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Protein

E3 ubiquitin-protein ligase NRDP1

Gene

RNF41

Organism
Homo sapiens (Human)
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. 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 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 similarity7 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

  • acid-amino acid ligase activity Source: InterPro
  • protein tag Source: InterPro
  • Ral GTPase binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: ParkinsonsUK-UCL
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • autophagy Source: UniProtKB-KW
  • ERBB2 signaling pathway Source: Reactome
  • extrinsic apoptotic signaling pathway Source: UniProtKB
  • negative regulation of cell migration Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • positive regulation of reactive oxygen species metabolic process Source: ParkinsonsUK-UCL
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  • proteasomal protein catabolic process Source: ParkinsonsUK-UCL
  • protein autoubiquitination Source: FlyBase
  • protein polyubiquitination Source: UniProtKB
  • regulation of establishment of cell polarity Source: Ensembl
  • regulation of lymphocyte differentiation Source: Ensembl
  • regulation of MAPK cascade Source: MGI
  • regulation of myeloid cell differentiation Source: Ensembl
  • regulation of protein kinase B signaling Source: MGI
  • regulation of reactive oxygen species metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Autophagy, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi6.3.2.19. 2681.
ReactomeiR-HSA-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
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
ORF Names:SBBI03
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:18401. RNF41.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341C → S: Loss of activity; when associated with Q-36. 2 Publications
Mutagenesisi36 – 361H → Q: Loss of activity; when associated with S-34. 2 Publications
Mutagenesisi56 – 561D → V: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA134875033.

Polymorphism and mutation databases

BioMutaiRNF41.
DMDMi88909120.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317E3 ubiquitin-protein ligase NRDP1PRO_0000223954Add
BLAST

Post-translational modificationi

Autoubiquitinated. Autoubiquitination leads to proteasomal degradation. Deubiquitinated by USP8 to get stabilized which induces apoptosis.3 Publications

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ9H4P4.
PaxDbiQ9H4P4.
PRIDEiQ9H4P4.

PTM databases

iPTMnetiQ9H4P4.
PhosphoSiteiQ9H4P4.

Expressioni

Tissue specificityi

Detected in ovary, testis and prostate.1 Publication

Gene expression databases

BgeeiQ9H4P4.
CleanExiHS_RNF41.
ExpressionAtlasiQ9H4P4. baseline and differential.
GenevisibleiQ9H4P4. HS.

Organism-specific databases

HPAiHPA016812.
HPA052170.

Interactioni

Subunit structurei

Interacts with USP8, ERBB3, PARK2 and BIRC6. Interacts with CSF2RB, EPOR, IL3RA, MYD88 and TBK1. Interacts with CLEC16A (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ARL6IP4Q66PJ3-33EBI-2130266,EBI-10248982
ASB6Q9NWX53EBI-2130266,EBI-6425205
C1orf109Q9NX043EBI-2130266,EBI-8643161
HOMER2Q9NSB83EBI-2130266,EBI-2126733
ISCA2Q86U283EBI-2130266,EBI-10258659
LZTS2Q9BRK43EBI-2130266,EBI-741037
RFC4P352494EBI-2130266,EBI-476655
TTC1Q996146EBI-2130266,EBI-742074
VPS52Q8N1B43EBI-2130266,EBI-2799833

GO - Molecular functioni

  • Ral GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115488. 66 interactions.
IntActiQ9H4P4. 45 interactions.
STRINGi9606.ENSP00000342755.

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi193 – 20513Combined sources
Beta strandi206 – 2116Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2204Combined sources
Helixi223 – 23513Combined sources
Helixi240 – 2489Combined sources
Helixi252 – 2543Combined sources
Turni257 – 2593Combined sources
Helixi262 – 2676Combined sources
Turni268 – 2703Combined sources
Helixi271 – 2744Combined sources
Beta strandi277 – 2793Combined 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
2FZPX-ray1.87A193-317[»]
2GWFX-ray2.30B/D/F193-317[»]
ProteinModelPortaliQ9H4P4.
SMRiQ9H4P4. Positions 2-107, 193-317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H4P4.

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.
InParanoidiQ9H4P4.
KOiK11981.
OMAiLMENCHE.
PhylomeDBiQ9H4P4.
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: Q9H4P4-1) [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 VVQQQQTRIA
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):35,905
Last modified:February 21, 2006 - v2
Checksum:i46AE87AF8BE1A369
GO
Isoform 2 (identifier: Q9H4P4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: Missing.

Note: No experimental confirmation available.
Show »
Length:246
Mass (Da):27,965
Checksum:iF21D7FD03FA53642
GO

Sequence cautioni

The sequence AAG01988.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7171Missing in isoform 2. 1 PublicationVSP_044670Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077599 mRNA. Translation: AAC27647.1.
AK314811 mRNA. Translation: BAG37335.1.
AC073896 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96909.1.
CH471054 Genomic DNA. Translation: EAW96910.1.
BC024284 mRNA. No translation available.
BC032637 mRNA. Translation: AAH32637.1.
AY007109 mRNA. Translation: AAG01988.1. Different initiation.
CCDSiCCDS8909.1. [Q9H4P4-1]
CCDS8910.1. [Q9H4P4-2]
RefSeqiNP_001229755.1. NM_001242826.1. [Q9H4P4-1]
NP_005776.1. NM_005785.3. [Q9H4P4-1]
NP_919339.1. NM_194358.2. [Q9H4P4-2]
NP_919340.1. NM_194359.2. [Q9H4P4-1]
XP_005268618.1. XM_005268561.3. [Q9H4P4-2]
XP_011536036.1. XM_011537734.1. [Q9H4P4-2]
XP_011536037.1. XM_011537735.1. [Q9H4P4-2]
UniGeneiHs.524502.

Genome annotation databases

EnsembliENST00000345093; ENSP00000342755; ENSG00000181852. [Q9H4P4-1]
ENST00000394013; ENSP00000377581; ENSG00000181852. [Q9H4P4-2]
ENST00000552656; ENSP00000447303; ENSG00000181852. [Q9H4P4-1]
ENST00000615206; ENSP00000484671; ENSG00000181852. [Q9H4P4-1]
GeneIDi10193.
KEGGihsa:10193.
UCSCiuc001ske.3. human. [Q9H4P4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077599 mRNA. Translation: AAC27647.1.
AK314811 mRNA. Translation: BAG37335.1.
AC073896 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96909.1.
CH471054 Genomic DNA. Translation: EAW96910.1.
BC024284 mRNA. No translation available.
BC032637 mRNA. Translation: AAH32637.1.
AY007109 mRNA. Translation: AAG01988.1. Different initiation.
CCDSiCCDS8909.1. [Q9H4P4-1]
CCDS8910.1. [Q9H4P4-2]
RefSeqiNP_001229755.1. NM_001242826.1. [Q9H4P4-1]
NP_005776.1. NM_005785.3. [Q9H4P4-1]
NP_919339.1. NM_194358.2. [Q9H4P4-2]
NP_919340.1. NM_194359.2. [Q9H4P4-1]
XP_005268618.1. XM_005268561.3. [Q9H4P4-2]
XP_011536036.1. XM_011537734.1. [Q9H4P4-2]
XP_011536037.1. XM_011537735.1. [Q9H4P4-2]
UniGeneiHs.524502.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FZPX-ray1.87A193-317[»]
2GWFX-ray2.30B/D/F193-317[»]
ProteinModelPortaliQ9H4P4.
SMRiQ9H4P4. Positions 2-107, 193-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115488. 66 interactions.
IntActiQ9H4P4. 45 interactions.
STRINGi9606.ENSP00000342755.

PTM databases

iPTMnetiQ9H4P4.
PhosphoSiteiQ9H4P4.

Polymorphism and mutation databases

BioMutaiRNF41.
DMDMi88909120.

Proteomic databases

MaxQBiQ9H4P4.
PaxDbiQ9H4P4.
PRIDEiQ9H4P4.

Protocols and materials databases

DNASUi10193.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000345093; ENSP00000342755; ENSG00000181852. [Q9H4P4-1]
ENST00000394013; ENSP00000377581; ENSG00000181852. [Q9H4P4-2]
ENST00000552656; ENSP00000447303; ENSG00000181852. [Q9H4P4-1]
ENST00000615206; ENSP00000484671; ENSG00000181852. [Q9H4P4-1]
GeneIDi10193.
KEGGihsa:10193.
UCSCiuc001ske.3. human. [Q9H4P4-1]

Organism-specific databases

CTDi10193.
GeneCardsiRNF41.
HGNCiHGNC:18401. RNF41.
HPAiHPA016812.
HPA052170.
neXtProtiNX_Q9H4P4.
PharmGKBiPA134875033.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ISDX. Eukaryota.
ENOG410XNN7. LUCA.
GeneTreeiENSGT00530000063647.
HOGENOMiHOG000006561.
HOVERGENiHBG053154.
InParanoidiQ9H4P4.
KOiK11981.
OMAiLMENCHE.
PhylomeDBiQ9H4P4.
TreeFamiTF351947.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 2681.
ReactomeiR-HSA-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiQ9H4P4.
GeneWikiiRNF41.
GenomeRNAii10193.
PROiQ9H4P4.

Gene expression databases

BgeeiQ9H4P4.
CleanExiHS_RNF41.
ExpressionAtlasiQ9H4P4. baseline and differential.
GenevisibleiQ9H4P4. HS.

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. "Hypothetical protein SBBI03."
    Zhang W., Cao X., Wan T., Yuan Z., He L., Li N., Zhu X., Tao Q.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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).
    Tissue: Leiomyosarcoma and Lymph.
  6. Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-317 (ISOFORM 1).
    Tissue: Lymphoblast.
  7. "Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3."
    Qiu X.-B., Goldberg A.L.
    Proc. Natl. Acad. Sci. U.S.A. 99:14843-14848(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ERBB3, MUTAGENESIS OF CYS-34; HIS-36 AND ASP-56, TISSUE SPECIFICITY.
  8. "Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel pathway for triggering apoptosis."
    Qiu X.B., Markant S.L., Yuan J., Goldberg A.L.
    EMBO J. 23:800-810(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BIRC6.
  9. "Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8."
    Wu X., Yen L., Irwin L., Sweeney C., Carraway K.L. III
    Mol. Cell. Biol. 24:7748-7757(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOUBIQUITINATION, INTERACTION WITH USP8, DEUBIQUITINATION BY USP8, MUTAGENESIS OF CYS-34 AND HIS-36.
  10. "RING finger ubiquitin-protein isopeptide ligase Nrdp1/FLRF regulates parkin stability and activity."
    Zhong L., Tan Y., Zhou A., Yu Q., Zhou J.
    J. Biol. Chem. 280:9425-9430(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PARK2.
  11. "Neuregulin-induced ErbB3 downregulation is mediated by a protein stability cascade involving the E3 ubiquitin ligase Nrdp1."
    Cao Z., Wu X., Yen L., Sweeney C., Carraway K.L. III
    Mol. Cell. Biol. 27:2180-2188(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION.
  12. "Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress."
    Yu F., Zhou J.
    Neurosci. Lett. 440:4-8(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PARK2.
  13. "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, UBIQUITINATION OF MYD88 AND TBK1.
  14. Cited for: FUNCTION IN MITOPHAGY.
  15. "Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)."
    Avvakumov G.V., Walker J.R., Xue S., Finerty P.J. Jr., Mackenzie F., Newman E.M., Dhe-Paganon S.
    J. Biol. Chem. 281:38061-38070(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 193-317 IN COMPLEX WITH USP8.

Entry informationi

Entry nameiRNF41_HUMAN
AccessioniPrimary (citable) accession number: Q9H4P4
Secondary accession number(s): A6NFW0, B2RBT8, O75598
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: February 21, 2006
Last modified: June 8, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  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.