CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008127
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein ERGIC-53 
Protein Synonyms/Alias
 ER-Golgi intermediate compartment 53 kDa protein; Gp58; Intracellular mannose-specific lectin MR60; Lectin mannose-binding 1 
Gene Name
 LMAN1 
Gene Synonyms/Alias
 ERGIC53; F5F8D 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
49PHRRFEYKYSFKGPHubiquitination[1]
87IRVAPSLKSQRGSVWubiquitination[1]
346NRIHLEIKQLNRQLDubiquitination[1, 2, 3, 4, 5, 6]
372SLTEEISKRGAGMPGubiquitination[1, 2, 5, 6]
407LRQVNEMKNSMSETVubiquitination[1, 6]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] 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]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. 
Sequence Annotation
 DOMAIN 44 267 L-type lectin-like.
 REGION 251 253 Carbohydrate binding (By similarity).
 MOTIF 509 510 ER export motif.
 METAL 152 152 Calcium.
 METAL 154 154 Calcium; via carbonyl oxygen.
 METAL 156 156 Calcium.
 METAL 181 181 Calcium.
 BINDING 88 88 Carbohydrate (By similarity).
 BINDING 121 121 Carbohydrate (By similarity).
 BINDING 156 156 Carbohydrate (By similarity).
 BINDING 178 178 Carbohydrate (By similarity).
 DISULFID 190 230
 DISULFID 466 466 Interchain.
 DISULFID 475 475 Interchain.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Lectin; Membrane; Metal-binding; Polymorphism; Protein transport; Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 510 AA 
Protein Sequence
MAGSRQRGLR ARVRPLFCAL LLSLGRFVRG DGVGGDPAVA LPHRRFEYKY SFKGPHLVQS 60
DGTVPFWAHA GNAIPSSDQI RVAPSLKSQR GSVWTKTKAA FENWEVEVTF RVTGRGRIGA 120
DGLAIWYAEN QGLEGPVFGS ADLWNGVGIF FDSFDNDGKK NNPAIVIIGN NGQIHYDHQN 180
DGASQALASC QRDFRNKPYP VRAKITYYQN TLTVMINNGF TPDKNDYEFC AKVENMIIPA 240
QGHFGISAAT GGLADDHDVL SFLTFQLTEP GKEPPTPDKE ISEKEKEKYQ EEFEHFQQEL 300
DKKKEEFQKG HPDLQGQPAE EIFESVGDRE LRQVFEGQNR IHLEIKQLNR QLDMILDEQR 360
RYVSSLTEEI SKRGAGMPGQ HGQITQQELD TVVKTQHEIL RQVNEMKNSM SETVRLVSGM 420
QHPGSAGGVY ETTQHFIDIK EHLHIVKRDI DNLVQRNMPS NEKPKCPELP PFPSCLSTVH 480
FIIFVVVQTV LFIGYIMYRS QQEAAAKKFF 510 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; TAS:ProtInc.
 GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
 GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
 GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
 GO:0000139; C:Golgi membrane; TAS:ProtInc.
 GO:0016021; C:integral to membrane; TAS:ProtInc.
 GO:0030017; C:sarcomere; IEA:Compara.
 GO:0005537; F:mannose binding; TAS:ProtInc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0051082; F:unfolded protein binding; TAS:ProtInc.
 GO:0007596; P:blood coagulation; TAS:ProtInc.
 GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:ProtInc.
 GO:0007030; P:Golgi organization; IMP:UniProtKB.
 GO:0010638; P:positive regulation of organelle organization; IMP:UniProtKB.
 GO:0043687; P:post-translational protein modification; TAS:Reactome.
 GO:0006457; P:protein folding; TAS:ProtInc.
 GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW. 
Interpro
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR005052; Lectin_leg. 
Pfam
 PF03388; Lectin_leg-like 
SMART
  
PROSITE
 PS51328; L_LECTIN_LIKE 
PRINTS