Reviewed, UniProtKB/Swiss-Prot Q8N488 (RYBP_HUMAN)

Names and origin

Protein names

Recommended name:
    RING1 and YY1-binding protein
Alternative name(s):
    Death effector domain-associated factor
      Short name=DED-associated factor
    YY1 and E4TF1-associated factor 1
    Apoptin-associating protein 1
      Short name=APAP-1

Gene names

Name:	RYBP
Synonyms:	DEDAF, YEAF1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	228 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May be implicated in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1. In tumor cell lines, may induce apoptosis. Ref.1 Ref.2 Ref.3
Subunit structure	Interacts with CBX2, YAF2, IFT57, RING1 and RNF2 By similarity. Interacts with apoptin, DEDD, FADD, CASP8, CASP10, YY1 and E4TF1B. Together with E4TF1B and YY1, it forms a ternary complex, probably being the bridge factor between these two transcription factors. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of BCOR, PCGF1, RING1 and RNF2/RING2.
Subcellular location	Nucleus. Cytoplasm. Note: Primarily found in the nucleus. Ref.1 Ref.2 Ref.3
Tissue specificity	Widely expressed with highest levels in lymphoid tissues and placenta. Ref.1 Ref.2 Ref.3
Sequence similarities	Contains 1 RanBP2-type zinc finger.

Ontologies

Keywords
Biological process	Apoptosis Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Repressor
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Traceable author statement. Source: ProtInc negative regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW transcription corepressor activity Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 228	228	RING1 and YY1-binding protein		PRO_0000097550
Regions
	Zinc finger	21 – 50	30	RanBP2-type
	Region	143 – 226	84	Interaction with E4TF1B
	Compositional bias	73 – 76	4	Poly-Pro
	Compositional bias	77 – 119	43	Lys-rich
	Compositional bias	179 – 214	36	Ser-rich
Amino acid modifications
	Modified residue	127	1	Phosphoserine Ref.7
	Modified residue	130	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	20	1	A → T in AAH36459. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q8N488-1 [UniParc]. Last modified May 10, 2005. Version 2. Checksum: EB9593460A3F0F4C	FASTA	228	24,822
	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

References

	« Hide 'large scale' referencesShow '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: 11395500] [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: 11953439] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH YY1 AND E4TF1B.
[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: 14765135] [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: 15489334] [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: 16943429] [Abstract] Cited for: INTERACTION WITH BCOR, PCGF1, RING1, 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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-130, MASS SPECTROMETRY.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00296594.
RefSeq	NP_036366.3.
UniGene	Hs.712596
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8N488. 1 interaction.
PTM databases
PhosphoSite	Q8N488.
Proteomic databases
PRIDE	Q8N488.
Genome annotation databases
Ensembl	ENSG00000163602. Homo sapiens. [Contig view]
GeneID	23429.
KEGG	hsa:23429.
Organism-specific databases
GeneCards	GC03M072506.
H-InvDB	HIX0003460.
HGNC	HGNC:10480. RYBP.
MIM	607535. gene.
PharmGKB	PA34893.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q8N488.
HOVERGEN	Q8N488.
Gene expression databases
ArrayExpress	Q8N488.
Bgee	Q8N488.
CleanEx	HS_RYBP.
GermOnline	ENSG00000163602. Homo sapiens.
Family and domain databases
InterPro	IPR001876. Znf_RanBP2. [Graphical view]
Pfam	PF00641. zf-RanBP. 1 hit. [Graphical view]
SMART	SM00547. ZnF_RBZ. 1 hit. [Graphical view]
PROSITE	PS01358. ZF_RANBP2_1. 1 hit. PS50199. ZF_RANBP2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	45669.
SOURCE	Search...

Entry information

Entry name

RYBP_HUMAN

Accession

Primary (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:	June 16, 2009
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)