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Protein

E3 ubiquitin-protein ligase RNF182

Gene

Rnf182

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

E3 ubiquitin-protein ligase that mediates the ubiquitination of ATP6V0C and targets it to degradation via the ubiquitin-proteasome pathway.By similarity

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 fingeri20 – 6849RING-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 RNF182 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 182
Gene namesi
Name:Rnf182
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:3045355. Rnf182.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei184 – 20421HelicalSequence analysisAdd
BLAST
Transmembranei211 – 23121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 247247E3 ubiquitin-protein ligase RNF182PRO_0000261621Add
BLAST

Proteomic databases

PaxDbiQ8C432.
PRIDEiQ8C432.

Expressioni

Tissue specificityi

Expressed in the cortex, hippocampus, cerebellum and spinal cord, but not in the heart, liver, kidney or skeletal muscle.1 Publication

Gene expression databases

BgeeiQ8C432.
CleanExiMM_RNF182.
ExpressionAtlasiQ8C432. baseline and differential.
GenevisibleiQ8C432. MM.

Interactioni

Subunit structurei

Interacts with ATP6V0C.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000062005.

Structurei

3D structure databases

ProteinModelPortaliQ8C432.
SMRiQ8C432. Positions 5-72.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The RING-type zinc finger domain is required for E3 ligase activity.By similarity

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri20 – 6849RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITF6. Eukaryota.
ENOG410XT90. LUCA.
GeneTreeiENSGT00730000111020.
HOGENOMiHOG000261678.
HOVERGENiHBG060481.
InParanoidiQ8C432.
KOiK11983.
OMAiCAKCLCK.
OrthoDBiEOG7CRTQT.
PhylomeDBiQ8C432.
TreeFamiTF331690.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8C432-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASQPLEEPA ESQASDELEC KICYNRYNLK QRKPKVLECC HRVCAKCLYK
60 70 80 90 100
IIDFGDSPQG VIVCPFCRFE TCLPDDEVSS LPDDNNILVN LTCGGKGKKC
110 120 130 140 150
LPENPTELLL TPKRLASLVS PSHTSSNCLV ITIMEVQRES SPSLSSTPVV
160 170 180 190 200
EFYRPASFDS VTTVSHNWTV WNCTSLLFQT SIRVLVWLLG LLYFSSLPLG
210 220 230 240
IYLLVSKKVT LGVVFVSLVP SSLVILMVYG FCQCVCHEFL DCMALPS
Length:247
Mass (Da):27,444
Last modified:March 1, 2003 - v1
Checksum:iF6CC9BEAFF18781E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK083175 mRNA. Translation: BAC38795.1.
BC089488 mRNA. Translation: AAH89488.1.
CCDSiCCDS26480.1.
RefSeqiNP_899027.1. NM_183204.4.
XP_006516996.1. XM_006516933.2.
UniGeneiMm.40588.

Genome annotation databases

EnsembliENSMUST00000059986; ENSMUSP00000062005; ENSMUSG00000044164.
GeneIDi328234.
KEGGimmu:328234.
UCSCiuc007qgh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK083175 mRNA. Translation: BAC38795.1.
BC089488 mRNA. Translation: AAH89488.1.
CCDSiCCDS26480.1.
RefSeqiNP_899027.1. NM_183204.4.
XP_006516996.1. XM_006516933.2.
UniGeneiMm.40588.

3D structure databases

ProteinModelPortaliQ8C432.
SMRiQ8C432. Positions 5-72.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000062005.

Proteomic databases

PaxDbiQ8C432.
PRIDEiQ8C432.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000059986; ENSMUSP00000062005; ENSMUSG00000044164.
GeneIDi328234.
KEGGimmu:328234.
UCSCiuc007qgh.2. mouse.

Organism-specific databases

CTDi221687.
MGIiMGI:3045355. Rnf182.

Phylogenomic databases

eggNOGiENOG410ITF6. Eukaryota.
ENOG410XT90. LUCA.
GeneTreeiENSGT00730000111020.
HOGENOMiHOG000261678.
HOVERGENiHBG060481.
InParanoidiQ8C432.
KOiK11983.
OMAiCAKCLCK.
OrthoDBiEOG7CRTQT.
PhylomeDBiQ8C432.
TreeFamiTF331690.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ8C432.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C432.
CleanExiMM_RNF182.
ExpressionAtlasiQ8C432. baseline and differential.
GenevisibleiQ8C432. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. 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: Hippocampus.
  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].
    Tissue: Tooth.
  3. "A novel brain-enriched E3 ubiquitin ligase RNF182 is up regulated in the brains of Alzheimer's patients and targets ATP6V0C for degradation."
    Liu Q.Y., Lei J.X., Sikorska M., Liu R.
    Mol. Neurodegener. 3:4-4(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiRN182_MOUSE
AccessioniPrimary (citable) accession number: Q8C432
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 109 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.