RNF25_HUMAN - dbPTM
RNF25_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF25_HUMAN
UniProt AC Q96BH1
Protein Name E3 ubiquitin-protein ligase RNF25
Gene Name RNF25
Organism Homo sapiens (Human).
Sequence Length 459
Subcellular Localization
Protein Description E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NKD2 (By similarity). Stimulates transcription mediated by NF-kappa-B..
Protein Sequence MAASASAAAGEEDWVLPSEVEVLESIYLDELQVIKGNGRTSPWEIYITLHPATAEDQDSQYVCFTLVLQVPAEYPHEVPQISIRNPRGLSDEQIHTILQVLGHVAKAGLGTAMLYELIEKGKEILTDNNIPHGQCVICLYGFQEKEAFTKTPCYHYFHCHCLARYIQHMEQELKAQGQEQEQERQHATTKQKAVGVQCPVCREPLVYDLASLKAAPEPQQPMELYQPSAESLRQQEERKRLYQRQQERGGIIDLEAERNRYFISLQQPPAPAEPESAVDVSKGSQPPSTLAAELSTSPAVQSTLPPPLPVATQHICEKIPGTRSNQQRLGETQKAMLDPPKPSRGPWRQPERRHPKGGECHAPKGTRDTQELPPPEGPLKEPMDLKPEPHSQGVEGPPQEKGPGSWQGPPPRRTRDCVRWERSKGRTPGSSYPRLPRGQGAYRPGTRRESLGLESKDGS
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
8UbiquitinationMAASASAAAGEEDWV
CCCCCHHHCCCCCCC		17.3223000965
10UbiquitinationASASAAAGEEDWVLP
CCCHHHCCCCCCCCC		33.8123000965
62UbiquitinationEDQDSQYVCFTLVLQ
CCCCCCEEEEEEEEE		1.3524816145
82PhosphorylationPHEVPQISIRNPRGL
CCCCCCEEECCCCCC		15.3924719451
90PhosphorylationIRNPRGLSDEQIHTI
ECCCCCCCHHHHHHH		41.76-
115PhosphorylationGLGTAMLYELIEKGK
CHHHHHHHHHHHHCC		8.8023403867
120UbiquitinationMLYELIEKGKEILTD
HHHHHHHHCCHHCCC		69.1823000965
120UbiquitinationMLYELIEKGKEILTD
HHHHHHHHCCHHCCC		69.1821890473
122UbiquitinationYELIEKGKEILTDNN
HHHHHHCCHHCCCCC		53.2823000965
145UbiquitinationCLYGFQEKEAFTKTP
EECCCCCCCCCCCCC		43.4929967540
174UbiquitinationQHMEQELKAQGQEQE
HHHHHHHHHHCHHHH		37.6024816145
206UbiquitinationPVCREPLVYDLASLK
CCCCCCCEEHHHHCC		5.2423000965
213AcetylationVYDLASLKAAPEPQQ
EEHHHHCCCCCCCCC		39.7519816911
222UbiquitinationAPEPQQPMELYQPSA
CCCCCCCCCHHCCCH		4.8823000965
229UbiquitinationMELYQPSAESLRQQE
CCHHCCCHHHHHHHH		19.6523000965
244UbiquitinationERKRLYQRQQERGGI
HHHHHHHHHHHHCCC		26.9623000965
252UbiquitinationQQERGGIIDLEAERN
HHHHCCCEEEEHHHC		5.8223000965
261PhosphorylationLEAERNRYFISLQQP
EEHHHCCEEEECCCC		14.6028176443
264PhosphorylationERNRYFISLQQPPAP
HHCCEEEECCCCCCC		15.3828176443
274UbiquitinationQPPAPAEPESAVDVS
CCCCCCCCCCCCCCC		42.8422817900
276PhosphorylationPAPAEPESAVDVSKG
CCCCCCCCCCCCCCC		44.2928176443
281PhosphorylationPESAVDVSKGSQPPS
CCCCCCCCCCCCCCC		27.1728176443
284PhosphorylationAVDVSKGSQPPSTLA
CCCCCCCCCCCCHHH		43.1628122231
288PhosphorylationSKGSQPPSTLAAELS
CCCCCCCCHHHHHHC		42.6128122231
289PhosphorylationKGSQPPSTLAAELST
CCCCCCCHHHHHHCC		26.6228122231
295PhosphorylationSTLAAELSTSPAVQS
CHHHHHHCCCCCHHH		20.5325159151
296PhosphorylationTLAAELSTSPAVQST
HHHHHHCCCCCHHHC		51.8925159151
297PhosphorylationLAAELSTSPAVQSTL
HHHHHCCCCCHHHCC		13.9026657352
302PhosphorylationSTSPAVQSTLPPPLP
CCCCCHHHCCCCCCC		25.8826657352
303PhosphorylationTSPAVQSTLPPPLPV
CCCCHHHCCCCCCCC		26.6225394399
312PhosphorylationPPPLPVATQHICEKI
CCCCCCHHHHHHHHC		22.4028122231
318UbiquitinationATQHICEKIPGTRSN
HHHHHHHHCCCCCCC		50.1923000965
334UbiquitinationQRLGETQKAMLDPPK
CCCCCHHHHHCCCCC		43.0921890473
334UbiquitinationQRLGETQKAMLDPPK
CCCCCHHHHHCCCCC		43.0923000965
341UbiquitinationKAMLDPPKPSRGPWR
HHHCCCCCCCCCCCC		62.1023000965
341UbiquitinationKAMLDPPKPSRGPWR
HHHCCCCCCCCCCCC		62.1021890473
344UbiquitinationLDPPKPSRGPWRQPE
CCCCCCCCCCCCCCC		64.8222053931
348MethylationKPSRGPWRQPERRHP
CCCCCCCCCCCCCCC		45.36115491425
356UbiquitinationQPERRHPKGGECHAP
CCCCCCCCCCCCCCC		73.7123000965
364UbiquitinationGGECHAPKGTRDTQE
CCCCCCCCCCCCCCC		73.9423000965
386UbiquitinationLKEPMDLKPEPHSQG
CCCCCCCCCCCCCCC		42.9722817900
391PhosphorylationDLKPEPHSQGVEGPP
CCCCCCCCCCCCCCC		39.0728555341
405PhosphorylationPQEKGPGSWQGPPPR
CCCCCCCCCCCCCCC		21.2522817900
427PhosphorylationWERSKGRTPGSSYPR
HHHHCCCCCCCCCCC		40.4428674419
430PhosphorylationSKGRTPGSSYPRLPR
HCCCCCCCCCCCCCC		28.0928152594
431PhosphorylationKGRTPGSSYPRLPRG
CCCCCCCCCCCCCCC		45.1028152594
432PhosphorylationGRTPGSSYPRLPRGQ
CCCCCCCCCCCCCCC		8.2828152594
434MethylationTPGSSYPRLPRGQGA
CCCCCCCCCCCCCCC		49.4480701993
437MethylationSSYPRLPRGQGAYRP
CCCCCCCCCCCCCCC		55.4418959381
442PhosphorylationLPRGQGAYRPGTRRE
CCCCCCCCCCCCHHH		24.94-
450PhosphorylationRPGTRRESLGLESKD
CCCCHHHHCCCCCCC		26.4029255136
455PhosphorylationRESLGLESKDGS---
HHHCCCCCCCCC---		40.8823403867
456UbiquitinationESLGLESKDGS----
HHCCCCCCCCC----		57.6521906983
459PhosphorylationGLESKDGS-------
CCCCCCCC-------		47.3721712546
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 RNF25_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF25_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 RNF25_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF65_HUMANRELAphysical
12748188
UB2D1_HUMANUBE2D1physical
14517261
UB2D2_HUMANUBE2D2physical
14517261
TRI27_HUMANTRIM27physical
22493164
UB2E3_HUMANUBE2E3physical
24901938
UB2D2_HUMANUBE2D2physical
24901938
UB2D2_HUMANUBE2D2physical
26475854
RNF25_HUMANRNF25physical
26475854
UB2E3_HUMANUBE2E3physical
26475854
UB2D4_HUMANUBE2D4physical
28514442
UB2E1_HUMANUBE2E1physical
28514442
UB2D3_HUMANUBE2D3physical
28514442
SPB4_HUMANSERPINB4physical
28514442
NGAL_HUMANLCN2physical
28514442
INVO_HUMANIVLphysical
28514442
S10A7_HUMANS100A7physical
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 RNF25_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND MASSSPECTROMETRY.

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