Human Gene RNF11 (uc001csi.4)
  Description: Homo sapiens ring finger protein 11 (RNF11), mRNA.
RefSeq Summary (NM_014372): The protein encoded by this gene contains a RING-H2 finger motif, which is known to be important for protein-protein interactions. The expression of this gene has been shown to be induced by mutant RET proteins (MEN2A/MEN2B). The germline mutations in RET gene are known to be responsible for the development of multiple endocrine neoplasia (MEN). [provided by RefSeq, Jul 2008].
Transcript (Including UTRs)
   Position: hg19 chr1:51,701,945-51,739,119 Size: 37,175 Total Exon Count: 3 Strand: +
Coding Region
   Position: hg19 chr1:51,702,429-51,736,994 Size: 34,566 Coding Exon Count: 3 

Page IndexSequence and LinksUniProtKB CommentsCTDGene AllelesRNA-Seq Expression
Microarray ExpressionRNA StructureProtein StructureOther SpeciesGO AnnotationsmRNA Descriptions
Other NamesModel InformationMethods
Data last updated at UCSC: 2013-06-14

-  Sequence and Links to Tools and Databases
Genomic Sequence (chr1:51,701,945-51,739,119)mRNA (may differ from genome)Protein (154 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
AlphaFoldBioGPSCGAPEnsemblEntrez GeneExonPrimer

-  Comments and Description Text from UniProtKB
DESCRIPTION: RecName: Full=RING finger protein 11;
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.
SUBUNIT: 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.
INTERACTION: Q9UJY5:GGA1; NbExp=2; IntAct=EBI-396669, EBI-447141; Q96J02:ITCH; NbExp=2; IntAct=EBI-396669, EBI-1564678; Q9HAU4:SMURF2; NbExp=3; IntAct=EBI-396669, EBI-396727; O95630:STAMBP; NbExp=2; IntAct=EBI-396669, EBI-396676; P0CG47:UBB; NbExp=2; IntAct=EBI-396669, EBI-413034; P51668:UBE2D1; NbExp=4; IntAct=EBI-396669, EBI-743540; P62837:UBE2D2; NbExp=4; IntAct=EBI-396669, EBI-347677; P61077:UBE2D3; NbExp=3; IntAct=EBI-396669, EBI-348268; P51965:UBE2E1; NbExp=2; IntAct=EBI-396669, EBI-348546; P61088:UBE2N; NbExp=3; IntAct=EBI-396669, EBI-1052908;
SUBCELLULAR LOCATION: Early endosome. Recycling endosome. Cytoplasm. Nucleus. Note=Predominantly cytoplasmic, when unphosphorylated, and nuclear, when phosphorylated by PKB/AKT1 (PubMed:16123141).
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.
DOMAIN: The WW-binding motif mediates interaction with NEDD4 (By similarity).
PTM: Ubiquitinated in the presence of ITCH, or SMURF2, and UBE2D1, as well as WWP1.
PTM: Phosphorylation by PKB/AKT1 may accelerate degradation by the proteasome.
PTM: May be acylated at Cys-4, possibly palmitoylated. Acylation at both Gly-2 and Cys-4 is required for proper localization to the endosomes.
SIMILARITY: Contains 1 RING-type zinc finger.

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 101.53 RPKM in Brain - Frontal Cortex (BA9)
Total median expression: 2146.35 RPKM

View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -262.40484-0.542 Picture PostScript Text
3' UTR -517.412125-0.243 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR001841 - Znf_RING

Pfam Domains:
PF00097 - Zinc finger, C3HC4 type (RING finger)
PF13445 - RING-type zinc-finger
PF13639 - Ring finger domain
PF13923 - Zinc finger, C3HC4 type (RING finger)
PF17123 - RING-like zinc finger

SCOP Domains:
57850 - RING/U-box

ModBase Predicted Comparative 3D Structure on Q9Y3C5
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologGenome BrowserGenome BrowserGenome BrowserNo ortholog
Gene Details  Gene DetailsGene Details 
Gene Sorter  Gene SorterGene Sorter 
  Protein SequenceProtein SequenceProtein Sequence 

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0003677 DNA binding
GO:0004842 ubiquitin-protein transferase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
GO:0061630 ubiquitin protein ligase activity

Biological Process:
GO:0006511 ubiquitin-dependent protein catabolic process
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0051865 protein autoubiquitination

Cellular Component:
GO:0000151 ubiquitin ligase complex
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005768 endosome
GO:0005769 early endosome
GO:0055037 recycling endosome
GO:0070062 extracellular exosome

-  Descriptions from all associated GenBank mRNAs
  AK293047 - Homo sapiens cDNA FLJ77817 complete cds, highly similar to Homo sapiens ring finger protein 11 (RNF11), mRNA.
BC036670 - Homo sapiens cDNA clone IMAGE:4794670, containing frame-shift errors.
BC047654 - Homo sapiens ring finger protein 11, mRNA (cDNA clone MGC:51169 IMAGE:5261966), complete cds.
JD407401 - Sequence 388425 from Patent EP1572962.
AK313140 - Homo sapiens cDNA, FLJ93630, Homo sapiens ring finger protein 11 (RNF11), mRNA.
AB024703 - Homo sapiens mRNA for Sid1669p, complete cds.
AF151881 - Homo sapiens CGI-123 protein mRNA, complete cds.
JD095197 - Sequence 76221 from Patent EP1572962.
BC020964 - Homo sapiens ring finger protein 11, mRNA (cDNA clone MGC:8915 IMAGE:3917224), complete cds.
JD382741 - Sequence 363765 from Patent EP1572962.
AB385089 - Synthetic construct DNA, clone: pF1KB5363, Homo sapiens RNF11 gene for RING finger protein 11, complete cds, without stop codon, in Flexi system.
JF432785 - Synthetic construct Homo sapiens clone IMAGE:100074030 ring finger protein 11 (RNF11) gene, encodes complete protein.
KJ893585 - Synthetic construct Homo sapiens clone ccsbBroadEn_02979 RNF11 gene, encodes complete protein.
JD504075 - Sequence 485099 from Patent EP1572962.
AL049294 - Homo sapiens mRNA; cDNA DKFZp564O033 (from clone DKFZp564O033).
JD347945 - Sequence 328969 from Patent EP1572962.
JD304091 - Sequence 285115 from Patent EP1572962.
JD244426 - Sequence 225450 from Patent EP1572962.
JD553537 - Sequence 534561 from Patent EP1572962.
JD298811 - Sequence 279835 from Patent EP1572962.
JD302518 - Sequence 283542 from Patent EP1572962.
JD386446 - Sequence 367470 from Patent EP1572962.
JD309017 - Sequence 290041 from Patent EP1572962.

-  Other Names for This Gene
  Alternate Gene Symbols: A8KAI2, CGI-123, NM_014372, NP_055187, Q5T7R8, Q9Y3C5, RNF11_HUMAN
UCSC ID: uc001csi.4
RefSeq Accession: NM_014372
Protein: Q9Y3C5 (aka RNF11_HUMAN or RN11_HUMAN)

-  Gene Model Information
category: coding nonsense-mediated-decay: no RNA accession: NM_014372.4
exon count: 3CDS single in 3' UTR: no RNA size: 3082
ORF size: 465CDS single in intron: no Alignment % ID: 100.00
txCdsPredict score: 974.00frame shift in genome: no % Coverage: 99.74
has start codon: yes stop codon in genome: no # of Alignments: 1
has end codon: yes retained intron: no # AT/AC introns 0
selenocysteine: no end bleed into intron: 0# strange splices: 0
Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.