Reviewed, UniProtKB/Swiss-Prot Q6ZN18 (AEBP2_HUMAN)

Names and origin

Protein names

Recommended name:
    Zinc finger protein AEBP2
Alternative name(s):
    Adipocyte enhancer-binding protein 2
      Short name(s)=AE-binding protein 2

Gene names

Name:

AEBP2

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	517 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subunit structure	Self-associates. Interacts with EED, EZH2, RBBP4 and SUZ12. May also interact with RBBP7.
Subcellular location	NucleusProbable.
Sequence similarities	Belongs to the AEBP2/jing C2H2-type zinc-finger family. Contains 3 C2H2-type zinc fingers.
Sequence caution	BAD18513.1 sequence differs from that shown. Reason: Erroneous termination at position 269. Translated as Gln.

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	Phosphoprotein
Gene Ontology (GO)
None. [Check GOA]

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
Molecule processing
	Chain	1 – 517	517	Zinc finger protein AEBP2
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	18	1	Phosphoserine
	Modified residue	24	1	Phosphoserine
	Modified residue	27	1	Phosphoserine
Natural variations
	Alternative sequence	1 – 216	216	Missing in isoform 3.
	Alternative sequence	217 – 223	7	SRMDSED → MYTRRYS in isoform 3.
	Alternative sequence	504 – 517	14	Missing in isoform 2.

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		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		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: 14702039] [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: 15489334] [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: 12351676] [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: 15225548] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-24, 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], MASS SPECTROMETRY.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
RefSeq	NP_001107648.1. NP_694939.2.
UniGene	Hs.126497
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q6ZN18.
Genome annotation databases
Ensembl	ENSG00000139154. Homo sapiens. [Contig view]
GeneID	121536.
KEGG	hsa:121536.
Organism-specific databases
HGNC	HGNC:24051. AEBP2.
PharmGKB	PA134875401.
GenAtlas	Search...
GeneCards	Search...
GeneLynx	Search...
Phylogenomic databases
HOVERGEN	Q6ZN18.
Gene expression databases
ArrayExpress	Q6ZN18.
Family and domain databases
InterPro	IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. [Graphical view]
Pfam	PF00096. zf-C2H2. 2 hits. [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]
ProDom	Q6ZN18. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

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:	July 22, 2008
This is version 34 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)