ZCCHL_HUMAN - dbPTM
ZCCHL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZCCHL_HUMAN
UniProt AC Q96H79
Protein Name Zinc finger CCCH-type antiviral protein 1-like
Gene Name ZC3HAV1L
Organism Homo sapiens (Human).
Sequence Length 300
Subcellular Localization
Protein Description
Protein Sequence MAEPTVCSFLTKVLCAHGGRMFLKDLRGHVELSEARLRDVLQRAGPERFLLQEVETQEGLGDAEAEAAAGAVGGGGTSAWRVVAVSSVRLCARYQRGECQACDQLHFCRRHMLGKCPNRDCWSTCTLSHDIHTPVNMQVLKSHGLFGLNENQLRILLLQNDPCLLPEVCLLYNKGEALYGYCNLKDKCNKFHVCKSFVKGECKLQTCKRSHQLIHAASLKLLQDQGLNIPSVVNFQIISTYKHMKLHKMLENTDNSSPSTEHSQGLEKQGVHAAGAAEAGPLASVPAQSAKKPCPVSCEK
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
2Acetylation------MAEPTVCSF
------CCCCCHHHH		31.3219413330
5Phosphorylation---MAEPTVCSFLTK
---CCCCCHHHHHHH		26.1627135362
8PhosphorylationMAEPTVCSFLTKVLC
CCCCCHHHHHHHHHH		20.9627135362
11PhosphorylationPTVCSFLTKVLCAHG
CCHHHHHHHHHHHCC		19.6620068231
12AcetylationTVCSFLTKVLCAHGG
CHHHHHHHHHHHCCC		35.047380129
12UbiquitinationTVCSFLTKVLCAHGG
CHHHHHHHHHHHCCC		35.04-
24UbiquitinationHGGRMFLKDLRGHVE
CCCHHHHHHHHCCHH		43.37-
24AcetylationHGGRMFLKDLRGHVE
CCCHHHHHHHHCCHH		43.3725953088
242-HydroxyisobutyrylationHGGRMFLKDLRGHVE
CCCHHHHHHHHCCHH		43.37-
43MethylationRLRDVLQRAGPERFL
HHHHHHHHHCHHHEE		37.03115920333
86PhosphorylationAWRVVAVSSVRLCAR
HHHEEHHHHHHHHHH		17.2428857561
87PhosphorylationWRVVAVSSVRLCARY
HHEEHHHHHHHHHHH		12.5028857561
115UbiquitinationCRRHMLGKCPNRDCW
HHHHHCCCCCCCCCC		42.42-
123PhosphorylationCPNRDCWSTCTLSHD
CCCCCCCCCCCCCCC		21.6727080861
124PhosphorylationPNRDCWSTCTLSHDI
CCCCCCCCCCCCCCC		5.7527080861
126PhosphorylationRDCWSTCTLSHDIHT
CCCCCCCCCCCCCCC		31.2427080861
128PhosphorylationCWSTCTLSHDIHTPV
CCCCCCCCCCCCCCC		10.8527080861
133PhosphorylationTLSHDIHTPVNMQVL
CCCCCCCCCCHHHHH		29.3027080861
141UbiquitinationPVNMQVLKSHGLFGL
CCHHHHHHHCCCCCC		41.3629967540
174UbiquitinationEVCLLYNKGEALYGY
HHHHHEECCCEEEEE		44.57-
179PhosphorylationYNKGEALYGYCNLKD
EECCCEEEEEECHHH		17.0725159151
185UbiquitinationLYGYCNLKDKCNKFH
EEEEECHHHHCCCEE		40.9429967540
190AcetylationNLKDKCNKFHVCKSF
CHHHHCCCEEECHHH		46.4425953088
195MalonylationCNKFHVCKSFVKGEC
CCCEEECHHHHCCCC		45.9326320211
195AcetylationCNKFHVCKSFVKGEC
CCCEEECHHHHCCCC		45.9325953088
195UbiquitinationCNKFHVCKSFVKGEC
CCCEEECHHHHCCCC		45.9329967540
199AcetylationHVCKSFVKGECKLQT
EECHHHHCCCCCHHC		47.1625953088
199UbiquitinationHVCKSFVKGECKLQT
EECHHHHCCCCCHHC		47.1629967540
203UbiquitinationSFVKGECKLQTCKRS
HHHCCCCCHHCCHHH		39.0529967540
203AcetylationSFVKGECKLQTCKRS
HHHCCCCCHHCCHHH		39.0525953088
218PhosphorylationHQLIHAASLKLLQDQ
HHHHHHHHHHHHHHC		27.1630108239
248UbiquitinationYKHMKLHKMLENTDN
HHHHHHHHHHHCCCC		56.4629967540
249SulfoxidationKHMKLHKMLENTDNS
HHHHHHHHHHCCCCC		3.8521406390
253PhosphorylationLHKMLENTDNSSPST
HHHHHHCCCCCCCCH		27.4730266825
256PhosphorylationMLENTDNSSPSTEHS
HHHCCCCCCCCHHHH		46.5717525332
257PhosphorylationLENTDNSSPSTEHSQ
HHCCCCCCCCHHHHH		29.1730266825
259PhosphorylationNTDNSSPSTEHSQGL
CCCCCCCCHHHHHHH		48.6630266825
260PhosphorylationTDNSSPSTEHSQGLE
CCCCCCCHHHHHHHH		40.8930266825
263PhosphorylationSSPSTEHSQGLEKQG
CCCCHHHHHHHHHCC		21.5117525332
268UbiquitinationEHSQGLEKQGVHAAG
HHHHHHHHCCCCCCC		58.3529967540
284PhosphorylationAEAGPLASVPAQSAK
HHHCCCCCCCCCCCC		35.9925627689
289PhosphorylationLASVPAQSAKKPCPV
CCCCCCCCCCCCCCC		44.1325159151
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 ZCCHL_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZCCHL_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 ZCCHL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 ZCCHL_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-257, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-257, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-263, ANDMASS SPECTROMETRY.

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