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Protein

E3 ubiquitin-protein ligase RNF182

Gene

RNF182

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

Functioni

E3 ubiquitin-protein ligase that mediates the ubiquitination of ATP6V0C and targets it to degradation via the ubiquitin-proteasome pathway.1 Publication

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

  • ligase activity Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • protein ubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:28522. RNF182.

Subcellular locationi

Topology

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

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134975171.

Polymorphism and mutation databases

BioMutaiRNF182.
DMDMi74751050.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 247247E3 ubiquitin-protein ligase RNF182PRO_0000261620Add
BLAST

Proteomic databases

PaxDbiQ8N6D2.
PeptideAtlasiQ8N6D2.
PRIDEiQ8N6D2.

PTM databases

iPTMnetiQ8N6D2.

Expressioni

Tissue specificityi

Up-regulated in neuronal cells subjected to cell death-inducing injuries, such as oxygen and glucose deprivation (at protein level). Could be up-regulated in Alzheimer disease brains.1 Publication

Gene expression databases

BgeeiQ8N6D2.
CleanExiHS_RNF182.
ExpressionAtlasiQ8N6D2. baseline and differential.
GenevisibleiQ8N6D2. HS.

Organism-specific databases

HPAiHPA012309.

Interactioni

Subunit structurei

Interacts with ATP6V0C.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
UBE2NP610882EBI-2130099,EBI-1052908

Protein-protein interaction databases

BioGridi128745. 5 interactions.
IntActiQ8N6D2. 3 interactions.
STRINGi9606.ENSP00000420465.

Structurei

3D structure databases

ProteinModelPortaliQ8N6D2.
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.
InParanoidiQ8N6D2.
KOiK11983.
OMAiCAKCLCK.
PhylomeDBiQ8N6D2.
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.

Q8N6D2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASQPPEDTA 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 DCMAPPS
Length:247
Mass (Da):27,402
Last modified:October 1, 2002 - v1
Checksum:i0012F055C7F2A233
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081L → P in BAC03481 (PubMed:14702039).Curated
Sequence conflicti139 – 1391E → K in BAC03481 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431V → A in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035959
Natural varianti58 – 581P → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035960

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK090576 mRNA. Translation: BAC03481.1.
AK315528 mRNA. Translation: BAG37909.1.
AL138718 Genomic DNA. No translation available.
CH471087 Genomic DNA. Translation: EAW55349.1.
BC030666 mRNA. Translation: AAH30666.1.
BC050030 mRNA. Translation: AAH50030.1.
CCDSiCCDS4531.1.
RefSeqiNP_001158504.1. NM_001165032.1.
NP_001158505.1. NM_001165033.1.
NP_001158506.1. NM_001165034.1.
NP_689950.1. NM_152737.3.
UniGeneiHs.111164.

Genome annotation databases

EnsembliENST00000488300; ENSP00000420465; ENSG00000180537.
ENST00000537388; ENSP00000441271; ENSG00000180537.
ENST00000537663; ENSP00000443228; ENSG00000180537.
ENST00000544682; ENSP00000442021; ENSG00000180537.
GeneIDi221687.
KEGGihsa:221687.
UCSCiuc003nbe.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK090576 mRNA. Translation: BAC03481.1.
AK315528 mRNA. Translation: BAG37909.1.
AL138718 Genomic DNA. No translation available.
CH471087 Genomic DNA. Translation: EAW55349.1.
BC030666 mRNA. Translation: AAH30666.1.
BC050030 mRNA. Translation: AAH50030.1.
CCDSiCCDS4531.1.
RefSeqiNP_001158504.1. NM_001165032.1.
NP_001158505.1. NM_001165033.1.
NP_001158506.1. NM_001165034.1.
NP_689950.1. NM_152737.3.
UniGeneiHs.111164.

3D structure databases

ProteinModelPortaliQ8N6D2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128745. 5 interactions.
IntActiQ8N6D2. 3 interactions.
STRINGi9606.ENSP00000420465.

PTM databases

iPTMnetiQ8N6D2.

Polymorphism and mutation databases

BioMutaiRNF182.
DMDMi74751050.

Proteomic databases

PaxDbiQ8N6D2.
PeptideAtlasiQ8N6D2.
PRIDEiQ8N6D2.

Protocols and materials databases

DNASUi221687.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000488300; ENSP00000420465; ENSG00000180537.
ENST00000537388; ENSP00000441271; ENSG00000180537.
ENST00000537663; ENSP00000443228; ENSG00000180537.
ENST00000544682; ENSP00000442021; ENSG00000180537.
GeneIDi221687.
KEGGihsa:221687.
UCSCiuc003nbe.4. human.

Organism-specific databases

CTDi221687.
GeneCardsiRNF182.
HGNCiHGNC:28522. RNF182.
HPAiHPA012309.
neXtProtiNX_Q8N6D2.
PharmGKBiPA134975171.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITF6. Eukaryota.
ENOG410XT90. LUCA.
GeneTreeiENSGT00730000111020.
HOGENOMiHOG000261678.
HOVERGENiHBG060481.
InParanoidiQ8N6D2.
KOiK11983.
OMAiCAKCLCK.
PhylomeDBiQ8N6D2.
TreeFamiTF331690.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GenomeRNAii221687.
PROiQ8N6D2.

Gene expression databases

BgeeiQ8N6D2.
CleanExiHS_RNF182.
ExpressionAtlasiQ8N6D2. baseline and differential.
GenevisibleiQ8N6D2. HS.

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. "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].
    Tissue: Brain.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 Testis.
  5. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-43 AND LEU-58.
  6. "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: FUNCTION, INTERACTION WITH ATP6V0C, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiRN182_HUMAN
AccessioniPrimary (citable) accession number: Q8N6D2
Secondary accession number(s): B2RDG2, Q8NBG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: October 1, 2002
Last modified: July 6, 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
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, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. 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.