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Q9BV10

- ALG12_HUMAN

UniProt

Q9BV10 - ALG12_HUMAN

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Protein
Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase
Gene
ALG12, PP14673
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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.

Pathwayi

GO - Molecular functioni

  1. alpha-1,6-mannosyltransferase activity Source: UniProtKB
  2. dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. dolichol-linked oligosaccharide biosynthetic process Source: MGI
  3. mannosylation Source: GOC
  4. post-translational protein modification Source: Reactome
  5. protein N-linked glycosylation Source: UniProtKB
  6. protein N-linked glycosylation via asparagine Source: Reactome
  7. protein folding Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.130. 2681.
ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT22. Glycosyltransferase Family 22.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ALG12
ORF Names:PP14673
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:19358. ALG12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121Helical; Reviewed prediction
Add
BLAST
Transmembranei68 – 8821Helical; Reviewed prediction
Add
BLAST
Transmembranei93 – 11321Helical; Reviewed prediction
Add
BLAST
Transmembranei122 – 14221Helical; Reviewed prediction
Add
BLAST
Transmembranei145 – 16521Helical; Reviewed prediction
Add
BLAST
Transmembranei177 – 19721Helical; Reviewed prediction
Add
BLAST
Transmembranei212 – 23221Helical; Reviewed prediction
Add
BLAST
Transmembranei264 – 28421Helical; Reviewed prediction
Add
BLAST
Transmembranei290 – 31021Helical; Reviewed prediction
Add
BLAST
Transmembranei312 – 33221Helical; Reviewed prediction
Add
BLAST
Transmembranei346 – 36621Helical; Reviewed prediction
Add
BLAST
Transmembranei423 – 44321Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: Reactome
  3. 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 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.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671T → M in CDG1G. 1 Publication
VAR_017904
Natural varianti101 – 1011G → R in CDG1G. 1 Publication
VAR_038428
Natural varianti142 – 1421F → V in CDG1G. 1 Publication
Corresponds to variant rs28942090 [ dbSNP | Ensembl ].
VAR_017905
Natural varianti146 – 1461R → Q in CDG1G. 2 Publications
VAR_017906
Natural varianti158 – 1581L → P in CDG1G. 1 Publication
VAR_017907

Keywords - Diseasei

Congenital disorder of glycosylation, Disease mutation

Organism-specific databases

MIMi607143. phenotype.
Orphaneti79324. ALG12-CDG.
PharmGKBiPA134987771.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase
PRO_0000215781Add
BLAST

Proteomic databases

MaxQBiQ9BV10.
PaxDbiQ9BV10.
PRIDEiQ9BV10.

PTM databases

PhosphoSiteiQ9BV10.

Expressioni

Tissue specificityi

Expressed in fibroblasts.

Gene expression databases

BgeeiQ9BV10.
CleanExiHS_ALG12.
GenevestigatoriQ9BV10.

Organism-specific databases

HPAiHPA051665.

Interactioni

Protein-protein interaction databases

BioGridi122535. 4 interactions.
IntActiQ9BV10. 2 interactions.
STRINGi9606.ENSP00000333813.

Structurei

3D structure databases

ProteinModelPortaliQ9BV10.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG256776.
HOGENOMiHOG000265945.
HOVERGENiHBG050486.
InParanoidiQ9BV10.
KOiK03847.
OMAiFHLMFYS.
OrthoDBiEOG7ZGX2X.
PhylomeDBiQ9BV10.
TreeFamiTF314453.

Family and domain databases

InterProiIPR005599. GPI_mannosylTrfase.
[Graphical view]
PANTHERiPTHR22760. PTHR22760. 1 hit.
PfamiPF03901. Glyco_transf_22. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BV10-1 [UniParc]FASTAAdd to Basket

« Hide

MAGKGSSGRR PLLLGLLVAV ATVHLVICPY TKVEESFNLQ ATHDLLYHWQ    50
DLEQYDHLEF PGVVPRTFLG PVVIAVFSSP AVYVLSLLEM SKFYSQLIVR 100
GVLGLGVIFG LWTLQKEVRR HFGAMVATMF CWVTAMQFHL MFYCTRTLPN 150
VLALPVVLLA LAAWLRHEWA RFIWLSAFAI IVFRVELCLF LGLLLLLALG 200
NRKVSVVRAL RHAVPAGILC LGLTVAVDSY FWRQLTWPEG KVLWYNTVLN 250
KSSNWGTSPL LWYFYSALPR GLGCSLLFIP LGLVDRRTHA PTVLALGFMA 300
LYSLLPHKEL RFIIYAFPML NITAARGCSY LLNNYKKSWL YKAGSLLVIG 350
HLVVNAAYSA TALYVSHFNY PGGVAMQRLH QLVPPQTDVL LHIDVAAAQT 400
GVSRFLQVNS AWRYDKREDV QPGTGMLAYT HILMEAAPGL LALYRDTHRV 450
LASVVGTTGV SLNLTQLPPF NVHLQTKLVL LERLPRPS 488
Length:488
Mass (Da):54,655
Last modified:June 1, 2001 - v1
Checksum:i8D4F921C21CBC8B6
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671T → M in CDG1G. 1 Publication
VAR_017904
Natural varianti101 – 1011G → R in CDG1G. 1 Publication
VAR_038428
Natural varianti142 – 1421F → V in CDG1G. 1 Publication
Corresponds to variant rs28942090 [ dbSNP | Ensembl ].
VAR_017905
Natural varianti146 – 1461R → Q in CDG1G. 2 Publications
VAR_017906
Natural varianti158 – 1581L → P in CDG1G. 1 Publication
VAR_017907
Natural varianti393 – 3931I → V.1 Publication
Corresponds to variant rs3922872 [ dbSNP | Ensembl ].
VAR_024466

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti267 – 2671A → T in AAM94900. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14081.1.
RefSeqiNP_077010.1. NM_024105.3.
UniGeneiHs.526711.

Genome annotation databases

EnsembliENST00000330817; ENSP00000333813; ENSG00000182858.
GeneIDi79087.
KEGGihsa:79087.
UCSCiuc003biy.3. human.

Polymorphism databases

DMDMi45476971.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14081.1.
RefSeqi NP_077010.1. NM_024105.3.
UniGenei Hs.526711.

3D structure databases

ProteinModelPortali Q9BV10.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122535. 4 interactions.
IntActi Q9BV10. 2 interactions.
STRINGi 9606.ENSP00000333813.

Protein family/group databases

CAZyi GT22. Glycosyltransferase Family 22.

PTM databases

PhosphoSitei Q9BV10.

Polymorphism databases

DMDMi 45476971.

Proteomic databases

MaxQBi Q9BV10.
PaxDbi Q9BV10.
PRIDEi Q9BV10.

Protocols and materials databases

DNASUi 79087.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330817 ; ENSP00000333813 ; ENSG00000182858 .
GeneIDi 79087.
KEGGi hsa:79087.
UCSCi uc003biy.3. human.

Organism-specific databases

CTDi 79087.
GeneCardsi GC22M050296.
GeneReviewsi ALG12.
H-InvDB HIX0175449.
HGNCi HGNC:19358. ALG12.
HPAi HPA051665.
MIMi 607143. phenotype.
607144. gene.
neXtProti NX_Q9BV10.
Orphaneti 79324. ALG12-CDG.
PharmGKBi PA134987771.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG256776.
HOGENOMi HOG000265945.
HOVERGENi HBG050486.
InParanoidi Q9BV10.
KOi K03847.
OMAi FHLMFYS.
OrthoDBi EOG7ZGX2X.
PhylomeDBi Q9BV10.
TreeFami TF314453.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.130. 2681.
Reactomei REACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

ChiTaRSi ALG12. human.
GeneWikii ALG12.
GenomeRNAii 79087.
NextBioi 67909.
PROi Q9BV10.
SOURCEi Search...

Gene expression databases

Bgeei Q9BV10.
CleanExi HS_ALG12.
Genevestigatori Q9BV10.

Family and domain databases

InterProi IPR005599. GPI_mannosylTrfase.
[Graphical view ]
PANTHERi PTHR22760. PTHR22760. 1 hit.
Pfami PF03901. Glyco_transf_22. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. 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.

Entry informationi

Entry nameiALG12_HUMAN
AccessioniPrimary (citable) accession number: Q9BV10
Secondary accession number(s): A6PWM1
, Q4KMH4, Q8NG10, Q96AA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 122 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 22
    Human chromosome 22: 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

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