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Protein

E3 ubiquitin-protein ligase RNF115

Gene

Rnf115

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

Functioni

E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys-48'- and/or 'Lys-63'-linked polyubiquitination of substrates and may play a role in diverse biological processes. Through their polyubiquitination, may play a role in the endosomal trafficking and degradation of membrane receptors including EGFR, FLT3, MET and CXCR4.1 Publication1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.2 Publications
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 fingeri229 – 27042RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF115Curated (EC:6.3.2.-2 Publications)
Alternative name(s):
RING finger protein 115Imported
Rabring 71 Publication
Zinc finger protein 364By similarity
Gene namesi
Name:Rnf115Imported
Synonyms:Zfp364Imported, Znf364By similarity
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1915095. Rnf115.

Subcellular locationi

  • Cytoplasmcytosol 1 Publication

  • Note: The GTP-bound form of RAB7A recruits RNF115 from the cytosol onto late endosomes/lysosomes.1 Publication

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221C → A: Loss of interaction with EGFR and FLT3. No effect on E3 ubiquitin protein ligase activity; when associated with A-25. 1 Publication
Mutagenesisi25 – 251C → A: Loss of interaction with EGFR and FLT3. No effect on E3 ubiquitin protein ligase activity; when associated with A-22. 1 Publication
Mutagenesisi229 – 2291C → S: Loss of E3 ubiquitin protein ligase activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 305304E3 ubiquitin-protein ligase RNF115PRO_0000056315Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Post-translational modificationi

RING-type zinc finger-dependent and E2-dependent autoubiquitination.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiQ9D0C1.
PaxDbiQ9D0C1.
PRIDEiQ9D0C1.

PTM databases

iPTMnetiQ9D0C1.
PhosphoSiteiQ9D0C1.

Expressioni

Gene expression databases

BgeeiQ9D0C1.
ExpressionAtlasiQ9D0C1. baseline and differential.
GenevisibleiQ9D0C1. MM.

Interactioni

Subunit structurei

Interacts with RAB7A. Interacts with EGFR and FLT3.2 Publications

Protein-protein interaction databases

BioGridi212475. 7 interactions.
IntActiQ9D0C1. 2 interactions.
MINTiMINT-217430.
STRINGi10090.ENSMUSP00000029740.

Structurei

3D structure databases

ProteinModelPortaliQ9D0C1.
SMRiQ9D0C1. Positions 219-278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri229 – 27042RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00530000062967.
HOGENOMiHOG000116417.
HOVERGENiHBG059832.
InParanoidiQ9D0C1.
KOiK11982.
OMAiMFFPDFR.
OrthoDBiEOG7353XB.
PhylomeDBiQ9D0C1.
TreeFamiTF317985.

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.

Q9D0C1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEASAAGAD AGSAVAAHRF FCHFCKGEVN PKLPEYICPR CDSGFIEEVT
60 70 80 90 100
DDSSFLGGGG SRTDNSTATH FAELWDHLDH TMFLQDFRPF LSSNPLDQDN
110 120 130 140 150
RANERGHQTH TDFWGPSRPP RLPMTRRYRS RGSTRPDRSP AIEGIIQQIF
160 170 180 190 200
AGFFANSAIP GSPHPFSWSG MLHSNPGDYA WGQTGLDAIV TQLLGQLENT
210 220 230 240 250
GPPPADKEKI TSLPTVTVTQ EQVNTGLECP VCKEDYTVEE KVRQLPCNHF
260 270 280 290 300
FHSSCIVPWL ELHDTCPVCR KSLNGEDSTR QTQSSEASAS NRFSNDSQLH

DRWTF
Length:305
Mass (Da):33,859
Last modified:June 1, 2001 - v1
Checksum:iDF89F268AFE91625
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401R → G in BAB25607 (PubMed:16141072).Curated
Sequence conflicti240 – 2401E → G in AAH23113 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008329 mRNA. Translation: BAB25607.1.
AK011584 mRNA. Translation: BAB27716.1.
BC023113 mRNA. Translation: AAH23113.1.
CCDSiCCDS17647.1.
RefSeqiNP_080682.3. NM_026406.3.
UniGeneiMm.386792.

Genome annotation databases

EnsembliENSMUST00000029740; ENSMUSP00000029740; ENSMUSG00000028098.
GeneIDi67845.
KEGGimmu:67845.
UCSCiuc008qoe.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008329 mRNA. Translation: BAB25607.1.
AK011584 mRNA. Translation: BAB27716.1.
BC023113 mRNA. Translation: AAH23113.1.
CCDSiCCDS17647.1.
RefSeqiNP_080682.3. NM_026406.3.
UniGeneiMm.386792.

3D structure databases

ProteinModelPortaliQ9D0C1.
SMRiQ9D0C1. Positions 219-278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212475. 7 interactions.
IntActiQ9D0C1. 2 interactions.
MINTiMINT-217430.
STRINGi10090.ENSMUSP00000029740.

PTM databases

iPTMnetiQ9D0C1.
PhosphoSiteiQ9D0C1.

Proteomic databases

MaxQBiQ9D0C1.
PaxDbiQ9D0C1.
PRIDEiQ9D0C1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029740; ENSMUSP00000029740; ENSMUSG00000028098.
GeneIDi67845.
KEGGimmu:67845.
UCSCiuc008qoe.2. mouse.

Organism-specific databases

CTDi27246.
MGIiMGI:1915095. Rnf115.

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00530000062967.
HOGENOMiHOG000116417.
HOVERGENiHBG059832.
InParanoidiQ9D0C1.
KOiK11982.
OMAiMFFPDFR.
OrthoDBiEOG7353XB.
PhylomeDBiQ9D0C1.
TreeFamiTF317985.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

NextBioi325695.
PROiQ9D0C1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0C1.
ExpressionAtlasiQ9D0C1. baseline and differential.
GenevisibleiQ9D0C1. MM.

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. "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].
    Strain: C57BL/6J.
    Tissue: Embryo and Small intestine.
  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].
    Strain: Czech II.
    Tissue: Mammary tumor.
  3. "Rabring7, a novel Rab7 target protein with a RING finger motif."
    Mizuno K., Kitamura A., Sasaki T.
    Mol. Biol. Cell 14:3741-3752(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB7A, SUBCELLULAR LOCATION.
  4. "Involvement of Rabring7 in EGF receptor degradation as an E3 ligase."
    Sakane A., Hatakeyama S., Sasaki T.
    Biochem. Biophys. Res. Commun. 357:1058-1064(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, AUTOUBIQUITINATION, MUTAGENESIS OF CYS-229.
  5. "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor."
    Smith C.J., Berry D.M., McGlade C.J.
    J. Cell Sci. 126:1366-1380(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, INTERACTION WITH EGFR AND FLT3, MUTAGENESIS OF CYS-22; CYS-25 AND CYS-229.

Entry informationi

Entry nameiRN115_MOUSE
AccessioniPrimary (citable) accession number: Q9D0C1
Secondary accession number(s): Q8R5A1, Q9D885
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 106 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

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. 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.