannosyltransferase hALG11 leads to congenital disorder of glycosylation-Ip."
    Rind N., Schmeiser V., Thiel C., Absmanner B., Lubbehusen J., Hocks J., Apeshiotis N., Wilichowski E., Lehle L., Korner C.
    Hum. Mol. Genet. 19:1413-1424(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, VARIANT CDG1P SER-86, CHARACTERIZATION OF VARIANT CDG1P SER-86, MUTAGENESIS OF LEU-86.
  5. "Improved diagnostics lead to identification of three new patients with congenital disorder of glycosylation-Ip."
    Thiel C., Rind N., Popovici D., Hoffmann G.F., Hanson K., Conway R.L., Adamski C.R., Butler E., Scanlon R., Lambert M., Apeshiotis N., Thiels C., Matthijs G., Korner C.
    Hum. Mutat. 33:485-487(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CDG1P SER-279; PRO-318; SER-381 AND LYS-398.

Entry informationi

Entry nameiALG11_HUMAN
AccessioniPrimary (citable) accession number: Q2TAA5
Secondary accession number(s): A5PLP3
, B4DKW9, Q5TAN9, Q6DKI6, Q96FI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: September 3, 2014
This is version 80 of the entry and version 2 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 13
    Human chromosome 13: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi