ZN618_HUMAN - dbPTM
ZN618_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN618_HUMAN
UniProt AC Q5T7W0
Protein Name Zinc finger protein 618
Gene Name ZNF618
Organism Homo sapiens (Human).
Sequence Length 954
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MNQPGGAAAPQADGASAAGRKSTASRERLKRSQKSTKVEGPEPVPAEASLSAEQGTMTEVKVKTELPDDYIQEVIWQGEAKEEKKAVSKDGTSDVPAEICVVIGGVRNQQTLDGKAPEGSPHGGSVRSRYSGTWIFDQALRYASGSYECGICGKKYKYYNCFQTHVRAHRDTEATSGEGASQSNNFRYTCDICGKKYKYYSCFQEHRDLHAVDVFSVEGAPENRADPFDQGVVATDEVKEEPPEPFQKIGPKTGNYTCEFCGKQYKYYTPYQEHVALHAPISTAPGWEPPDDPDTGSECSHPEVSPSPRFVAAKTQTNQSGKKAPASVVRCATLLHRTPPATQTQTFRTPNSGSPASKATAAESAFSRRVEGKAQNHFEETNSSSQNSSEPYTCGACGIQFQFYNNLLEHMQSHAADNENNIASNQSRSPPAVVEEKWKPQAQRNSANNTTTSGLTPNSMIPEKERQNIAERLLRVMCADLGALSVVSGKEFLKLAQTLVDSGARYGAFSVTEILGNFNTLALKHLPRMYNQVKVKVTCALGSNACLGIGVTCHSQSVGPDSCYILTAYQAEGNHIKSYVLGVKGADIRDSGDLVHHWVQNVLSEFVMSEIRTVYVTDCRVSTSAFSKAGMCLRCSACALNSVVQSVLSKRTLQARSMHEVIELLNVCEDLAGSTGLAKETFGSLEETSPPPCWNSVTDSLLLVHERYEQICEFYSRAKKMNLIQSLNKHLLSNLAAILTPVKQAVIELSNESQPTLQLVLPTYVRLEKLFTAKANDAGTVSKLCHLFLEALKENFKVHPAHKVAMILDPQQKLRPVPPYQHEEIIGKVCELINEVKESWAEEADFEPAAKKPRSAAVENPAAQEDDRLGKNEVYDYLQEPLFQATPDLFQYWSCVTQKHTKLAKLAFWLLAVPAVGARSGCVNMCEQALLIKRRRLLSPEDMNKLMFLKSNML
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
1Acetylation-------MNQPGGAA
-------CCCCCCCC		10.6922814378
16PhosphorylationAPQADGASAAGRKST
CCCCCCCCCCCCCCH		24.9618669648
49PhosphorylationEPVPAEASLSAEQGT
CCCCCCCEEECCCCC		17.8627251275
63SumoylationTMTEVKVKTELPDDY
CEEEEEEECCCCCHH		30.4828112733
81SumoylationVIWQGEAKEEKKAVS
HHHHCCHHHHHHHCC		63.2028112733
92PhosphorylationKAVSKDGTSDVPAEI
HHCCCCCCCCCCCEE		31.7127251275
93PhosphorylationAVSKDGTSDVPAEIC
HCCCCCCCCCCCEEE		41.9827251275
120PhosphorylationDGKAPEGSPHGGSVR
CCCCCCCCCCCCCCC		16.4428450419
125PhosphorylationEGSPHGGSVRSRYSG
CCCCCCCCCCCCCCC		20.9626425664
128PhosphorylationPHGGSVRSRYSGTWI
CCCCCCCCCCCCCEE		33.1528450419
130PhosphorylationGGSVRSRYSGTWIFD
CCCCCCCCCCCEEHH		16.8228450419
131PhosphorylationGSVRSRYSGTWIFDQ
CCCCCCCCCCEEHHH		28.7427732954
133PhosphorylationVRSRYSGTWIFDQAL
CCCCCCCCEEHHHHH		14.9427732954
144PhosphorylationDQALRYASGSYECGI
HHHHHHHCCCEECCC		21.2427251275
172PhosphorylationHVRAHRDTEATSGEG
HHHHHCCCCCCCCCC		27.7226852163
175PhosphorylationAHRDTEATSGEGASQ
HHCCCCCCCCCCCCC		30.9128450419
176PhosphorylationHRDTEATSGEGASQS
HCCCCCCCCCCCCCC		41.7323401153
181PhosphorylationATSGEGASQSNNFRY
CCCCCCCCCCCCCEE		45.0228450419
183PhosphorylationSGEGASQSNNFRYTC
CCCCCCCCCCCEEEE		31.1126852163
184PhosphorylationGEGASQSNNFRYTCD
CCCCCCCCCCEEEEE		43.9824719451
188PhosphorylationSQSNNFRYTCDICGK
CCCCCCEEEEECCCC		13.95-
216PhosphorylationLHAVDVFSVEGAPEN
CCEEEEEEECCCCCC		21.0730266825
239SumoylationVVATDEVKEEPPEPF
CCCCHHCCCCCCCCH		55.0728112733
307PhosphorylationSHPEVSPSPRFVAAK
CCCCCCCCCCEEEEE		22.6217081983
315PhosphorylationPRFVAAKTQTNQSGK
CCEEEEECEECCCCC		35.58-
317PhosphorylationFVAAKTQTNQSGKKA
EEEEECEECCCCCCC		40.22-
327PhosphorylationSGKKAPASVVRCATL
CCCCCCHHHHHHHHH		21.7823403867
336PhosphorylationVRCATLLHRTPPATQ
HHHHHHHHCCCCCCC		34.3824719451
363PhosphorylationASKATAAESAFSRRV
CHHHHHHHHHHHHHH		39.8927251275
401UbiquitinationCGACGIQFQFYNNLL
CCCCCCCHHHHHHHH		5.25-
429PhosphorylationIASNQSRSPPAVVEE
CCCCCCCCCCHHHHC		40.2529255136
437SumoylationPPAVVEEKWKPQAQR
CCHHHHCCCCCHHHH		47.1928112733
456PhosphorylationNTTTSGLTPNSMIPE
CCCCCCCCCCCCCCH		24.7727251275
485PhosphorylationCADLGALSVVSGKEF
HHHHCCCEECCHHHH		21.6824114839
490UbiquitinationALSVVSGKEFLKLAQ
CCEECCHHHHHHHHH		37.47-
530PhosphorylationLKHLPRMYNQVKVKV
HHHHHHHHCCCEEEE		12.06-
636PhosphorylationAGMCLRCSACALNSV
CCCHHHHHHHHHHHH		21.6826552605
642PhosphorylationCSACALNSVVQSVLS
HHHHHHHHHHHHHHC		25.2326552605
646PhosphorylationALNSVVQSVLSKRTL
HHHHHHHHHHCCCCH		17.2626552605
649PhosphorylationSVVQSVLSKRTLQAR
HHHHHHHCCCCHHHH		20.2426552605
708PhosphorylationLLLVHERYEQICEFY
HHHHHHHHHHHHHHH		14.8124260401
715PhosphorylationYEQICEFYSRAKKMN
HHHHHHHHHHHHHCC		3.8024260401
716PhosphorylationEQICEFYSRAKKMNL
HHHHHHHHHHHHCCH		30.9624260401
733PhosphorylationSLNKHLLSNLAAILT
HHHHHHHHHHHHHHH		35.84-
740PhosphorylationSNLAAILTPVKQAVI
HHHHHHHHHHHHHHH		21.66-
759UbiquitinationESQPTLQLVLPTYVR
CCCCCEEEECCCEEH		4.8629967540
772PhosphorylationVRLEKLFTAKANDAG
EHHHHHHEECCCCHH		37.37-
782PhosphorylationANDAGTVSKLCHLFL
CCCHHHHHHHHHHHH		21.54-
857MethylationAKKPRSAAVENPAAQ
CCCCCCHHCCCCCCC		15.48-
857UbiquitinationAKKPRSAAVENPAAQ
CCCCCCHHCCCCCCC		15.48-
939PhosphorylationIKRRRLLSPEDMNKL
HHHHCCCCHHHHHHH		30.7324719451
950UbiquitinationMNKLMFLKSNML---
HHHHHHHHHCCC---		28.63-
950MethylationMNKLMFLKSNML---
HHHHHHHHHCCC---		28.63115978111
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 ZN618_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN618_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 ZN618_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UHRF2_HUMANUHRF2physical
27129234
GAPD1_HUMANGAPVD1physical
27129234
RL11_HUMANRPL11physical
27129234
HSP7C_HUMANHSPA8physical
27129234
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 ZN618_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 MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-16, AND MASSSPECTROMETRY.

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