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Protein

E3 ubiquitin-protein ligase NRDP1

Gene

Rnf41

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins. Polyubiquitinates MYD88 (By similarity). Negatively regulates MYD88-dependent production of proinflammatory cytokines. Can promote TRIF-dependent production of type I interferon and inhibits infection with vesicular stomatitis virus. Promotes also activation of TBK1 and IRF3 (PubMed:19483718). 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 (PubMed:18495327). 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 PARK2 modifier that accelerates its degradation, resulting in a reduction of PARK2 activity, influencing the balance of intracellular redox state. The RNF41-PARK2 pathway regulates autophagosome-lysosome fusion during late mitophagy. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control (PubMed:24949970).By similarity3 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri18 – 5740RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri78 – 13861SIAH-type; degeneratePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Autophagy, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1358803. Downregulation of ERBB2:ERBB3 signaling.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase NRDP1 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 41
Gene namesi
Name:Rnf41
Synonyms:Flrf, Nrdp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1914838. Rnf41.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317E3 ubiquitin-protein ligase NRDP1PRO_0000223955Add
BLAST

Post-translational modificationi

Autoubiquitinated. Autoubiquitination leads to proteasomal degradation. Deubiquitinated by USP8 to get stabilized which induces apoptosis.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ8BH75.
PaxDbiQ8BH75.
PRIDEiQ8BH75.

PTM databases

iPTMnetiQ8BH75.
PhosphoSiteiQ8BH75.

Expressioni

Gene expression databases

BgeeiQ8BH75.
CleanExiMM_RNF41.
GenevisibleiQ8BH75. MM.

Interactioni

Subunit structurei

Interacts with USP8, ERBB3, PARK2 and BIRC6 (By similarity). Interacts with CSF2RB, EPOR, IL3RA, MYD88 and TBK1. Interacts with Clec16a (PubMed:24949970).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Clec16aQ80U30-23EBI-7059583,EBI-9696757

GO - Molecular functioni

  • erythropoietin receptor binding Source: MGI
  • interleukin-3 receptor binding Source: MGI
  • Ral GTPase binding Source: MGI

Protein-protein interaction databases

BioGridi212296. 26 interactions.
IntActiQ8BH75. 3 interactions.
MINTiMINT-7148521.
STRINGi10090.ENSMUSP00000100869.

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi196 – 20510Combined sources
Beta strandi208 – 2125Combined sources
Helixi214 – 2163Combined sources
Helixi223 – 23513Combined sources
Helixi240 – 2489Combined sources
Helixi252 – 2543Combined sources
Turni257 – 2593Combined sources
Helixi262 – 2676Combined sources
Helixi269 – 2724Combined sources
Beta strandi283 – 2897Combined sources
Helixi290 – 2923Combined sources
Turni298 – 3003Combined sources
Beta strandi303 – 31210Combined sources
Beta strandi314 – 3163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OGBX-ray1.95A/B193-317[»]
ProteinModelPortaliQ8BH75.
SMRiQ8BH75. Positions 2-107, 193-317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8BH75.

Family & Domainsi

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 1 SIAH-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri18 – 5740RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri78 – 13861SIAH-type; degeneratePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410ISDX. Eukaryota.
ENOG410XNN7. LUCA.
GeneTreeiENSGT00530000063647.
HOGENOMiHOG000006561.
HOVERGENiHBG053154.
InParanoidiQ8BH75.
KOiK11981.
OMAiLMENCHE.
OrthoDBiEOG7D2FDT.
PhylomeDBiQ8BH75.
TreeFamiTF351947.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.90.890.10. 1 hit.
InterProiIPR013323. SIAH-type.
IPR008974. TRAF-like.
IPR015036. USP8_interacting.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
IPR013010. Znf_SIAH.
[Graphical view]
PfamiPF08941. USP8_interact. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS51081. ZF_SIAH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BH75-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGYDVTRFQG DVDEDLICPI CSGVLEEPVQ APHCEHAFCN ACITQWFSQQ
60 70 80 90 100
QTCPVDRSVV TVAHLRPVPR IMRNMLSKLQ IACDNAVFGC SAVVRLDNLM
110 120 130 140 150
SHLSDCEHNP KRPVTCEQGC GLEMPKDELP NHNCIKHLRS VVQQQQSRIA
160 170 180 190 200
ELEKTSAEHK HQLAEQKRDI QLLKAYMRAI RSVNPNLQNL EETIEYNEIL
210 220 230 240 250
EWVNSLQPAR VTRWGGMIST PDAVLQAVIK RSLVESGCPA SIVNELIENA
260 270 280 290 300
HERSWPQGLA TLETRQMNRR YYENYVAKRI PGKQAVVVMA CENQHMGDDM
310
VQEPGLVMIF AHGVEEI
Length:317
Mass (Da):35,891
Last modified:March 1, 2003 - v1
Checksum:i43FE844C06392802
GO
Isoform 2 (identifier: Q8BH75-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-123: Missing.

Show »
Length:194
Mass (Da):22,233
Checksum:i93CB1AC957CE7B3D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1561S → R in AAH19415 (PubMed:15489334).Curated
Sequence conflicti178 – 1781R → Q in BAC28054 (PubMed:16141072).Curated
Sequence conflicti278 – 2781K → E in BAB29953 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 123123Missing in isoform 2. 2 PublicationsVSP_017316Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK015745 mRNA. Translation: BAB29953.1.
AK020527 mRNA. Translation: BAB32125.1.
AK028551 mRNA. Translation: BAC26004.1.
AK030558 mRNA. Translation: BAC27020.1.
AK031657 mRNA. Translation: BAC27496.1.
AK032848 mRNA. Translation: BAC28054.1.
AK034551 mRNA. Translation: BAC28750.1.
AK044103 mRNA. Translation: BAC31779.1.
AK077466 mRNA. Translation: BAC36813.1.
BC019415 mRNA. Translation: AAH19415.1.
BC049078 mRNA. Translation: AAH49078.1.
CCDSiCCDS24277.1. [Q8BH75-1]
RefSeqiNP_001157709.1. NM_001164237.1. [Q8BH75-1]
NP_080535.2. NM_026259.3. [Q8BH75-1]
XP_011241842.1. XM_011243540.1. [Q8BH75-1]
XP_011241843.1. XM_011243541.1. [Q8BH75-2]
UniGeneiMm.294120.

Genome annotation databases

EnsembliENSMUST00000096386; ENSMUSP00000100869; ENSMUSG00000025373. [Q8BH75-1]
ENSMUST00000171342; ENSMUSP00000132751; ENSMUSG00000025373. [Q8BH75-1]
GeneIDi67588.
KEGGimmu:67588.
UCSCiuc007hmr.2. mouse. [Q8BH75-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK015745 mRNA. Translation: BAB29953.1.
AK020527 mRNA. Translation: BAB32125.1.
AK028551 mRNA. Translation: BAC26004.1.
AK030558 mRNA. Translation: BAC27020.1.
AK031657 mRNA. Translation: BAC27496.1.
AK032848 mRNA. Translation: BAC28054.1.
AK034551 mRNA. Translation: BAC28750.1.
AK044103 mRNA. Translation: BAC31779.1.
AK077466 mRNA. Translation: BAC36813.1.
BC019415 mRNA. Translation: AAH19415.1.
BC049078 mRNA. Translation: AAH49078.1.
CCDSiCCDS24277.1. [Q8BH75-1]
RefSeqiNP_001157709.1. NM_001164237.1. [Q8BH75-1]
NP_080535.2. NM_026259.3. [Q8BH75-1]
XP_011241842.1. XM_011243540.1. [Q8BH75-1]
XP_011241843.1. XM_011243541.1. [Q8BH75-2]
UniGeneiMm.294120.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OGBX-ray1.95A/B193-317[»]
ProteinModelPortaliQ8BH75.
SMRiQ8BH75. Positions 2-107, 193-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212296. 26 interactions.
IntActiQ8BH75. 3 interactions.
MINTiMINT-7148521.
STRINGi10090.ENSMUSP00000100869.

PTM databases

iPTMnetiQ8BH75.
PhosphoSiteiQ8BH75.

Proteomic databases

MaxQBiQ8BH75.
PaxDbiQ8BH75.
PRIDEiQ8BH75.

Protocols and materials databases

DNASUi67588.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000096386; ENSMUSP00000100869; ENSMUSG00000025373. [Q8BH75-1]
ENSMUST00000171342; ENSMUSP00000132751; ENSMUSG00000025373. [Q8BH75-1]
GeneIDi67588.
KEGGimmu:67588.
UCSCiuc007hmr.2. mouse. [Q8BH75-1]

Organism-specific databases

CTDi10193.
MGIiMGI:1914838. Rnf41.

Phylogenomic databases

eggNOGiENOG410ISDX. Eukaryota.
ENOG410XNN7. LUCA.
GeneTreeiENSGT00530000063647.
HOGENOMiHOG000006561.
HOVERGENiHBG053154.
InParanoidiQ8BH75.
KOiK11981.
OMAiLMENCHE.
OrthoDBiEOG7D2FDT.
PhylomeDBiQ8BH75.
TreeFamiTF351947.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-1358803. Downregulation of ERBB2:ERBB3 signaling.

Miscellaneous databases

EvolutionaryTraceiQ8BH75.
PROiQ8BH75.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BH75.
CleanExiMM_RNF41.
GenevisibleiQ8BH75. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.90.890.10. 1 hit.
InterProiIPR013323. SIAH-type.
IPR008974. TRAF-like.
IPR015036. USP8_interacting.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
IPR013010. Znf_SIAH.
[Graphical view]
PfamiPF08941. USP8_interact. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS51081. ZF_SIAH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Brain cortex, Embryo, Pituitary, Skin, Testis and Wolffian duct.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and Czech II.
    Tissue: Brain and Mammary tumor.
  3. "E3 ligase FLRF (Rnf41) regulates differentiation of hematopoietic progenitors by governing steady-state levels of cytokine and retinoic acid receptors."
    Jing X., Infante J., Nachtman R.G., Jurecic R.
    Exp. Hematol. 36:1110-1120(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EPOR; IL3RA AND CSF2RB.
  4. "The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon."
    Wang C., Chen T., Zhang J., Yang M., Li N., Xu X., Cao X.
    Nat. Immunol. 10:744-752(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYD88 AND TBK1.
  5. Cited for: FUNCTION IN MITOPHAGY, INTERACTION WITH CLEC16A.
  6. "Structure-based mutagenesis of the substrate-recognition domain of Nrdp1/FLRF identifies the binding site for the receptor tyrosine kinase ErbB3."
    Bouyain S., Leahy D.J.
    Protein Sci. 16:654-661(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 193-317, INTERACTION WITH ERBB3.

Entry informationi

Entry nameiRNF41_MOUSE
AccessioniPrimary (citable) accession number: Q8BH75
Secondary accession number(s): Q8BGJ2
, Q8BMC9, Q8VEA2, Q9CRK6, Q9D568
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.