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O60476 (MA1A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. 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:
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB

EC=3.2.1.113
Alternative name(s):
Mannosidase alpha class 1A member 2
Processing alpha-1,2-mannosidase IB
Short name=Alpha-1,2-mannosidase IB
Gene names
Name:MAN1A2
Synonyms:MAN1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length641 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.

Catalytic activity

Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.

Cofactor

Calcium.

Enzyme regulation

Inhibited by both 1-deoxymannojirimycin and kifunensine.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein.

Tissue specificity

Highest levels of expression in placenta and testis.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 641640Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
PRO_0000210312

Regions

Topological domain2 – 3635Cytoplasmic Potential
Transmembrane37 – 5721Helical; Signal-anchor for type II membrane protein; Potential
Topological domain58 – 641584Lumenal Potential

Amino acid modifications

Modified residue21N-acetylthreonine Ref.4
Glycosylation6311N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O60476 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 19DA691A9C4B0ED3

FASTA64173,004
        10         20         30         40         50         60 
MTTPALLPLS GRRIPPLNLG PPSFPHHRAT LRLSEKFILL LILSAFITLC FGAFFFLPDS 

        70         80         90        100        110        120 
SKHKRFDLGL EDVLIPHVDA GKGAKNPGVF LIHGPDEHRH REEEERLRNK IRADHEKALE 

       130        140        150        160        170        180 
EAKEKLRKSR EEIRAEIQTE KNKVVQEMKI KENKPLPPVP IPNLVGIRGG DPEDNDIREK 

       190        200        210        220        230        240 
REKIKEMMKH AWDNYRTYGW GHNELRPIAR KGHSPNIFGS SQMGATIVDA LDTLYIMGLH 

       250        260        270        280        290        300 
DEFLDGQRWI EDNLDFSVNS EVSVFEVNIR FIGGLLAAYY LSGEEIFKIK AVQLAEKLLP 

       310        320        330        340        350        360 
AFNTPTGIPW AMVNLKSGVG RNWGWASAGS SILAEFGTLH MEFIHLSYLT GDLTYYKKVM 

       370        380        390        400        410        420 
HIRKLLQKMD RPNGLYPNYL NPRTGRWGQY HTSVGGLGDS FYEYLLKAWL MSDKTDHEAR 

       430        440        450        460        470        480 
KMYDDAIEAI EKHLIKKSRG GLTFIGEWKN GHLEKKMGHL ACFAGGMFAL GADGSRADKA 

       490        500        510        520        530        540 
GHYLELGAEI ARTCHESYDR TALKLGPESF KFDGAVEAVA VRQAEKYYIL RPEVIETYWY 

       550        560        570        580        590        600 
LWRFTHDPRY RQWGWEAALA IEKYCRVNGG FSGVKDVYSS TPTHDDVQQS FFLAETLKYL 

       610        620        630        640 
YLLFSGDDLL PLDHWVFNTE AHPLPVLHLA NTTLSGNPAV R 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human alpha-1,2-mannosidase gene involved in N-glycan maturation."
Tremblay L.O., Campbell-Dyke N., Herscovics A.
Glycobiology 8:585-595(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Brain and Placenta.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [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: Brain.
[4]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[5]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF053626 expand/collapse EMBL AC list , AF053622, AF053623, AF053624, AF053625 Genomic DNA. Translation: AAC26201.1.
AF027156 mRNA. Translation: AAC26169.1.
AF053621 expand/collapse EMBL AC list , AF053619, AF053620, AF053615, AF053616, AF053617, AF053618 Genomic DNA. Translation: AAC26200.1.
AL157902, AL358072 Genomic DNA. Translation: CAI22315.1.
AL358072, AL157902 Genomic DNA. Translation: CAH71079.1.
BC063300 mRNA. Translation: AAH63300.1.
CCDSCCDS895.1.
RefSeqNP_006690.1. NM_006699.3.
UniGeneHs.435938.
Hs.602811.

3D structure databases

ProteinModelPortalO60476.
SMRO60476. Positions 156-627.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116111. 2 interactions.
IntActO60476. 4 interactions.
MINTMINT-1184386.
STRING9606.ENSP00000348959.

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

PTM databases

PhosphoSiteO60476.

Proteomic databases

MaxQBO60476.
PaxDbO60476.
PRIDEO60476.

Protocols and materials databases

DNASU10905.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356554; ENSP00000348959; ENSG00000198162.
GeneID10905.
KEGGhsa:10905.
UCSCuc001ehd.1. human.

Organism-specific databases

CTD10905.
GeneCardsGC01P117910.
HGNCHGNC:6822. MAN1A2.
HPAHPA034559.
MIM604345. gene.
neXtProtNX_O60476.
PharmGKBPA30571.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300315.
HOGENOMHOG000181988.
HOVERGENHBG052389.
InParanoidO60476.
KOK01230.
OMADPEDNDI.
OrthoDBEOG7X0VH1.
PhylomeDBO60476.
TreeFamTF313420.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressO60476.
BgeeO60476.
CleanExHS_MAN1A2.
GenevestigatorO60476.

Family and domain databases

Gene3D1.50.10.50. 1 hit.
InterProIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERPTHR11742. PTHR11742. 1 hit.
PfamPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSPR00747. GLYHDRLASE47.
SUPFAMSSF48225. SSF48225. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMAN1A2. human.
GeneWikiMAN1A2.
GenomeRNAi10905.
NextBio41419.
PROO60476.
SOURCESearch...

Entry information

Entry nameMA1A2_HUMAN
AccessionPrimary (citable) accession number: O60476
Secondary accession number(s): Q9H510
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 125 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries