RNF41_HUMAN - dbPTM
RNF41_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF41_HUMAN
UniProt AC Q9H4P4
Protein Name E3 ubiquitin-protein ligase NRDP1
Gene Name RNF41
Organism Homo sapiens (Human).
Sequence Length 317
Subcellular Localization
Protein Description Acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins. Polyubiquitinates MYD88. Negatively regulates MYD88-dependent production of proinflammatory cytokines. Can promote TRIF-dependent production of type I interferon and inhibits infection with vesicular stomatitis virus (By similarity). Promotes also activation of TBK1 and IRF3. Involved in the ubiquitination of erythropoietin (EPO) and interleukin-3 (IL-3) receptors. Thus, through maintaining basal levels of cytokine receptors, RNF41 is involved in the control of hematopoietic progenitor cell differentiation into myeloerythroid lineages (By similarity). Contributes to the maintenance of steady-state ERBB3 levels by mediating its growth factor-independent degradation. Involved in the degradation of the inhibitor of apoptosis BIRC6 and thus is an important regulator of cell death by promoting apoptosis. Acts also as a PRKN modifier that accelerates its degradation, resulting in a reduction of PRKN activity, influencing the balance of intracellular redox state. The RNF41-PRKN pathway regulates autophagosome-lysosome fusion during late mitophagy. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control. [PubMed: 24949970]
Protein Sequence MGYDVTRFQGDVDEDLICPICSGVLEEPVQAPHCEHAFCNACITQWFSQQQTCPVDRSVVTVAHLRPVPRIMRNMLSKLQIACDNAVFGCSAVVRLDNLMSHLSDCEHNPKRPVTCEQGCGLEMPKDELPNHNCIKHLRSVVQQQQTRIAELEKTSAEHKHQLAEQKRDIQLLKAYMRAIRSVNPNLQNLEETIEYNEILEWVNSLQPARVTRWGGMISTPDAVLQAVIKRSLVESGCPASIVNELIENAHERSWPQGLATLETRQMNRRYYENYVAKRIPGKQAVVVMACENQHMGDDMVQEPGLVMIFAHGVEEI
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
103UbiquitinationLDNLMSHLSDCEHNP
HHHHHHHHHCCCCCC
3.4721890473
106S-nitrosylationLMSHLSDCEHNPKRP
HHHHHHCCCCCCCCC
5.2824105792
134S-nitrosylationDELPNHNCIKHLRSV
CCCCCCHHHHHHHHH
3.2224105792
136UbiquitinationLPNHNCIKHLRSVVQ
CCCCHHHHHHHHHHH
38.49-
154UbiquitinationTRIAELEKTSAEHKH
HHHHHHHHHHHHHHH
61.48-
167AcetylationKHQLAEQKRDIQLLK
HHHHHHHHHHHHHHH
43.4730591977
167UbiquitinationKHQLAEQKRDIQLLK
HHHHHHHHHHHHHHH
43.47-
174UbiquitinationKRDIQLLKAYMRAIR
HHHHHHHHHHHHHHH
46.1721890473
238S-nitrosylationRSLVESGCPASIVNE
HHHHHCCCCHHHHHH
3.3724105792
254PhosphorylationIENAHERSWPQGLAT
HHHHHHCCCCCHHHH
39.87-
264PhosphorylationQGLATLETRQMNRRY
CHHHHHHHHHHHHHH
29.3424850871

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
254SPhosphorylationKinaseMARK2Q7KZI7
PSP
-KUbiquitinationE3 ubiquitin ligaseRNF41Q9H4P4
PMID:15314180

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF41_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 RNF41_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBP8_HUMANUSP8physical
15314180
BIRC6_HUMANBIRC6physical
15314180
ERBB3_HUMANERBB3physical
11867753
ERBB4_HUMANERBB4physical
11867753
PRKN_HUMANPARK2physical
18541373
ERBB3_HUMANERBB3physical
12411582
PRKN_HUMANPARK2physical
15632191
ERBB3_HUMANERBB3physical
21576364
BIRC6_HUMANBIRC6physical
14765125
ERBB3_HUMANERBB3physical
17384230
LEPR_HUMANLEPRphysical
21378310
UB2D3_HUMANUBE2D3physical
18541373
UB2D3_HUMANUBE2D3physical
14765125
A4_HUMANAPPphysical
21832049
RNF41_HUMANRNF41physical
22493164
MARK2_HUMANMARK2physical
24259665
RNF41_HUMANRNF41physical
25416956
AR6P4_HUMANARL6IP4physical
25416956
CA109_HUMANC1orf109physical
25416956
LZTS2_HUMANLZTS2physical
25416956
ISCA2_HUMANISCA2physical
25416956
ASB6_HUMANASB6physical
25416956
RFC4_HUMANRFC4physical
21516116
KIFC3_HUMANKIFC3physical
26496610
NPAT_HUMANNPATphysical
26496610
P4HA1_HUMANP4HA1physical
26496610
SF01_HUMANSF1physical
26496610
EVI5_HUMANEVI5physical
26496610
LGAT1_HUMANLPGAT1physical
26496610
N4BP3_HUMANN4BP3physical
26496610
MTCL1_HUMANMTCL1physical
26496610
CL16A_HUMANCLEC16Aphysical
26496610
CLAP1_HUMANCLASP1physical
26496610
C1GLC_HUMANC1GALT1C1physical
26496610
ITSN2_HUMANITSN2physical
26496610
RAIN_HUMANRASIP1physical
26496610
RFWD3_HUMANRFWD3physical
26496610
REN3A_HUMANUPF3Aphysical
26496610
NAV1_HUMANNAV1physical
26496610
SOGA1_HUMANSOGA1physical
26496610
ZAP70_HUMANZAP70physical
26390156
UBS3B_HUMANUBASH3Bphysical
26390156
UBS3A_HUMANUBASH3Aphysical
26390156
CD3Z_HUMANCD247physical
26390156
VE2_HPV16E2physical
26963794
VANG1_HUMANVANGL1physical
27648936
DVL2_HUMANDVL2physical
27648936
ERBB4_HUMANERBB4physical
27648936
IRS4_HUMANIRS4physical
28973533
UBP8_HUMANUSP8physical
28973533
VPS52_HUMANVPS52physical
28973533
VPS52_HUMANVPS52physical
28542518
KDM3B_HUMANKDM3Bphysical
28542518
HOME2_HUMANHOMER2physical
28542518
ASB6_HUMANASB6physical
28542518
RNF41_HUMANRNF41physical
28542518
RTN4_HUMANRTN4physical
27353365

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 RNF41_HUMAN

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Related Literatures of Post-Translational Modification

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