EPN4_HUMAN - dbPTM
EPN4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPN4_HUMAN
UniProt AC Q14677
Protein Name Clathrin interactor 1
Gene Name CLINT1
Organism Homo sapiens (Human).
Sequence Length 625
Subcellular Localization Cytoplasm. Cytoplasm, perinuclear region. Membrane
Peripheral membrane protein. Cytoplasmic vesicle, clathrin-coated vesicle. Found throughout the cell, with the exception of the cell surface. Concentrated in the perinuclear region and associated wi
Protein 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..
Protein Sequence MLNMWKVRELVDKATNVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREERKKAKKNKDKYVGVSSDSVGGFRYSERYDPEPKSKWDEEWDKNKSAFPFSDKLGELSDKIGSTIDDTISKFRRKDREDSPERCSDSDEEKKARRGRSPKGEFKDEEETVTTKHIHITQATETTTTRHKRTANPSKTIDLGAAAHYTGDKASPDQNASTHTPQSSVKTSVPSSKSSGDLVDLFDGTSQSTGGSADLFGGFADFGSAAASGSFPSQVTATSGNGDFGDWSAFNQAPSGPVASSGEFFGSASQPAVELVSGSQSALGPPPAASNSSDLFDLMGSSQATMTSSQSMNFSMMSTNTVGLGLPMSRSQNTDMVQKSVSKTLPSTWSDPSVNISLDNLLPGMQPSKPQQPSLNTMIQQQNMQQPMNVMTQSFGAVNLSSPSNMLPVRPQTNALIGGPMPMSMPNVMTGTMGMAPLGNTPMMNQSMMGMNMNIGMSAAGMGLTGTMGMGMPNIAMTSGTVQPKQDAFANFANFSK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
6Ubiquitination--MLNMWKVRELVDK
--CCCHHHHHHHHHH		22.20-
13UbiquitinationKVRELVDKATNVVMN
HHHHHHHHHHCEECC		50.0221906983
13 (in isoform 1)Ubiquitination-50.0221890473
15PhosphorylationRELVDKATNVVMNYS
HHHHHHHHCEECCHH		34.0020068231
19SulfoxidationDKATNVVMNYSEIES
HHHHCEECCHHHHHH		3.2030846556
21PhosphorylationATNVVMNYSEIESKV
HHCEECCHHHHHHHH		6.9225219547
22PhosphorylationTNVVMNYSEIESKVR
HCEECCHHHHHHHHH		27.3925219547
26PhosphorylationMNYSEIESKVREATN
CCHHHHHHHHHHHHC		41.9525219547
27UbiquitinationNYSEIESKVREATND
CHHHHHHHHHHHHCC		32.30-
82PhosphorylationNWRRVYKSLLLLAYL
HHHHHHHHHHHHHHH		13.43-
94PhosphorylationAYLIRNGSERVVTSA
HHHHHCCCCEEEECH		26.27-
104 (in isoform 2)Ubiquitination-20.53-
106PhosphorylationTSAREHIYDLRSLEN
ECHHHHHHCHHHCCC		15.72-
109MethylationREHIYDLRSLENYHF
HHHHHCHHHCCCCEE		35.98-
110PhosphorylationEHIYDLRSLENYHFV
HHHHCHHHCCCCEEE		47.5420873877
114PhosphorylationDLRSLENYHFVDEHG
CHHHCCCCEEECCCC		6.30-
122UbiquitinationHFVDEHGKDQGINIR
EEECCCCCCCCCCHH		49.11-
133UbiquitinationINIRQKVKELVEFAQ
CCHHHHHHHHHHHHH		52.98-
140 (in isoform 2)Ubiquitination-61.0521890473
156MalonylationRKKAKKNKDKYVGVS
HHHHHHCCCCCCCCC		65.5626320211
156UbiquitinationRKKAKKNKDKYVGVS
HHHHHHCCCCCCCCC		65.56-
156 (in isoform 3)Malonylation-65.5626320211
158UbiquitinationKAKKNKDKYVGVSSD
HHHHCCCCCCCCCCC		43.3721890473
158UbiquitinationKAKKNKDKYVGVSSD
HHHHCCCCCCCCCCC		43.3721890473
158 (in isoform 1)Ubiquitination-43.3721890473
158 (in isoform 3)Ubiquitination-43.37-
159PhosphorylationAKKNKDKYVGVSSDS
HHHCCCCCCCCCCCC		16.7525159151
163PhosphorylationKDKYVGVSSDSVGGF
CCCCCCCCCCCCCCC		23.6225159151
164PhosphorylationDKYVGVSSDSVGGFR
CCCCCCCCCCCCCCC		31.3423401153
165 (in isoform 2)Ubiquitination-39.5821890473
166PhosphorylationYVGVSSDSVGGFRYS
CCCCCCCCCCCCCCC		25.3028355574
172PhosphorylationDSVGGFRYSERYDPE
CCCCCCCCCCCCCCC		16.7826434776
172 (in isoform 2)Ubiquitination-16.7821890473
173PhosphorylationSVGGFRYSERYDPEP
CCCCCCCCCCCCCCC		16.0228857561
174 (in isoform 2)Ubiquitination-46.45-
176PhosphorylationGFRYSERYDPEPKSK
CCCCCCCCCCCCCCC		31.6223312004
181UbiquitinationERYDPEPKSKWDEEW
CCCCCCCCCCCCHHH		64.11-
182PhosphorylationRYDPEPKSKWDEEWD
CCCCCCCCCCCHHHH		50.0924719451
182 (in isoform 2)Ubiquitination-50.0921890473
183UbiquitinationYDPEPKSKWDEEWDK
CCCCCCCCCCHHHHH		65.8621890473
183UbiquitinationYDPEPKSKWDEEWDK
CCCCCCCCCCHHHHH		65.8621890473
183 (in isoform 1)Ubiquitination-65.8621890473
183 (in isoform 3)Ubiquitination-65.86-
189 (in isoform 2)Ubiquitination-48.1821890473
190UbiquitinationKWDEEWDKNKSAFPF
CCCHHHHHCCCCCCH		68.311906983
190 (in isoform 1)Ubiquitination-68.3121890473
192UbiquitinationDEEWDKNKSAFPFSD
CHHHHHCCCCCCHHH		49.23-
193PhosphorylationEEWDKNKSAFPFSDK
HHHHHCCCCCCHHHH		44.5328555341
200UbiquitinationSAFPFSDKLGELSDK
CCCCHHHHHHHHHHH		58.1321890473
2002-HydroxyisobutyrylationSAFPFSDKLGELSDK
CCCCHHHHHHHHHHH		58.13-
200AcetylationSAFPFSDKLGELSDK
CCCCHHHHHHHHHHH		58.1325953088
200UbiquitinationSAFPFSDKLGELSDK
CCCCHHHHHHHHHHH		58.1321890473
200 (in isoform 1)Ubiquitination-58.1321890473
200 (in isoform 2)Ubiquitination-58.1321890473
200 (in isoform 3)Ubiquitination-58.13-
205PhosphorylationSDKLGELSDKIGSTI
HHHHHHHHHHHCCCH		32.3326657352
207AcetylationKLGELSDKIGSTIDD
HHHHHHHHHCCCHHH		45.6625953088
207UbiquitinationKLGELSDKIGSTIDD
HHHHHHHHHCCCHHH		45.6621906983
207 (in isoform 1)Ubiquitination-45.6621890473
210PhosphorylationELSDKIGSTIDDTIS
HHHHHHCCCHHHHHH		26.1825159151
211PhosphorylationLSDKIGSTIDDTISK
HHHHHCCCHHHHHHH		24.1829255136
215PhosphorylationIGSTIDDTISKFRRK
HCCCHHHHHHHHHHH		24.3329255136
217PhosphorylationSTIDDTISKFRRKDR
CCHHHHHHHHHHHCC		28.0329255136
218UbiquitinationTIDDTISKFRRKDRE
CHHHHHHHHHHHCCC		38.7521890473
218AcetylationTIDDTISKFRRKDRE
CHHHHHHHHHHHCCC		38.7525953088
218UbiquitinationTIDDTISKFRRKDRE
CHHHHHHHHHHHCCC		38.7521890473
218 (in isoform 1)Ubiquitination-38.7521890473
218 (in isoform 3)Ubiquitination-38.75-
227PhosphorylationRRKDREDSPERCSDS
HHHCCCCCCCCCCCC		24.7328355574
229 (in isoform 2)Ubiquitination-70.9821890473
232PhosphorylationEDSPERCSDSDEEKK
CCCCCCCCCCHHHHH		46.5025159151
233 (in isoform 2)Ubiquitination-64.8321890473
234PhosphorylationSPERCSDSDEEKKAR
CCCCCCCCHHHHHHH		30.5425159151
245PhosphorylationKKARRGRSPKGEFKD
HHHHCCCCCCCCCCC		33.5123401153
247UbiquitinationARRGRSPKGEFKDEE
HHCCCCCCCCCCCCC		72.7721906983
247 (in isoform 1)Ubiquitination-72.7721890473
251AcetylationRSPKGEFKDEEETVT
CCCCCCCCCCCCCEE		60.9925953088
251UbiquitinationRSPKGEFKDEEETVT
CCCCCCCCCCCCCEE		60.9921906983
251 (in isoform 1)Ubiquitination-60.9921890473
256PhosphorylationEFKDEEETVTTKHIH
CCCCCCCCEEEEEEE		26.8220068231
258PhosphorylationKDEEETVTTKHIHIT
CCCCCCEEEEEEEEE		37.2326074081
259PhosphorylationDEEETVTTKHIHITQ
CCCCCEEEEEEEEEE		19.1126074081
260UbiquitinationEEETVTTKHIHITQA
CCCCEEEEEEEEEEC		31.06-
265PhosphorylationTTKHIHITQATETTT
EEEEEEEEECCCCCC		9.6621406692
268PhosphorylationHIHITQATETTTTRH
EEEEEECCCCCCCCC		24.8521406692
270PhosphorylationHITQATETTTTRHKR
EEEECCCCCCCCCCC		25.7021406692
271PhosphorylationITQATETTTTRHKRT
EEECCCCCCCCCCCC		21.6721406692
272PhosphorylationTQATETTTTRHKRTA
EECCCCCCCCCCCCC		29.2921406692
273PhosphorylationQATETTTTRHKRTAN
ECCCCCCCCCCCCCC		28.7821406692
278PhosphorylationTTTRHKRTANPSKTI
CCCCCCCCCCCCCCE		35.2729978859
279 (in isoform 2)Ubiquitination-29.9321890473
282PhosphorylationHKRTANPSKTIDLGA
CCCCCCCCCCEEECC		42.0929978859
283AcetylationKRTANPSKTIDLGAA
CCCCCCCCCEEECCC		51.2423954790
283UbiquitinationKRTANPSKTIDLGAA
CCCCCCCCCEEECCC		51.24-
284PhosphorylationRTANPSKTIDLGAAA
CCCCCCCCEEECCCC		24.8621945579
293PhosphorylationDLGAAAHYTGDKASP
EECCCCHHCCCCCCC		14.0022167270
294PhosphorylationLGAAAHYTGDKASPD
ECCCCHHCCCCCCCC		29.1022167270
296 (in isoform 2)Ubiquitination-35.23-
297AcetylationAAHYTGDKASPDQNA
CCHHCCCCCCCCCCC		52.7025953088
297UbiquitinationAAHYTGDKASPDQNA
CCHHCCCCCCCCCCC		52.7021906983
297 (in isoform 1)Ubiquitination-52.7021890473
299PhosphorylationHYTGDKASPDQNAST
HHCCCCCCCCCCCCC		34.4529255136
305PhosphorylationASPDQNASTHTPQSS
CCCCCCCCCCCCCHH		28.4229255136
306PhosphorylationSPDQNASTHTPQSSV
CCCCCCCCCCCCHHH		27.6229255136
308PhosphorylationDQNASTHTPQSSVKT
CCCCCCCCCCHHHCC		24.1029255136
311PhosphorylationASTHTPQSSVKTSVP
CCCCCCCHHHCCCCC		38.0023401153
312PhosphorylationSTHTPQSSVKTSVPS
CCCCCCHHHCCCCCC		23.5323401153
314UbiquitinationHTPQSSVKTSVPSSK
CCCCHHHCCCCCCCC		36.71-
315PhosphorylationTPQSSVKTSVPSSKS
CCCHHHCCCCCCCCC		32.5726074081
316PhosphorylationPQSSVKTSVPSSKSS
CCHHHCCCCCCCCCC		26.7226074081
319PhosphorylationSVKTSVPSSKSSGDL
HHCCCCCCCCCCCCC		48.5226074081
320PhosphorylationVKTSVPSSKSSGDLV
HCCCCCCCCCCCCCE		30.4126074081
322PhosphorylationTSVPSSKSSGDLVDL
CCCCCCCCCCCCEEC		41.3126074081
323PhosphorylationSVPSSKSSGDLVDLF
CCCCCCCCCCCEECC		39.8126074081
441 (in isoform 2)Phosphorylation-30.9625849741
449PhosphorylationFSMMSTNTVGLGLPM
EEECCCCCCCCCCCC		18.95-
453 (in isoform 2)Ubiquitination-23.0821890473
457PhosphorylationVGLGLPMSRSQNTDM
CCCCCCCCCCCCCHH		27.17-
458 (in isoform 2)Phosphorylation-35.69-
459PhosphorylationLGLPMSRSQNTDMVQ
CCCCCCCCCCCHHHH		22.0726657352
459 (in isoform 3)Phosphorylation-22.0725849741
462PhosphorylationPMSRSQNTDMVQKSV
CCCCCCCCHHHHHHH		20.1728634120
462 (in isoform 2)Phosphorylation-20.17-
467AcetylationQNTDMVQKSVSKTLP
CCCHHHHHHHHHCCC		41.2225953088
467UbiquitinationQNTDMVQKSVSKTLP
CCCHHHHHHHHHCCC		41.222189047
467 (in isoform 2)Ubiquitination-41.2221890473
468PhosphorylationNTDMVQKSVSKTLPS
CCHHHHHHHHHCCCC		17.9621712546
471UbiquitinationMVQKSVSKTLPSTWS
HHHHHHHHCCCCCCC		52.5021890473
471UbiquitinationMVQKSVSKTLPSTWS
HHHHHHHHCCCCCCC		52.50-
471 (in isoform 1)Ubiquitination-52.5021890473
471 (in isoform 2)Ubiquitination-52.50-
471 (in isoform 3)Ubiquitination-52.50-
476 (in isoform 3)Phosphorylation-27.35-
480 (in isoform 3)Phosphorylation-34.36-
485UbiquitinationSDPSVNISLDNLLPG
CCCCCCEEHHHCCCC		25.1921890473
485 (in isoform 1)Ubiquitination-25.1921890473
485 (in isoform 3)Ubiquitination-25.19-
538DimethylationPSNMLPVRPQTNALI
CCCCCCCCCCCCCCC		18.70-
538MethylationPSNMLPVRPQTNALI
CCCCCCCCCCCCCCC		18.70-
624PhosphorylationFANFANFSK------
HHHHCCCCC------		36.9425159151
625AcetylationANFANFSK-------
HHHCCCCC-------		61.2971039
625UbiquitinationANFANFSK-------
HHHCCCCC-------		61.29-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of EPN4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPN4_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of EPN4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLH1_HUMANCLTCphysical
12429846
AP1B1_HUMANAP1B1physical
12429846
EPS15_HUMANEPS15physical
12429846
DYN1_HUMANDNM1physical
12429846
GGA2_HUMANGGA2physical
12429846
AP2A1_HUMANAP2A1physical
12429846
AP2B1_HUMANAP2B1physical
12429846
AP1G1_HUMANAP1G1physical
12429846
AP1B1_HUMANAP1B1physical
12538641
AP1G1_HUMANAP1G1physical
12538641
EPN4_HUMANCLINT1physical
12538641
CLH1_HUMANCLTCphysical
12538641
RL5_HUMANRPL5physical
22939629
RS28_HUMANRPS28physical
22939629
RS6_HUMANRPS6physical
22939629
NFXL1_HUMANNFXL1physical
22939629
AP2B1_HUMANAP2B1physical
26344197
CLH2_HUMANCLTCL1physical
28514442
BMP2K_HUMANBMP2Kphysical
28514442
P3C2A_HUMANPIK3C2Aphysical
28514442
SMAP2_HUMANSMAP2physical
28514442
STON2_HUMANSTON2physical
28514442
REPS1_HUMANREPS1physical
28514442
LOXL3_HUMANLOXL3physical
28514442
RBP1_HUMANRALBP1physical
28514442
STX8_HUMANSTX8physical
28514442
AP2A1_HUMANAP2A1physical
28514442
CSTFT_HUMANCSTF2Tphysical
28514442
AP2A2_HUMANAP2A2physical
28514442
AP1B1_HUMANAP1B1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPN4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-299, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-305 ANDSER-312, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-299, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-299, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND THR-272, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-26, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-232; SER-234AND SER-299, AND MASS SPECTROMETRY.

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