CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023103
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase 
Protein Synonyms/Alias
 ER alpha-1,2-mannosidase; ER mannosidase 1; ERMan1; Man9GlcNAc2-specific-processing alpha-mannosidase; Mannosidase alpha class 1B member 1 
Gene Name
 MAN1B1 
Gene Synonyms/Alias
 UNQ747/PRO1477 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
156LPEISSQKTQRHIQRubiquitination[1]
371PAFRTPSKIPYSDVNubiquitination[1]
478KQWIQGGKQETQLLEubiquitination[1, 2]
588GRRDVEVKPADRHNLubiquitination[1]
649NNVQDPQKPEPRDKMubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2). 
Sequence Annotation
 ACT_SITE 330 330 Proton donor (Probable).
 ACT_SITE 463 463 Probable.
 ACT_SITE 599 599 Probable.
 DISULFID 527 556  
Keyword
 3D-structure; Calcium; Complete proteome; Disease mutation; Disulfide bond; Endoplasmic reticulum; Glycosidase; Hydrolase; Membrane; Mental retardation; Polymorphism; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 699 AA 
Protein Sequence
MAACEGRRSG ALGSSQSDFL TPPVGGAPWA VATTVVMYPP PPPPPHRDFI SVTLSFGENY 60
DNSKSWRRRS CWRKWKQLSR LQRNMILFLL AFLLFCGLLF YINLADHWKA LAFRLEEEQK 120
MRPEIAGLKP ANPPVLPAPQ KADTDPENLP EISSQKTQRH IQRGPPHLQI RPPSQDLKDG 180
TQEEATKRQE APVDPRPEGD PQRTVISWRG AVIEPEQGTE LPSRRAEVPT KPPLPPARTQ 240
GTPVHLNYRQ KGVIDVFLHA WKGYRKFAWG HDELKPVSRS FSEWFGLGLT LIDALDTMWI 300
LGLRKEFEEA RKWVSKKLHF EKDVDVNLFE STIRILGGLL SAYHLSGDSL FLRKAEDFGN 360
RLMPAFRTPS KIPYSDVNIG TGVAHPPRWT SDSTVAEVTS IQLEFRELSR LTGDKKFQEA 420
VEKVTQHIHG LSGKKDGLVP MFINTHSGLF THLGVFTLGA RADSYYEYLL KQWIQGGKQE 480
TQLLEDYVEA IEGVRTHLLR HSEPSKLTFV GELAHGRFSA KMDHLVCFLP GTLALGVYHG 540
LPASHMELAQ ELMETCYQMN RQMETGLSPE IVHFNLYPQP GRRDVEVKPA DRHNLLRPET 600
VESLFYLYRV TGDRKYQDWG WEILQSFSRF TRVPSGGYSS INNVQDPQKP EPRDKMESFF 660
LGETLKYLFL LFSDDPNLLS LDAYVFNTEA HPLPIWTPA 699 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0044322; C:endoplasmic reticulum quality control compartment; TAS:Reactome.
 GO:0016021; C:integral to membrane; TAS:UniProtKB.
 GO:0005509; F:calcium ion binding; TAS:UniProtKB.
 GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IDA:UniProtKB.
 GO:0030433; P:ER-associated protein catabolic process; IMP:UniProtKB.
 GO:0009311; P:oligosaccharide metabolic process; TAS:ProtInc.
 GO:0043687; P:post-translational protein modification; TAS:Reactome.
 GO:0006457; P:protein folding; TAS:Reactome.
 GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome. 
Interpro
 IPR001382; Glyco_hydro_47. 
Pfam
 PF01532; Glyco_hydro_47 
SMART
  
PROSITE
  
PRINTS
 PR00747; GLYHDRLASE47.