CBP_RAT
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 03-AUG-2022, entry version 137.
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). Also acetylates non-histone
CC proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1
CC (By similarity). Binds specifically to phosphorylated CREB and enhances
CC its transcriptional activity toward cAMP-responsive genes. Acts as a
CC coactivator of ALX1. Acts as a circadian transcriptional coactivator
CC which enhances the activity of the circadian transcriptional
CC activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers (By
CC similarity). Acetylates PCNA; acetylation promotes removal of
CC chromatin-bound PCNA and its degradation during nucleotide excision
CC repair (NER) (By similarity). Acetylates POLR1E/PAF53, leading to
CC decreased association of RNA polymerase I with the rDNA promoter region
CC and coding region (By similarity). Acetylates DDX21, thereby inhibiting
CC DDX21 helicase activity (By similarity). Acetylates FBL, preventing
CC methylation of 'Gln-105' of histone H2A (H2AQ104me) (By similarity).
CC Functions as a transcriptional coactivator for SMAD4 in the TGF-beta
CC signaling pathway (By similarity). {ECO:0000250|UniProtKB:P45481,
CC 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: 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 ARNTL/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).
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}.
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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; Q6JHU9; -.
DR PRIDE; Q6JHU9; -.
DR UCSC; RGD:2401; rat.
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-918233; TRAF3-dependent IRF activation pathway.
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; IDA:RGD.
DR GO; GO:0000940; C:outer kinetochore; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA: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: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: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:0008283; P:cell population proliferation; IDA:RGD.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; 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:0016573; P:histone acetylation; IDA:RGD.
DR GO; GO:1990258; P:histone glutamine methylation; ISS:UniProtKB.
DR GO; GO:0007616; P:long-term memory; IMP:RGD.
DR GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; ISO:RGD.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:RGD.
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:0060355; P:positive regulation of cell adhesion molecule production; IMP:RGD.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISO:RGD.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD.
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 NIK/NF-kappaB signaling; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0006473; P:protein acetylation; ISO:RGD.
DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd15802; RING_CBP-p300; 1.
DR Gene3D; 1.10.1630.10; -; 1.
DR Gene3D; 1.10.246.20; -; 1.
DR Gene3D; 1.20.1020.10; -; 2.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.60.90; -; 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; PTHR13808; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF09030; Creb_binding; 1.
DR Pfam; PF06001; DUF902; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 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; SSF47040; SSF47040; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57933; SSF57933; 2.
DR SUPFAM; SSF69125; SSF69125; 1.
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
