ZCHC3_HUMAN - dbPTM
ZCHC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZCHC3_HUMAN
UniProt AC Q9NUD5
Protein Name Zinc finger CCHC domain-containing protein 3
Gene Name ZCCHC3
Organism Homo sapiens (Human).
Sequence Length 404
Subcellular Localization
Protein Description
Protein Sequence MATGGGAEEERKRGRPQLLPPARPAARGEEADGGREKMGWAQVVKNLAEKKGEFREPRPPRREEESGGGGGSAGLGGPAGLAAPDLGDFPPAGRGDPKGRRRDPAGEAVDPRKKKGAAEAGRRKKAEAAAAAMATPARPGEAEDAAERPLQDEPAAAAAGPGKGRFLVRICFQGDEGACPTRDFVVGALILRSIGMDPSDIYAVIQIPGSREFDVSFRSAEKLALFLRVYEEKREQEDCWENFVVLGRSKSSLKTLFILFRNETVDVEDIVTWLKRHCDVLAVPVKVTDRFGIWTGEYKCEIELRQGEGGVRHLPGAFFLGAERGYSWYKGQPKTCFKCGSRTHMSGSCTQDRCFRCGEEGHLSPYCRKGIVCNLCGKRGHAFAQCPKAVHNSVAAQLTGVAGH
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
45UbiquitinationMGWAQVVKNLAEKKG
CCHHHHHHHHHHHCC
47.6022817900
45UbiquitinationMGWAQVVKNLAEKKG
CCHHHHHHHHHHHCC
47.60-
50UbiquitinationVVKNLAEKKGEFREP
HHHHHHHHCCCCCCC
61.5422817900
94MethylationGDFPPAGRGDPKGRR
CCCCCCCCCCCCCCC
48.7480702665
124AcetylationAAEAGRRKKAEAAAA
HHHHHHHHHHHHHHH
55.7870875
125AcetylationAEAGRRKKAEAAAAA
HHHHHHHHHHHHHHH
50.0470879
201PhosphorylationIGMDPSDIYAVIQIP
CCCCHHHCEEEEECC
2.5315592455
202PhosphorylationGMDPSDIYAVIQIPG
CCCHHHCEEEEECCC
10.3725147952
222UbiquitinationVSFRSAEKLALFLRV
EECHHHHHHHHHHHH
38.48-
275UbiquitinationEDIVTWLKRHCDVLA
HHHHHHHHHHCCEEE
31.49-
285UbiquitinationCDVLAVPVKVTDRFG
CCEEEEEEEEECCCC
6.6424816145
286UbiquitinationDVLAVPVKVTDRFGI
CEEEEEEEEECCCCC
33.09-
329UbiquitinationAERGYSWYKGQPKTC
CCCCCCCCCCCCCEE
10.1732015554
329NeddylationAERGYSWYKGQPKTC
CCCCCCCCCCCCCEE
10.1732015554
330UbiquitinationERGYSWYKGQPKTCF
CCCCCCCCCCCCEEE
44.82-
350PhosphorylationTHMSGSCTQDRCFRC
CCCCCCCCCCCEECC
34.89-
353MethylationSGSCTQDRCFRCGEE
CCCCCCCCEECCCCC
16.20115920341
363PhosphorylationRCGEEGHLSPYCRKG
CCCCCCCCCCCCCCC
8.9624719451
364PhosphorylationCGEEGHLSPYCRKGI
CCCCCCCCCCCCCCE
14.2425159151
366PhosphorylationEEGHLSPYCRKGIVC
CCCCCCCCCCCCEEE
11.0829396449
369UbiquitinationHLSPYCRKGIVCNLC
CCCCCCCCCEEECCC
49.80-
377UbiquitinationGIVCNLCGKRGHAFA
CEEECCCCCCCCCHH
26.3432015554
387UbiquitinationGHAFAQCPKAVHNSV
CCCHHHCCHHHHHHH
18.6332015554

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 ZCHC3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZCHC3_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 ZCHC3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZCHC3_HUMAN !!

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 ZCHC3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-202, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-45, AND MASSSPECTROMETRY.

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