CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012363
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Clathrin interactor 1 
Protein Synonyms/Alias
 Clathrin-interacting protein localized in the trans-Golgi region; Clint; Enthoprotin; Epsin-4; Epsin-related protein; EpsinR 
Gene Name
 CLINT1 
Gene Synonyms/Alias
 ENTH; EPN4; EPNR; KIAA0171 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MLNMWKVRELVDKubiquitination[1, 2]
13KVRELVDKATNVVMNubiquitination[3, 4]
122HFVDEHGKDQGINIRubiquitination[2, 4, 5, 6]
133INIRQKVKELVEFAQubiquitination[4]
156RKKAKKNKDKYVGVSubiquitination[2, 4]
158KAKKNKDKYVGVSSDubiquitination[2, 4, 7]
181ERYDPEPKSKWDEEWubiquitination[2]
183YDPEPKSKWDEEWDKubiquitination[1, 2, 4, 5, 6, 7]
190KWDEEWDKNKSAFPFubiquitination[1, 2, 3, 4, 6]
192DEEWDKNKSAFPFSDubiquitination[2, 3, 4, 6]
200SAFPFSDKLGELSDKubiquitination[2, 3, 4, 5, 6, 7]
207KLGELSDKIGSTIDDubiquitination[1, 2, 3, 4, 5, 6]
218TIDDTISKFRRKDREubiquitination[1, 2, 3, 4, 5, 6, 7]
247ARRGRSPKGEFKDEEubiquitination[2, 3, 4, 5, 6]
251RSPKGEFKDEEETVTubiquitination[2, 3]
260EEETVTTKHIHITQAubiquitination[5]
283KRTANPSKTIDLGAAacetylation[4, 8]
283KRTANPSKTIDLGAAubiquitination[2, 4, 5]
297AAHYTGDKASPDQNAubiquitination[1, 2, 3, 4, 5]
314HTPQSSVKTSVPSSKubiquitination[1, 2, 3]
467QNTDMVQKSVSKTLPubiquitination[1, 2, 3, 6, 7]
471MVQKSVSKTLPSTWSubiquitination[1, 3, 7]
625ANFANFSK*******ubiquitination[3, 4, 9]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] 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
 Binds to membranes enriched in phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly. 
Sequence Annotation
 DOMAIN 16 149 ENTH.
 BINDING 29 29 Phosphatidylinositol lipid headgroup (By
 BINDING 67 67 Phosphatidylinositol lipid headgroup (By
 MOD_RES 163 163 Phosphoserine (By similarity).
 MOD_RES 227 227 Phosphoserine.
 MOD_RES 232 232 Phosphoserine (By similarity).
 MOD_RES 234 234 Phosphoserine (By similarity).
 MOD_RES 245 245 Phosphoserine.
 MOD_RES 299 299 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Endocytosis; Lipid-binding; Membrane; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 625 AA 
Protein Sequence
MLNMWKVREL VDKATNVVMN YSEIESKVRE ATNDDPWGPS GQLMGEIAKA TFMYEQFPEL 60
MNMLWSRMLK DNKKNWRRVY KSLLLLAYLI RNGSERVVTS AREHIYDLRS LENYHFVDEH 120
GKDQGINIRQ KVKELVEFAQ DDDRLREERK KAKKNKDKYV GVSSDSVGGF RYSERYDPEP 180
KSKWDEEWDK NKSAFPFSDK LGELSDKIGS TIDDTISKFR RKDREDSPER CSDSDEEKKA 240
RRGRSPKGEF KDEEETVTTK HIHITQATET TTTRHKRTAN PSKTIDLGAA AHYTGDKASP 300
DQNASTHTPQ SSVKTSVPSS KSSGDLVDLF DGTSQSTGGS ADLFGGFADF GSAAASGSFP 360
SQVTATSGNG DFGDWSAFNQ APSGPVASSG EFFGSASQPA VELVSGSQSA LGPPPAASNS 420
SDLFDLMGSS QATMTSSQSM NFSMMSTNTV GLGLPMSRSQ NTDMVQKSVS KTLPSTWSDP 480
SVNISLDNLL PGMQPSKPQQ PSLNTMIQQQ NMQQPMNVMT QSFGAVNLSS PSNMLPVRPQ 540
TNALIGGPMP MSMPNVMTGT MGMAPLGNTP MMNQSMMGMN MNIGMSAAGM GLTGTMGMGM 600
PNIAMTSGTV QPKQDAFANF ANFSK 625 
Gene Ontology
 GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
 GO:0016044; P:cellular membrane organization; TAS:Reactome.
 GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
 GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome. 
Interpro
 IPR008942; ENTH_VHS.
 IPR013809; Epsin-like_N.
 IPR001026; Epsin_dom_N. 
Pfam
 PF01417; ENTH 
SMART
 SM00273; ENTH 
PROSITE
 PS50942; ENTH 
PRINTS