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Q6ZN18 (AEBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger protein AEBP2
Alternative name(s):
Adipocyte enhancer-binding protein 2
Short name=AE-binding protein 2
Gene names
Name:AEBP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 517516Zinc finger protein AEBP2
PRO_0000341590

Regions

Zinc finger261 – 28626C2H2-type 1
Zinc finger300 – 32223C2H2-type 2; degenerate
Zinc finger328 – 35225C2H2-type 3
Region209 – 29486Interaction with RBBP4
Region353 – 517165Interaction with SUZ12
Compositional bias34 – 12390Glu-rich
Compositional bias61 – 205145Gly-rich
Compositional bias110 – 256147Ser-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.10 Ref.12 Ref.14
Modified residue181Phosphoserine Ref.7 Ref.12
Modified residue241Phosphoserine Ref.7 Ref.12
Modified residue2061Phosphoserine Ref.9 Ref.11 Ref.13
Modified residue2101Phosphoserine Ref.9
Modified residue2111Phosphoserine Ref.9
Modified residue3901Phosphoserine Ref.12 Ref.13

Natural variations

Alternative sequence1 – 216216Missing in isoform 3.
VSP_034357
Alternative sequence217 – 2237SRMDSED → MYTRRYS in isoform 3.
VSP_034358
Alternative sequence504 – 51714Missing in isoform 2.
VSP_034359

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 10, 2008. Version 2.
Checksum: 6C59888ACEE4F9AF

FASTA51754,467
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 032090A790243D07
Show »

FASTA50352,761
Isoform 3 [UniParc].

Checksum: DD766CAAB61DADB3
Show »

FASTA30133,981

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
RefSeqNP_001107648.1. NM_001114176.1.
NP_001253972.1. NM_001267043.1.
NP_694939.2. NM_153207.4.
UniGeneHs.126497.

3D structure databases

ProteinModelPortalQ6ZN18.
SMRQ6ZN18. Positions 259-388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125736. 13 interactions.
DIPDIP-58581N.
IntActQ6ZN18. 3 interactions.
MINTMINT-1439056.
STRING9606.ENSP00000381840.

PTM databases

PhosphoSiteQ6ZN18.

Polymorphism databases

DMDM190358163.

Proteomic databases

PaxDbQ6ZN18.
PRIDEQ6ZN18.

Protocols and materials databases

DNASU121536.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266508; ENSP00000266508; ENSG00000139154. [Q6ZN18-2]
ENST00000360995; ENSP00000354267; ENSG00000139154. [Q6ZN18-3]
ENST00000398864; ENSP00000381840; ENSG00000139154. [Q6ZN18-1]
GeneID121536.
KEGGhsa:121536.
UCSCuc001ree.2. human. [Q6ZN18-1]
uc001reg.2. human. [Q6ZN18-3]

Organism-specific databases

CTD121536.
GeneCardsGC12P019556.
HGNCHGNC:24051. AEBP2.
HPAHPA020893.
HPA022282.
neXtProtNX_Q6ZN18.
PharmGKBPA134875401.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291563.
HOGENOMHOG000033826.
InParanoidQ6ZN18.
KOK17452.
OMAQTXVIAK.
PhylomeDBQ6ZN18.
TreeFamTF328864.

Gene expression databases

ArrayExpressQ6ZN18.
BgeeQ6ZN18.
CleanExHS_AEBP2.
GenevestigatorQ6ZN18.

Family and domain databases

Gene3D3.30.160.60. 2 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAEBP2. human.
GenomeRNAi121536.
NextBio80766.
PROQ6ZN18.

Entry information

Entry nameAEBP2_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM