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Q2TAA5 (ALG11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ALG11
Synonyms:GT8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Catalytic activity

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. Ref.4

Subcellular location

Endoplasmic reticulum. Endoplasmic reticulum membrane; Multi-pass membrane protein Probable Ref.4.

Involvement in disease

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. Ref.4 Ref.5

Sequence similarities

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

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase
PRO_0000295616

Regions

Transmembrane20 – 4021Helical; Potential
Transmembrane234 – 25421Helical; Potential

Amino acid modifications

Glycosylation2571N-linked (GlcNAc...) Potential
Glycosylation2731N-linked (GlcNAc...) Potential

Natural variations

Natural variant861L → S in CDG1P; does not affect subcellular localization; results in the accumulation of under-glycosylated proteins. Ref.4
VAR_064908
Natural variant1081N → S.
Corresponds to variant rs17480245 [ dbSNP | Ensembl ].
VAR_055902
Natural variant2791Y → S in CDG1P. Ref.5
VAR_068070
Natural variant3181Q → P in CDG1P. Ref.5
VAR_068071
Natural variant3811L → S in CDG1P. Ref.5
VAR_068072
Natural variant3981E → K in CDG1P. Ref.5
VAR_068073

Experimental info

Mutagenesis861L → A: Does not affect function. Ref.4
Mutagenesis861L → P: Loss of function. Ref.4
Sequence conflict961A → V in AAI42999. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q2TAA5 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 1B3B0789030777FC

FASTA49255,651
        10         20         30         40         50         60 
MAAGERSWCL CKLLRFFYSL FFPGLIVCGT LCVCLVIVLW GIRLLLQRKK KLVSTSKNGK 

        70         80         90        100        110        120 
NQMVIAFFHP YCNAGGGGER VLWCALRALQ KKYPEAVYVV YTGDVNVNGQ QILEGAFRRF 

       130        140        150        160        170        180 
NIRLIHPVQF VFLRKRYLVE DSLYPHFTLL GQSLGSIFLG WEALMQCVPD VYIDSMGYAF 

       190        200        210        220        230        240 
TLPLFKYIGG CQVGSYVHYP TISTDMLSVV KNQNIGFNNA AFITRNPFLS KVKLIYYYLF 

       250        260        270        280        290        300 
AFIYGLVGSC SDVVMVNSSW TLNHILSLWK VGNCTNIVYP PCDVQTFLDI PLHEKKMTPG 

       310        320        330        340        350        360 
HLLVSVGQFR PEKNHPLQIR AFAKLLNKKM VESPPSLKLV LIGGCRNKDD ELRVNQLRRL 

       370        380        390        400        410        420 
SEDLGVQEYV EFKINIPFDE LKNYLSEATI GLHTMWNEHF GIGVVECMAA GTIILAHNSG 

       430        440        450        460        470        480 
GPKLDIVVPH EGDITGFLAE SEEDYAETIA HILSMSAEKR LQIRKSARAS VSRFSDQEFE 

       490 
VTFLSSVEKL FK 

« Hide

References

« Hide 'large scale' references
[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. 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].
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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS31977.1.
RefSeqNP_001004127.2. NM_001004127.2.
UniGeneHs.512963.
Hs.732220.

3D structure databases

ProteinModelPortalQ2TAA5.
SMRQ2TAA5. Positions 251-475.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid136328. 1 interaction.

Protein family/group databases

CAZyGT4. Glycosyltransferase Family 4.

PTM databases

PhosphoSiteQ2TAA5.

Polymorphism databases

DMDM156631015.

Proteomic databases

MaxQBQ2TAA5.
PaxDbQ2TAA5.
PRIDEQ2TAA5.

Protocols and materials databases

DNASU440138.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000521508; ENSP00000430236; ENSG00000253710.
GeneID440138.
KEGGhsa:440138.
UCSCuc001vga.3. human.

Organism-specific databases

CTD440138.
GeneCardsGC13P052587.
GeneReviewsALG11.
H-InvDBHIX0011337.
HGNCHGNC:32456. ALG11.
HPAHPA047214.
MIM613661. phenotype.
613666. gene.
neXtProtNX_Q2TAA5.
Orphanet280071. ALG11-CDG.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5644.
HOGENOMHOG000209670.
HOVERGENHBG057178.
InParanoidQ2TAA5.
KOK03844.
OMAGTVILAH.
PhylomeDBQ2TAA5.
TreeFamTF313056.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

BgeeQ2TAA5.
CleanExHS_ALG11.
GenevestigatorQ2TAA5.

Family and domain databases

InterProIPR001296. Glyco_trans_1.
[Graphical view]
PfamPF00534. Glycos_transf_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALG11. human.
GeneWikiALG11.
GenomeRNAi440138.
NextBio108982.
PROQ2TAA5.
SOURCESearch...

Entry information

Entry nameALG11_HUMAN
AccessionPrimary (citable) accession number: Q2TAA5
Secondary accession number(s): A5PLP3 expand/collapse secondary AC list , B4DKW9, Q5TAN9, Q6DKI6, Q96FI7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: July 9, 2014
This is version 79 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

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 13

Human chromosome 13: entries, gene names and cross-references to MIM