Mikä sinkkisormilöytö p300 histoniasetyylitransferaasilla!

1. P300 asetyylitransferaasilla on  runsanstyyppinen  sinkkisormikirjo.  Se pystyy asetyloimaan sekä histonia että ei-histoneita.  Otan kopion konservoiduista domeeneista tähän. Niisä on apytyyppisiksi mainittuja joukossa.   
2. Lähde: https://www.ncbi.nlm.nih.gov/protein/NP_001349772.1
3. 
   NM_001362843.2 → NP_001349772.1  histone acetyltransferase p300 isoform 2
   
   Status: REVIEWED

   Description

   Transcript Variant: This variant (2) lacks an in-frame exon in the central coding region, compared to variant 1, which results in a shorter protein (isoform 2) compared to isoform 1.

   Source sequence(s)

   AL035658, AL080243, AL096765

   Conserved Domains (11) summary

   cd05495
   Location:1025 → 1132

   Bromo_cbp_like; Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to ...

   smart00551
   Location:1703 → 1781

   ZnF_TAZ; TAZ zinc finger, present in p300 and CBP 

   Zinc finger, ZZ type. 

   Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.

   cd02337
   Location:1642 → 1682

   ZZ_CBP; Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that ...Evidence:
   

   • Comment:6 conserved cysteines and 2 conserved histidines coordinate 2 zinc ions

   cd15802
   Location:1144 → 1216

   RING_CBP-p300; atypical RING domain found in CREB-binding protein and p300 histone acetyltransferasesCBP and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This ring domain contains only a single zinc ion-binding cluster(CCCC) instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902.

   cd15646
   Location:1217 → 1251

   PHD_p300; PHD finger found in histone acetyltransferase p300
   

    also termed KAT3B, or E1A-associated protein p300 (EP300)
   

   Conserved feature residue pattern:C C C C H C C C

   Evidence:Structure:Human P300 HAT binds two Zn2+ ions through its PHD finger.

   pfam02172
   Location:566 → 646

   KIX; KIX domain

   pfam02135
   Location:347 → 414

   zf-TAZ; TAZ zinc finger

   pfam08214
   Location:1280 → 1586

   HAT_KAT11; Histone acetylation protein

   pfam09030
   Location:1979 → 2071

   Creb_binding; Creb binding

   pfam09606
   Location:1958 → 2382

   Med15; ARC105 or Med15 subunit of Mediator complex non-fungal

   cl25526
   Location:935 → 1038

   TonB_N; TonB N-terminal region