ZN184_HUMAN - dbPTM
ZN184_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN184_HUMAN
UniProt AC Q99676
Protein Name Zinc finger protein 184
Gene Name ZNF184
Organism Homo sapiens (Human).
Sequence Length 751
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MEDLSSPDSTLLQGGHNLLSSASFQEAVTFKDVIVDFTQEEWKQLDPGQRDLFRDVTLENYTHLVSIGLQVSKPDVISQLEQGTEPWIMEPSIPVGTCADWETRLENSVSAPEPDISEEELSPEVIVEKHKRDDSWSSNLLESWEYEGSLERQQANQQTLPKEIKVTEKTIPSWEKGPVNNEFGKSVNVSSNLVTQEPSPEETSTKRSIKQNSNPVKKEKSCKCNECGKAFSYCSALIRHQRTHTGEKPYKCNECEKAFSRSENLINHQRIHTGDKPYKCDQCGKGFIEGPSLTQHQRIHTGEKPYKCDECGKAFSQRTHLVQHQRIHTGEKPYTCNECGKAFSQRGHFMEHQKIHTGEKPFKCDECDKTFTRSTHLTQHQKIHTGEKTYKCNECGKAFNGPSTFIRHHMIHTGEKPYECNECGKAFSQHSNLTQHQKTHTGEKPYDCAECGKSFSYWSSLAQHLKIHTGEKPYKCNECGKAFSYCSSLTQHRRIHTREKPFECSECGKAFSYLSNLNQHQKTHTQEKAYECKECGKAFIRSSSLAKHERIHTGEKPYQCHECGKTFSYGSSLIQHRKIHTGERPYKCNECGRAFNQNIHLTQHKRIHTGAKPYECAECGKAFRHCSSLAQHQKTHTEEKPYQCNKCEKTFSQSSHLTQHQRIHTGEKPYKCNECDKAFSRSTHLTEHQNTHTGEKPYNCNECRKTFSQSTYLIQHQRIHSGEKPFGCNDCGKSFRYRSALNKHQRLHPGI
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
108PhosphorylationWETRLENSVSAPEPD
HHHHHHHCCCCCCCC		14.2020873877
110PhosphorylationTRLENSVSAPEPDIS
HHHHHCCCCCCCCCC		37.6228450419
117PhosphorylationSAPEPDISEEELSPE
CCCCCCCCHHHCCHH		46.4630278072
122PhosphorylationDISEEELSPEVIVEK
CCCHHHCCHHHEEEE		23.4625159151
135PhosphorylationEKHKRDDSWSSNLLE
EECCCCCCCCCHHHH		32.9028787133
137PhosphorylationHKRDDSWSSNLLESW
CCCCCCCCCHHHHHH		17.1928787133
138PhosphorylationKRDDSWSSNLLESWE
CCCCCCCCHHHHHHH		25.8228787133
149PhosphorylationESWEYEGSLERQQAN
HHHHCCCCHHHHHHH		18.3426091039
159PhosphorylationRQQANQQTLPKEIKV
HHHHHHCCCCCEEEC		34.9524117733
162SumoylationANQQTLPKEIKVTEK
HHHCCCCCEEECCCC		75.16-
162SumoylationANQQTLPKEIKVTEK
HHHCCCCCEEECCCC		75.16-
169UbiquitinationKEIKVTEKTIPSWEK
CEEECCCCCCCCCCC		42.25-
176UbiquitinationKTIPSWEKGPVNNEF
CCCCCCCCCCCCCCC		63.36-
190PhosphorylationFGKSVNVSSNLVTQE
CCCEEECCCCCCCCC		14.3325954137
191PhosphorylationGKSVNVSSNLVTQEP
CCEEECCCCCCCCCC		29.8725954137
195PhosphorylationNVSSNLVTQEPSPEE
ECCCCCCCCCCCCCH		30.3125954137
199PhosphorylationNLVTQEPSPEETSTK
CCCCCCCCCCHHHCH		44.1625159151
203PhosphorylationQEPSPEETSTKRSIK
CCCCCCHHHCHHHHH		39.7825954137
204PhosphorylationEPSPEETSTKRSIKQ
CCCCCHHHCHHHHHH		34.9028111955
205PhosphorylationPSPEETSTKRSIKQN
CCCCHHHCHHHHHHC		37.5928111955
206SumoylationSPEETSTKRSIKQNS
CCCHHHCHHHHHHCC		43.8728112733
206SumoylationSPEETSTKRSIKQNS
CCCHHHCHHHHHHCC		43.87-
213PhosphorylationKRSIKQNSNPVKKEK
HHHHHHCCCCCCCCC		39.7629083192
243PhosphorylationALIRHQRTHTGEKPY
HHHHCCCCCCCCCCC		19.7428348404
245PhosphorylationIRHQRTHTGEKPYKC
HHCCCCCCCCCCCCC		46.5624719451
248UbiquitinationQRTHTGEKPYKCNEC
CCCCCCCCCCCCCHH		55.80-
273PhosphorylationINHQRIHTGDKPYKC
CCCCCCCCCCCCCCC		44.7124719451
278PhosphorylationIHTGDKPYKCDQCGK
CCCCCCCCCCCCCCC		29.9522964224
292PhosphorylationKGFIEGPSLTQHQRI
CCCCCCCCCCCCCCE		55.7128555341
301PhosphorylationTQHQRIHTGEKPYKC
CCCCCEECCCCCCCC		44.6729496963
307UbiquitinationHTGEKPYKCDECGKA
ECCCCCCCCCCCCHH		43.68-
316PhosphorylationDECGKAFSQRTHLVQ
CCCCHHHHHCHHCEE		24.5027174698
319PhosphorylationGKAFSQRTHLVQHQR
CHHHHHCHHCEEECC		16.3627174698
329PhosphorylationVQHQRIHTGEKPYTC
EEECCCCCCCCCEEC		44.6726055452
332SumoylationQRIHTGEKPYTCNEC
CCCCCCCCCEECCCH		44.67-
332SumoylationQRIHTGEKPYTCNEC
CCCCCCCCCEECCCH		44.67-
354UbiquitinationGHFMEHQKIHTGEKP
CCHHHCCCCCCCCCC		38.06-
357PhosphorylationMEHQKIHTGEKPFKC
HHCCCCCCCCCCCCC		50.9718669648
413PhosphorylationIRHHMIHTGEKPYEC
HEECEEECCCCCCCC		35.7928152594
416UbiquitinationHMIHTGEKPYECNEC
CEEECCCCCCCCCCC		55.00-
418PhosphorylationIHTGEKPYECNECGK
EECCCCCCCCCCCHH		44.1528152594
466UbiquitinationSSLAQHLKIHTGEKP
HHHHHHHCHHCCCCC		30.25-
469PhosphorylationAQHLKIHTGEKPYKC
HHHHCHHCCCCCEEC		50.9729496963
474PhosphorylationIHTGEKPYKCNECGK
HHCCCCCEECCCCCH		38.9618767875
475SumoylationHTGEKPYKCNECGKA
HCCCCCEECCCCCHH		38.83-
475SumoylationHTGEKPYKCNECGKA
HCCCCCEECCCCCHH		38.83-
537UbiquitinationYECKECGKAFIRSSS
HHHHHHHHHHHHHHH		52.35-
553PhosphorylationAKHERIHTGEKPYQC
HCCCCCCCCCCCEEC		44.6728111955
581PhosphorylationIQHRKIHTGERPYKC
HCCCCCCCCCCCCCC		44.1824719451
602PhosphorylationFNQNIHLTQHKRIHT
HHCCCCCCCCCCCCC		17.9228555341
652PhosphorylationNKCEKTFSQSSHLTQ
CCCCCCCCCCCCCCH		34.0922817900
658PhosphorylationFSQSSHLTQHQRIHT
CCCCCCCCHHCEECC		20.6922817900
665PhosphorylationTQHQRIHTGEKPYKC
CHHCEECCCCCCCCC		44.6729496963
721PhosphorylationIQHQRIHSGEKPFGC
EEEEECCCCCCCCCC		46.4028555341
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 ZN184_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN184_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 ZN184_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN184_HUMAN !!
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 ZN184_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-117 AND SER-122, ANDMASS SPECTROMETRY.

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