ZSC22_HUMAN - dbPTM
ZSC22_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZSC22_HUMAN
UniProt AC P10073
Protein Name Zinc finger and SCAN domain-containing protein 22
Gene Name ZSCAN22
Organism Homo sapiens (Human).
Sequence Length 491
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MAIPKHSLSPVPWEEDSFLQVKVEEEEEASLSQGGESSHDHIAHSEAARLRFRHFRYEEASGPHEALAHLRALCCQWLQPEAHSKEQILELLVLEQFLGALPPEIQAWVGAQSPKSGEEAAVLVEDLTQVLDKRGWDPGAEPTEASCKQSDLGESEPSNVTETLMGGVSLGPAFVKACEPEGSSERSGLSGEIWTKSVTQQIHFKKTSGPYKDVPTDQRGRESGASRNSSSAWPNLTSQEKPPSEDKFDLVDAYGTEPPYTYSGKRSSKCRECRKMFQSASALEAHQKTHSRKTPYACSECGKAFSRSTHLAQHQVVHTGAKPHECKECGKAFSRVTHLTQHQRIHTGEKPYKCGECGKTFSRSTHLTQHQRVHTGERPYECDACGKAFSQSTHLTQHQRIHTGEKPYKCDACGRAFSDCSALIRHLRIHSGEKPYQCKVCPKAFAQSSSLIEHQRIHTGEKPYKCSDCGKAFSRSSALMVHLRIHITVLQ
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
7Phosphorylation-MAIPKHSLSPVPWE
-CCCCCCCCCCCCCC		36.3528450419
9PhosphorylationAIPKHSLSPVPWEED
CCCCCCCCCCCCCCC		27.1925159151
32PhosphorylationEEEEASLSQGGESSH
HHHHHHHHCCCCCCC		25.0417525332
133UbiquitinationDLTQVLDKRGWDPGA
HHHHHHHHCCCCCCC		48.9629967540
186UbiquitinationEPEGSSERSGLSGEI
CCCCCCCCCCCCCEE		37.6622505724
199PhosphorylationEIWTKSVTQQIHFKK
EEEEEEHHEEEEEEC		23.1124719451
207PhosphorylationQQIHFKKTSGPYKDV
EEEEEECCCCCCCCC		39.2325002506
208PhosphorylationQIHFKKTSGPYKDVP
EEEEECCCCCCCCCC		46.8025002506
211PhosphorylationFKKTSGPYKDVPTDQ
EECCCCCCCCCCCCC		24.2825002506
216PhosphorylationGPYKDVPTDQRGRES
CCCCCCCCCCCCCCC		44.6125002506
242UbiquitinationNLTSQEKPPSEDKFD
CCCCCCCCCCCCCCC		36.5822505724
279PhosphorylationECRKMFQSASALEAH
HHHHHHHHHHHHHHH		16.9625690035
294PhosphorylationQKTHSRKTPYACSEC
HHHCCCCCCCCHHHH		22.0330243723
296PhosphorylationTHSRKTPYACSECGK
HCCCCCCCCHHHHHH		26.0230243723
298UbiquitinationSRKTPYACSECGKAF
CCCCCCCHHHHHHHH		2.6522505724
299PhosphorylationRKTPYACSECGKAFS
CCCCCCHHHHHHHHH		27.9630243723
303UbiquitinationYACSECGKAFSRSTH
CCHHHHHHHHHCCHH		58.90-
340PhosphorylationFSRVTHLTQHQRIHT
HHHHHHHHCCCCCCC		19.19-
347PhosphorylationTQHQRIHTGEKPYKC
HCCCCCCCCCCCEEC		44.6729496963
353SumoylationHTGEKPYKCGECGKT
CCCCCCEECCCCCCE		44.27-
353SumoylationHTGEKPYKCGECGKT
CCCCCCEECCCCCCE		44.27-
375PhosphorylationTQHQRVHTGERPYEC
CCCCEECCCCCCCCC		37.5723898821
403PhosphorylationTQHQRIHTGEKPYKC
CCCCCCCCCCCCCCC		44.6729496963
443SumoylationYQCKVCPKAFAQSSS
CCCEECCHHHHCCCC		51.5128112733
443SumoylationYQCKVCPKAFAQSSS
CCCEECCHHHHCCCC		51.51-
459PhosphorylationIEHQRIHTGEKPYKC
HCCCCCCCCCCCEEC		44.6729496963
467PhosphorylationGEKPYKCSDCGKAFS
CCCCEECCCCCCCCC		31.61-
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 ZSC22_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZSC22_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 ZSC22_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZSC22_HUMANZSCAN22physical
25416956
SCND1_HUMANSCAND1physical
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 ZSC22_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-32, AND MASSSPECTROMETRY.

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