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Protein

Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB

Gene

MAN1A2

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

Functioni

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

Catalytic activityi

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

Cofactori

Enzyme regulationi

Inhibited by both 1-deoxymannojirimycin and kifunensine.

Pathway: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BRENDAi3.2.1.113. 2681.
ReactomeiREACT_25396. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MAN1A2
Synonyms:MAN1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6822. MAN1A2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 3635CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei37 – 5721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini58 – 641584LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: HPA
  • Golgi membrane Source: Reactome
  • integral component of membrane Source: ProtInc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30571.

Polymorphism and mutation databases

BioMutaiMAN1A2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 641640Mannosyl-oligosaccharide 1,2-alpha-mannosidase IBPRO_0000210312Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiO60476.
PaxDbiO60476.
PRIDEiO60476.

PTM databases

PhosphoSiteiO60476.

Expressioni

Tissue specificityi

Highest levels of expression in placenta and testis.

Gene expression databases

BgeeiO60476.
CleanExiHS_MAN1A2.
ExpressionAtlasiO60476. baseline and differential.
GenevisibleiO60476. HS.

Organism-specific databases

HPAiHPA034559.
HPA057364.

Interactioni

Protein-protein interaction databases

BioGridi116111. 5 interactions.
IntActiO60476. 4 interactions.
MINTiMINT-1184386.
STRINGi9606.ENSP00000348959.

Structurei

3D structure databases

ProteinModelPortaliO60476.
SMRiO60476. Positions 156-627.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 47 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG300315.
GeneTreeiENSGT00390000016529.
HOGENOMiHOG000181988.
HOVERGENiHBG052389.
InParanoidiO60476.
KOiK01230.
OMAiRQYGWGH.
OrthoDBiEOG7X0VH1.
PhylomeDBiO60476.
TreeFamiTF313420.

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERiPTHR11742. PTHR11742. 1 hit.
PfamiPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O60476-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTPALLPLS GRRIPPLNLG PPSFPHHRAT LRLSEKFILL LILSAFITLC
60 70 80 90 100
FGAFFFLPDS SKHKRFDLGL EDVLIPHVDA GKGAKNPGVF LIHGPDEHRH
110 120 130 140 150
REEEERLRNK IRADHEKALE EAKEKLRKSR EEIRAEIQTE KNKVVQEMKI
160 170 180 190 200
KENKPLPPVP IPNLVGIRGG DPEDNDIREK REKIKEMMKH AWDNYRTYGW
210 220 230 240 250
GHNELRPIAR KGHSPNIFGS SQMGATIVDA LDTLYIMGLH DEFLDGQRWI
260 270 280 290 300
EDNLDFSVNS EVSVFEVNIR FIGGLLAAYY LSGEEIFKIK AVQLAEKLLP
310 320 330 340 350
AFNTPTGIPW AMVNLKSGVG RNWGWASAGS SILAEFGTLH MEFIHLSYLT
360 370 380 390 400
GDLTYYKKVM HIRKLLQKMD RPNGLYPNYL NPRTGRWGQY HTSVGGLGDS
410 420 430 440 450
FYEYLLKAWL MSDKTDHEAR KMYDDAIEAI EKHLIKKSRG GLTFIGEWKN
460 470 480 490 500
GHLEKKMGHL ACFAGGMFAL GADGSRADKA GHYLELGAEI ARTCHESYDR
510 520 530 540 550
TALKLGPESF KFDGAVEAVA VRQAEKYYIL RPEVIETYWY LWRFTHDPRY
560 570 580 590 600
RQWGWEAALA IEKYCRVNGG FSGVKDVYSS TPTHDDVQQS FFLAETLKYL
610 620 630 640
YLLFSGDDLL PLDHWVFNTE AHPLPVLHLA NTTLSGNPAV R
Length:641
Mass (Da):73,004
Last modified:August 1, 1998 - v1
Checksum:i19DA691A9C4B0ED3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053626
, AF053622, AF053623, AF053624, AF053625 Genomic DNA. Translation: AAC26201.1.
AF027156 mRNA. Translation: AAC26169.1.
AF053621
, 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.
CCDSiCCDS895.1.
RefSeqiNP_006690.1. NM_006699.3.
UniGeneiHs.435938.
Hs.602811.

Genome annotation databases

EnsembliENST00000356554; ENSP00000348959; ENSG00000198162.
GeneIDi10905.
KEGGihsa:10905.
UCSCiuc001ehd.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053626
, AF053622, AF053623, AF053624, AF053625 Genomic DNA. Translation: AAC26201.1.
AF027156 mRNA. Translation: AAC26169.1.
AF053621
, 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.
CCDSiCCDS895.1.
RefSeqiNP_006690.1. NM_006699.3.
UniGeneiHs.435938.
Hs.602811.

3D structure databases

ProteinModelPortaliO60476.
SMRiO60476. Positions 156-627.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116111. 5 interactions.
IntActiO60476. 4 interactions.
MINTiMINT-1184386.
STRINGi9606.ENSP00000348959.

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.

PTM databases

PhosphoSiteiO60476.

Polymorphism and mutation databases

BioMutaiMAN1A2.

Proteomic databases

MaxQBiO60476.
PaxDbiO60476.
PRIDEiO60476.

Protocols and materials databases

DNASUi10905.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356554; ENSP00000348959; ENSG00000198162.
GeneIDi10905.
KEGGihsa:10905.
UCSCiuc001ehd.1. human.

Organism-specific databases

CTDi10905.
GeneCardsiGC01P117910.
HGNCiHGNC:6822. MAN1A2.
HPAiHPA034559.
HPA057364.
MIMi604345. gene.
neXtProtiNX_O60476.
PharmGKBiPA30571.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300315.
GeneTreeiENSGT00390000016529.
HOGENOMiHOG000181988.
HOVERGENiHBG052389.
InParanoidiO60476.
KOiK01230.
OMAiRQYGWGH.
OrthoDBiEOG7X0VH1.
PhylomeDBiO60476.
TreeFamiTF313420.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi3.2.1.113. 2681.
ReactomeiREACT_25396. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.

Miscellaneous databases

ChiTaRSiMAN1A2. human.
GeneWikiiMAN1A2.
GenomeRNAii10905.
NextBioi41419.
PROiO60476.
SOURCEiSearch...

Gene expression databases

BgeeiO60476.
CleanExiHS_MAN1A2.
ExpressionAtlasiO60476. baseline and differential.
GenevisibleiO60476. HS.

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERiPTHR11742. PTHR11742. 1 hit.
PfamiPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMA1A2_HUMAN
AccessioniPrimary (citable) accession number: O60476
Secondary accession number(s): Q9H510
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: August 1, 1998
Last modified: June 24, 2015
This is version 136 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. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.