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Q99496 (RING2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. 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:
E3 ubiquitin-protein ligase RING2

EC=6.3.2.-
Alternative name(s):
Huntingtin-interacting protein 2-interacting protein 3
Short name=HIP2-interacting protein 3
Protein DinG
RING finger protein 1B
Short name=RING1b
RING finger protein 2
RING finger protein BAP-1
Gene names
Name:RNF2
Synonyms:BAP1, DING, HIPI3, RING1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes. Ref.7 Ref.11 Ref.13 Ref.19 Ref.21

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with CBX2 and PHC1. Interacts with CHTOP. Interacts with AURKB By similarity. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RNF1/RING1, RNF2/RING2, MBLR, L3MBTL2 and YAF2. Component of a PRC1-like complex. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with RYBP, HIP2 and TFCP2. Association to the chromosomal DNA is cell-cycle dependent. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RING1. Component of chromatin-associated Polycomb (PcG) complexes. Interacts with RYBP, PCGF2, CBX4, CBX6, CBX7 and CBX8. Interacts with RNF1/RING1, BMI1 and PHC2. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.18 Ref.19 Ref.20

Subcellular location

Nucleus. Chromosome By similarity. Note: Enriched on inactive X chromosome (Xi) in female trophoblast stem (TS) cells as well as differentiating embryonic stem (ES) cells. The enrichment on Xi is transient during TS and ES cell differentiation. The association with Xi is mitotically stable in non-differentiated TS cells By similarity. Ref.18

Post-translational modification

Polyubiquitinated in the presence of UBE2D3 (in vitro) By similarity.

Monoubiquitinated, by auto-ubiquitination By similarity.

Miscellaneous

The hPRC-H complex purification reported by Ref.9 probably presents a mixture of different PRC1-like complexes.

Sequence similarities

Contains 1 RING-type zinc finger.

Sequence caution

The sequence CAI17849.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI17850.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentChromosome
Nucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
Repressor
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior/posterior axis specification

Inferred from electronic annotation. Source: Ensembl

gastrulation with mouth forming second

Inferred from electronic annotation. Source: Ensembl

histone H2A monoubiquitination

Inferred from direct assay Ref.14. Source: UniProtKB

histone H2A-K119 monoubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMLL1 complex

Inferred from direct assay Ref.12. Source: UniProtKB

PRC1 complex

Inferred from direct assay Ref.9Ref.16. Source: UniProtKB

PcG protein complex

Inferred from direct assay Ref.14Ref.18. Source: UniProtKB

nuclear body

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.18. Source: UniProtKB

sex chromatin

Inferred from electronic annotation. Source: Ensembl

ubiquitin ligase complex

Inferred from direct assay Ref.19. Source: UniProtKB

   Molecular_functionRING-like zinc finger domain binding

Inferred from physical interaction Ref.19. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

ubiquitin-protein ligase activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from direct assay Ref.19. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 336335E3 ubiquitin-protein ligase RING2
PRO_0000056038

Regions

Zinc finger51 – 9141RING-type
Region2 – 179178Interaction with HIP2

Amino acid modifications

Modified residue21N-acetylserine Ref.15
Cross-link112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Mutagenesis511C → W: Strong decrease in HIP2-binding; when associated with S-54. Ref.7
Mutagenesis541C → S: Strong decrease in HIP2-binding; when associated with W-51. Ref.7
Mutagenesis691H → Y: Loss of HIP2-binding and loss of ubiquitin ligase activity on histone H2A. Ref.7 Ref.11
Mutagenesis701R → C: Loss of ubiquitin ligase activity on histone H2A. Ref.11
Mutagenesis2471Y → A: Reduced interaction with CBX7. Ref.21
Mutagenesis2581H → A: Reduced interaction with CBX7. Ref.21
Mutagenesis2621Y → A: Reduced interaction with CBX7. Ref.20 Ref.21

Secondary structure

............................................. 336
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99496 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 90EA546E1F4DB7EC

FASTA33637,655
        10         20         30         40         50         60 
MSQAVQTNGT QPLSKTWELS LYELQRTPQE AITDGLEIVV SPRSLHSELM CPICLDMLKN 

        70         80         90        100        110        120 
TMTTKECLHR FCADCIITAL RSGNKECPTC RKKLVSKRSL RPDPNFDALI SKIYPSRDEY 

       130        140        150        160        170        180 
EAHQERVLAR INKHNNQQAL SHSIEEGLKI QAMNRLQRGK KQQIENGSGA EDNGDSSHCS 

       190        200        210        220        230        240 
NASTHSNQEA GPSNKRTKTS DDSGLELDNN NAAMAIDPVM DGASEIELVF RPHPTLMEKD 

       250        260        270        280        290        300 
DSAQTRYIKT SGNATVDHLS KYLAVRLALE ELRSKGESNQ MNLDTASEKQ YTIYIATASG 

       310        320        330 
QFTVLNGSFS LELVSEKYWK VNKPMELYYA PTKEHK 

« Hide

References

« Hide 'large scale' references
[1]"Interactions of BCL7A with novel ring finger proteins."
Dyer M.J.S., Abdul-Rauf M., Heward J.M., Cui X., Cleary M.L., Catovsky D.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Identification of Bap-1, a protein that binds to integrin and is involved in integrin-mediated signal transduction."
Li S.-F.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [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 (JUL-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.
[7]"E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme."
Lee S.-J., Choi J.-Y., Sung Y.-M., Park H., Rhim H., Kang S.
FEBS Lett. 503:61-64(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIP2, FUNCTION, MUTAGENESIS OF CYS-51; CYS-54 AND HIS-69.
[8]"Binding of the RING polycomb proteins to specific target genes in complex with the grainyhead-like family of developmental transcription factors."
Tuckfield A., Clouston D.R., Wilanowski T.M., Zhao L.-L., Cunningham J.M., Jane S.M.
Mol. Cell. Biol. 22:1936-1946(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TFCP2.
[9]"The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans."
Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P., Kingston R.E.
Mol. Cell. Biol. 22:6070-6078(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A PRC1-LIKE HPRC-H COMPLEX.
[10]"A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells."
Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.
Science 296:1132-1136(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; BAT8; CBX3; RNF1; MBLR; L3MBTL2 AND YAF2.
[11]"Role of histone H2A ubiquitination in Polycomb silencing."
Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S., Zhang Y.
Nature 431:873-878(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A PRC1-LIKE COMPLEX WITH RING1; PHC2 AND BMI1, FUNCTION, ENZYME ACTIVITY, MUTAGENESIS OF HIS-69 AND ARG-70.
[12]"Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[13]"Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing."
Cao R., Tsukada Y., Zhang Y.
Mol. Cell 20:845-854(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets."
Gearhart M.D., Corcoran C.M., Wamstad J.A., Bardwell V.J.
Mol. Cell. Biol. 26:6880-6889(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RYBP; PCGF1; BCOR AND RING1.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"Several distinct polycomb complexes regulate and co-localize on the INK4a tumor suppressor locus."
Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G.
PLoS ONE 4:E6380-E6380(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH PCGF2.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Interaction proteomics analysis of polycomb proteins defines distinct PRC1 Complexes in mammalian cells."
Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX4; CBX6; CBX7 AND CBX8, SUBCELLULAR LOCATION.
[19]"Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex."
Li Z., Cao R., Wang M., Myers M.P., Zhang Y., Xu R.M.
J. Biol. Chem. 281:20643-20649(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 15-114 IN COMPLEX WITH BMI1 AND ZINC IONS, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
[20]"Ring1B contains a ubiquitin-like docking module for interaction with Cbx proteins."
Bezsonova I., Walker J.R., Bacik J.P., Duan S., Dhe-Paganon S., Arrowsmith C.H.
Biochemistry 48:10542-10548(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 220-330, INTERACTION WITH CBX7, MUTAGENESIS OF TYR-262.
[21]"Polycomb group targeting through different binding partners of RING1B C-terminal domain."
Wang R., Taylor A.B., Leal B.Z., Chadwell L.V., Ilangovan U., Robinson A.K., Schirf V., Hart P.J., Lafer E.M., Demeler B., Hinck A.P., McEwen D.G., Kim C.A.
Structure 18:966-975(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 223-333 IN COMPLEXES WITH CBX7 AND RYBP, FUNCTION, MUTAGENESIS OF TYR-247; HIS-258 AND TYR-262.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y10571 mRNA. Translation: CAA71596.1.
AF141327 mRNA. Translation: AAD29717.1.
AK314793 mRNA. Translation: BAG37324.1.
AL109865 Genomic DNA. Translation: CAC00611.1.
AL109865 Genomic DNA. Translation: CAI17849.1. Sequence problems.
AL109865 Genomic DNA. Translation: CAI17850.1. Sequence problems.
CH471067 Genomic DNA. Translation: EAW91188.1.
BC012583 mRNA. Translation: AAH12583.1.
RefSeqNP_009143.1. NM_007212.3.
UniGeneHs.591490.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H0DX-ray2.50B15-114[»]
3GS2X-ray1.70A/C223-333[»]
3H8HX-ray2.00A220-330[»]
3IXSX-ray1.70A/C/E/G/I/K223-333[»]
3RPGX-ray2.65C1-116[»]
ProteinModelPortalQ99496.
SMRQ99496. Positions 15-114, 223-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111972. 101 interactions.
DIPDIP-40034N.
IntActQ99496. 49 interactions.
MINTMINT-1420125.
STRING9606.ENSP00000356480.

PTM databases

PhosphoSiteQ99496.

Polymorphism databases

DMDM62901044.

Proteomic databases

PaxDbQ99496.
PRIDEQ99496.

Protocols and materials databases

DNASU6045.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367510; ENSP00000356480; ENSG00000121481.
GeneID6045.
KEGGhsa:6045.
UCSCuc001grc.1. human.

Organism-specific databases

CTD6045.
GeneCardsGC01P185014.
HGNCHGNC:10061. RNF2.
HPAHPA026803.
MIM608985. gene.
neXtProtNX_Q99496.
PharmGKBPA34426.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG324386.
HOGENOMHOG000273917.
HOVERGENHBG079942.
InParanoidQ99496.
KOK10695.
OMASDCIITA.
OrthoDBEOG7NGQC3.
PhylomeDBQ99496.
TreeFamTF105501.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ99496.
BgeeQ99496.
CleanExHS_BAP1.
HS_RNF2.
GenevestigatorQ99496.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ99496.
GeneWikiRNF2.
GenomeRNAi6045.
NextBio23553.
PROQ99496.
SOURCESearch...

Entry information

Entry nameRING2_HUMAN
AccessionPrimary (citable) accession number: Q99496
Secondary accession number(s): B2RBS7, Q5TEN1, Q5TEN2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 135 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 1

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