UniProt Accession

 RYBP_HUMAN; Q8N488; Q9P2W5; Q9UMW4 

Genbank Protein ID

 AF179286; AB029551; AY228125; AF227959; BC014959; BC036459 

Genbank Nucleotide ID

 AAD51858.1; BAA89486.1; AAO73587.1; AAK63197.1; AAH14959.1; AAH36459.1 

Protein Name

 RING1 and YY1-binding protein 

Protein Synonyms/Alias

 Apoptin-associating protein 1; APAP-1; Death effector domain-associated factor; DED-associated factor; YY1 and E4TF1-associated factor 1 

Gene Name

 RYBP 

Gene Synonyms/Alias

 DEDAF; YEAF1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
119	KPKSDILKDPPSEAN	ubiquitination	[1, 2, 3, 4, 5]
136	QSANATTKTSETNHT	ubiquitination	[2, 6]
208	SGSESTDKGSSRSST	ubiquitination	[1]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 

Functional Description

 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. 

Sequence Annotation

 ZN_FING 21 50 RanBP2-type.
 REGION 143 226 Interaction with E4TF1B.
 MOD_RES 99 99 Phosphoserine.
 MOD_RES 127 127 Phosphoserine.
 MOD_RES 130 130 Phosphoserine.
 MOD_RES 227 227 Phosphoserine.  

Keyword

 3D-structure; Apoptosis; Complete proteome; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 228 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
 GO:0007275; P:multicellular organismal development; TAS:ProtInc.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR001876; Znf_RanBP2. 

Pfam

 PF00641; zf-RanBP 

SMART

 SM00547; ZnF_RBZ 

PROSITE

 PS01358; ZF_RANBP2_1
 PS50199; ZF_RANBP2_2 

PRINTS