CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015884
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Endoplasmic reticulum metallopeptidase 1 
Protein Synonyms/Alias
 Felix-ina 
Gene Name
 ERMP1 
Gene Synonyms/Alias
 FXNA; KIAA1815 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
356NGYIYHTKYDTADRIubiquitination[1]
380DNILAVLKHLATSDMubiquitination[1, 2]
393DMLAAASKYRHGNMVubiquitination[1, 2]
704DLEGNAVKRDSGIWIubiquitination[1, 2, 3]
758PVHFLIRKNWYLPAPubiquitination[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] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [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] 
Functional Description
 Within the ovary, required for the organization of somatic cells and oocytes into discrete follicular structures (By similarity). 
Sequence Annotation
 ACT_SITE 207 207 By similarity.
 ACT_SITE 251 251 By similarity.
 METAL 205 205 Zinc 2 (By similarity).
 METAL 217 217 Zinc 1 (By similarity).
 METAL 217 217 Zinc 2 (By similarity).
 METAL 252 252 Zinc 1 (By similarity).
 METAL 278 278 Zinc 2 (By similarity).
 METAL 354 354 Zinc 1 (By similarity).
 CARBOHYD 182 182 N-linked (GlcNAc...) (Potential).
 CARBOHYD 730 730 N-linked (GlcNAc...).
 DISULFID 204 222 By similarity.  
Keyword
 Complete proteome; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; Polymorphism; Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 904 AA 
Protein Sequence
MEWGSESAAV RRHRVGVERR EGAAAAPPPE REARAQEPLV DGCSGGGRTR KRSPGGSGGA 60
SRGAGTGLSE VRAALGLALY LIALRTLVQL SLQQLVLRGA AGHRGEFDAL QARDYLEHIT 120
SIGPRTTGSP ENEILTVHYL LEQIKLIEVQ SNSLHKISVD VQRPTGSFSI DFLGGFTSYY 180
DNITNVVVKL EPRDGAQHAV LANCHFDSVA NSPGASDDAV SCSVMLEVLR VLSTSSEALH 240
HAVIFLFNGA EENVLQASHG FITQHPWASL IRAFINLEAA GVGGKELVFQ TGPENPWLVQ 300
AYVSAAKHPF ASVVAQEVFQ SGIIPSDTDF RIYRDFGNIP GIDLAFIENG YIYHTKYDTA 360
DRILTDSIQR AGDNILAVLK HLATSDMLAA ASKYRHGNMV FFDVLGLFVI AYPSRIGSII 420
NYMVVMGVVL YLGKKFLQPK HKTGNYKKDF LCGLGITLIS WFTSLVTVLI IAVFISLIGQ 480
SLSWYNHFYV SVCLYGTATV AKIILIHTLA KRFYYMNASA QYLGEVFFDI SLFVHCCFLV 540
TLTYQGLCSA FISAVWVAFP LLTKLCVHKD FKQHGAQGKF IAFYLLGMFI PYLYALYLIW 600
AVFEMFTPIL GRSGSEIPPD VVLASILAGC TMILSSYFIN FIYLAKSTKK TMLTLTLVCA 660
ITFLLVCSGT FFPYSSNPAN PKPKRVFLQH MTRTFHDLEG NAVKRDSGIW INGFDYTGIS 720
HITPHIPEIN DSIRAHCEEN APLCGFPWYL PVHFLIRKNW YLPAPEVSPR NPPHFRLISK 780
EQTPWDSIKL TFEATGPSHM SFYVRAHKGS TLSQWSLGNG TPVTSKGGDY FVFYSHGLQA 840
SAWQFWIEVQ VSEEHPEGMV TVAIAAHYLS GEDKRSPQLD ALKEKFPDWT FPSAWVCTYD 900
LFVF 904 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR007484; Peptidase_M28. 
Pfam
 PF04389; Peptidase_M28 
SMART
  
PROSITE
  
PRINTS