RNF34_HUMAN - dbPTM
RNF34_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF34_HUMAN
UniProt AC Q969K3
Protein Name E3 ubiquitin-protein ligase RNF34 {ECO:0000305}
Gene Name RNF34 {ECO:0000312|HGNC:HGNC:17297}
Organism Homo sapiens (Human).
Sequence Length 372
Subcellular Localization Cell membrane
Peripheral membrane protein . Endomembrane system
Peripheral membrane protein . Nucleus . Nucleus speckle . Cytoplasm, cytosol .
Protein Description E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. [PubMed: 15069192 May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway (Ref.13 Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation]
Protein Sequence MKAGATSMWASCCGLLNEVMGTGAVRGQQSAFAGATGPFRFTPNPEFSTYPPAATEGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSVCSVLQENLRRCSTCHLLQETAFQRPQLMRLKVKDLRQYLILRNIPIDTCREKEDLVDLVLCHHGLGSEDDMDTSSLNSSRSQTSSFFTRSFFSNYTAPSATMSSFQGELMDGDQTSRSGVPAQVQSEITSANTEDDDDDDDEDDDDEEENAEDRNPGLSKERVRASLSDLSSLDDVEGMSVRQLKEILARNFVNYSGCCEKWELVEKVNRLYKENEENQKSYGERLQLQDEEDDSLCRICMDAVIDCVLLECGHMVTCTKCGKRMSECPICRQYVVRAVHVFKS
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
2Ubiquitination------MKAGATSMW
------CCCCHHHHH		56.37-
11PhosphorylationGATSMWASCCGLLNE
CHHHHHHHHHHHHHH		8.4030631047
23 (in isoform 2)Phosphorylation-19.1522210691
70PhosphorylationKACGLSFSVFRKKHV
CCCCCCCHHHCCCCE		19.5724076635
83UbiquitinationHVCCDCKKDFCSVCS
CEECCCCCCHHHHHH		63.47-
90PhosphorylationKDFCSVCSVLQENLR
CCHHHHHHHHHHHHH		24.57-
100PhosphorylationQENLRRCSTCHLLQE
HHHHHHCHHHHHHHH		32.0524719451
101PhosphorylationENLRRCSTCHLLQET
HHHHHCHHHHHHHHH		13.9424719451
121UbiquitinationQLMRLKVKDLRQYLI
HHHHCCHHHHHHHHH		49.83-
155PhosphorylationLCHHGLGSEDDMDTS
HCCCCCCCCCCCCCH		42.7826471730
161PhosphorylationGSEDDMDTSSLNSSR
CCCCCCCCHHHCCCC		17.3626471730
162PhosphorylationSEDDMDTSSLNSSRS
CCCCCCCHHHCCCCH		28.6726471730
163PhosphorylationEDDMDTSSLNSSRSQ
CCCCCCHHHCCCCHH		33.3927251275
164PhosphorylationDDMDTSSLNSSRSQT
CCCCCHHHCCCCHHH		7.8427251275
166PhosphorylationMDTSSLNSSRSQTSS
CCCHHHCCCCHHHHH		32.2126471730
167PhosphorylationDTSSLNSSRSQTSSF
CCHHHCCCCHHHHHH		34.5726471730
169PhosphorylationSSLNSSRSQTSSFFT
HHHCCCCHHHHHHHH		39.4928857561
170PhosphorylationSLNSSRSQTSSFFTR
HHCCCCHHHHHHHHH		44.2724719451
171PhosphorylationLNSSRSQTSSFFTRS
HCCCCHHHHHHHHHH		27.8223186163
172PhosphorylationNSSRSQTSSFFTRSF
CCCCHHHHHHHHHHH		19.9428555341
173PhosphorylationSSRSQTSSFFTRSFF
CCCHHHHHHHHHHHH		27.9728857561
187PhosphorylationFSNYTAPSATMSSFQ
HCCCCCCCCCCCHHC		33.6328348404
189PhosphorylationNYTAPSATMSSFQGE
CCCCCCCCCCHHCCE		23.1728348404
191PhosphorylationTAPSATMSSFQGELM
CCCCCCCCHHCCEEC		24.5228348404
192PhosphorylationAPSATMSSFQGELMD
CCCCCCCHHCCEECC		15.6928348404
214PhosphorylationGVPAQVQSEITSANT
CCCHHHHHHHHCCCC		31.9123090842
217PhosphorylationAQVQSEITSANTEDD
HHHHHHHHCCCCCCC		20.1023090842
218PhosphorylationQVQSEITSANTEDDD
HHHHHHHCCCCCCCC		25.7823090842
221PhosphorylationSEITSANTEDDDDDD
HHHHCCCCCCCCCCC		40.2730576142
247PhosphorylationEDRNPGLSKERVRAS
HHCCCCCCHHHHHHH		38.0826074081
248UbiquitinationDRNPGLSKERVRASL
HCCCCCCHHHHHHHH		55.36-
254PhosphorylationSKERVRASLSDLSSL
CHHHHHHHHHHHHCC		20.1729255136
255PhosphorylationKERVRASLSDLSSLD
HHHHHHHHHHHHCCC		4.5124719451
256PhosphorylationERVRASLSDLSSLDD
HHHHHHHHHHHCCCC		33.7329255136
259PhosphorylationRASLSDLSSLDDVEG
HHHHHHHHCCCCCCC		33.5723927012
260PhosphorylationASLSDLSSLDDVEGM
HHHHHHHCCCCCCCC		43.0223927012
261PhosphorylationSLSDLSSLDDVEGMS
HHHHHHCCCCCCCCC		6.1527251275
268PhosphorylationLDDVEGMSVRQLKEI
CCCCCCCCHHHHHHH		25.6323403867
273UbiquitinationGMSVRQLKEILARNF
CCCHHHHHHHHHHCC		34.08-
284PhosphorylationARNFVNYSGCCEKWE
HHCCCCCCCHHHHHH		21.8325159151
289UbiquitinationNYSGCCEKWELVEKV
CCCCHHHHHHHHHHH		31.86-
295UbiquitinationEKWELVEKVNRLYKE
HHHHHHHHHHHHHHH		37.01-
300PhosphorylationVEKVNRLYKENEENQ
HHHHHHHHHHCHHHH		17.0230622161
301UbiquitinationEKVNRLYKENEENQK
HHHHHHHHHCHHHHC		59.67-
308UbiquitinationKENEENQKSYGERLQ
HHCHHHHCCHHHHHC		58.17-
309PhosphorylationENEENQKSYGERLQL
HCHHHHCCHHHHHCC		28.7129496907
323PhosphorylationLQDEEDDSLCRICMD
CCCCCCCHHHHHHHH		41.5125159151
354PhosphorylationTKCGKRMSECPICRQ
CCCCCCHHCCHHHHH		39.8324719451
355PhosphorylationKCGKRMSECPICRQY
CCCCCHHCCHHHHHH		34.6624719451
372PhosphorylationRAVHVFKS-------
HHHHHCCC-------		33.7121712546
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 RNF34_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF34_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 RNF34_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
17121812
ANC2_HUMANANAPC2physical
21903591
CDC20_HUMANCDC20physical
21903591
FZR1_HUMANFZR1physical
21903591
A4_HUMANAPPphysical
21832049
TRI23_HUMANTRIM23physical
22493164
NOD1_HUMANNOD1physical
25012219
UB2D2_HUMANUBE2D2physical
15069192
CASP8_HUMANCASP8physical
15069192
CASP9_HUMANCASP9physical
15069192
CASPA_HUMANCASP10physical
15069192
U119B_HUMANUNC119Bphysical
28514442
EFCB7_HUMANEFCAB7physical
28514442
KLH15_HUMANKLHL15physical
28514442
HSP7C_HUMANHSPA8physical
28514442
TSR3_HUMANTSR3physical
28514442
HSP72_HUMANHSPA2physical
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 RNF34_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-254, AND MASSSPECTROMETRY.
"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-254, AND MASSSPECTROMETRY.

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