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Q9Y3C5 (RNF11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RING finger protein 11
Gene names
Name:RNF11
ORF Names:CGI-123
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15

Subcellular location

Early endosome. Recycling endosome. Cytoplasm. Nucleus. Note: Predominantly cytoplasmic, when unphosphorylated, and nuclear, when phosphorylated by PKB/AKT1 (Ref.7). Ref.7 Ref.8 Ref.9

Tissue specificity

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. Ref.8 Ref.9 Ref.11

Domain

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

Post-translational modification

Ubiquitinated in the presence of ITCH, or SMURF2, and UBE2D1, as well as WWP1. Ref.9 Ref.15

Phosphorylation by PKB/AKT1 may accelerate degradation by the proteasome.

Acylation at both Gly-2 and Cys-4 is required for proper localization to the endosomes (Ref.15).

Sequence similarities

Contains 1 RING-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 154153RING finger protein 11
PRO_0000056050

Regions

Zinc finger99 – 14042RING-type
Motif37 – 404WW-binding

Amino acid modifications

Modified residue1351Phosphothreonine; by PKB/AKT1 Ref.7
Lipidation21N-myristoyl glycine Ref.15 Ref.16
Lipidation41S-palmitoyl cysteine Ref.15

Natural variations

Natural variant111D → E.
Corresponds to variant rs12077069 [ dbSNP | Ensembl ].
VAR_058272

Experimental info

Mutagenesis21G → A: Loss of myristoylation. Change in subcellular location: Becomes diffused throughout the cytosol. Strong reduction of ubiquitination. Reduced efficiency of ITCH-binding. Ref.15
Mutagenesis41C → S: Change in subcellular location: Becomes partially cytosolic and retained in association with the Golgi apparatus. Partial reduction of ubiquitination. Ref.15
Mutagenesis121D → A: Loss of GGA1-binding. Ref.15
Mutagenesis151L → A: Loss of GGA1-binding. Ref.15
Mutagenesis161L → A: Loss of GGA1-binding. Ref.15
Mutagenesis401Y → 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. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13
Mutagenesis991C → 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. Ref.9 Ref.10 Ref.13 Ref.15
Mutagenesis1021C → 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. Ref.9 Ref.10 Ref.15
Mutagenesis1031M → A or G: Loss of UBE2N-binding. No gain of UBE2L3-binding. Ref.14
Mutagenesis1031M → L: No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-127 and L-128. Ref.14
Mutagenesis1031M → V: No effect on UBE2N-binding. Gain of UBE2L3-binding. Ref.14
Mutagenesis1271D → L: No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-128. Ref.14
Mutagenesis1281D → L: No effect on UBE2N-binding. No gain of UBE2L3-binding. Ref.14
Mutagenesis1351T → E: Loss of phosphorylation and of 14-3-3-binding. Ref.7
Sequence conflict1241D → G in BAF85736. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9Y3C5 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: C368E38148FC1D0D

FASTA15417,444
        10         20         30         40         50         60 
MGNCLKSPTS DDISLLHESQ SDRASFGEGT EPDQEPPPPY QEQVPVPVYH PTPSQTRLAT 

        70         80         90        100        110        120 
QLTEEEQIRI AQRIGLIQHL PKGVYDPGRD GSEKKIRECV ICMMDFVYGD PIRFLPCMHI 

       130        140        150 
YHLDCIDDWL MRSFTCPSCM EPVDAALLSS YETN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_055187.1. NM_014372.4.
UniGeneHs.309641.

3D structure databases

ProteinModelPortalQ9Y3C5.
SMRQ9Y3C5. Positions 98-139.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117941. 91 interactions.
IntActQ9Y3C5. 60 interactions.
MINTMINT-1180165.
STRING9606.ENSP00000242719.

PTM databases

PhosphoSiteQ9Y3C5.

Polymorphism databases

DMDM21362884.

Proteomic databases

PaxDbQ9Y3C5.
PRIDEQ9Y3C5.

Protocols and materials databases

DNASU26994.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242719; ENSP00000242719; ENSG00000123091.
GeneID26994.
KEGGhsa:26994.
UCSCuc001csi.4. human.

Organism-specific databases

CTD26994.
GeneCardsGC01P051701.
HGNCHGNC:10056. RNF11.
HPAHPA045781.
HPA050359.
MIM612598. gene.
neXtProtNX_Q9Y3C5.
PharmGKBPA34420.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265447.
HOGENOMHOG000007448.
HOVERGENHBG058444.
InParanoidQ9Y3C5.
KOK11980.
OMADPDQEPP.
OrthoDBEOG7H4DVW.
PhylomeDBQ9Y3C5.
TreeFamTF318022.

Gene expression databases

BgeeQ9Y3C5.
CleanExHS_RNF11.
GenevestigatorQ9Y3C5.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRNF11. human.
GeneWikiRNF11.
GenomeRNAi26994.
NextBio49462.
PROQ9Y3C5.
SOURCESearch...

Entry information

Entry nameRNF11_HUMAN
AccessionPrimary (citable) accession number: Q9Y3C5
Secondary accession number(s): A8KAI2, Q5T7R8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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