Q8IY57 (YAF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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.
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.6 Ref.8
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.6 Ref.8
Subcellular location	Nucleus Ref.6.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9 Ref.10 Ref.11 Ref.12
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 Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.8. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.6. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay Ref.6. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction Ref.6Ref.8Ref.1. Source: UniProtKB transcription coactivator activity Inferred from direct assay Ref.6. Source: UniProtKB transcription corepressor activity Inferred from direct assay Ref.8. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
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.

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.9

Modified residue

149

1

Phosphoserine Ref.10

Modified residue

167

1

Phosphoserine Ref.11 Ref.12

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 [UniParc]. 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]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"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].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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: Cervix carcinoma.
[10]	"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. Tissue: Embryonic kidney.
[11]	"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. Tissue: Cervix carcinoma.
[12]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U72209 mRNA. Translation: AAC51116.1.
AK291355 mRNA. Translation: BAF84044.1.
AC020629 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW57839.1.
BC037777 mRNA. Translation: AAH37777.1.

IPI

IPI00024740.
IPI00377181.

RefSeq

NP_001177906.1. NM_001190977.1.
NP_001177908.1. NM_001190979.1.
NP_005739.2. NM_005748.4.

UniGene

Hs.649195.
Hs.708084.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q8IY57.

SMR

Q8IY57. Positions 19-58, 101-133.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-44919N.

IntAct

Q8IY57. 5 interactions.

STRING

Q8IY57.

PTM databases

PhosphoSite

Q8IY57.

Polymorphism databases

DMDM

215274199.

Proteomic databases

PRIDE

Q8IY57.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000327791; ENSP00000328004; ENSG00000015153.

GeneID

10138.

KEGG

hsa:10138.

Organism-specific databases

CTD

10138.

GeneCards

GC12M042550.

H-InvDB

HIX0026367.

HGNC

HGNC:17363. YAF2.

HPA

HPA026867.

MIM

607534. gene.

neXtProt

NX_Q8IY57.

PharmGKB

PA38236.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20472.

GeneTree

ENSGT00390000013995.

HOGENOM

HBG713531.

HOVERGEN

HBG001768.

InParanoid

Q8IY57.

OMA

DQHSQSS.

OrthoDB

EOG45QHFK.

PhylomeDB

Q8IY57.

Gene expression databases

ArrayExpress

Q8IY57.

Bgee

Q8IY57.

CleanEx

HS_YAF2.

Genevestigator

Q8IY57.

GermOnline

ENSG00000015153. Homo sapiens.

Family and domain databases

InterPro

IPR001876. Znf_RanBP2.
[Graphical view]

KO

K11468.

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

NextBio

38355.

SOURCE

Search...

Entry information

Entry name

YAF2_HUMAN

Accession

Primary (citable) accession number: Q8IY57
Secondary accession number(s): A8K5P0, Q99710

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	November 25, 2008
Last modified:	January 25, 2012
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.