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Protein

RING finger protein 11

Gene

RNF11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri99 – 14042RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. ubiquitin-protein transferase activity Source: FlyBase
  3. zinc ion binding Source: ProtInc

GO - Biological processi

  1. protein autoubiquitination Source: FlyBase
  2. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
RING finger protein 11
Gene namesi
Name:RNF11
ORF Names:CGI-123
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10056. RNF11.

Subcellular locationi

Early endosome. Recycling endosome. Cytoplasm. Nucleus
Note: Predominantly cytoplasmic, when unphosphorylated, and nuclear, when phosphorylated by PKB/AKT1.1 Publication

GO - Cellular componenti

  1. early endosome Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProtKB
  3. nucleus Source: UniProtKB-SubCell
  4. recycling endosome Source: UniProtKB-SubCell
  5. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: Loss of myristoylation. Change in subcellular location: Becomes diffused throughout the cytosol. Strong reduction of ubiquitination. Reduced efficiency of ITCH-binding. 1 Publication
Mutagenesisi4 – 41C → S: Change in subcellular location: Becomes partially cytosolic and retained in association with the Golgi apparatus. Partial reduction of ubiquitination. 1 Publication
Mutagenesisi12 – 121D → A: Loss of GGA1-binding. 1 Publication
Mutagenesisi15 – 151L → A: Loss of GGA1-binding. 1 Publication
Mutagenesisi16 – 161L → A: Loss of GGA1-binding. 1 Publication
Mutagenesisi40 – 401Y → A: Loss of ITCH-, SMURF2- and WWP1-binding. Partial loss of ubiquitination by ITCH. No effect on STAMBP-binding; when associated with S-99 and S-102. Persistent TNF-mediated NFKBIA phosphorylation. Loss of stimulus-dependent complex formation with TAX1BP1, TNFAIP3 and RIPK1. 5 Publications
Mutagenesisi99 – 991C → S: No effect on STAMBP- and SMURF2-binding; when associated with S-102. Persistent TNF-mediated NFKBIA phosphorylation. No effect on STAMBP-binding; when associated with A-40 and S-102. No effect on ubiquitination by ITCH; when associated with S-102. Loss of stimulus-dependent complex formation with TAX1BP1, TNFAIP3 and RIPK1. 4 Publications
Mutagenesisi102 – 1021C → S: No effect on STAMBP- and SMURF2-binding; when associated with S-99. No effect on ubiquitination by ITCH; when associated with S-102. No effect on STAMBP-binding; when associated with A-40 and S-99. 3 Publications
Mutagenesisi103 – 1031M → A or G: Loss of UBE2N-binding. No gain of UBE2L3-binding. 1 Publication
Mutagenesisi103 – 1031M → L: No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-127 and L-128. 1 Publication
Mutagenesisi103 – 1031M → V: No effect on UBE2N-binding. Gain of UBE2L3-binding. 1 Publication
Mutagenesisi127 – 1271D → L: No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-128. 1 Publication
Mutagenesisi128 – 1281D → L: No effect on UBE2N-binding. No gain of UBE2L3-binding. 1 Publication
Mutagenesisi135 – 1351T → E: Loss of phosphorylation and of 14-3-3-binding. 1 Publication

Organism-specific databases

PharmGKBiPA34420.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 154153RING finger protein 11PRO_0000056050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine2 Publications
Lipidationi4 – 41S-palmitoyl cysteine1 Publication
Modified residuei135 – 1351Phosphothreonine; by PKB/AKT11 Publication

Post-translational modificationi

Ubiquitinated in the presence of ITCH, or SMURF2, and UBE2D1, as well as WWP1.2 Publications
Phosphorylation by PKB/AKT1 may accelerate degradation by the proteasome.1 Publication
Acylation at both Gly-2 and Cys-4 is required for proper localization to the endosomes.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y3C5.
PaxDbiQ9Y3C5.
PRIDEiQ9Y3C5.

PTM databases

PhosphoSiteiQ9Y3C5.

Expressioni

Tissue specificityi

Expressed at low levels in the lung, liver, kidney, pancreas, spleen, prostate, thymus, ovary, small intestine, colon, and peripheral blood lymphocytes, and, at intermediate levels, in the testis, heart, brain and placenta. Highest expression in the skeletal muscle. In the brain, expressed at different levels in several regions: high levels in the amygdala, moderate in the hippocampus and thalamus, low in the caudate and extremely low levels in the corpus callosum (at protein level). Restricted to neurons, enriched in somatodendritic compartments and excluded from white matter (at protein level). In substantia nigra, present in cell bodies and processes of dopaminergic and nondopaminergic cells (at protein level). In Parkinson disease, sequestered in Lewy bodies and neurites. Overexpressed in breast cancer cells, but not detected in the surrounding stroma and weakly, if at all, in normal breast epithelial cells (at protein level). Also expressed in several tumor cell lines.3 Publications

Gene expression databases

BgeeiQ9Y3C5.
CleanExiHS_RNF11.
GenevestigatoriQ9Y3C5.

Organism-specific databases

HPAiHPA045781.
HPA050359.

Interactioni

Subunit structurei

Interacts (when phosphorylated) with 14-3-3. Interacts with the E3 ubiquitin-ligases NEDD4, ITCH, SMURF2 and WWP1 (By similarity). Also interacts with the E2 ubiquitin-conjugating enzymes UBE2D1 and UBE2N, but neither with CDC34, nor with UBE2L3. Interacts with ZNF350, EPS15 and STAMBP. After TNF stimulation, interacts with TAX1BP1, TNFAIP3 and RIPK1; these interaction are transient and they are lost after 1 hour of stimulation with TNF (By similarity). Interacts with GGA1.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GGA1Q9UJY53EBI-396669,EBI-447141
ITCHQ96J022EBI-396669,EBI-1564678
NEDD4P469342EBI-396669,EBI-726944
SMURF2Q9HAU45EBI-396669,EBI-396727
STAMBPO956302EBI-396669,EBI-396676
TAX1BP1Q86VP12EBI-396669,EBI-529518
TNFAIP3P215802EBI-396669,EBI-527670
UBBP0CG472EBI-396669,EBI-413034
UBE2D1P516684EBI-396669,EBI-743540
UBE2D2P628375EBI-396669,EBI-347677
UBE2D3P610773EBI-396669,EBI-348268
UBE2D4Q9Y2X84EBI-396669,EBI-745527
UBE2E1P519652EBI-396669,EBI-348546
UBE2NP610884EBI-396669,EBI-1052908

Protein-protein interaction databases

BioGridi117941. 93 interactions.
IntActiQ9Y3C5. 60 interactions.
MINTiMINT-1180165.
STRINGi9606.ENSP00000242719.

Structurei

3D structure databases

ProteinModelPortaliQ9Y3C5.
SMRiQ9Y3C5. Positions 98-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi37 – 404WW-binding

Domaini

The WW-binding motif mediates interaction with NEDD4.By similarity

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri99 – 14042RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG265447.
GeneTreeiENSGT00730000110988.
HOGENOMiHOG000007448.
HOVERGENiHBG058444.
InParanoidiQ9Y3C5.
KOiK11980.
OMAiDPDQEPP.
OrthoDBiEOG7H4DVW.
PhylomeDBiQ9Y3C5.
TreeFamiTF318022.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y3C5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGNCLKSPTS DDISLLHESQ SDRASFGEGT EPDQEPPPPY QEQVPVPVYH
60 70 80 90 100
PTPSQTRLAT QLTEEEQIRI AQRIGLIQHL PKGVYDPGRD GSEKKIRECV
110 120 130 140 150
ICMMDFVYGD PIRFLPCMHI YHLDCIDDWL MRSFTCPSCM EPVDAALLSS

YETN
Length:154
Mass (Da):17,444
Last modified:November 1, 1999 - v1
Checksum:iC368E38148FC1D0D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241D → G in BAF85736. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111D → E.
Corresponds to variant rs12077069 [ dbSNP | Ensembl ].
VAR_058272

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024703 mRNA. Translation: BAA84683.1.
AF151881 mRNA. Translation: AAD34118.1.
AK293047 mRNA. Translation: BAF85736.1.
AK313140 mRNA. Translation: BAG35959.1.
AL162430 Genomic DNA. Translation: CAI13140.1.
CH471059 Genomic DNA. Translation: EAX06831.1.
BC020964 mRNA. Translation: AAH20964.1.
BC047654 mRNA. Translation: AAH47654.1.
CCDSiCCDS556.1.
RefSeqiNP_055187.1. NM_014372.4.
UniGeneiHs.309641.

Genome annotation databases

EnsembliENST00000242719; ENSP00000242719; ENSG00000123091.
GeneIDi26994.
KEGGihsa:26994.
UCSCiuc001csi.4. human.

Polymorphism databases

DMDMi21362884.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024703 mRNA. Translation: BAA84683.1.
AF151881 mRNA. Translation: AAD34118.1.
AK293047 mRNA. Translation: BAF85736.1.
AK313140 mRNA. Translation: BAG35959.1.
AL162430 Genomic DNA. Translation: CAI13140.1.
CH471059 Genomic DNA. Translation: EAX06831.1.
BC020964 mRNA. Translation: AAH20964.1.
BC047654 mRNA. Translation: AAH47654.1.
CCDSiCCDS556.1.
RefSeqiNP_055187.1. NM_014372.4.
UniGeneiHs.309641.

3D structure databases

ProteinModelPortaliQ9Y3C5.
SMRiQ9Y3C5. Positions 98-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117941. 93 interactions.
IntActiQ9Y3C5. 60 interactions.
MINTiMINT-1180165.
STRINGi9606.ENSP00000242719.

PTM databases

PhosphoSiteiQ9Y3C5.

Polymorphism databases

DMDMi21362884.

Proteomic databases

MaxQBiQ9Y3C5.
PaxDbiQ9Y3C5.
PRIDEiQ9Y3C5.

Protocols and materials databases

DNASUi26994.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000242719; ENSP00000242719; ENSG00000123091.
GeneIDi26994.
KEGGihsa:26994.
UCSCiuc001csi.4. human.

Organism-specific databases

CTDi26994.
GeneCardsiGC01P051701.
HGNCiHGNC:10056. RNF11.
HPAiHPA045781.
HPA050359.
MIMi612598. gene.
neXtProtiNX_Q9Y3C5.
PharmGKBiPA34420.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG265447.
GeneTreeiENSGT00730000110988.
HOGENOMiHOG000007448.
HOVERGENiHBG058444.
InParanoidiQ9Y3C5.
KOiK11980.
OMAiDPDQEPP.
OrthoDBiEOG7H4DVW.
PhylomeDBiQ9Y3C5.
TreeFamiTF318022.

Miscellaneous databases

ChiTaRSiRNF11. human.
GeneWikiiRNF11.
GenomeRNAii26994.
NextBioi49462.
PROiQ9Y3C5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y3C5.
CleanExiHS_RNF11.
GenevestigatoriQ9Y3C5.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression profile of mouse and human genes, Rnf11/RNF11, encoding a novel RING-H2 finger protein."
    Seki N., Hattori A., Hayashi A., Kozuma S., Sasaki M., Suzuki Y., Sugano S., Muramatsu M., Saito T.
    Biochim. Biophys. Acta 1489:421-427(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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].
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Brain and Skin.
  7. "Molecular characterization of ring finger protein 11."
    Connor M.K., Azmi P.B., Subramaniam V., Li H., Seth A.K.
    Mol. Cancer Res. 3:453-461(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 70-113 AND 132-154, PHOSPHORYLATION AT THR-135, SUBCELLULAR LOCATION, INTERACTION WITH 14-3-3, MUTAGENESIS OF THR-135.
  8. "The RING-H2 protein RNF11 is differentially expressed in breast tumours and interacts with HECT-type E3 ligases."
    Kitching R., Wong M.J., Koehler D., Burger A.M., Landberg G., Gish G., Seth A.K.
    Biochim. Biophys. Acta 1639:104-112(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ITCH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF TYR-40.
  9. "The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase."
    Subramaniam V., Li H., Wong M.J., Kitching R., Attisano L., Wrana J., Zubovits J., Burger A.M., Seth A.K.
    Br. J. Cancer 89:1538-1544(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH SMURF2 AND UBE2D1, UBIQUITINATION, MUTAGENESIS OF TYR-40; CYS-99 AND CYS-102.
  10. "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein."
    Li H., Seth A.K.
    Oncogene 23:1801-1808(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ZNF350; EPS15 AND STAMBP, MUTAGENESIS OF TYR-40; CYS-99 AND CYS-102.
  11. "PARK10 candidate RNF11 is expressed by vulnerable neurons and localizes to Lewy bodies in Parkinson disease brain."
    Anderson L.R., Betarbet R., Gearing M., Gulcher J., Hicks A.A., Stefansson K., Lah J.J., Levey A.I.
    J. Neuropathol. Exp. Neurol. 66:955-964(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  12. "The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11."
    Chen C., Zhou Z., Liu R., Li Y., Azmi P.B., Seth A.K.
    Oncogene 27:6845-6855(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WWP1, MUTAGENESIS OF TYR-40.
  13. "The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB signalling."
    Shembade N., Parvatiyar K., Harhaj N.S., Harhaj E.W.
    EMBO J. 28:513-522(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAX1BP1; TNFAIP3 AND RIPK1, MUTAGENESIS OF TYR-40 AND CYS-99.
  14. "Analysis of electrostatic contributions to the selectivity of interactions between RING-finger domains and ubiquitin-conjugating enzymes."
    Scheper J., Oliva B., Villa-Freixa J., Thomson T.M.
    Proteins 74:92-103(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBE2N, MUTAGENESIS OF MET-103; ASP-127 AND ASP-128.
  15. "Multiple modification and protein interaction signals drive the Ring finger protein 11 (RNF11) E3 ligase to the endosomal compartment."
    Santonico E., Belleudi F., Panni S., Torrisi M.R., Cesareni G., Castagnoli L.
    Oncogene 29:5604-5618(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GGA1, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-4, UBIQUITINATION BY ITCH, MUTAGENESIS OF GLY-2; CYS-4; ASP-12; LEU-15; LEU-16; CYS-99 AND CYS-102.
  16. "Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
    Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
    Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.

Entry informationi

Entry nameiRNF11_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3C5
Secondary accession number(s): A8KAI2, Q5T7R8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 1, 1999
Last modified: February 4, 2015
This is version 122 of the entry and version 1 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.