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O60476

- MA1A2_HUMAN

UniProt

O60476 - MA1A2_HUMAN

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Protein

Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB

Gene

MAN1A2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Calcium.

Enzyme regulationi

Inhibited by both 1-deoxymannojirimycin and kifunensine.

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. lung alveolus development Source: Ensembl
  3. N-glycan processing Source: ProtInc
  4. post-translational protein modification Source: Reactome
  5. protein N-linked glycosylation via asparagine Source: Reactome
  6. respiratory gaseous exchange Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium

Enzyme and pathway databases

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: Chromosome 1

Organism-specific databases

HGNCiHGNC:6822. MAN1A2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. Golgi apparatus Source: HPA
  3. Golgi membrane Source: Reactome
  4. integral component of membrane Source: ProtInc
  5. membrane Source: UniProtKB
  6. nucleolus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30571.

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.
GenevestigatoriO60476.

Organism-specific databases

HPAiHPA034559.

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...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 3635CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini58 – 641584LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei37 – 5721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

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.
OMAiDPEDNDI.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS895.1.
RefSeqi NP_006690.1. NM_006699.3.
UniGenei Hs.435938.
Hs.602811.

3D structure databases

ProteinModelPortali O60476.
SMRi O60476. Positions 156-627.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116111. 5 interactions.
IntActi O60476. 4 interactions.
MINTi MINT-1184386.
STRINGi 9606.ENSP00000348959.

Protein family/group databases

CAZyi GH47. Glycoside Hydrolase Family 47.

PTM databases

PhosphoSitei O60476.

Proteomic databases

MaxQBi O60476.
PaxDbi O60476.
PRIDEi O60476.

Protocols and materials databases

DNASUi 10905.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356554 ; ENSP00000348959 ; ENSG00000198162 .
GeneIDi 10905.
KEGGi hsa:10905.
UCSCi uc001ehd.1. human.

Organism-specific databases

CTDi 10905.
GeneCardsi GC01P117910.
HGNCi HGNC:6822. MAN1A2.
HPAi HPA034559.
MIMi 604345. gene.
neXtProti NX_O60476.
PharmGKBi PA30571.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300315.
GeneTreei ENSGT00390000016529.
HOGENOMi HOG000181988.
HOVERGENi HBG052389.
InParanoidi O60476.
KOi K01230.
OMAi DPEDNDI.
OrthoDBi EOG7X0VH1.
PhylomeDBi O60476.
TreeFami TF313420.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_25396. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.

Miscellaneous databases

ChiTaRSi MAN1A2. human.
GeneWikii MAN1A2.
GenomeRNAii 10905.
NextBioi 41419.
PROi O60476.
SOURCEi Search...

Gene expression databases

Bgeei O60476.
CleanExi HS_MAN1A2.
ExpressionAtlasi O60476. baseline and differential.
Genevestigatori O60476.

Family and domain databases

Gene3Di 1.50.10.50. 1 hit.
InterProi IPR001382. Glyco_hydro_47.
[Graphical view ]
PANTHERi PTHR11742. PTHR11742. 1 hit.
Pfami PF01532. Glyco_hydro_47. 1 hit.
[Graphical view ]
PRINTSi PR00747. GLYHDRLASE47.
SUPFAMi SSF48225. SSF48225. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 128 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