Q6ZN18 (AEBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc finger protein AEBP2

Alternative name(s):
Adipocyte enhancer-binding protein 2
Short name=AE-binding protein 2

Gene names

Name:

AEBP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	517 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA-binding transcriptional repressor. May interact with and stimulate the activity of the PRC2 complex, which methylates 'Lys-9' and 'Lys-27' residues of histone H3. Ref.6
Subunit structure	Self-associates. Interacts with EED, EZH2, RBBP4 and SUZ12. Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2 By similarity. May also interact with RBBP7. Ref.5 Ref.6
Subcellular location	Nucleus Probable.
Sequence similarities	Belongs to the AEBP2/jing C2H2-type zinc-finger family. Contains 3 C2H2-type zinc fingers.
Sequence caution	The sequence AAH15624.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH22220.1 differs from that shown. Reason: Erroneous initiation. The sequence BAD18513.1 differs from that shown. Reason: Erroneous termination at position 269. Translated as Gln. The sequence EAW96400.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Chromatin regulator Repressor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	ESC/E(Z) complex Inferred from direct assay PubMed 20075857. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW transcription corepressor activity Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6ZN18-1)

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 2 (identifier: Q6ZN18-2)

The sequence of this isoform differs from the canonical sequence as follows:
     504-517: Missing.

Isoform 3 (identifier: Q6ZN18-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-216: Missing.
     217-223: SRMDSED → MYTRRYS

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.11
	Chain	2 – 517	516	Zinc finger protein AEBP2		PRO_0000341590
Regions
	Zinc finger	261 – 286	26	C2H2-type 1
	Zinc finger	300 – 322	23	C2H2-type 2; degenerate
	Zinc finger	328 – 352	25	C2H2-type 3
	Region	209 – 294	86	Interaction with RBBP4
	Region	353 – 517	165	Interaction with SUZ12
	Compositional bias	34 – 123	90	Glu-rich
	Compositional bias	61 – 205	145	Gly-rich
	Compositional bias	110 – 256	147	Ser-rich
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.11
	Modified residue	18	1	Phosphoserine Ref.7 Ref.11
	Modified residue	24	1	Phosphoserine Ref.7 Ref.11
	Modified residue	206	1	Phosphoserine Ref.9 Ref.10 Ref.12
	Modified residue	210	1	Phosphoserine Ref.9
	Modified residue	211	1	Phosphoserine Ref.9
	Modified residue	390	1	Phosphoserine Ref.11 Ref.12
Natural variations
	Alternative sequence	1 – 216	216	Missing in isoform 3.		VSP_034357
	Alternative sequence	217 – 223	7	SRMDSED → MYTRRYS in isoform 3.		VSP_034358
	Alternative sequence	504 – 517	14	Missing in isoform 2.		VSP_034359

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 10, 2008. Version 2. Checksum: 6C59888ACEE4F9AF	FASTA	517	54,467
	10 20 30 40 50 60 MAAAITDMAD LEELSRLSPL PPGSPGSAAR GRAEPPEEEE EEEEEEEEAE AEAVAALLLN 70 80 90 100 110 120 GGSGGGGGGG GGGVGGGEAE TMSEPSPESA SQAGEDEDEE EDDEEEEDES SSSGGGEEES 130 140 150 160 170 180 SAESLVGSSG GSSSDETRSL SPGAASSSSG DGDGKEGLEE PKGPRGSQGG GGGGSSSSSV 190 200 210 220 230 240 VSSGGDEGYG TGGGGSSATS GGRRGSLEMS SDGEPLSRMD SEDSISSTIM DVDSTISSGR 250 260 270 280 290 300 STPAMMNGQG STTSSSKNIA YNCCWDQCQA CFNSSPDLAD HIRSIHVDGQ RGGVFVCLWK 310 320 330 340 350 360 GCKVYNTPST SQSWLQRHML THSGDKPFKC VVGGCNASFA SQGGLARHVP THFSQQNSSK 370 380 390 400 410 420 VSSQPKAKEE SPSKAGMNKR RKLKNKRRRS LPRPHDFFDA QTLDAIRHRA ICFNLSAHIE 430 440 450 460 470 480 SLGKGHSVVF HSTVIAKRKE DSGKIKLLLH WMPEDILPDV WVNESERHQL KTKVVHLSKL 490 500 510 PKDTALLLDP NIYRTMPQKR LKRTLIRKVF NLYLSKQ
	Isoform 2 [UniParc]. Checksum: 032090A790243D07	FASTA	503	52,761
	10 20 30 40 50 60 MAAAITDMAD LEELSRLSPL PPGSPGSAAR GRAEPPEEEE EEEEEEEEAE AEAVAALLLN 70 80 90 100 110 120 GGSGGGGGGG GGGVGGGEAE TMSEPSPESA SQAGEDEDEE EDDEEEEDES SSSGGGEEES 130 140 150 160 170 180 SAESLVGSSG GSSSDETRSL SPGAASSSSG DGDGKEGLEE PKGPRGSQGG GGGGSSSSSV 190 200 210 220 230 240 VSSGGDEGYG TGGGGSSATS GGRRGSLEMS SDGEPLSRMD SEDSISSTIM DVDSTISSGR 250 260 270 280 290 300 STPAMMNGQG STTSSSKNIA YNCCWDQCQA CFNSSPDLAD HIRSIHVDGQ RGGVFVCLWK 310 320 330 340 350 360 GCKVYNTPST SQSWLQRHML THSGDKPFKC VVGGCNASFA SQGGLARHVP THFSQQNSSK 370 380 390 400 410 420 VSSQPKAKEE SPSKAGMNKR RKLKNKRRRS LPRPHDFFDA QTLDAIRHRA ICFNLSAHIE 430 440 450 460 470 480 SLGKGHSVVF HSTVIAKRKE DSGKIKLLLH WMPEDILPDV WVNESERHQL KTKVVHLSKL 490 500 PKDTALLLDP NIYRTMPQKR LKR
	Isoform 3 [UniParc]. Checksum: DD766CAAB61DADB3	FASTA	301	33,981
	10 20 30 40 50 60 MYTRRYSSIS STIMDVDSTI SSGRSTPAMM NGQGSTTSSS KNIAYNCCWD QCQACFNSSP 70 80 90 100 110 120 DLADHIRSIH VDGQRGGVFV CLWKGCKVYN TPSTSQSWLQ RHMLTHSGDK PFKCVVGGCN 130 140 150 160 170 180 ASFASQGGLA RHVPTHFSQQ NSSKVSSQPK AKEESPSKAG MNKRRKLKNK RRRSLPRPHD 190 200 210 220 230 240 FFDAQTLDAI RHRAICFNLS AHIESLGKGH SVVFHSTVIA KRKEDSGKIK LLLHWMPEDI 250 260 270 280 290 300 LPDVWVNESE RHQLKTKVVH LSKLPKDTAL LLDPNIYRTM PQKRLKRTLI RKVFNLYLSK Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: Teratocarcinoma and Uterus.
[2]	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].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Eye and Uterus.
[4]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-517 (ISOFORM 1). Tissue: Brain.
[5]	"Role of histone H3 lysine 27 methylation in Polycomb-group silencing." Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., Jones R.S., Zhang Y. Science 298:1039-1043(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH EED; EZH2; RBBP4; RBBP7 AND SUZ12.
[6]	"SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex." Cao R., Zhang Y. Mol. Cell 15:57-67(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH EED; EZH2; RBBP4 AND SUZ12.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-24, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-210 AND SER-211, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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-206, MASS SPECTROMETRY. 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-24 AND SER-390, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[12]	"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-206 AND SER-390, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK131361 mRNA. Translation: BAD18513.1. Sequence problems. AK131410 mRNA. Translation: BAD18557.1. CH471094 Genomic DNA. Translation: EAW96400.1. Different initiation. BC015624 mRNA. Translation: AAH15624.1. Different initiation. BC022220 mRNA. Translation: AAH22220.1. Different initiation. AB209384 mRNA. Translation: BAD92621.1.
IPI	IPI00303560. IPI00796417. IPI00895818.
RefSeq	NP_001107648.1. NM_001114176.1. NP_001253972.1. NM_001267043.1. NP_694939.2. NM_153207.4.
UniGene	Hs.126497.
3D structure databases
ProteinModelPortal	Q6ZN18.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-58581N.
IntAct	Q6ZN18. 2 interactions.
MINT	MINT-1439056.
STRING	9606.ENSP00000381840.
PTM databases
PhosphoSite	Q6ZN18.
Polymorphism databases
DMDM	190358163.
Proteomic databases
PaxDb	Q6ZN18.
PRIDE	Q6ZN18.
Protocols and materials databases
DNASU	121536.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000266508; ENSP00000266508; ENSG00000139154. ENST00000360995; ENSP00000354267; ENSG00000139154. ENST00000398864; ENSP00000381840; ENSG00000139154.
GeneID	121536.
KEGG	hsa:121536.
UCSC	uc001ree.2. human.
Organism-specific databases
CTD	121536.
GeneCards	GC12P019556.
HGNC	HGNC:24051. AEBP2.
HPA	HPA020893. HPA022282.
neXtProt	NX_Q6ZN18.
PharmGKB	PA134875401.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG291563.
HOGENOM	HOG000033826.
InParanoid	Q6ZN18.
OMA	ASSKHIA.
OrthoDB	EOG4RR6HS.
Gene expression databases
ArrayExpress	Q6ZN18.
Bgee	Q6ZN18.
CleanEx	HS_AEBP2.
Genevestigator	Q6ZN18.
Family and domain databases
Gene3D	3.30.160.60. 2 hits.
InterPro	IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
SMART	SM00355. ZnF_C2H2. 3 hits. [Graphical view]
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 2 hits. PS50157. ZINC_FINGER_C2H2_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	AEBP2. human.
GenomeRNAi	121536.
NextBio	80766.

Entry information

Entry name

AEBP2_HUMAN

Accession

Primary (citable) accession number: Q6ZN18
Secondary accession number(s): Q59FS5, Q6ZN62, Q96BG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	June 10, 2008
Last modified:	May 1, 2013
This is version 79 of the entry and version 2 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.