Q06587 (RING1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Ligase Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anterior/posterior pattern specification Inferred from electronic annotation. Source: Compara camera-type eye morphogenesis Inferred from electronic annotation. Source: Compara histone H2A monoubiquitination Inferred from direct assay Ref.13. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.6. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PRC1 complex Inferred from direct assay Ref.9Ref.16. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell sex chromatin Inferred from electronic annotation. Source: Compara ubiquitin ligase complex Inferred from electronic annotation. Source: Compara
Molecular_function	chromatin binding Inferred from electronic annotation. Source: Compara ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara zinc ion binding Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BMI1	P35226	9	EBI-752313,EBI-2341576
CBX6	O95503	3	EBI-752313,EBI-3951758
CBX7	O95931	3	EBI-752313,EBI-3923843
CBX8	Q9HC52	3	EBI-752313,EBI-712912
PCGF1	Q9BSM1	5	EBI-752313,EBI-749901
PCGF2	P35227	4	EBI-752313,EBI-2129767
PCGF3	Q3KNV8	2	EBI-752313,EBI-2339807
PCGF5	Q86SE9	2	EBI-752313,EBI-2827999
RNF2	Q99496	4	EBI-752313,EBI-722416
RYBP	Q8N488	2	EBI-752313,EBI-752324

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 406	406	E3 ubiquitin-protein ligase RING1		PRO_0000056384
Regions
	Zinc finger	48 – 88	41	RING-type
	Region	30 – 234	205	Necessary for transcriptional repression By similarity
	Region	230 – 406	177	Necessary for interaction with CBX2 By similarity
	Motif	201 – 204	4	Nuclear localization signal Potential
	Compositional bias	205 – 260	56	Gly-rich
	Compositional bias	314 – 377	64	Gly-rich
Amino acid modifications
	Modified residue	38	1	Phosphoserine Ref.14 Ref.15
	Modified residue	140	1	Phosphoserine Ref.18
	Modified residue	187	1	Phosphoserine Ref.15
	Modified residue	190	1	Phosphoserine Ref.15
	Modified residue	220	1	Phosphothreonine Ref.17
	Modified residue	248	1	Phosphoserine Ref.18
	Modified residue	254	1	Phosphoserine Ref.18
Natural variations
	Alternative sequence	1 – 29	29	Missing in isoform 2.		VSP_017694

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 21, 2006. Version 2. Checksum: 6959787479DE9DAB	FASTA	406	42,429
	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
	Isoform 2 [UniParc]. Checksum: F406E93593E0CF69	FASTA	377	39,146
	10 20 30 40 50 60 MDGTEIAVSP RSLHSELMCP ICLDMLKNTM TTKECLHRFC SDCIVTALRS GNKECPTCRK 70 80 90 100 110 120 KLVSKRSLRP DPNFDALISK IYPSREEYEA HQDRVLIRLS RLHNQQALSS SIEEGLRMQA 130 140 150 160 170 180 MHRAQRVRRP IPGSDQTTTM SGGEGEPGEG EGDGEDVSSD SAPDSAPGPA PKRPRGGGAG 190 200 210 220 230 240 GSSVGTGGGG TGGVGGGAGS EDSGDRGGTL GGGTLGPPSP PGAPSPPEPG GEIELVFRPH 250 260 270 280 290 300 PLLVEKGEYC QTRYVKTTGN ATVDHLSKYL ALRIALERRQ QQEAGEPGGP GGGASDTGGP 310 320 330 340 350 360 DGCGGEGGGA GGGDGPEEPA LPSLEGVSEK QYTIYIAPGG GAFTTLNGSL TLELVNEKFW 370 KVSRPLELCY APTKDPK

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.
IPI	IPI00455876. IPI00641330.
PIR	A47380.
RefSeq	NP_002922.2. NM_002931.3.
UniGene	Hs.631989.
3D structure databases
ProteinModelPortal	Q06587.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-42043N.
IntAct	Q06587. 29 interactions.
MINT	MINT-1327105.
STRING	9606.ENSP00000363787.
PTM databases
PhosphoSite	Q06587.
Polymorphism databases
DMDM	90110053.
Proteomic databases
PaxDb	Q06587.
PeptideAtlas	Q06587.
PRIDE	Q06587.
Protocols and materials databases
DNASU	6015.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374656; ENSP00000363787; ENSG00000204227. ENST00000383212; ENSP00000372699; ENSG00000206287. ENST00000415941; ENSP00000412190; ENSG00000226788. ENST00000427374; ENSP00000400572; ENSG00000231115. ENST00000430233; ENSP00000396271; ENSG00000228520. ENST00000436128; ENSP00000396439; ENSG00000235107.
GeneID	6015.
KEGG	hsa:6015.
UCSC	uc003odk.3. human.
Organism-specific databases
CTD	6015.
GeneCards	GC06P033177.
HGNC	HGNC:10018. RING1.
HPA	HPA008701.
MIM	602045. gene.
neXtProt	NX_Q06587.
PharmGKB	PA34393.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG324386.
HOGENOM	HOG000273917.
HOVERGEN	HBG079942.
InParanoid	Q06587.
KO	K10695.
OMA	QSASKTW.
OrthoDB	EOG4SXND4.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q06587.
Bgee	Q06587.
CleanEx	HS_RING1.
Genevestigator	Q06587.
GermOnline	ENSG00000204227. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00097. zf-C3HC4. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	6015.
NextBio	23467.
SOURCE	Search...

Entry information

Entry name

RING1_HUMAN

Accession

Primary (citable) accession number: Q06587
Secondary accession number(s): A8JZZ0 , Q5JP96, Q5SQW2, Q86V19

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	March 21, 2006
Last modified:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.