ZN655_HUMAN - dbPTM
ZN655_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN655_HUMAN
UniProt AC Q8N720
Protein Name Zinc finger protein 655
Gene Name ZNF655
Organism Homo sapiens (Human).
Sequence Length 491
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MEEIPAQEAAGSPRVQFQSLETQSECLSPEPQFVQDTDMEQGLTGDGETREENKLLIPKQKISEEVHSYKVRVGRLKHDITQVPETREVYKSEDRLERLQEILRKFLYLEREFRQITISKETFTSEKNNECHEPEKSFSLDSTIDADQRVLRIQNTDDNDKYDMSFNQNSASGKHEHLNLTEDFQSSECKESLMDLSHLNKWESIPNTEKSYKCDVCGKIFHQSSALTRHQRIHTREKPYKCKECEKSFSQSSSLSRHKRIHTREKPYKCEASDKSCEASDKSCSPSSGIIQHKKIHTRAKSYKCSSCERVFSRSVHLTQHQKIHKEMPCKCTVCGSDFCHTSYLLEHQRVHHEEKAYEYDEYGLAYIKQQGIHFREKPYTCSECGKDFRLNSHLIQHQRIHTGEKAHECNECGKAFSQTSCLIQHHKMHRKEKSYECNEYEGSFSHSSDLILQQEVLTRQKAFDCDVWEKNSSQRAHLVQHQSIHTKENS
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-------MEEIPAQE
-------CCCCCHHH		10.60-
12PhosphorylationPAQEAAGSPRVQFQS
CHHHHCCCCCEEEEE		12.5729255136
22 (in isoform 2)Phosphorylation-42.5628348404
24PhosphorylationFQSLETQSECLSPEP
EEECCCHHHHCCCCC		37.3826471730
24 (in isoform 2)Phosphorylation-37.3828348404
28PhosphorylationETQSECLSPEPQFVQ
CCHHHHCCCCCCCCC		38.5926471730
28 (in isoform 2)Phosphorylation-38.5928348404
37PhosphorylationEPQFVQDTDMEQGLT
CCCCCCCCCCCCCCC		21.8326471730
37 (in isoform 2)Phosphorylation-21.8328348404
44PhosphorylationTDMEQGLTGDGETRE
CCCCCCCCCCCCCHH		39.8026471730
44 (in isoform 2)Phosphorylation-39.8028348404
59UbiquitinationENKLLIPKQKISEEV
HCCEEECHHHHCHHH		58.17-
60 (in isoform 2)Phosphorylation-42.8530266825
68PhosphorylationKISEEVHSYKVRVGR
HHCHHHHHCEEEECC		31.6523684312
69PhosphorylationISEEVHSYKVRVGRL
HCHHHHHCEEEECCC		9.9123684312
70 (in isoform 2)Phosphorylation-26.9530266825
70UbiquitinationSEEVHSYKVRVGRLK
CHHHHHCEEEECCCC		26.95-
71 (in isoform 3)Phosphorylation-4.5622210691
77SumoylationKVRVGRLKHDITQVP
EEEECCCCCCCCCCC		37.5628112733
77UbiquitinationKVRVGRLKHDITQVP
EEEECCCCCCCCCCC		37.56-
77SumoylationKVRVGRLKHDITQVP
EEEECCCCCCCCCCC		37.56-
80 (in isoform 3)Phosphorylation-2.6525159151
84 (in isoform 3)Phosphorylation-27.6828111955
91SumoylationPETREVYKSEDRLER
CCHHHHHCCHHHHHH		53.17-
91UbiquitinationPETREVYKSEDRLER
CCHHHHHCCHHHHHH		53.17-
91SumoylationPETREVYKSEDRLER
CCHHHHHCCHHHHHH		53.17-
92 (in isoform 4)Phosphorylation-27.3520049867
103 (in isoform 4)Phosphorylation-4.8520049867
105 (in isoform 3)Ubiquitination-35.95-
105 (in isoform 4)Phosphorylation-35.9520049867
110 (in isoform 2)Phosphorylation-36.2926503514
112 (in isoform 3)Ubiquitination-35.49-
115 (in isoform 2)Phosphorylation-42.3626503514
136UbiquitinationNECHEPEKSFSLDST
CCCCCCCCCCCCCCE		68.47-
137PhosphorylationECHEPEKSFSLDSTI
CCCCCCCCCCCCCEE		20.5725627689
139PhosphorylationHEPEKSFSLDSTIDA
CCCCCCCCCCCEECC		38.0629507054
142PhosphorylationEKSFSLDSTIDADQR
CCCCCCCCEECCCCC		32.3324247654
162PhosphorylationNTDDNDKYDMSFNQN
CCCCCCCCCCCCCCC		21.5329759185
163 (in isoform 2)Phosphorylation-31.8020049867
165PhosphorylationDNDKYDMSFNQNSAS
CCCCCCCCCCCCCCC		20.3928555341
170PhosphorylationDMSFNQNSASGKHEH
CCCCCCCCCCCCCCC		17.6629759185
172PhosphorylationSFNQNSASGKHEHLN
CCCCCCCCCCCCCCC		48.4729759185
174 (in isoform 2)Phosphorylation-43.2420049867
176 (in isoform 2)Phosphorylation-54.2620049867
190SumoylationDFQSSECKESLMDLS
HHCCHHHHHHHHCHH		46.4128112733
197PhosphorylationKESLMDLSHLNKWES
HHHHHCHHHHHCCCC		22.9728555341
201SumoylationMDLSHLNKWESIPNT
HCHHHHHCCCCCCCC		59.7128112733
201UbiquitinationMDLSHLNKWESIPNT
HCHHHHHCCCCCCCC		59.71-
210UbiquitinationESIPNTEKSYKCDVC
CCCCCCCCCCCCCCC		57.98-
247UbiquitinationYKCKECEKSFSQSSS
CCCCHHHHHCCCCCC		69.34-
248PhosphorylationKCKECEKSFSQSSSL
CCCHHHHHCCCCCCH		14.0825159151
250PhosphorylationKECEKSFSQSSSLSR
CHHHHHCCCCCCHHH		35.9225627689
252PhosphorylationCEKSFSQSSSLSRHK
HHHHCCCCCCHHHHC		22.2427732954
253PhosphorylationEKSFSQSSSLSRHKR
HHHCCCCCCHHHHCC		27.8827732954
254PhosphorylationKSFSQSSSLSRHKRI
HHCCCCCCHHHHCCC		35.2925159151
256PhosphorylationFSQSSSLSRHKRIHT
CCCCCCHHHHCCCCC		34.0027732954
268PhosphorylationIHTREKPYKCEASDK
CCCCCCCCCCCCCCC		39.0626657352
269SumoylationHTREKPYKCEASDKS
CCCCCCCCCCCCCCC		33.84-
269SumoylationHTREKPYKCEASDKS
CCCCCCCCCCCCCCC		33.84-
276PhosphorylationKCEASDKSCEASDKS
CCCCCCCCCCCCCCC		23.3726657352
280PhosphorylationSDKSCEASDKSCSPS
CCCCCCCCCCCCCCC		24.2326657352
282UbiquitinationKSCEASDKSCSPSSG
CCCCCCCCCCCCCCC		51.36-
283PhosphorylationSCEASDKSCSPSSGI
CCCCCCCCCCCCCCC		25.4730108239
285PhosphorylationEASDKSCSPSSGIIQ
CCCCCCCCCCCCCCC		34.6025159151
287PhosphorylationSDKSCSPSSGIIQHK
CCCCCCCCCCCCCCC		25.5428450419
288PhosphorylationDKSCSPSSGIIQHKK
CCCCCCCCCCCCCCC		37.0826074081
294UbiquitinationSSGIIQHKKIHTRAK
CCCCCCCCCCCCCCC		36.73-
323UbiquitinationVHLTQHQKIHKEMPC
HHHHHHHHHHHCCCC		44.65-
356UbiquitinationQRVHHEEKAYEYDEY
HCCCCCHHHHCCCHH		53.97-
358PhosphorylationVHHEEKAYEYDEYGL
CCCCHHHHCCCHHHH		26.53-
363PhosphorylationKAYEYDEYGLAYIKQ
HHHCCCHHHHHHHHH		17.9729978859
367PhosphorylationYDEYGLAYIKQQGIH
CCHHHHHHHHHCCCC		17.4429978859
369UbiquitinationEYGLAYIKQQGIHFR
HHHHHHHHHCCCCCC		24.72-
387UbiquitinationYTCSECGKDFRLNSH
CCCCCCCCCEEECHH		66.41-
393PhosphorylationGKDFRLNSHLIQHQR
CCCEEECHHHHCCCC		25.0228555341
421PhosphorylationGKAFSQTSCLIQHHK
HHHHHHHHHHHHHHH		10.1728555341
422 (in isoform 3)Ubiquitination-4.39-
462UbiquitinationQEVLTRQKAFDCDVW
HHHHHHCHHHCCCCC		47.97-
471UbiquitinationFDCDVWEKNSSQRAH
HCCCCCCCCHHHHHH		46.55-
484PhosphorylationAHLVQHQSIHTKENS
HHHEEECHHCCCCCC		17.7628348404
488SumoylationQHQSIHTKENS----
EECHHCCCCCC----		40.51-
488SumoylationQHQSIHTKENS----
EECHHCCCCCC----		40.51-
488UbiquitinationQHQSIHTKENS----
EECHHCCCCCC----		40.51-
491PhosphorylationSIHTKENS-------
HHCCCCCC-------		42.5626714015
497 (in isoform 3)Ubiquitination--
506 (in isoform 3)Ubiquitination--
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 ZN655_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN655_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 ZN655_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR412_HUMANKRTAP4-12physical
16189514
K1C40_HUMANKRT40physical
25416956
SPERT_HUMANSPERTphysical
25416956
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 ZN655_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-12, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-12, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, PHOSPHORYLATION[LARGE SCALE ANALYSIS] AT SER-60 (ISOFORM 2), AND MASS SPECTROMETRY.

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