ID CBP_RAT Reviewed; 2442 AA. AC Q6JHU9; DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 146. DE RecName: Full=Histone lysine acetyltransferase CREBBP; DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92793}; DE AltName: Full=Protein-lysine acetyltransferase CREBBP; DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q92793}; GN Name=Crebbp; Synonyms=Cbp; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION. RC STRAIN=Sprague-Dawley; RX PubMed=15950780; DOI=10.1016/j.molbrainres.2005.03.009; RA Tang C., Sula M.J., Bohnet S., Rehman A., Taishi P., Krueger J.M.; RT "Interleukin-1beta induces CREB-binding protein (CBP) mRNA in brain and the RT sequencing of rat CBP."; RL Brain Res. Mol. Brain Res. 137:213-222(2005). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2064, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: Acetylates histones, giving a specific tag for CC transcriptional activation (By similarity). Mediates acetylation of CC histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) CC (By similarity). Also acetylates non-histone proteins, like DDX21, FBL, CC IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1 (By similarity). Binds CC specifically to phosphorylated CREB and enhances its transcriptional CC activity toward cAMP-responsive genes. Acts as a coactivator of ALX1. CC Acts as a circadian transcriptional coactivator which enhances the CC activity of the circadian transcriptional activators: NPAS2-BMAL1 and CC CLOCK-BMAL1 heterodimers (By similarity). Acetylates PCNA; acetylation CC promotes removal of chromatin-bound PCNA and its degradation during CC nucleotide excision repair (NER) (By similarity). Acetylates CC POLR1E/PAF53, leading to decreased association of RNA polymerase I with CC the rDNA promoter region and coding region (By similarity). Acetylates CC DDX21, thereby inhibiting DDX21 helicase activity (By similarity). CC Acetylates FBL, preventing methylation of 'Gln-105' of histone H2A CC (H2AQ104me) (By similarity). Functions as a transcriptional coactivator CC for SMAD4 in the TGF-beta signaling pathway (By similarity). CC {ECO:0000250|UniProtKB:P45481, ECO:0000250|UniProtKB:Q92793}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000250|UniProtKB:Q92793}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; CC Evidence={ECO:0000250|UniProtKB:Q92793}; CC -!- SUBUNIT: Part of a complex composed of MSX3, CREBBP/CBP AND EP300/p300; CC the interaction with MSX3 decreases histone acetylation activity (By CC similarity). Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and CC IKBKG. Probably part of a complex with HIF1A and EP300. Interacts with CC phosphorylated CREB1. Interacts with the C-terminal region of CITED4. CC The TAZ-type 1 domain interacts with HIF1A. Interacts with SRCAP, CC CARM1, ELF3, MLLT7/FOXO4, N4BP2, NCOA1, NCOA3, NCOA6, PCAF, DDX5, CC DDX17, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB, TRERF1 and ZCCHC12. CC Interacts with KLF1; the interaction results in acetylation and CC enhancement of transcriptional activity of KLF1. Interacts with DAXX; CC the interaction is dependent on CBP sumoylation and results in CC suppression of the transcriptional activity via recruitment of HDAC2 to CC DAXX. Interacts with MAF. Interacts with MTDH. Interacts with MAFG; the CC interaction acetylates MAFG in the basic region and stimulates NFE2 CC transcriptional activity through increasing its DNA-binding activity. CC Interacts with IRF2; the interaction acetylates IRF2 and regulates its CC activity on the H4 promoter. Interacts (via N-terminus) with CC SS18L1/CREST (via C-terminus) (By similarity). Interacts with IRF3 CC (when phosphorylated); forming the dsRNA-activated factor 1 (DRAF1), a CC complex which activates the transcription of the type I interferon CC genes (By similarity). Interacts with MECOM. Interacts with CITED1 (via CC C-terminus) Interacts with GATA1; the interaction results in CC acetylation and enhancement of transcriptional activity of GATA1. CC Interacts with FOXO1; the interaction acetylates FOXO1 and inhibits its CC transcriptional activity. Interacts with NPAS2, CLOCK and BMAL1. CC Interacts with ASF1A and ASF1B; this promotes histone acetylation. CC Interacts with acetylated TP53/p53 and with the acetylated histones H3 CC and H4. Interacts (via transactivation domain and C-terminus) with CC PCNA; the interaction occurs on chromatin in UV-irradiated damaged CC cells. Interacts with DHX9 (via N-terminus); this interaction mediates CC association with RNA polymerase II holoenzyme and stimulates CREB- CC dependent transcriptional activation (By similarity). Interacts with CC SMAD4; negatively regulated by ZBTB7A (By similarity). Forms a complex CC with KMT2A and CREB1 (By similarity). Interacts with DDX3X; this CC interaction may facilitate HNF4A acetylation (By similarity). Interacts CC with MSX1; the interaction may inhibit MSX1 autoinactivation (By CC similarity). Interacts with MSX3 (By similarity). Interacts with ACSS2 CC (By similarity). {ECO:0000250|UniProtKB:P45481, CC ECO:0000250|UniProtKB:Q92793}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92793}. Nucleus CC {ECO:0000255|PROSITE-ProRule:PRU00311}. Note=Recruited to nuclear CC bodies by SS18L1/CREST. In the presence of ALX1 relocalizes from the CC cytoplasm to the nucleus. {ECO:0000250|UniProtKB:Q92793}. CC -!- TISSUE SPECIFICITY: Expressed in hypothalamus and cortex. CC {ECO:0000269|PubMed:15950780}. CC -!- INDUCTION: Up-regulated by IL-1 treatment. CC {ECO:0000269|PubMed:15950780}. CC -!- PTM: Methylation of the KIX domain by CARM1 blocks association with CC CREB. This results in the blockade of CREB signaling, and in activation CC of apoptotic response (By similarity). {ECO:0000250|UniProtKB:P45481}. CC -!- PTM: Phosphorylated by CHUK/IKKA at Ser-1383 and Ser-1387; these CC phosphorylations promote cell growth by switching the binding CC preference of CREBBP from TP53 to NF-kappa-B. CC {ECO:0000250|UniProtKB:Q92793}. CC -!- PTM: Sumoylation negatively regulates transcriptional activity via the CC recruitment of DAAX. {ECO:0000250|UniProtKB:P45481}. CC -!- PTM: Autoacetylation is required for binding to protein substrates, CC such as acetylated histones and acetylated TP53/p53. Autoacetylation is CC induced by glucose and fatty acids. {ECO:0000250|UniProtKB:Q92793}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY462245; AAR23149.1; -; mRNA. DR AlphaFoldDB; Q6JHU9; -. DR BMRB; Q6JHU9; -. DR SMR; Q6JHU9; -. DR IntAct; Q6JHU9; 1. DR MINT; Q6JHU9; -. DR STRING; 10116.ENSRNOP00000007079; -. DR iPTMnet; Q6JHU9; -. DR PhosphoSitePlus; Q6JHU9; -. DR PaxDb; 10116-ENSRNOP00000007079; -. DR UCSC; RGD:2401; rat. DR AGR; RGD:2401; -. DR RGD; 2401; Crebbp. DR eggNOG; KOG1778; Eukaryota. DR InParanoid; Q6JHU9; -. DR Reactome; R-RNO-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-RNO-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production. DR Reactome; R-RNO-3371568; Attenuation phase. DR Reactome; R-RNO-400206; Regulation of lipid metabolism by PPARalpha. DR Reactome; R-RNO-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells. DR Reactome; R-RNO-933541; TRAF6 mediated IRF7 activation. DR Reactome; R-RNO-9617629; Regulation of FOXO transcriptional activity by acetylation. DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1. DR Reactome; R-RNO-9759194; Nuclear events mediated by NFE2L2. DR PRO; PR:Q6JHU9; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0000785; C:chromatin; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0000123; C:histone acetyltransferase complex; ISO:RGD. DR GO; GO:0016604; C:nuclear body; IDA:RGD. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0000940; C:outer kinetochore; ISO:RGD. DR GO; GO:0032991; C:protein-containing complex; ISO:RGD. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD. DR GO; GO:0005667; C:transcription regulator complex; IDA:RGD. DR GO; GO:0016407; F:acetyltransferase activity; ISS:UniProtKB. DR GO; GO:0008140; F:cAMP response element binding protein binding; ISO:RGD. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central. DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB. DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD. DR GO; GO:0003677; F:DNA binding; ISO:RGD. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:RGD. DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:RGD. DR GO; GO:0043993; F:histone H3K18 acetyltransferase activity; ISS:UniProtKB. DR GO; GO:0044017; F:histone H3K27 acetyltransferase activity; ISS:UniProtKB. DR GO; GO:0060090; F:molecular adaptor activity; ISO:RGD. DR GO; GO:0043426; F:MRF binding; ISS:UniProtKB. DR GO; GO:0002039; F:p53 binding; ISO:RGD. DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISO:RGD. DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IDA:RGD. DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD. DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD. DR GO; GO:0046332; F:SMAD binding; IPI:RGD. DR GO; GO:0001093; F:TFIIB-class transcription factor binding; ISO:RGD. DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD. DR GO; GO:0001223; F:transcription coactivator binding; IPI:RGD. DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD. DR GO; GO:0008270; F:zinc ion binding; ISO:RGD. DR GO; GO:0048148; P:behavioral response to cocaine; IMP:RGD. DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISO:RGD. DR GO; GO:0031669; P:cellular response to nutrient levels; ISO:RGD. DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB. DR GO; GO:0098586; P:cellular response to virus; ISO:RGD. DR GO; GO:0060325; P:face morphogenesis; ISO:RGD. DR GO; GO:0030718; P:germ-line stem cell population maintenance; ISO:RGD. DR GO; GO:0007616; P:long-term memory; IMP:RGD. DR GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:RGD. DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0048525; P:negative regulation of viral process; ISO:RGD. DR GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; ISO:RGD. DR GO; GO:0060355; P:positive regulation of cell adhesion molecule production; IMP:RGD. DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:RGD. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD. DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IMP:RGD. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD. DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD. DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB. DR GO; GO:0036211; P:protein modification process; IDA:RGD. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:RGD. DR GO; GO:0070555; P:response to interleukin-1; IEP:RGD. DR GO; GO:0002931; P:response to ischemia; IEP:RGD. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR CDD; cd05495; Bromo_cbp_like; 1. DR CDD; cd20910; NCBD_CREBBP-p300_like; 1. DR CDD; cd15557; PHD_CBP_p300; 1. DR CDD; cd15802; RING_CBP-p300; 1. DR CDD; cd02337; ZZ_CBP; 1. DR Gene3D; 2.10.110.40; -; 1. DR Gene3D; 3.30.60.90; -; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1. DR Gene3D; 1.10.1630.10; Nuclear receptor coactivator, CREB-bp-like, interlocking domain; 1. DR Gene3D; 1.20.1020.10; TAZ domain; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR031162; CBP_P300_HAT. DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP. DR InterPro; IPR003101; KIX_dom. DR InterPro; IPR036529; KIX_dom_sf. DR InterPro; IPR009110; Nuc_rcpt_coact. DR InterPro; IPR014744; Nuc_rcpt_coact_CREBbp. DR InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf. DR InterPro; IPR010303; RING_CBP-p300. DR InterPro; IPR038547; RING_CBP-p300_sf. DR InterPro; IPR035898; TAZ_dom_sf. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR000197; Znf_TAZ. DR InterPro; IPR000433; Znf_ZZ. DR InterPro; IPR043145; Znf_ZZ_sf. DR PANTHER; PTHR13808; CBP/P300-RELATED; 1. DR PANTHER; PTHR13808:SF34; CREB-BINDING PROTEIN; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF09030; Creb_binding; 1. DR Pfam; PF08214; HAT_KAT11; 1. DR Pfam; PF02172; KIX; 1. DR Pfam; PF06001; RING_CBP-p300; 1. DR Pfam; PF02135; zf-TAZ; 2. DR Pfam; PF00569; ZZ; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 1. DR SMART; SM01250; KAT11; 1. DR SMART; SM00551; ZnF_TAZ; 2. DR SMART; SM00291; ZnF_ZZ; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1. DR SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF57933; TAZ domain; 2. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PROSITE; PS51727; CBP_P300_HAT; 1. DR PROSITE; PS50952; KIX; 1. DR PROSITE; PS50134; ZF_TAZ; 2. DR PROSITE; PS01357; ZF_ZZ_1; 1. DR PROSITE; PS50135; ZF_ZZ_2; 1. PE 1: Evidence at protein level; KW Acetylation; Activator; Acyltransferase; Biological rhythms; Bromodomain; KW Coiled coil; Cytoplasm; Isopeptide bond; Metal-binding; Methylation; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT CHAIN 2..2442 FT /note="Histone lysine acetyltransferase CREBBP" FT /id="PRO_0000409385" FT DOMAIN 586..665 FT /note="KIX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00311" FT DOMAIN 1104..1176 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 1324..1701 FT /note="CBP/p300-type HAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065" FT ZN_FING 346..432 FT /note="TAZ-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203" FT ZN_FING 1703..1751 FT /note="ZZ-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT ZN_FING 1766..1847 FT /note="TAZ-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203" FT REGION 1..40 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 74..168 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 226..409 FT /note="Interaction with SRCAP" FT /evidence="ECO:0000250" FT REGION 261..290 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 792..1084 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1125..1171 FT /note="Interaction with histone" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT REGION 1163..1181 FT /note="Interaction with ASF1A" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT REGION 1434..1436 FT /note="Interaction with histone" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT REGION 1557..1616 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1875..1960 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2112..2421 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1548..1575 FT /evidence="ECO:0000255" FT COMPBIAS 18..32 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 262..290 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 792..849 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 850..864 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 874..889 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 890..930 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 939..991 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 999..1066 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1067..1082 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1557..1572 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1589..1603 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1884..1917 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1922..1939 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1941..1955 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2112..2146 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2163..2187 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2196..2266 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2277..2350 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2351..2378 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2395..2421 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 362 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 366 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 379 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 384 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 393 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 397 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 403 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 408 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 417 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 421 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 426 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 429 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 1435..1437 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1447..1448 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1494 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1499 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1503 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1708 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1711 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1721 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1724 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1730 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1733 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1739 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1741 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 120 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 219 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 600 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250" FT MOD_RES 624 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250" FT MOD_RES 656 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P45481" FT MOD_RES 1015 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1031 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1077 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1217 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1383 FT /note="Phosphoserine; by IKKA" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1387 FT /note="Phosphoserine; by IKKA" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1584 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1592 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1593 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1596 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1598 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1742 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1745 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1764 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 2064 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 2077 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 2080 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 2351 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P45481" FT CROSSLNK 999 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000250|UniProtKB:P45481" FT CROSSLNK 1034 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000250|UniProtKB:P45481" FT CROSSLNK 1057 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000250|UniProtKB:P45481" SQ SEQUENCE 2442 AA; 265424 MW; 2E77EF213C72C024 CRC64; MAENLLDGPP NPKRAKLSSP GFSANDSTDF GSLFDLENDL PDELIPNGEL SLLNSGNLVP DAASKHKQLS ELLRGGSGSS ITPGIGNVSA SSPVQQGLGG QAQGQPNSTS MASLGAMGKS PLNPGDSSTP SLPKQAASTS GPTPPASQAL NPQAQKQVGL VTSSPATSQT GPGICMNANF NQTHPGLLNS NSGHSLMNQA QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE TLTQVSPQMA GHAGLNTAQA GGMTKMGMTG NTSPFGQPFS QTGGQPMGAT GVNPQLASKQ SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPAQGIA TGPTADPEKR KLIQQQLVLL LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAG KACQVAHCAS SRQIISHWKN CTRHDCPVCL PLKNASDKRN QQTILGSPAS GIQNTIGSVG AGQQNATSLS NPNPIDPSSM QRAYAALGLP YMNQPQTQLQ PQVPGQQPAQ PPAHQQMRTL NALGNNPMSI PAGGITTDQQ PPNLISESAL PTSLGATNPL MNDGSNSDSI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY HLLAEKIYKI QKELEEKRRS RLHKQGILGN QPALPAPGAQ PPVIPPTQSV RPPNGPLSLP VNRVQVSQGM NSFNPMSLGN VQLPQAPMGP RAASPMNHSV QMNSMASVPG MAISPSRMPQ PPNMMGTHAN NIMAQAPTQN QFLPQNQFPS SSGAMSVNSV GMGQPATQAG VSQGQVPGGT LPNPLNMLAP QTSQLPCPPV TQSPLHPTPP PASTAAGMPS LQHPTPPGMT PPQPAAPTQP STPVSSGQTP TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP TPVHTQPPGT PLSQAAASID NRVPTPSSVT SAETSSQQPG PDVPMLEMKT EVQTDDAEPD PAESKGEPRS EMMEEDLQGS SQVKEETDTT EQKSEPMEVE EKKPEVKVEA KEEEENSANG TASQSTSPSQ PRKKIFKPEE LRQALMPTLE ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK RKLDTGQYQE PWQYVDDVWL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCEK CFTEIQGENV TLGDDPSQPQ TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD IIWPSGFVCD NCLKKTGRPR KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ NHPEAGEVFV RVVASSDKTV EVKPGMKSRF VDSGEMSESF PYRTKALFAF EEIDGVDVCF FGMHVQEYGS DCPPPNTRRV YISYLDSIHF FRPRCLRTAV YHEILIGYLE YVKKLGYVTG HIWACPPSEG DDYIFHCHPP DQKIPKPKRL QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL EESIKELEQE EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS ISRANKKKPS MPNVSNDLSQ KLYATMEKHK EVFFVIHLHA GPVISTQPPI VDPDPLLSCD LMDGRDAFLT LARDKHWEFS SLRRSKWSTL CMLVELHTQG QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT HKMVKWGLGL DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHK LRQQQIQHRL QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST PQTPQPPAQP QPSPVNMSPA GFPSVARTQP PTIVSAGKPT NQVPAPPPPA QPPPAAVEAA RQIEREGQQQ QHLYRANINN GMPPGRAGMG TPGSQMAPVG LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV MSMQAQAAVA GPRMPNVQPP RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV PRPGVPPPQQ AMGGLNPQGQ ALNIMNPGHN PNMANMNPQY REMVRRQLLQ HQQQQQQQQQ QQQQQQQSSA SLAGGMAGHS QFQQPQGPGG YAPAMQQQRM QQHLPIQGSS MGQMAAPMGQ LGQMGQPGLG ADSTPNIQQA LQQRILQQQQ MKQQIGSPGQ PNPMSPQQHM LSGQPQASHL PGQQIATSLS NQVRSPAPVQ SPRPQSQPPH SSPSPRIQPQ PSPHHVSPQT GSPHPGLAVT MASSMDQGHL GNPEQSAMLP QLNTPNRSAL SSELSLVGDT TGDTLEKFVE GL //