ZNF7_HUMAN - dbPTM
ZNF7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNF7_HUMAN
UniProt AC P17097
Protein Name Zinc finger protein 7
Gene Name ZNF7
Organism Homo sapiens (Human).
Sequence Length 686
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MEVVTFGDVAVHFSREEWQCLDPGQRALYREVMLENHSSVAGLAGFLVFKPELISRLEQGEEPWVLDLQGAEGTEAPRTSKTDSTIRTENEQACEDMDILKSESYGTVVRISPQDFPQNPGFGDVSDSEVWLDSHLGSPGLKVTGFTFQNNCLNEETVVPKTFTKDAPQGCKELGSSGLDCQPLESQGESAEGMSQRCEECGKGIRATSDIALHWEINTQKISRCQECQKKLSDCLQGKHTNNCHGEKPYECAECGKVFRLCSQLNQHQRIHTGEKPFKCTECGKAFRLSSKLIQHQRIHTGEKPYRCEECGKAFGQSSSLIHHQRIHTGERPYGCRECGKAFSQQSQLVRHQRTHTGERPYPCKECGKAFSQSSTLAQHQRMHTGEKAQILKASDSPSLVAHQRIHAVEKPFKCDECGKAFRWISRLSQHQLIHTGEKPYKCNKCTKAFGCSSRLIRHQRTHTGEKPFKCDECGKGFVQGSHLIQHQRIHTGEKPYVCNDCGKAFSQSSSLIYHQRIHKGEKPYECLQCGKAFSMSTQLTIHQRVHTGERPYKCNECGKAFSQNSTLFQHQIIHAGVKPYECSECGKAFSRSSYLIEHQRIHTRAQWFYEYGNALEGSTFVSRKKVNTIKKLHQCEDCEKIFRWRSHLIIHQRIHTGEKPYKCNDCGKAFNRSSRLTQHQKIHMG
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
55PhosphorylationVFKPELISRLEQGEE
EECHHHHHHHHCCCC		43.3624719451
79PhosphorylationEGTEAPRTSKTDSTI
CCCCCCCCCCCCCCC		33.25-
80PhosphorylationGTEAPRTSKTDSTIR
CCCCCCCCCCCCCCC		34.53-
81SumoylationTEAPRTSKTDSTIRT
CCCCCCCCCCCCCCC		56.5928112733
82PhosphorylationEAPRTSKTDSTIRTE
CCCCCCCCCCCCCCC		34.64-
101SumoylationCEDMDILKSESYGTV
HHHCHHHCCCCCCEE		53.14-
101SumoylationCEDMDILKSESYGTV
HHHCHHHCCCCCCEE		53.1428112733
102PhosphorylationEDMDILKSESYGTVV
HHCHHHCCCCCCEEE		28.4723663014
104PhosphorylationMDILKSESYGTVVRI
CHHHCCCCCCEEEEE		35.6323663014
105PhosphorylationDILKSESYGTVVRIS
HHHCCCCCCEEEEEC		16.8623663014
107PhosphorylationLKSESYGTVVRISPQ
HCCCCCCEEEEECCC		13.9523663014
112PhosphorylationYGTVVRISPQDFPQN
CCEEEEECCCCCCCC		13.1226425664
126PhosphorylationNPGFGDVSDSEVWLD
CCCCCCCCCHHHHHH		39.9122817900
128PhosphorylationGFGDVSDSEVWLDSH
CCCCCCCHHHHHHHC		26.9228387310
134PhosphorylationDSEVWLDSHLGSPGL
CHHHHHHHCCCCCCE		20.5925921289
138PhosphorylationWLDSHLGSPGLKVTG
HHHHCCCCCCEEEEE		23.3525218447
161SumoylationNEETVVPKTFTKDAP
CCCCCCCCCCCCCCC		44.66-
161SumoylationNEETVVPKTFTKDAP
CCCCCCCCCCCCCCC		44.66-
165SumoylationVVPKTFTKDAPQGCK
CCCCCCCCCCCCHHH		47.94-
165UbiquitinationVVPKTFTKDAPQGCK
CCCCCCCCCCCCHHH		47.94-
165SumoylationVVPKTFTKDAPQGCK
CCCCCCCCCCCCHHH		47.94-
221SumoylationHWEINTQKISRCQEC
EEEECHHHHHHHHHH		40.38-
221SumoylationHWEINTQKISRCQEC
EEEECHHHHHHHHHH		40.38-
273PhosphorylationNQHQRIHTGEKPFKC
CCCCCCCCCCCCCCC		44.6718669648
279SumoylationHTGEKPFKCTECGKA
CCCCCCCCCCCCHHH		49.09-
279SumoylationHTGEKPFKCTECGKA
CCCCCCCCCCCCHHH		49.0928112733
285UbiquitinationFKCTECGKAFRLSSK
CCCCCCHHHHHHHHH		56.88-
292SumoylationKAFRLSSKLIQHQRI
HHHHHHHHHHCCCCC		46.35-
292SumoylationKAFRLSSKLIQHQRI
HHHHHHHHHHCCCCC		46.3528112733
296UbiquitinationLSSKLIQHQRIHTGE
HHHHHHCCCCCCCCC		16.34-
301PhosphorylationIQHQRIHTGEKPYRC
HCCCCCCCCCCCEEH		44.6729496963
304SumoylationQRIHTGEKPYRCEEC
CCCCCCCCCEEHHHH		49.01-
304UbiquitinationQRIHTGEKPYRCEEC
CCCCCCCCCEEHHHH		49.01-
304SumoylationQRIHTGEKPYRCEEC
CCCCCCCCCEEHHHH		49.01-
319PhosphorylationGKAFGQSSSLIHHQR
HHHHCCCCCCCEECC		22.6728555341
329PhosphorylationIHHQRIHTGERPYGC
CEECCCCCCCCCCCH		38.0628674419
341SumoylationYGCRECGKAFSQQSQ
CCHHHHHHHHHHHHH		58.90-
341UbiquitinationYGCRECGKAFSQQSQ
CCHHHHHHHHHHHHH		58.90-
341SumoylationYGCRECGKAFSQQSQ
CCHHHHHHHHHHHHH		58.90-
352UbiquitinationQQSQLVRHQRTHTGE
HHHHHHHHCCCCCCC		17.62-
357PhosphorylationVRHQRTHTGERPYPC
HHHCCCCCCCCCCCH		39.8721857030
365UbiquitinationGERPYPCKECGKAFS
CCCCCCHHHHHCCCC		52.08-
369UbiquitinationYPCKECGKAFSQSST
CCHHHHHCCCCCCHH		58.90-
369SumoylationYPCKECGKAFSQSST
CCHHHHHCCCCCCHH		58.90-
369SumoylationYPCKECGKAFSQSST
CCHHHHHCCCCCCHH		58.90-
376UbiquitinationKAFSQSSTLAQHQRM
CCCCCCHHHHHHHHC		31.21-
388SumoylationQRMHTGEKAQILKAS
HHCCCCCHHHHHHCC		47.11-
388UbiquitinationQRMHTGEKAQILKAS
HHCCCCCHHHHHHCC		47.11-
388SumoylationQRMHTGEKAQILKAS
HHCCCCCHHHHHHCC		47.11-
393SumoylationGEKAQILKASDSPSL
CCHHHHHHCCCCCCH		47.69-
393UbiquitinationGEKAQILKASDSPSL
CCHHHHHHCCCCCCH		47.69-
393SumoylationGEKAQILKASDSPSL
CCHHHHHHCCCCCCH		47.6928112733
395PhosphorylationKAQILKASDSPSLVA
HHHHHHCCCCCCHHH		36.7128450419
397PhosphorylationQILKASDSPSLVAHQ
HHHHCCCCCCHHHHH		17.5625849741
399PhosphorylationLKASDSPSLVAHQRI
HHCCCCCCHHHHHHH		39.1528450419
404UbiquitinationSPSLVAHQRIHAVEK
CCCHHHHHHHHEECC		35.96-
436PhosphorylationSQHQLIHTGEKPYKC
CCCCCEECCCCCCCC		39.7929496963
439SumoylationQLIHTGEKPYKCNKC
CCEECCCCCCCCCCC		55.80-
439SumoylationQLIHTGEKPYKCNKC
CCEECCCCCCCCCCC		55.80-
462PhosphorylationRLIRHQRTHTGEKPF
HHHHCCCCCCCCCCC		19.7423312004
464PhosphorylationIRHQRTHTGEKPFKC
HHCCCCCCCCCCCCC		46.5629496963
492PhosphorylationIQHQRIHTGEKPYVC
HEEEECCCCCCCEEE		44.6728111955
495SumoylationQRIHTGEKPYVCNDC
EECCCCCCCEEECCC		42.89-
495SumoylationQRIHTGEKPYVCNDC
EECCCCCCCEEECCC		42.89-
548PhosphorylationTIHQRVHTGERPYKC
EEEEECCCCCCCEEC		37.5727251275
554SumoylationHTGERPYKCNECGKA
CCCCCCEECCCCCCC		33.01-
554SumoylationHTGERPYKCNECGKA
CCCCCCEECCCCCCC		33.01-
588UbiquitinationYECSECGKAFSRSSY
EECCHHHCCCCCCCH		58.90-
599UbiquitinationRSSYLIEHQRIHTRA
CCCHHHHCCHHHHHH		18.41-
657PhosphorylationIIHQRIHTGEKPYKC
EEEEEECCCCCCCCC		44.6729496963
660AcetylationQRIHTGEKPYKCNDC
EEECCCCCCCCCCCH		55.807963327
663AcetylationHTGEKPYKCNDCGKA
CCCCCCCCCCCHHHH		34.787963337
669UbiquitinationYKCNDCGKAFNRSSR
CCCCCHHHHCCCHHC		57.02-
680UbiquitinationRSSRLTQHQKIHMG-
CHHCCCHHCCCCCC-		26.18-
682UbiquitinationSRLTQHQKIHMG---
HCCCHHCCCCCC---		32.24-
693UbiquitinationG--------------
C--------------		-
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 ZNF7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNF7_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 ZNF7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TADA3_HUMANTADA3physical
16169070
RL7_HUMANRPL7physical
9268371
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 ZNF7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-138, ANDMASS SPECTROMETRY.

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