ZC3HF_HUMAN - dbPTM
ZC3HF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZC3HF_HUMAN
UniProt AC Q8WU90
Protein Name Zinc finger CCCH domain-containing protein 15
Gene Name ZC3H15
Organism Homo sapiens (Human).
Sequence Length 426
Subcellular Localization Cytoplasm . Nucleus. The DRG1-DFRP2/ZC3H15 complex associates with polysomes.
Protein Description Protects DRG1 from proteolytic degradation..
Protein Sequence MPPKKQAQAGGSKKAEQKKKEKIIEDKTFGLKNKKGAKQQKFIKAVTHQVKFGQQNPRQVAQSEAEKKLKKDDKKKELQELNELFKPVVAAQKISKGADPKSVVCAFFKQGQCTKGDKCKFSHDLTLERKCEKRSVYIDARDEELEKDTMDNWDEKKLEEVVNKKHGEAEKKKPKTQIVCKHFLEAIENNKYGWFWVCPGGGDICMYRHALPPGFVLKKDKKKEEKEDEISLEDLIERERSALGPNVTKITLESFLAWKKRKRQEKIDKLEQDMERRKADFKAGKALVISGREVFEFRPELVNDDDEEADDTRYTQGTGGDEVDDSVSVNDIDLSLYIPRDVDETGITVASLERFSTYTSDKDENKLSEASGGRAENGERSDLEEDNEREGTENGAIDAVPVDENLFTGEDLDELEEELNTLDLEE
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
12PhosphorylationKQAQAGGSKKAEQKK
HHHCCCCCHHHHHHH		30.0221601212
22UbiquitinationAEQKKKEKIIEDKTF
HHHHHHHHHHHCCCC		58.8423000965
27UbiquitinationKEKIIEDKTFGLKNK
HHHHHHCCCCCCCCC		32.7223000965
272-HydroxyisobutyrylationKEKIIEDKTFGLKNK
HHHHHHCCCCCCCCC		32.72-
27AcetylationKEKIIEDKTFGLKNK
HHHHHHCCCCCCCCC		32.7291341
28PhosphorylationEKIIEDKTFGLKNKK
HHHHHCCCCCCCCCC		34.9518212344
32UbiquitinationEDKTFGLKNKKGAKQ
HCCCCCCCCCCCHHH		68.0823000965
35AcetylationTFGLKNKKGAKQQKF
CCCCCCCCCHHHHHH		73.777495747
38AcetylationLKNKKGAKQQKFIKA
CCCCCCHHHHHHHHH		63.037495757
38UbiquitinationLKNKKGAKQQKFIKA
CCCCCCHHHHHHHHH		63.0323000965
41UbiquitinationKKGAKQQKFIKAVTH
CCCHHHHHHHHHHHH		46.7123000965
44AcetylationAKQQKFIKAVTHQVK
HHHHHHHHHHHHHHH		39.687495767
44UbiquitinationAKQQKFIKAVTHQVK
HHHHHHHHHHHHHHH		39.6823000965
51UbiquitinationKAVTHQVKFGQQNPR
HHHHHHHHCCCCCHH		36.8923000965
51AcetylationKAVTHQVKFGQQNPR
HHHHHHHHCCCCCHH		36.8926051181
54UbiquitinationTHQVKFGQQNPRQVA
HHHHHCCCCCHHHHH		42.90-
61UbiquitinationQQNPRQVAQSEAEKK
CCCHHHHHHHHHHHH		9.9924816145
63PhosphorylationNPRQVAQSEAEKKLK
CHHHHHHHHHHHHHC		29.0926546556
64AcetylationPRQVAQSEAEKKLKK
HHHHHHHHHHHHHCH		49.09-
64UbiquitinationPRQVAQSEAEKKLKK
HHHHHHHHHHHHHCH		49.0924816145
67AcetylationVAQSEAEKKLKKDDK
HHHHHHHHHHCHHHH		71.1525953088
76UbiquitinationLKKDDKKKELQELNE
HCHHHHHHHHHHHHH		70.20-
80UbiquitinationDKKKELQELNELFKP
HHHHHHHHHHHHHHH		67.21-
80UbiquitinationDKKKELQELNELFKP
HHHHHHHHHHHHHHH		67.2122053931
86AcetylationQELNELFKPVVAAQK
HHHHHHHHHHHHHHH		49.9123954790
86UbiquitinationQELNELFKPVVAAQK
HHHHHHHHHHHHHHH		49.9129967540
93AcetylationKPVVAAQKISKGADP
HHHHHHHHHHCCCCC		44.1925953088
93UbiquitinationKPVVAAQKISKGADP
HHHHHHHHHHCCCCC		44.1933845483
95PhosphorylationVVAAQKISKGADPKS
HHHHHHHHCCCCCCC		31.88-
109AcetylationSVVCAFFKQGQCTKG
CEEEEEEECCCCCCC		47.2525953088
135PhosphorylationERKCEKRSVYIDARD
CCHHHCCCEEEECCC		30.2726552605
137PhosphorylationKCEKRSVYIDARDEE
HHHCCCEEEECCCHH		8.3728796482
147UbiquitinationARDEELEKDTMDNWD
CCCHHHHHHCCCCCC		71.7429967540
147AcetylationARDEELEKDTMDNWD
CCCHHHHHHCCCCCC		71.7426051181
149PhosphorylationDEELEKDTMDNWDEK
CHHHHHHCCCCCCHH		37.18-
157UbiquitinationMDNWDEKKLEEVVNK
CCCCCHHHHHHHHHH		60.1122053931
161UbiquitinationDEKKLEEVVNKKHGE
CHHHHHHHHHHHCCH		4.1422817900
1642-HydroxyisobutyrylationKLEEVVNKKHGEAEK
HHHHHHHHHCCHHHH		34.24-
181AcetylationPKTQIVCKHFLEAIE
CCHHHHHHHHHHHHH		26.8826051181
218AcetylationLPPGFVLKKDKKKEE
CCCCEEEECCCCCHH		54.3326051181
226UbiquitinationKDKKKEEKEDEISLE
CCCCCHHCCCCCCHH		72.1229967540
231PhosphorylationEEKEDEISLEDLIER
HHCCCCCCHHHHHHH		24.5329255136
241PhosphorylationDLIERERSALGPNVT
HHHHHHHHCCCCCCE		24.0828258704
259AcetylationLESFLAWKKRKRQEK
HHHHHHHHHHHHHHH		36.7724431543
259UbiquitinationLESFLAWKKRKRQEK
HHHHHHHHHHHHHHH		36.77-
260UbiquitinationESFLAWKKRKRQEKI
HHHHHHHHHHHHHHH		53.07-
266UbiquitinationKKRKRQEKIDKLEQD
HHHHHHHHHHHHHHH		48.1124816145
269UbiquitinationKRQEKIDKLEQDMER
HHHHHHHHHHHHHHH		58.3524816145
269AcetylationKRQEKIDKLEQDMER
HHHHHHHHHHHHHHH		58.3523236377
274SulfoxidationIDKLEQDMERRKADF
HHHHHHHHHHHHHHH		4.2821406390
285AcetylationKADFKAGKALVISGR
HHHHHCCCEEEECCC		43.3325953088
285UbiquitinationKADFKAGKALVISGR
HHHHHCCCEEEECCC		43.3321890473
314PhosphorylationEEADDTRYTQGTGGD
CCCCCCCCCCCCCCC		12.9020873877
315PhosphorylationEADDTRYTQGTGGDE
CCCCCCCCCCCCCCC		19.7520873877
318PhosphorylationDTRYTQGTGGDEVDD
CCCCCCCCCCCCCCC		28.3320873877
326PhosphorylationGGDEVDDSVSVNDID
CCCCCCCCCEECCEE		16.3020873877
328PhosphorylationDEVDDSVSVNDIDLS
CCCCCCCEECCEEEE		21.1028348404
335PhosphorylationSVNDIDLSLYIPRDV
EECCEEEEEECCCCC		18.5129978859
337PhosphorylationNDIDLSLYIPRDVDE
CCEEEEEECCCCCCC		12.9027080861
345PhosphorylationIPRDVDETGITVASL
CCCCCCCCCCEEEEE		29.4423663014
348PhosphorylationDVDETGITVASLERF
CCCCCCCEEEEEEEE		16.0323663014
351PhosphorylationETGITVASLERFSTY
CCCCEEEEEEEEECC		26.8230266825
356PhosphorylationVASLERFSTYTSDKD
EEEEEEEECCCCCCC		27.0723927012
357PhosphorylationASLERFSTYTSDKDE
EEEEEEECCCCCCCC		28.2723927012
358PhosphorylationSLERFSTYTSDKDEN
EEEEEECCCCCCCCC		11.7523927012
359PhosphorylationLERFSTYTSDKDENK
EEEEECCCCCCCCCC		30.4523927012
360PhosphorylationERFSTYTSDKDENKL
EEEECCCCCCCCCCH		32.0523401153
362UbiquitinationFSTYTSDKDENKLSE
EECCCCCCCCCCHHH		67.7121906983
3622-HydroxyisobutyrylationFSTYTSDKDENKLSE
EECCCCCCCCCCHHH		67.71-
362AcetylationFSTYTSDKDENKLSE
EECCCCCCCCCCHHH		67.7123749302
366UbiquitinationTSDKDENKLSEASGG
CCCCCCCCHHHHCCC		51.8733845483
366AcetylationTSDKDENKLSEASGG
CCCCCCCCHHHHCCC		51.8726051181
368PhosphorylationDKDENKLSEASGGRA
CCCCCCHHHHCCCCC		32.5023927012
371PhosphorylationENKLSEASGGRAENG
CCCHHHHCCCCCCCC		37.4225159151
381PhosphorylationRAENGERSDLEEDNE
CCCCCCCCCCCCCCC		42.0929255136
392PhosphorylationEDNEREGTENGAIDA
CCCCCCCCCCCCCCE		22.8626074081
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 ZC3HF_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZC3HF_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 ZC3HF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DRG1_HUMANDRG1physical
15676025
ZCHC8_HUMANZCCHC8physical
22939629
TRAF2_HUMANTRAF2physical
23624947
ABCF2_HUMANABCF2physical
26344197
DRG1_HUMANDRG1physical
26344197
FAF1_HUMANFAF1physical
26344197
PSF3_HUMANGINS3physical
26344197
HMGN5_HUMANHMGN5physical
26344197
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 ZC3HF_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-351, 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-381, AND MASSSPECTROMETRY.

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