Reviewed, UniProtKB/Swiss-Prot Q8IY57 (YAF2_HUMAN)

Names and origin

Protein names

Recommended name:
    YY1-associated factor 2

Gene names

Name:

YAF2

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

General annotation (Comments)

Function	Binds to MYC and inhibits MYC-mediated transactivation. Also binds to MYCN and enhances MYCN-dependent transcriptional activation. Increases calpain 2-mediated proteolysis of YY1 in vitro. Component of the E2F6.com-1 complex, a repressive complex that methylates 'Lys-9' of histone H3, suggesting that it is involved in chromatin-remodeling. Ref.1 Ref.4 Ref.6
Subunit structure	Interacts with MYC, MYCN, RNF2/RING1B and YY1. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Ref.1 Ref.4 Ref.6
Subcellular location	Nucleus. Ref.4
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.8 Ref.9
Sequence similarities	Contains 1 RanBP2-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	negative regulation of transcription Ref.6 Inferred from direct assay. Source: UniProtKB positive regulation of transcription Ref.4 Inferred from direct assay. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Ref.4 Inferred from direct assay. Source: UniProtKB
Molecular function	transcription coactivator activity Ref.4 Inferred from direct assay. Source: UniProtKB transcription corepressor activity Ref.6 Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: Q8IY57-1)

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.

Note: No experimental confirmation available.

Isoform 1 (identifier: Q8IY57-2)

The sequence of this isoform differs from the canonical sequence as follows:
     51-74: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 180

180

YY1-associated factor 2

PRO_0000066113

Regions

Zinc finger

19 – 48

30

RanBP2-type

Amino acid modifications

Modified residue

6

1

Phosphoserine Ref.7

Modified residue

149

1

Phosphoserine Ref.8

Modified residue

167

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

51 – 74

24

Missing in isoform 1.

VSP_050621

Experimental info

Sequence conflict

13 – 14

2

QP → HA in AAC51116. Ref.1

Secondary structure

1

.

.

.

.

.

180

Helix Strand Turn

Details...

Beta strand

26 – 28

3

Beta strand

40 – 42

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified November 25, 2008. Version 3. Checksum: 199A56EE06BB4FBE	FASTA	180	19,901
	10 20 30 40 50 60 MGDKKSPTRP KRQPKPSSDE GYWDCSVCTF RNSAEAFKCM MCDVRKGTST RKPRPVSQLV 70 80 90 100 110 120 AQQVTQQFVP PTQSKKEKKD KVEKEKSEKE TTSKKNSHKK TRPRLKNVDR SSAQHLEVTV 130 140 150 160 170 180 GDLTVIITDF KEKTKSPPAS SAASADQHSQ SGSSSDNTER GMSRSSSPRG EASSLNGESH
	Isoform 1. Checksum: 3156410B7FD6E616	FASTA	156	17,199
	10 20 30 40 50 60 MGDKKSPTRP KRQPKPSSDE GYWDCSVCTF RNSAEAFKCM MCDVRKGTST KKEKKDKVEK 70 80 90 100 110 120 EKSEKETTSK KNSHKKTRPR LKNVDRSSAQ HLEVTVGDLT VIITDFKEKT KSPPASSAAS 130 140 150 ADQHSQSGSS SDNTERGMSR SSSPRGEASS LNGESH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Yeast two-hybrid cloning of a novel zinc finger protein that interacts with the multifunctional transcription factor YY1." Kalenik J.L., Chen D., Bradley M.E., Chen S.-J., Lee T.-C. Nucleic Acids Res. 25:843-849(1997) [PubMed: 9016636] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH YY1. Tissue: Skeletal muscle.
[2]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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] (ISOFORM 2). Tissue: Brain.
[4]	"Functional interaction of Yaf2 with the central region of MycN." Bannasch D., Maedge B., Schwab M. Oncogene 20:5913-5919(2001) [PubMed: 11593398] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MYCN.
[5]	"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: 12004135] [Abstract] Cited for: IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND BAT8.
[6]	"Yaf2 inhibits Myc biological function." Maedge B., Geisen C., Moeroey T., Schwab M. Cancer Lett. 193:171-176(2003) [PubMed: 12706874] [Abstract] Cited for: FUNCTION, INTERACTION WITH MYC.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, MASS SPECTROMETRY.
[9]	"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-167, MASS SPECTROMETRY.
[10]	"Solution structure of the ZF-RANBP domain of YY1-associated factor 2." RIKEN structural genomics initiative (RSGI) Submitted (JUN-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 17-58.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U72209 mRNA. Translation: AAC51116.1.
AC020629 Genomic DNA. No translation available.
BC037777 mRNA. Translation: AAH37777.1.

IPI

IPI00024740.
IPI00377181.

RefSeq

NP_005739.2.

UniGene

Hs.708084

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D9G	NMR	-	A	19-58	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q8IY57.

Proteomic databases

PRIDE

Q8IY57.

Genome annotation databases

Ensembl

ENSG00000015153. Homo sapiens. [Contig view]

GeneID

10138.

KEGG

hsa:10138.

Organism-specific databases

GeneCards

GC12M040839.

H-InvDB

HIX0026367.

HGNC

HGNC:17363. YAF2.

MIM

607534. gene.

PharmGKB

PA38236.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q8IY57.

HOVERGEN

Q8IY57.

OMA

Q8IY57. DNTERGV.

Gene expression databases

ArrayExpress

Q8IY57.

Bgee

Q8IY57.

CleanEx

HS_YAF2.

GermOnline

ENSG00000015153. 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

38355.

SOURCE

Search...

Entry information

Entry name

YAF2_HUMAN

Accession

Primary (citable) accession number: Q8IY57
Secondary accession number(s): Q99710

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	November 25, 2008
Last modified:	June 16, 2009
This is version 63 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)