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HUMAN:MA1B1

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) MAN1B1
Protein Name(s) Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase

ER alpha-1,2-mannosidase ER mannosidase 1 ERMan1 Man9GlcNAc2-specific-processing alpha-mannosidase Mannosidase alpha class 1B member 1

External Links
UniProt Q9UKM7
EMBL AF148509
AF145732
AY358465
AL929554
AL807752
AL807752
AL929554
BC002953
BC006079
CCDS CCDS7029.1
RefSeq NP_057303.2
UniGene Hs.279881
PDB 1FMI
1FO2
1FO3
1X9D
PDBsum 1FMI
1FO2
1FO3
1X9D
ProteinModelPortal Q9UKM7
SMR Q9UKM7
BioGrid 116414
IntAct Q9UKM7
MINT MINT-6610355
STRING 9606.ENSP00000360645
BindingDB Q9UKM7
ChEMBL CHEMBL2308
CAZy GH47
PhosphoSite Q9UKM7
DMDM 93195043
MaxQB Q9UKM7
PaxDb Q9UKM7
PRIDE Q9UKM7
DNASU 11253
Ensembl ENST00000371589
GeneID 11253
KEGG hsa:11253
UCSC uc004cld.3
CTD 11253
GeneCards GC09P139981
H-InvDB HIX0035043
HGNC HGNC:6823
HPA HPA051516
MIM 604346
614202
neXtProt NX_Q9UKM7
Orphanet 88616
397941
PharmGKB PA30572
eggNOG NOG300315
GeneTree ENSGT00390000016529
HOGENOM HOG000181987
HOVERGEN HBG052389
InParanoid Q9UKM7
KO K01230
OMA KEFAWGH
OrthoDB EOG7ZGX2S
PhylomeDB Q9UKM7
TreeFam TF354274
BRENDA 3.2.1.113
Reactome REACT_25091
UniPathway UPA00378
ChiTaRS MAN1B1
EvolutionaryTrace Q9UKM7
GeneWiki MAN1B1
GenomeRNAi 11253
NextBio 42822
PRO PR:Q9UKM7
Proteomes UP000005640
Bgee Q9UKM7
CleanEx HS_MAN1B1
ExpressionAtlas Q9UKM7
Genevestigator Q9UKM7
GO GO:0005783
GO:0005789
GO:0044322
GO:0016021
GO:0016020
GO:0031982
GO:0005509
GO:0004571
GO:0044267
GO:0030433
GO:0009311
GO:0043687
GO:0006457
GO:0006487
GO:0018279
Gene3D 1.50.10.50
InterPro IPR001382
PANTHER PTHR11742
Pfam PF01532
PRINTS PR00747
SUPFAM SSF48225

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0036509

trimming of terminal mannose on B branch

PMID:10521544[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1904382

mannose trimming involved in glycoprotein ERAD pathway

PMID:21062743[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

occurs_in:(GO:0005783)

Seeded From UniProt

complete

involved_in

GO:0036509

trimming of terminal mannose on B branch

PMID:18003979[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1904380

endoplasmic reticulum mannose trimming

PMID:18003979[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1904382

mannose trimming involved in glycoprotein ERAD pathway

PMID:18003979[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

occurs_in:(GO:0044322)

Seeded From UniProt

complete

part_of

GO:0044322

endoplasmic reticulum quality control compartment

PMID:18003979[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004571

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity

PMID:18003979[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

part_of:(GO:0097466)

Seeded From UniProt

complete

enables

GO:0004571

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity

PMID:22160784[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0036508

protein alpha-1,2-demannosylation

PMID:22160784[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:1903561

extracellular vesicle

PMID:24769233[5]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001359)

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:19946888[6]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0036508

protein alpha-1,2-demannosylation

PMID:10521544[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004571

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity

PMID:10521544[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0030433

ubiquitin-dependent ERAD pathway

PMID:18003979[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:18003979[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0036508

protein alpha-1,2-demannosylation

PMID:10521544[1]

ECO:0000303

author statement without traceable support used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

PMID:18003979[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004571

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity

PMID:12090241[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0030433

ubiquitin-dependent ERAD pathway

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:2684954
PANTHER:PTN002482736
PomBase:SPAC2E1P5.01c
SGD:S000003892
UniProtKB:Q9UKM7

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002482736
UniProtKB:A0A1D8PD38
UniProtKB:Q9UKM7

C

Seeded From UniProt

complete

involved_in

GO:0006491

N-glycan processing

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000201533
TAIR:locus:2017597
TAIR:locus:2092965
TAIR:locus:2198299
UniProtKB:A0A1D8PD38

P

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000201533
SGD:S000003892
SGD:S000004047
UniProtKB:A0A1D8PD38
UniProtKB:Q9UKM7

C

Seeded From UniProt

complete

enables

GO:0004571

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0259170
MGI:MGI:2684954
PANTHER:PTN000201533
PomBase:SPAC2E1P5.01c
SGD:S000003892
UniProtKB:A0A1D5PBZ7
UniProtKB:A0A1D8PD38
UniProtKB:Q9UKM7

F

Seeded From UniProt

complete

involved_in

GO:0030433

ubiquitin-dependent ERAD pathway

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:A2AJ15
ensembl:ENSMUSP00000036996

P

Seeded From UniProt

complete

enables

GO:0004571

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:A2AJ15
ensembl:ENSMUSP00000036996

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012341

F

Seeded From UniProt

complete

enables

GO:0004571

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001382
InterPro:IPR036026

F

Seeded From UniProt

complete

enables

GO:0005509

calcium ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001382
InterPro:IPR036026

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001382
InterPro:IPR036026

C

Seeded From UniProt

complete

enables

GO:0004571

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.2.1.113

F

Seeded From UniProt

complete

part_of

GO:0044322

endoplasmic reticulum quality control compartment

PMID:21062743[2]
Reactome:R-HSA-901074
Reactome:R-HSA-901039
Reactome:R-HSA-901036
Reactome:R-HSA-901024

ECO:0000304

author statement supported by traceable reference used in manual assertion





C

Seeded From UniProt

complete

part_of

GO:0005794

Golgi apparatus

PMID:22160784[4]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

PMID:22160784[4]
PMID:10409699[9]

ECO:0000304

author statement supported by traceable reference used in manual assertion


C

Seeded From UniProt

complete

involved_in

GO:1904382

mannose trimming involved in glycoprotein ERAD pathway

PMID:22160784[4]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009311

oligosaccharide metabolic process

PMID:10409699[9]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004571

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity

PMID:10409699[9]
PMID:10521544[1]

ECO:0000304

author statement supported by traceable reference used in manual assertion


F

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

PMID:10521544[1]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005509

calcium ion binding

PMID:10521544[1]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0036512

trimming of second mannose on A branch

Reactome:R-HSA-901036

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0036511

trimming of first mannose on A branch

Reactome:R-HSA-901024

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0036510

trimming of terminal mannose on C branch

Reactome:R-HSA-901039

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0036509

trimming of terminal mannose on B branch

Reactome:R-HSA-901074

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326

P

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0256

C

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016798

hydrolase activity, acting on glycosyl bonds

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326

F

Seeded From UniProt

complete

part_of

GO:0005789

endoplasmic reticulum membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0097

C

Seeded From UniProt

complete

involved_in

GO:0006486

protein glycosylation

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00378

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Tremblay, LO & Herscovics, A (1999) Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis. Glycobiology 9 1073-8 PubMed GONUTS page
  2. 2.0 2.1 Groisman, B et al. (2011) Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps. J. Biol. Chem. 286 1292-300 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 3.5 3.6 3.7 Avezov, E et al. (2008) Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation. Mol. Biol. Cell 19 216-25 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 4.4 Aikawa, J et al. (2012) In vitro mannose trimming property of human ER α-1,2 mannosidase I. Glycoconj. J. 29 35-45 PubMed GONUTS page
  5. Chiasserini, D et al. (2014) Proteomic analysis of cerebrospinal fluid extracellular vesicles: a comprehensive dataset. J Proteomics 106 191-204 PubMed GONUTS page
  6. Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
  7. Herscovics, A et al. (2002) The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported. Glycobiology 12 14G-15G PubMed GONUTS page
  8. 8.0 8.1 8.2 8.3 8.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  9. 9.0 9.1 9.2 Gonzalez, DS et al. (1999) Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis. J. Biol. Chem. 274 21375-86 PubMed GONUTS page