CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001203
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Erlin-1 
Protein Synonyms/Alias
 Endoplasmic reticulum lipid raft-associated protein 1; Protein KE04; Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 1; SPFH domain-containing protein 1 
Gene Name
 ERLIN1 
Gene Synonyms/Alias
 C10orf69; KE04; KEO4; SPFH1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
113NYTADYDKTLIFNKIubiquitination[1]
154NLKQALQKDLNLMAPubiquitination[1, 2]
192LMEAEKTKLLIAAQKubiquitination[1]
199KLLIAAQKQKVVEKEubiquitination[3]
226EKIAQVAKIRFQQKVubiquitination[3]
257FLAREKAKADAEYYAubiquitination[3]
267AEYYAAHKYATSNKHacetylation[4]
267AEYYAAHKYATSNKHubiquitination[3]
328RESSLPSKEALEPSGubiquitination[1, 3]
342GENVIQNKESTG***ubiquitination[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] 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] 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]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). 
Sequence Annotation
 MOD_RES 267 267 N6-acetyllysine.
 CARBOHYD 106 106 N-linked (GlcNAc...).  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 346 AA 
Protein Sequence
MTQARVLVAA VVGLVAVLLY ASIHKIEEGH LAVYYRGGAL LTSPSGPGYH IMLPFITTFR 60
SVQTTLQTDE VKNVPCGTSG GVMIYIDRIE VVNMLAPYAV FDIVRNYTAD YDKTLIFNKI 120
HHELNQFCSA HTLQEVYIEL FDQIDENLKQ ALQKDLNLMA PGLTIQAVRV TKPKIPEAIR 180
RNFELMEAEK TKLLIAAQKQ KVVEKEAETE RKKAVIEAEK IAQVAKIRFQ QKVMEKETEK 240
RISEIEDAAF LAREKAKADA EYYAAHKYAT SNKHKLTPEY LELKKYQAIA SNSKIYFGSN 300
IPNMFVDSSC ALKYSDIRTG RESSLPSKEA LEPSGENVIQ NKESTG 346 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0043234; C:protein complex; IDA:MGI.
 GO:0030433; P:ER-associated protein catabolic process; IDA:UniProtKB. 
Interpro
 IPR001107; Band_7. 
Pfam
 PF01145; Band_7 
SMART
 SM00244; PHB 
PROSITE
  
PRINTS