Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q06587 (RING1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase RING1

EC=6.3.2.-
Alternative name(s):
Polycomb complex protein RING1
RING finger protein 1
Really interesting new gene 1 protein
Gene names
Name:RING1
Synonyms:RNF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. 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. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity. Ref.12

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Component of chromatin-associated Polycomb (PcG) complexes. Interacts with BMI1 By similarity. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2/RING2 MBLR, L3MBTL2 and YAF2. Interacts with CBX2 and PCGF6. Component of a PRC1-like complex. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RNF2/RING2. Interacts with PCGF2, RNF2; CBX6, CBX7 and CBX8. Interacts with PHC2 By similarity. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.16 Ref.20

Subcellular location

Nucleus. Nucleus speckle Ref.20.

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.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Ligase
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

histone H2A monoubiquitination

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.6. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPRC1 complex

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

PcG protein complex

Inferred from direct assay Ref.13Ref.20. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.20Ref.6. Source: UniProtKB

sex chromatin

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.13. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q06587-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q06587-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406E3 ubiquitin-protein ligase RING1
PRO_0000056384

Regions

Zinc finger48 – 8841RING-type
Region30 – 234205Necessary for transcriptional repression By similarity
Region230 – 406177Necessary for interaction with CBX2 By similarity
Motif201 – 2044Nuclear localization signal Potential
Compositional bias205 – 26056Gly-rich
Compositional bias314 – 37764Gly-rich

Amino acid modifications

Modified residue381Phosphoserine Ref.14 Ref.15
Modified residue1401Phosphoserine Ref.18
Modified residue1871Phosphoserine Ref.15
Modified residue1901Phosphoserine Ref.15
Modified residue2201Phosphothreonine Ref.17
Modified residue2481Phosphoserine Ref.18
Modified residue2541Phosphoserine Ref.18

Natural variations

Alternative sequence1 – 2929Missing in isoform 2.
VSP_017694

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 21, 2006. Version 2.
Checksum: 6959787479DE9DAB

FASTA40642,429
        10         20         30         40         50         60 
MTTPANAQNA SKTWELSLYE LHRTPQEAIM DGTEIAVSPR SLHSELMCPI CLDMLKNTMT 

        70         80         90        100        110        120 
TKECLHRFCS DCIVTALRSG NKECPTCRKK LVSKRSLRPD PNFDALISKI YPSREEYEAH 

       130        140        150        160        170        180 
QDRVLIRLSR LHNQQALSSS IEEGLRMQAM HRAQRVRRPI PGSDQTTTMS GGEGEPGEGE 

       190        200        210        220        230        240 
GDGEDVSSDS APDSAPGPAP KRPRGGGAGG SSVGTGGGGT GGVGGGAGSE DSGDRGGTLG 

       250        260        270        280        290        300 
GGTLGPPSPP GAPSPPEPGG EIELVFRPHP LLVEKGEYCQ TRYVKTTGNA TVDHLSKYLA 

       310        320        330        340        350        360 
LRIALERRQQ QEAGEPGGPG GGASDTGGPD GCGGEGGGAG GGDGPEEPAL PSLEGVSEKQ 

       370        380        390        400 
YTIYIAPGGG AFTTLNGSLT LELVNEKFWK VSRPLELCYA PTKDPK 

« Hide

Isoform 2 [UniParc].

Checksum: F406E93593E0CF69
Show »

FASTA37739,146

References

« Hide 'large scale' references
[1]"Identification and preliminary characterization of a protein motif related to the zinc finger."
Lovering R., Hanson I.M., Borden K.L.B., Martin S., O'Reilly N.J., Evan G.I., Rahman D., Pappin D.J.C., Trowsdale J., Freemont P.S.
Proc. Natl. Acad. Sci. U.S.A. 90:2112-2116(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[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 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. expand/collapse author list , 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].
[5]"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] (ISOFORM 1).
Tissue: Eye and Skin.
[6]"RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor."
Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W., Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.
Mol. Cell. Biol. 17:4105-4113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, INTERACTION WITH PHC2.
[7]"RING1 interacts with multiple Polycomb-group proteins and displays tumorigenic activity."
Satijn D.P.E., Otte A.P.
Mol. Cell. Biol. 19:57-68(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"MBLR, a new RING finger protein resembling mammalian Polycomb gene products, is regulated by cell cycle-dependent phosphorylation."
Akasaka T., Takahashi N., Suzuki M., Koseki H., Bodmer R., Koga H.
Genes Cells 7:835-850(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PCGF6.
[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; RNF2; 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 IN A PRC1-LIKE COMPLEX WITH RNF2; BMI1 AND PHC2.
[12]"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.
[13]"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 RNF2.
[14]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-187 AND SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-248 AND SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"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 CBX6; CBX7 AND CBX8, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z14000 mRNA. Translation: CAA78389.1.
BT007352 mRNA. Translation: AAP36016.1.
AK289355 mRNA. Translation: BAF82044.1.
AL031228 Genomic DNA. Translation: CAA20235.1.
AL031228 Genomic DNA. Translation: CAI95620.1.
AL713971 Genomic DNA. Translation: CAI17650.1.
AL645940 Genomic DNA. Translation: CAI18069.1.
AL844527 Genomic DNA. Translation: CAI41841.1.
CR759786 Genomic DNA. Translation: CAQ08246.1.
CR759733 Genomic DNA. Translation: CAQ10303.1.
CR847841, CR547129 Genomic DNA. Translation: CAQ10314.1.
CR547129, CR847841 Genomic DNA. Translation: CAQ10355.1.
BC002922 mRNA. Translation: AAH02922.2.
BC051866 mRNA. Translation: AAH51866.1.
CCDSCCDS34424.1. [Q06587-1]
PIRA47380.
RefSeqNP_002922.2. NM_002931.3. [Q06587-1]
UniGeneHs.631989.

3D structure databases

ProteinModelPortalQ06587.
SMRQ06587. Positions 12-111, 261-403.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111947. 57 interactions.
DIPDIP-42043N.
IntActQ06587. 34 interactions.
MINTMINT-1327105.
STRING9606.ENSP00000363787.

PTM databases

PhosphoSiteQ06587.

Polymorphism databases

DMDM90110053.

Proteomic databases

MaxQBQ06587.
PaxDbQ06587.
PeptideAtlasQ06587.
PRIDEQ06587.

Protocols and materials databases

DNASU6015.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374656; ENSP00000363787; ENSG00000204227. [Q06587-1]
ENST00000383212; ENSP00000372699; ENSG00000206287. [Q06587-1]
ENST00000415941; ENSP00000412190; ENSG00000226788. [Q06587-1]
ENST00000427374; ENSP00000400572; ENSG00000231115. [Q06587-1]
ENST00000430233; ENSP00000396271; ENSG00000228520. [Q06587-1]
ENST00000436128; ENSP00000396439; ENSG00000235107. [Q06587-1]
GeneID6015.
KEGGhsa:6015.
UCSCuc003odk.3. human. [Q06587-1]

Organism-specific databases

CTD6015.
GeneCardsGC06P033196.
GC06Pj33097.
GC06Pk33154.
GC06Pl33330.
GC06Pm33346.
GC06Pn33105.
HGNCHGNC:10018. RING1.
HPAHPA008701.
MIM602045. gene.
neXtProtNX_Q06587.
PharmGKBPA34393.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG324386.
HOGENOMHOG000273917.
HOVERGENHBG079942.
InParanoidQ06587.
KOK10695.
OMAQSASKTW.
OrthoDBEOG7NGQC3.
PhylomeDBQ06587.
TreeFamTF105501.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ06587.
BgeeQ06587.
CleanExHS_RING1.
GenevestigatorQ06587.

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

GeneWikiRING1.
GenomeRNAi6015.
NextBio23467.
PROQ06587.
SOURCESearch...

Entry information

Entry nameRING1_HUMAN
AccessionPrimary (citable) accession number: Q06587
Secondary accession number(s): A8JZZ0 expand/collapse secondary AC list , Q5JP96, Q5SQW2, Q86V19
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: March 21, 2006
Last modified: July 9, 2014
This is version 143 of the entry and version 2 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

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 6

Human chromosome 6: entries, gene names and cross-references to MIM