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P78317

- RNF4_HUMAN

UniProt

P78317 - RNF4_HUMAN

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Protein
E3 ubiquitin-protein ligase RNF4
Gene
RNF4, SNURF, RES4-26
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation.6 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri132 – 17746RING-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. SUMO polymer binding Source: UniProtKB
  3. androgen receptor binding Source: UniProtKB
  4. ligase activity Source: UniProtKB-KW
  5. nucleosome binding Source: UniProtKB
  6. protein binding Source: UniProtKB
  7. sequence-specific DNA binding transcription factor activity Source: ProtInc
  8. transcription coactivator activity Source: UniProtKB
  9. ubiquitin-protein transferase activity Source: UniProtKB
  10. zinc ion binding Source: ProtInc

GO - Biological processi

  1. androgen receptor signaling pathway Source: UniProtKB
  2. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  3. positive regulation of transcription, DNA-templated Source: UniProtKB
  4. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  5. protein K11-linked ubiquitination Source: UniProtKB
  6. protein K48-linked ubiquitination Source: UniProtKB
  7. protein K6-linked ubiquitination Source: UniProtKB
  8. protein K63-linked ubiquitination Source: UniProtKB
  9. protein autoubiquitination Source: UniProtKB
  10. regulation of kinetochore assembly Source: UniProtKB
  11. regulation of spindle assembly Source: UniProtKB
  12. response to arsenic-containing substance Source: UniProtKB
  13. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Ligase

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF4 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 4
Small nuclear ring finger protein
Short name:
Protein SNURF
Gene namesi
Name:RNF4
Synonyms:SNURF
ORF Names:RES4-26
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:10067. RNF4.

Subcellular locationi

Cytoplasm. Nucleus. NucleusPML body. Nucleusnucleoplasm 3 Publications

GO - Cellular componenti

  1. PML body Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34439.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190E3 ubiquitin-protein ligase RNF4
PRO_0000056043Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941Phosphoserine2 Publications
Modified residuei95 – 951Phosphoserine2 Publications

Post-translational modificationi

Sumoylated; conjugated by one or two SUMO1 moieties By similarity.
Autoubiquitinated By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP78317.
PaxDbiP78317.
PRIDEiP78317.

PTM databases

PhosphoSiteiP78317.

Expressioni

Tissue specificityi

Widely expressed at low levels in many tissues; highly expressed in testis.1 Publication

Gene expression databases

ArrayExpressiP78317.
BgeeiP78317.
CleanExiHS_RNF4.
GenevestigatoriP78317.

Organism-specific databases

HPAiHPA049356.

Interactioni

Subunit structurei

Homodimer (via RING-type zinc finger domain). Interacts with GSC2 By similarity. Interacts with AR/the androgen receptor and TBP By similarity. Interacts with TCF20 By similarity. Interacts with PATZ1. Interacts with TRPS1; negatively regulates TRPS1 transcriptional repressor activity. Interacts with PML; SUMO1-dependent. Interacts with PML; SUMO2-dependent. Interacts with PARP1. Interacts with PML (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6).6 Publications

Protein-protein interaction databases

BioGridi111974. 44 interactions.
IntActiP78317. 19 interactions.
MINTiMINT-271054.
STRINGi9606.ENSP00000315212.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni133 – 1353
Helixi139 – 1446
Beta strandi149 – 1524
Beta strandi153 – 1553
Beta strandi157 – 1593
Helixi160 – 16910
Turni174 – 1763
Turni181 – 1833
Beta strandi185 – 1873

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EA6NMR-A122-183[»]
2XEUX-ray1.50A130-190[»]
4PPEX-ray2.00A/B120-190[»]
ProteinModelPortaliP78317.
SMRiP78317. Positions 124-190.

Miscellaneous databases

EvolutionaryTraceiP78317.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 1616Required for ubiquitination activity By similarity
Add
BLAST
Regioni4 – 6158Mediates interaction with TRPS1 By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi36 – 394SUMO interaction motif 1; mediates the binding to polysumoylated substrates
Motifi46 – 494SUMO interaction motif 2; mediates the binding to polysumoylated substrates
Motifi57 – 593SUMO interaction motif 3; mediates the binding to polysumoylated substrates
Motifi67 – 704SUMO interaction motif 4; mediates the binding to polysumoylated substrates

Domaini

The RING-type zinc finger domain is required for the ubiquitination of polysumoylated substrates By similarity.

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG327779.
HOGENOMiHOG000059548.
HOVERGENiHBG018577.
InParanoidiP78317.
OMAiTHRQYHP.
PhylomeDBiP78317.
TreeFamiTF328387.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P78317-1) [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

MSTRKRRGGA INSRQAQKRT REATSTPEIS LEAEPIELVE TAGDEIVDLT    50
CESLEPVVVD LTHNDSVVIV DERRRPRRNA RRLPQDHADS CVVSSDDEEL 100
SRDRDVYVTT HTPRNARDEG ATGLRPSGTV SCPICMDGYS EIVQNGRLIV 150
STECGHVFCS QCLRDSLKNA NTCPTCRKKI NHKRYHPIYI 190
Length:190
Mass (Da):21,319
Last modified:May 1, 1997 - v1
Checksum:iE5E3AE4A9B28CF9D
GO
Isoform 2 (identifier: P78317-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     72-113: ERRRPRRNAR...RDVYVTTHTP → GPQVLSVVPS...SSVASASVIP
     114-190: Missing.

Note: No experimental confirmation available.

Show »
Length:113
Mass (Da):12,126
Checksum:iC65BF8B284670597
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei72 – 11342ERRRP…TTHTP → GPQVLSVVPSAWTDTQRSCR MDVSSFPQNAAMSSVASASV IP in isoform 2.
VSP_045789Add
BLAST
Alternative sequencei114 – 19077Missing in isoform 2.
VSP_045790Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB000468 mRNA. Translation: BAA19122.1.
U95140 mRNA. Translation: AAC52022.1.
AK128038 mRNA. Translation: BAG54620.1.
AK309509 mRNA. No translation available.
AK312534 mRNA. Translation: BAG35433.1.
AL110117 Genomic DNA. No translation available.
AL645924 Genomic DNA. No translation available.
BX322586 Genomic DNA. No translation available.
CR450722 Genomic DNA. No translation available.
CR545473 Genomic DNA. No translation available.
BC031935 mRNA. Translation: AAH31935.1.
CCDSiCCDS47001.1. [P78317-1]
CCDS54713.1. [P78317-2]
RefSeqiNP_001171938.1. NM_001185009.2. [P78317-1]
NP_001171939.1. NM_001185010.2. [P78317-2]
NP_002929.1. NM_002938.4. [P78317-1]
UniGeneiHs.66394.

Genome annotation databases

EnsembliENST00000314289; ENSP00000315212; ENSG00000063978. [P78317-1]
ENST00000506706; ENSP00000424076; ENSG00000063978. [P78317-1]
ENST00000511600; ENSP00000426503; ENSG00000063978. [P78317-1]
ENST00000511859; ENSP00000426615; ENSG00000063978. [P78317-2]
GeneIDi6047.
KEGGihsa:6047.
UCSCiuc003gfb.3. human. [P78317-1]

Polymorphism databases

DMDMi18202358.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB000468 mRNA. Translation: BAA19122.1 .
U95140 mRNA. Translation: AAC52022.1 .
AK128038 mRNA. Translation: BAG54620.1 .
AK309509 mRNA. No translation available.
AK312534 mRNA. Translation: BAG35433.1 .
AL110117 Genomic DNA. No translation available.
AL645924 Genomic DNA. No translation available.
BX322586 Genomic DNA. No translation available.
CR450722 Genomic DNA. No translation available.
CR545473 Genomic DNA. No translation available.
BC031935 mRNA. Translation: AAH31935.1 .
CCDSi CCDS47001.1. [P78317-1 ]
CCDS54713.1. [P78317-2 ]
RefSeqi NP_001171938.1. NM_001185009.2. [P78317-1 ]
NP_001171939.1. NM_001185010.2. [P78317-2 ]
NP_002929.1. NM_002938.4. [P78317-1 ]
UniGenei Hs.66394.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EA6 NMR - A 122-183 [» ]
2XEU X-ray 1.50 A 130-190 [» ]
4PPE X-ray 2.00 A/B 120-190 [» ]
ProteinModelPortali P78317.
SMRi P78317. Positions 124-190.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111974. 44 interactions.
IntActi P78317. 19 interactions.
MINTi MINT-271054.
STRINGi 9606.ENSP00000315212.

PTM databases

PhosphoSitei P78317.

Polymorphism databases

DMDMi 18202358.

Proteomic databases

MaxQBi P78317.
PaxDbi P78317.
PRIDEi P78317.

Protocols and materials databases

DNASUi 6047.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314289 ; ENSP00000315212 ; ENSG00000063978 . [P78317-1 ]
ENST00000506706 ; ENSP00000424076 ; ENSG00000063978 . [P78317-1 ]
ENST00000511600 ; ENSP00000426503 ; ENSG00000063978 . [P78317-1 ]
ENST00000511859 ; ENSP00000426615 ; ENSG00000063978 . [P78317-2 ]
GeneIDi 6047.
KEGGi hsa:6047.
UCSCi uc003gfb.3. human. [P78317-1 ]

Organism-specific databases

CTDi 6047.
GeneCardsi GC04P002463.
HGNCi HGNC:10067. RNF4.
HPAi HPA049356.
MIMi 602850. gene.
neXtProti NX_P78317.
PharmGKBi PA34439.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG327779.
HOGENOMi HOG000059548.
HOVERGENi HBG018577.
InParanoidi P78317.
OMAi THRQYHP.
PhylomeDBi P78317.
TreeFami TF328387.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSi RNF4. human.
EvolutionaryTracei P78317.
GeneWikii RNF4.
GenomeRNAii 6047.
NextBioi 23561.
PROi P78317.
SOURCEi Search...

Gene expression databases

ArrayExpressi P78317.
Bgeei P78317.
CleanExi HS_RNF4.
Genevestigatori P78317.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF13639. zf-RING_2. 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. "The primary structure and genomic organization of five novel transcripts located close to the Huntington's disease gene on human chromosome 4p16.3."
    Hadano S., Ishida Y., Ikeda J.-E.
    DNA Res. 5:177-186(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Identification and characterization of a novel RING-finger gene (RNF4) mapping at 4p16.3."
    Chiariotti L., Benvenuto G., Fedele M., Santoro M., Simeone A., Fusco A., Bruni C.B.
    Genomics 47:258-265(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Brain.
  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: Hair follicle dermal papilla, Testis and Tongue.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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: Testis.
  6. "A novel member of the BTB/POZ family, PATZ, associates with the RNF4 RING finger protein and acts as a transcriptional repressor."
    Fedele M., Benvenuto G., Pero R., Majello B., Battista S., Lembo F., Vollono E., Day P.M., Santoro M., Lania L., Bruni C.B., Fusco A., Chiatiotti L.
    J. Biol. Chem. 275:7894-7901(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PATZ1.
  7. "The RING finger protein RNF4, a co-regulator of transcription, interacts with the TRPS1 transcription factor."
    Kaiser F.J., Moeroey T., Chang G.T., Horsthemke B., Luedecke H.J.
    J. Biol. Chem. 278:38780-38785(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRPS1, SUBCELLULAR LOCATION.
  8. "SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies."
    Haekli M., Karvonen U., Jaenne O.A., Palvimo J.J.
    Exp. Cell Res. 304:224-233(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PML, SUBCELLULAR LOCATION.
  9. "RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation."
    Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N., Jaffray E.G., Palvimo J.J., Hay R.T.
    Nat. Cell Biol. 10:538-546(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "PARP-1 transcriptional activity is regulated by sumoylation upon heat shock."
    Martin N., Schwamborn K., Schreiber V., Werner A., Guillier C., Zhang X.D., Bischof O., Seeler J.S., Dejean A.
    EMBO J. 28:3534-3548(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARP1.
  12. "Extracellular signal-regulated kinase mitogen-activated protein kinase signaling initiates a dynamic interplay between sumoylation and ubiquitination to regulate the activity of the transcriptional activator PEA3."
    Guo B., Sharrocks A.D.
    Mol. Cell. Biol. 29:3204-3218(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "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 SER-94 AND SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "The SUMO protease SENP6 is essential for inner kinetochore assembly."
    Mukhopadhyay D., Arnaoutov A., Dasso M.
    J. Cell Biol. 188:681-692(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies."
    Geoffroy M.C., Jaffray E.G., Walker K.J., Hay R.T.
    Mol. Biol. Cell 21:4227-4239(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SUMOYLATED PML, SUBCELLULAR LOCATION.
  16. "RNF4 and VHL regulate the proteasomal degradation of SUMO-conjugated Hypoxia-Inducible Factor-2alpha."
    van Hagen M., Overmeer R.M., Abolvardi S.S., Vertegaal A.C.
    Nucleic Acids Res. 38:1922-1931(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Requirement of PML SUMO interacting motif for RNF4- or arsenic trioxide-induced degradation of nuclear PML isoforms."
    Maroui M.A., Kheddache-Atmane S., El Asmi F., Dianoux L., Aubry M., Chelbi-Alix M.K.
    PLoS ONE 7:E44949-E44949(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PML.
  18. "Solution structure of the RING domain of the human RING finger protein 4."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 122-183.

Entry informationi

Entry nameiRNF4_HUMAN
AccessioniPrimary (citable) accession number: P78317
Secondary accession number(s): B2R6D6, D6RF58, Q49AR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 1997
Last modified: September 3, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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

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