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Q8N488 (RYBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RING1 and YY1-binding protein
Alternative name(s):
Apoptin-associating protein 1
Short name=APAP-1
Death effector domain-associated factor
Short name=DED-associated factor
YY1 and E4TF1-associated factor 1
Gene names
Name:RYBP
Synonyms:DEDAF, YEAF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits ubiquitination and subsequent degradation of TP53, and thereby plays a role in regulating transcription of TP53 target genes. May be implicated in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1. May bind to DNA. Promotes apoptosis. Ref.1 Ref.2 Ref.3 Ref.9

Subunit structure

Monomer. Interacts with apoptin, DEDD, FADD, CASP8, CASP10, YY1 and GABPB1. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of BCOR, PCGF1, RING1 and RNF2/RING2. Together with GABPB1 and YY1, it forms a ternary complex, probably being the bridge factor between these two transcription factors. Interacts with CBX2, YAF2, RING1 and RNF2. Interacts with ubiquitin and ubiquitinated proteins. Interacts with ubiquitinated histone H2A By similarity. Interacts with MDM2, and thereby inhibits ubiquitination of TP53. Identified in a ternary complex containing MDM2, TP53 and RYBP. Ref.1 Ref.2 Ref.3 Ref.6 Ref.9 Ref.14

Subcellular location

Nucleus. Cytoplasm. Nucleusnucleoplasm By similarity. Note: Primarily found in the nucleus. Detected in a punctate pattern likely to represent Polycomb group (PcG) bodies By similarity. Ref.1 Ref.2 Ref.3

Tissue specificity

Widely expressed with highest levels in lymphoid tissues and placenta. Ref.1 Ref.2 Ref.3

Domain

Intrinsically unstructured in the absence of binding partners. Folds upon binding to DNA or RNF2 By similarity.

Post-translational modification

Monoubiquitinated By similarity.

Sequence similarities

Contains 1 RanBP2-type zinc finger.

Sequence caution

The sequence AAK63197.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAO73587.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA89486.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 228228RING1 and YY1-binding protein
PRO_0000097550

Regions

Zinc finger21 – 5030RanBP2-type
Region143 – 22684Interaction with E4TF1B
Compositional bias73 – 764Poly-Pro
Compositional bias77 – 11943Lys-rich
Compositional bias179 – 21436Ser-rich

Amino acid modifications

Modified residue991Phosphoserine Ref.11 Ref.13
Modified residue1271Phosphoserine Ref.10
Modified residue1301Phosphoserine Ref.7 Ref.10
Modified residue2271Phosphoserine Ref.13

Experimental info

Sequence conflict201A → T in AAH36459. Ref.5

Secondary structure

..... 228
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8N488 [UniParc].

Last modified May 10, 2005. Version 2.
Checksum: EB9593460A3F0F4C

FASTA22824,822
        10         20         30         40         50         60 
MTMGDKKSPT RPKRQAKPAA DEGFWDCSVC TFRNSAEAFK CSICDVRKGT STRKPRINSQ 

        70         80         90        100        110        120 
LVAQQVAQQY ATPPPPKKEK KEKVEKQDKE KPEKDKEISP SVTKKNTNKK TKPKSDILKD 

       130        140        150        160        170        180 
PPSEANSIQS ANATTKTSET NHTSRPRLKN VDRSTAQQLA VTVGNVTVII TDFKEKTRSS 

       190        200        210        220 
STSSSTVTSS AGSEQQNQSS SGSESTDKGS SRSSTPKGDM SAVNDESF 

« Hide

References

« Hide 'large scale' references
[1]"The death effector domain-associated factor plays distinct regulatory roles in the nucleus and cytoplasm."
Zheng L., Schickling O., Peter M.E., Lenardo M.J.
J. Biol. Chem. 276:31945-31952(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH DEDD; FADD; CASP8 AND CASP10.
[2]"YEAF1/RYBP and YAF-2 are functionally distinct members of a cofactor family for the YY1 and E4TF1/hGABP transcription factors."
Sawa C., Yoshikawa T., Matsuda-Suzuki F., Delehouzee S., Goto M., Watanabe H., Sawada J., Kataoka K., Handa H.
J. Biol. Chem. 277:22484-22490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH YY1 AND GABPB1.
[3]"Human death effector domain-associated factor interacts with the viral apoptosis agonist Apoptin and exerts tumor-preferential cell killing."
Danen-van Oorschot A.A.M.M., Voskamp P., Seelen M.C.M.J., van Miltenburg M.H.A.M., Bolk M.W., Tait S.W., Boesen-de Cock J.G.R., Rohn J.L., Borst J., Noteborn M.H.M.
Cell Death Differ. 11:564-573(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH APOPTIN.
[4]"The chicken anemia virus protein apoptin is associated with a human apoptotic protein, APAP1."
Cheng C.M., Yuo C.Y.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Tissue: Brain and Muscle.
[6]"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 BCOR; PCGF1; RING1 AND RNF2.
[7]"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-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"RYBP stabilizes p53 by modulating MDM2."
Chen D., Zhang J., Li M., Rayburn E.R., Wang H., Zhang R.
EMBO Rep. 10:166-172(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MDM2, IDENTIFICATION IN A COMPLEX WITH MDM2 AND TP53.
[10]"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-127 AND SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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 145-179 IN COMPLEX WITH RNF2/RING1B, INTERACTION WITH RNF2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF179286 mRNA. Translation: AAD51858.1.
AB029551 mRNA. Translation: BAA89486.1. Different initiation.
AY228125 mRNA. Translation: AAO73587.1. Different initiation.
AF227959 mRNA. Translation: AAK63197.1. Different initiation.
BC014959 mRNA. Translation: AAH14959.1.
BC036459 mRNA. Translation: AAH36459.1.
RefSeqNP_036366.3. NM_012234.5.
UniGeneHs.7910.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IXSX-ray1.70B/D/F/H/J/L145-179[»]
DisProtDP00694.
ProteinModelPortalQ8N488.
SMRQ8N488. Positions 21-60, 145-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116997. 42 interactions.
DIPDIP-41435N.
IntActQ8N488. 10 interactions.
MINTMINT-158357.
STRING9606.ENSP00000419494.

PTM databases

PhosphoSiteQ8N488.

Polymorphism databases

DMDM78102506.

Proteomic databases

PaxDbQ8N488.
PRIDEQ8N488.

Protocols and materials databases

DNASU23429.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000477973; ENSP00000419494; ENSG00000163602.
GeneID23429.
KEGGhsa:23429.
UCSCuc003dpe.3. human.

Organism-specific databases

CTD23429.
GeneCardsGC03M072506.
HGNCHGNC:10480. RYBP.
HPAHPA053357.
MIM607535. gene.
neXtProtNX_Q8N488.
PharmGKBPA34893.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG328071.
HOVERGENHBG001768.
InParanoidQ8N488.
KOK11469.
OrthoDBEOG7B8S61.
PhylomeDBQ8N488.
TreeFamTF350501.

Enzyme and pathway databases

SignaLinkQ8N488.

Gene expression databases

BgeeQ8N488.
CleanExHS_RYBP.
GenevestigatorQ8N488.

Family and domain databases

InterProIPR001876. Znf_RanBP2.
[Graphical view]
PfamPF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTSM00547. ZnF_RBZ. 1 hit.
[Graphical view]
PROSITEPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRYBP. human.
EvolutionaryTraceQ8N488.
GeneWikiRYBP.
GenomeRNAi23429.
NextBio45669.
PROQ8N488.
SOURCESearch...

Entry information

Entry nameRYBP_HUMAN
AccessionPrimary (citable) accession number: Q8N488
Secondary accession number(s): Q9P2W5, Q9UMW4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: April 16, 2014
This is version 105 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM