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Q99496

- RING2_HUMAN

UniProt

Q99496 - RING2_HUMAN

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Protein

E3 ubiquitin-protein ligase RING2

Gene

RNF2

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

Functioni

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.5 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri51 – 9141RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. ligase activity Source: UniProtKB-KW
  3. RING-like zinc finger domain binding Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: Ensembl
  5. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. anterior/posterior axis specification Source: Ensembl
  2. gastrulation with mouth forming second Source: Ensembl
  3. histone H2A-K119 monoubiquitination Source: UniProtKB
  4. histone H2A monoubiquitination Source: UniProtKB
  5. mitotic cell cycle Source: Ensembl
  6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RNF2
Synonyms:BAP1, DING, HIPI3, RING1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10061. RNF2.

Subcellular locationi

Nucleus 1 Publication. 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).By similarity

GO - Cellular componenti

  1. euchromatin Source: Ensembl
  2. MLL1 complex Source: UniProtKB
  3. nuclear body Source: Ensembl
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. PcG protein complex Source: UniProtKB
  7. PRC1 complex Source: UniProtKB
  8. sex chromatin Source: Ensembl
  9. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi51 – 511C → W: Strong decrease in HIP2-binding; when associated with S-54. 1 Publication
Mutagenesisi54 – 541C → S: Strong decrease in HIP2-binding; when associated with W-51. 1 Publication
Mutagenesisi69 – 691H → Y: Loss of HIP2-binding and loss of ubiquitin ligase activity on histone H2A. 2 Publications
Mutagenesisi70 – 701R → C: Loss of ubiquitin ligase activity on histone H2A. 1 Publication
Mutagenesisi247 – 2471Y → A: Reduced interaction with CBX7. 1 Publication
Mutagenesisi258 – 2581H → A: Reduced interaction with CBX7. 1 Publication
Mutagenesisi262 – 2621Y → A: Reduced interaction with CBX7. 2 Publications

Organism-specific databases

PharmGKBiPA34426.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 336335E3 ubiquitin-protein ligase RING2PRO_0000056038Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Cross-linki112 – 112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Polyubiquitinated in the presence of UBE2D3 (in vitro).By similarity
Monoubiquitinated, by auto-ubiquitination.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ99496.
PaxDbiQ99496.
PRIDEiQ99496.

PTM databases

PhosphoSiteiQ99496.

Expressioni

Gene expression databases

BgeeiQ99496.
CleanExiHS_BAP1.
HS_RNF2.
ExpressionAtlasiQ99496. baseline.
GenevestigatoriQ99496.

Organism-specific databases

HPAiHPA026803.

Interactioni

Subunit structurei

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.By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABCB1P081832EBI-722416,EBI-1057359
BMI1P352269EBI-722416,EBI-2341576
CBX4O00257-32EBI-722416,EBI-4392727
CBX6O955033EBI-722416,EBI-3951758
CBX7O959313EBI-722416,EBI-3923843
CBX8Q9HC525EBI-722416,EBI-712912
KAT8Q9H7Z62EBI-722416,EBI-896414
PCGF1Q9BSM14EBI-722416,EBI-749901
PCGF2P352277EBI-722416,EBI-2129767
PCGF3Q3KNV82EBI-722416,EBI-2339807
PCGF5Q86SE92EBI-722416,EBI-2827999
RING1Q065874EBI-722416,EBI-752313
USP11P517844EBI-722416,EBI-306876
USP7Q930094EBI-722416,EBI-302474

Protein-protein interaction databases

BioGridi111972. 703 interactions.
DIPiDIP-40034N.
IntActiQ99496. 49 interactions.
MINTiMINT-1420125.
STRINGi9606.ENSP00000356480.

Structurei

Secondary structure

1
336
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 255
Beta strandi37 – 393
Beta strandi43 – 453
Helixi47 – 493
Turni52 – 543
Beta strandi60 – 645
Turni65 – 673
Beta strandi70 – 723
Helixi73 – 819
Turni88 – 903
Helixi97 – 993
Beta strandi100 – 1023
Helixi104 – 11310
Beta strandi225 – 2328
Turni234 – 2363
Beta strandi246 – 2516
Helixi256 – 27722
Helixi283 – 2853
Helixi288 – 2903
Beta strandi291 – 2966
Beta strandi302 – 3043
Helixi311 – 3188
Beta strandi321 – 3233
Beta strandi325 – 3317

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ99496.
SMRiQ99496. Positions 15-114, 223-333.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99496.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 179178Interaction with HIP2Add
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri51 – 9141RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG324386.
GeneTreeiENSGT00390000016977.
HOGENOMiHOG000273917.
HOVERGENiHBG079942.
InParanoidiQ99496.
KOiK10695.
OMAiSDCIITA.
OrthoDBiEOG7NGQC3.
PhylomeDBiQ99496.
TreeFamiTF105501.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99496-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSQAVQTNGT QPLSKTWELS LYELQRTPQE AITDGLEIVV SPRSLHSELM
60 70 80 90 100
CPICLDMLKN TMTTKECLHR FCADCIITAL RSGNKECPTC RKKLVSKRSL
110 120 130 140 150
RPDPNFDALI SKIYPSRDEY EAHQERVLAR INKHNNQQAL SHSIEEGLKI
160 170 180 190 200
QAMNRLQRGK KQQIENGSGA EDNGDSSHCS NASTHSNQEA GPSNKRTKTS
210 220 230 240 250
DDSGLELDNN NAAMAIDPVM DGASEIELVF RPHPTLMEKD DSAQTRYIKT
260 270 280 290 300
SGNATVDHLS KYLAVRLALE ELRSKGESNQ MNLDTASEKQ YTIYIATASG
310 320 330
QFTVLNGSFS LELVSEKYWK VNKPMELYYA PTKEHK
Length:336
Mass (Da):37,655
Last modified:May 1, 1997 - v1
Checksum:i90EA546E1F4DB7EC
GO
Isoform 2 (identifier: Q99496-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     84-155: Missing.

Note: No experimental confirmation available.

Show »
Length:264
Mass (Da):29,258
Checksum:i332219DF283B16C8
GO

Sequence cautioni

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei84 – 15572Missing in isoform 2. 1 PublicationVSP_055439Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10571 mRNA. Translation: CAA71596.1.
AF141327 mRNA. Translation: AAD29717.1.
AK091574 mRNA. Translation: BAG52383.1.
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: EAW91187.1.
CH471067 Genomic DNA. Translation: EAW91188.1.
BC012583 mRNA. Translation: AAH12583.1.
CCDSiCCDS1365.1. [Q99496-1]
RefSeqiNP_009143.1. NM_007212.3. [Q99496-1]
UniGeneiHs.591490.

Genome annotation databases

EnsembliENST00000367509; ENSP00000356479; ENSG00000121481. [Q99496-2]
ENST00000367510; ENSP00000356480; ENSG00000121481. [Q99496-1]
GeneIDi6045.
KEGGihsa:6045.
UCSCiuc001grc.1. human. [Q99496-1]

Polymorphism databases

DMDMi62901044.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10571 mRNA. Translation: CAA71596.1 .
AF141327 mRNA. Translation: AAD29717.1 .
AK091574 mRNA. Translation: BAG52383.1 .
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: EAW91187.1 .
CH471067 Genomic DNA. Translation: EAW91188.1 .
BC012583 mRNA. Translation: AAH12583.1 .
CCDSi CCDS1365.1. [Q99496-1 ]
RefSeqi NP_009143.1. NM_007212.3. [Q99496-1 ]
UniGenei Hs.591490.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2H0D X-ray 2.50 B 15-114 [» ]
3GS2 X-ray 1.70 A/C 223-333 [» ]
3H8H X-ray 2.00 A 220-330 [» ]
3IXS X-ray 1.70 A/C/E/G/I/K 223-333 [» ]
3RPG X-ray 2.65 C 1-116 [» ]
ProteinModelPortali Q99496.
SMRi Q99496. Positions 15-114, 223-333.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111972. 703 interactions.
DIPi DIP-40034N.
IntActi Q99496. 49 interactions.
MINTi MINT-1420125.
STRINGi 9606.ENSP00000356480.

PTM databases

PhosphoSitei Q99496.

Polymorphism databases

DMDMi 62901044.

Proteomic databases

MaxQBi Q99496.
PaxDbi Q99496.
PRIDEi Q99496.

Protocols and materials databases

DNASUi 6045.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367509 ; ENSP00000356479 ; ENSG00000121481 . [Q99496-2 ]
ENST00000367510 ; ENSP00000356480 ; ENSG00000121481 . [Q99496-1 ]
GeneIDi 6045.
KEGGi hsa:6045.
UCSCi uc001grc.1. human. [Q99496-1 ]

Organism-specific databases

CTDi 6045.
GeneCardsi GC01P185014.
HGNCi HGNC:10061. RNF2.
HPAi HPA026803.
MIMi 608985. gene.
neXtProti NX_Q99496.
PharmGKBi PA34426.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG324386.
GeneTreei ENSGT00390000016977.
HOGENOMi HOG000273917.
HOVERGENi HBG079942.
InParanoidi Q99496.
KOi K10695.
OMAi SDCIITA.
OrthoDBi EOG7NGQC3.
PhylomeDBi Q99496.
TreeFami TF105501.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_169436. Oxidative Stress Induced Senescence.

Miscellaneous databases

EvolutionaryTracei Q99496.
GeneWikii RNF2.
GenomeRNAii 6045.
NextBioi 23553.
PROi Q99496.
SOURCEi Search...

Gene expression databases

Bgeei Q99496.
CleanExi HS_BAP1.
HS_RNF2.
ExpressionAtlasi Q99496. baseline.
Genevestigatori Q99496.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF00097. zf-C3HC4. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
    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] (ISOFORM 1).
  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] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  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.
    , 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. 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] (ISOFORM 1).
    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. 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.

Entry informationi

Entry nameiRING2_HUMAN
AccessioniPrimary (citable) accession number: Q99496
Secondary accession number(s): B2RBS7
, B3KRH1, Q5TEN1, Q5TEN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: May 1, 1997
Last modified: October 29, 2014
This is version 141 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

Miscellaneous

The hPRC-H complex purification reported by PubMed:12167701 probably presents a mixture of different PRC1-like complexes.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3