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Q9BV10 (ALG12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase

EC=2.4.1.260
Alternative name(s):
Asparagine-linked glycosylation protein 12 homolog
Short name=hALG12
Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase
Mannosyltransferase ALG12 homolog
Membrane protein SB87
Gene names
Name:ALG12
ORF Names:PP14673
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man7GlcNAc2) required for protein glycosylation.

Catalytic activity

Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(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 = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Probable.

Tissue specificity

Expressed in fibroblasts.

Involvement in disease

Congenital disorder of glycosylation 1G (CDG1G) [MIM:607143]: 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.1 Ref.8 Ref.9 Ref.10 Ref.11

Sequence similarities

Belongs to the glycosyltransferase 22 family.

Sequence caution

The sequence AAM94900.1 differs from that shown. Reason: Frameshift at position 468.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase
PRO_0000215781

Regions

Transmembrane11 – 3121Helical; Potential
Transmembrane68 – 8821Helical; Potential
Transmembrane93 – 11321Helical; Potential
Transmembrane122 – 14221Helical; Potential
Transmembrane145 – 16521Helical; Potential
Transmembrane177 – 19721Helical; Potential
Transmembrane212 – 23221Helical; Potential
Transmembrane264 – 28421Helical; Potential
Transmembrane290 – 31021Helical; Potential
Transmembrane312 – 33221Helical; Potential
Transmembrane346 – 36621Helical; Potential
Transmembrane423 – 44321Helical; Potential

Natural variations

Natural variant671T → M in CDG1G. Ref.8
VAR_017904
Natural variant1011G → R in CDG1G. Ref.11
VAR_038428
Natural variant1421F → V in CDG1G. Ref.1
Corresponds to variant rs28942090 [ dbSNP | Ensembl ].
VAR_017905
Natural variant1461R → Q in CDG1G. Ref.8 Ref.11
VAR_017906
Natural variant1581L → P in CDG1G. Ref.9
VAR_017907
Natural variant3931I → V. Ref.7
Corresponds to variant rs3922872 [ dbSNP | Ensembl ].
VAR_024466

Experimental info

Sequence conflict2671A → T in AAM94900. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9BV10 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 8D4F921C21CBC8B6

FASTA48854,655
        10         20         30         40         50         60 
MAGKGSSGRR PLLLGLLVAV ATVHLVICPY TKVEESFNLQ ATHDLLYHWQ DLEQYDHLEF 

        70         80         90        100        110        120 
PGVVPRTFLG PVVIAVFSSP AVYVLSLLEM SKFYSQLIVR GVLGLGVIFG LWTLQKEVRR 

       130        140        150        160        170        180 
HFGAMVATMF CWVTAMQFHL MFYCTRTLPN VLALPVVLLA LAAWLRHEWA RFIWLSAFAI 

       190        200        210        220        230        240 
IVFRVELCLF LGLLLLLALG NRKVSVVRAL RHAVPAGILC LGLTVAVDSY FWRQLTWPEG 

       250        260        270        280        290        300 
KVLWYNTVLN KSSNWGTSPL LWYFYSALPR GLGCSLLFIP LGLVDRRTHA PTVLALGFMA 

       310        320        330        340        350        360 
LYSLLPHKEL RFIIYAFPML NITAARGCSY LLNNYKKSWL YKAGSLLVIG HLVVNAAYSA 

       370        380        390        400        410        420 
TALYVSHFNY PGGVAMQRLH QLVPPQTDVL LHIDVAAAQT GVSRFLQVNS AWRYDKREDV 

       430        440        450        460        470        480 
QPGTGMLAYT HILMEAAPGL LALYRDTHRV LASVVGTTGV SLNLTQLPPF NVHLQTKLVL 


LERLPRPS 

« Hide

References

« Hide 'large scale' references
[1]"Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase."
Chantret I., Dupre T., Delenda C., Bucher S., Dancourt J., Barnier A., Charollais A., Heron D., Bader-Meunier B., Danos O., Seta N., Durand G., Oriol R., Codogno P., Moore S.E.H.
J. Biol. Chem. 277:25815-25822(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CDG1G VAL-142.
Tissue: Skin.
[2]"Identification of novel membrane proteins."
Zhang W., Li N., Wan T., Cao X.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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], VARIANT VAL-393.
Tissue: Eye.
[8]"ALG12 mannosyltransferase defect in congenital disorder of glycosylation type Ig."
Grubenmann C.E., Frank C.G., Kjaergaard S., Berger E.G., Aebi M., Hennet T.
Hum. Mol. Genet. 11:2331-2339(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS CDG1G MET-67 AND GLN-146.
[9]"Deficiency of dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl mannosyltransferase causes congenital disorder of glycosylation type Ig."
Thiel C., Schwarz M., Hasilik M., Grieben U., Hanefeld F., Lehle L., von Figura K., Koerner C.
Biochem. J. 367:195-201(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT CDG1G PRO-158.
[10]"Abnormal glycosylation of red cell membrane band 3 in the congenital disorder of glycosylation Ig."
Zdebska E., Bader-Meunier B., Schischmanoff P.-O., Dupre T., Seta N., Tchernia G., Koscielak J., Delaunay J.
Pediatr. Res. 54:224-229(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CDG1G.
[11]"Expanding spectrum of congenital disorder of glycosylation Ig (CDG-Ig): sibs with a unique skeletal dysplasia, hypogammaglobulinemia, cardiomyopathy, genital malformations, and early lethality."
Kranz C., Basinger A.A., Guecsavas-Calikoglu M., Sun L., Powell C.M., Henderson F.W., Aylsworth A.S., Freeze H.H.
Am. J. Med. Genet. A 143:1371-1378(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CDG1G ARG-101 AND GLN-146.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ290427 mRNA. Translation: CAC83681.1.
AJ303120 mRNA. Translation: CAC67488.1.
AF311904 mRNA. Translation: AAM94900.1. Frameshift.
AF318343 mRNA. Translation: AAL55850.1.
CR456369 mRNA. Translation: CAG30255.1.
AL671710 Genomic DNA. Translation: CAO72064.1.
CH471138 Genomic DNA. Translation: EAW73480.1.
BC001729 mRNA. Translation: AAH01729.1.
BC098562 mRNA. Translation: AAH98562.1.
CCDSCCDS14081.1.
RefSeqNP_077010.1. NM_024105.3.
UniGeneHs.526711.

3D structure databases

ProteinModelPortalQ9BV10.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122535. 4 interactions.
IntActQ9BV10. 2 interactions.
STRING9606.ENSP00000333813.

Protein family/group databases

CAZyGT22. Glycosyltransferase Family 22.

PTM databases

PhosphoSiteQ9BV10.

Polymorphism databases

DMDM45476971.

Proteomic databases

MaxQBQ9BV10.
PaxDbQ9BV10.
PRIDEQ9BV10.

Protocols and materials databases

DNASU79087.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330817; ENSP00000333813; ENSG00000182858.
GeneID79087.
KEGGhsa:79087.
UCSCuc003biy.3. human.

Organism-specific databases

CTD79087.
GeneCardsGC22M050296.
GeneReviewsALG12.
H-InvDBHIX0175449.
HGNCHGNC:19358. ALG12.
HPAHPA051665.
MIM607143. phenotype.
607144. gene.
neXtProtNX_Q9BV10.
Orphanet79324. ALG12-CDG.
PharmGKBPA134987771.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG256776.
HOGENOMHOG000265945.
HOVERGENHBG050486.
InParanoidQ9BV10.
KOK03847.
OMAFHLMFYS.
OrthoDBEOG7ZGX2X.
PhylomeDBQ9BV10.
TreeFamTF314453.

Enzyme and pathway databases

BRENDA2.4.1.130. 2681.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

BgeeQ9BV10.
CleanExHS_ALG12.
GenevestigatorQ9BV10.

Family and domain databases

InterProIPR005599. GPI_mannosylTrfase.
[Graphical view]
PANTHERPTHR22760. PTHR22760. 1 hit.
PfamPF03901. Glyco_transf_22. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALG12. human.
GeneWikiALG12.
GenomeRNAi79087.
NextBio67909.
PROQ9BV10.
SOURCESearch...

Entry information

Entry nameALG12_HUMAN
AccessionPrimary (citable) accession number: Q9BV10
Secondary accession number(s): A6PWM1 expand/collapse secondary AC list , Q4KMH4, Q8NG10, Q96AA4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 121 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 22

Human chromosome 22: entries, gene names and cross-references to MIM