RNF38_HUMAN - dbPTM
RNF38_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF38_HUMAN
UniProt AC Q9H0F5
Protein Name E3 ubiquitin-protein ligase RNF38
Gene Name RNF38
Organism Homo sapiens (Human).
Sequence Length 515
Subcellular Localization Nucleus .
Protein Description Acts as an E3 ubiquitin-protein ligase able to ubiquitinate p53/TP53 which promotes its relocalization to discrete foci associated with PML nuclear bodies. Exhibits preference for UBE2D2 as a E2 enzyme..
Protein Sequence MACKISPGANSASLPGHPNKVICERVRLQSLFPLLPSDQNTTVQEDAHFKAFFQSEDSPSPKRQRLSHSVFDYTSASPAPSPPMRPWEMTSNRQPPSVRPSQHHFSGERCNTPARNRRSPPVRRQRGRRDRLSRHNSISQDENYHHLPYAQQQAIEEPRAFHPPNVSPRLLHPAAHPPQQNAVMVDIHDQLHQGTVPVSYTVTTVAPHGIPLCTGQHIPACSTQQVPGCSVVFSGQHLPVCSVPPPMLQACSVQHLPVPYAAFPPLISSDPFLIHPPHLSPHHPPHLPPPGQFVPFQTQQSRSPLQRIENEVELLGEHLPVGGFTYPPSAHPPTLPPSAPLQFLTHDPLHQEVSFGVPYPPFMPRRLTGRSRYRSQQPIPPPPYHPSLLPYVLSMLPVPPAVGPTFSFELDVEDGEVENYEALLNLAERLGEAKPRGLTKADIEQLPSYRFNPNNHQSEQTLCVVCMCDFESRQLLRVLPCNHEFHAKCVDKWLKANRTCPICRADASEVHRDSE
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
6Phosphorylation--MACKISPGANSAS
--CCCEECCCCCCCC
11.6324719451
13PhosphorylationSPGANSASLPGHPNK
CCCCCCCCCCCCCCC
34.6124719451
55PhosphorylationHFKAFFQSEDSPSPK
HHHHHHCCCCCCCHH
37.9129978859
58PhosphorylationAFFQSEDSPSPKRQR
HHHCCCCCCCHHHHH
24.1925850435
60PhosphorylationFQSEDSPSPKRQRLS
HCCCCCCCHHHHHCC
47.1825850435
81PhosphorylationTSASPAPSPPMRPWE
CCCCCCCCCCCCCCC
43.6824719451
119PhosphorylationTPARNRRSPPVRRQR
CCCHHCCCCCCHHHH
30.25-
137PhosphorylationDRLSRHNSISQDENY
HHHHHCCCCCCCCCC
19.9327080861
139PhosphorylationLSRHNSISQDENYHH
HHHCCCCCCCCCCCC
31.2527080861
144PhosphorylationSISQDENYHHLPYAQ
CCCCCCCCCCCCHHH
6.6427080861
149PhosphorylationENYHHLPYAQQQAIE
CCCCCCCHHHHHHHH
24.3327080861
167PhosphorylationAFHPPNVSPRLLHPA
HCCCCCCCHHHCCCC
15.7924719451
327UbiquitinationPVGGFTYPPSAHPPT
CCCCCCCCCCCCCCC
17.2021963094
357 (in isoform 3)Ubiquitination-3.7521906983
357UbiquitinationHQEVSFGVPYPPFMP
CCCCCCCCCCCCCCC
3.7521963094
364UbiquitinationVPYPPFMPRRLTGRS
CCCCCCCCCCCCCCC
20.7221906983
369UbiquitinationFMPRRLTGRSRYRSQ
CCCCCCCCCCCCCCC
30.1121963094
390UbiquitinationPYHPSLLPYVLSMLP
CCCHHHHHHHHHCCC
23.6021963094
390 (in isoform 2)Ubiquitination-23.6021906983
409UbiquitinationVGPTFSFELDVEDGE
CCCCEEEEEECCCCC
42.7529967540
419UbiquitinationVEDGEVENYEALLNL
CCCCCEECHHHHHHH
45.16-
434AcetylationAERLGEAKPRGLTKA
HHHHHCCCCCCCCHH
30.8312656617
440UbiquitinationAKPRGLTKADIEQLP
CCCCCCCHHHHHHCC
49.4521963094
440 (in isoform 1)Ubiquitination-49.4521906983
442UbiquitinationPRGLTKADIEQLPSY
CCCCCHHHHHHCCCC
46.6529967540
448PhosphorylationADIEQLPSYRFNPNN
HHHHHCCCCCCCCCC
37.2224719451
492UbiquitinationFHAKCVDKWLKANRT
HHHHHHHHHHHHCCC
33.7529967540
495UbiquitinationKCVDKWLKANRTCPI
HHHHHHHHHCCCCCC
42.36-
514PhosphorylationASEVHRDSE------
HHHHHCCCC------
45.20-

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 RNF38_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF38_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 RNF38_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DTX3_HUMANDTX3physical
22493164
RNF38_HUMANRNF38physical
23973461
UB2D2_HUMANUBE2D2physical
23973461
P53_HUMANTP53physical
23973461
RNF38_HUMANRNF38physical
25801170
UB2D2_HUMANUBE2D2physical
25801170
UBC_HUMANUBCphysical
25801170

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 RNF38_HUMAN

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Related Literatures of Post-Translational Modification

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