| Tag | Content |
|---|
| CPLM ID | CPLM-017100 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ZZ-type zinc finger-containing protein 3 |
Protein Synonyms/Alias | |
Gene Name | ZZZ3 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 701 | QVASRVQKYFIKLTK | acetylation | [1] | | 725 | PNLYIYSKKSSTSRR | acetylation | [1] | | 738 | RRQHPLNKHLFKPST | acetylation | [1] |
|
Reference | [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M. Science. 2009 Aug 14;325(5942):834-40. [ PMID: 19608861] |
Functional Description | Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. |
Sequence Annotation | DOMAIN 647 707 HTH myb-type.
DNA_BIND 680 703 H-T-H motif (By similarity).
ZN_FING 817 867 ZZ-type.
MOD_RES 113 113 Phosphoserine.
MOD_RES 130 130 Phosphoserine.
MOD_RES 131 131 Phosphoserine.
MOD_RES 135 135 Phosphoserine.
MOD_RES 701 701 N6-acetyllysine. |
Keyword | 3D-structure; Acetylation; Alternative splicing; Complete proteome; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 903 AA |
Protein Sequence | MAASRSTRVT RSTVGLNGLD ESFCGRTLRN RSIAHPEEIS SNSQVRSRSP KKRPEPVPIQ 60
KGNNNGRTTD LKQQSTRESW VSPRKRGLSS SEKDNIERQA IENCERRQTE PVSPVLKRIK 120
RCLRSEAPNS SEEDSPIKSD KESVEQRSTV VDNDADFQGT KRACRCLILD DCEKREIKKV 180
NVSEEGPLNS AVVEEITGYL AVNGVDDSDS AVINCDDCQP DGNTKQNSIG SYVLQEKSVA 240
ENGDTDTQTS MFLDSRKEDS YIDHKVPCTD SQVQVKLEDH KIVTACLPVE HVNQLTTEPA 300
TGPFSETQSS LRDSEEEVDV VGDSSASKEQ CKENTNNELD TSLESMPASG EPEPSPVLDC 360
VSAQMMSLSE PQEHRYTLRT SPRRAAPTRG SPTKNSSPYR ENGQFEENNL SPNETNATVS 420
DNVSQSPTNP GEISQNEKGI CCDSQNNGSE GVSKPPSEAR LNIGHLPSAK ESASQHITEE 480
EDDDPDVYYF ESDHVALKHN KDYQRLLQTI AVLEAQRSQA VQDLESLGRH QREALKNPIG 540
FVEKLQKKAD IGLPYPQRVV QLPEIVWDQY THSLGNFERE FKNRKRHTRR VKLVFDKVGL 600
PARPKSPLDP KKDGESLSYS MLPLSDGPEG SSSRPQMIRG RLCDDTKPET FNQLWTVEEQ 660
KKLEQLLIKY PPEEVESRRW QKIADELGNR TAKQVASRVQ KYFIKLTKAG IPVPGRTPNL 720
YIYSKKSSTS RRQHPLNKHL FKPSTFMTSH EPPVYMDEDD DRSCFHSHMN TAVEDASDDE 780
SIPIMYRNLP EYKELLQFKK LKKQKLQQMQ AESGFVQHVG FKCDNCGIEP IQGVRWHCQD 840
CPPEMSLDFC DSCSDCLHET DIHKEDHQLE PIYRSETFLD RDYCVSQGTS YNYLDPNYFP 900
ANR 903 |
Gene Ontology | GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IEA:Compara. GO:0003682; F:chromatin binding; IEA:InterPro. GO:0003677; F:DNA binding; IEA:UniProtKB-KW. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |