CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024001
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Epsin-1 
Protein Synonyms/Alias
 EH domain-binding mitotic phosphoprotein; EPS-15-interacting protein 1 
Gene Name
 EPN1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
122SSLRRQMKNIVHNYSubiquitination[1, 2, 3]
134NYSEAEIKVREATSNubiquitination[3]
197TLMEYLIKTGSERVSubiquitination[1, 2, 3]
208ERVSQQCKENMYAVQubiquitination[1, 3]
218MYAVQTLKDFQYVDRubiquitination[1, 2, 3]
228QYVDRDGKDQGVNVRubiquitination[1, 2, 3]
239VNVREKAKQLVALLRubiquitination[1, 3]
332QMAIEESKRETGGKEubiquitination[1, 2]
555TPTPPTRKTPESFLGubiquitination[3]
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] 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] 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] 
Functional Description
 Binds to membranes enriched in phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis. 
Sequence Annotation
 DOMAIN 12 144 ENTH.
 REPEAT 183 202 UIM 1.
 REPEAT 208 227 UIM 2.
 REPEAT 233 252 UIM 3.
 REPEAT 274 276 1.
 REPEAT 294 296 2.
 REPEAT 306 308 3.
 REPEAT 319 321 4.
 REPEAT 332 334 5.
 REPEAT 349 351 6.
 REPEAT 367 369 7.
 REPEAT 377 379 8.
 REPEAT 502 504 1.
 REPEAT 518 520 2.
 REPEAT 572 574 3.
 REGION 274 379 8 X 3 AA repeats of [ED]-P-W.
 REGION 502 574 3 X 3 AA repeats of N-P-F.
 MOTIF 402 411 [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif.
 BINDING 8 8 Phosphatidylinositol lipid headgroup (By
 BINDING 11 11 Phosphatidylinositol lipid headgroup (By
 BINDING 25 25 Phosphatidylinositol lipid headgroup (By
 BINDING 30 30 Phosphatidylinositol lipid headgroup (By
 BINDING 63 63 Phosphatidylinositol lipid headgroup (By
 BINDING 73 73 Phosphatidylinositol lipid headgroup (By
 MOD_RES 382 382 Phosphoserine; by CDK1.
 MOD_RES 419 419 Phosphoserine.
 MOD_RES 420 420 Phosphoserine.
 MOD_RES 435 435 Phosphoserine.
 MOD_RES 454 454 Phosphoserine.
 MOD_RES 460 460 Phosphothreonine.
 MOD_RES 470 470 Phosphothreonine.
 MOD_RES 494 494 Phosphothreonine.  
Keyword
 3D-structure; Alternative splicing; Cell membrane; Coated pit; Complete proteome; Cytoplasm; Endocytosis; Lipid-binding; Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 576 AA 
Protein Sequence
MGDQSWLWNQ AAPGVRSPVF ACSVEKGNVP LVLSEHLAHS RDPGSGAVRF LISPEPWASA 60
ILGTSGLLAS PVLPAALDAV TCQHLPQPSS GSRPISPRIG ALCPLLLQPG TMSTSSLRRQ 120
MKNIVHNYSE AEIKVREATS NDPWGPSSSL MSEIADLTYN VVAFSEIMSM IWKRLNDHGK 180
NWRHVYKAMT LMEYLIKTGS ERVSQQCKEN MYAVQTLKDF QYVDRDGKDQ GVNVREKAKQ 240
LVALLRDEDR LREERAHALK TKEKLAQTAT ASSAAVGSGP PPEAEQAWPQ SSGEEELQLQ 300
LALAMSKEEA DQEERIRRGD DLRLQMAIEE SKRETGGKEE SSLMDLADVF TAPAPAPTTD 360
PWGGPAPMAA AVPTAAPTSD PWGGPPVPPA ADPWGGPAPT PASGDPWRPA APAGPSVDPW 420
GGTPAPAAGE GPTPDPWGSS DGGVPVSGPS ASDPWTPAPA FSDPWGGSPA KPSTNGTTAA 480
GGFDTEPDEF SDFDRLRTAL PTSGSSAGEL ELLAGEVPAR SPGAFDMSGV RGSLAEAVGS 540
PPPAATPTPT PPTRKTPESF LGPNAALVDL DSLVSRPGPT PPGAKASNPF LPGGGPATGP 600
SVTNPFQPAP PATLTLNQLR LSPVPPVPGA PPTYISPLGG GPGLPPMMPP GPPAPNTNPF 660
LL 662 
Gene Ontology
 GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
 GO:0048568; P:embryonic organ development; IEA:Compara.
 GO:0006897; P:endocytosis; TAS:ProtInc.
 GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0007565; P:female pregnancy; IEA:Compara.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0007219; P:Notch signaling pathway; IEA:Compara. 
Interpro
 IPR008942; ENTH_VHS.
 IPR027320; Epsin-1_mammalian.
 IPR013809; Epsin-like_N.
 IPR001026; Epsin_dom_N.
 IPR003903; Ubiquitin-int_motif. 
Pfam
 PF01417; ENTH
 PF02809; UIM 
SMART
 SM00273; ENTH
 SM00726; UIM 
PROSITE
 PS50942; ENTH
 PS50330; UIM 
PRINTS