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Q6JHU9

- CBP_RAT

UniProt

Q6JHU9 - CBP_RAT

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Protein

CREB-binding protein

Gene

Crebbp

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 and FOXO1. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1 in the presence of EP300. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers.By similarity

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi362 – 3621Zinc 1By similarity
Metal bindingi366 – 3661Zinc 1By similarity
Metal bindingi379 – 3791Zinc 1By similarity
Metal bindingi384 – 3841Zinc 1By similarity
Metal bindingi393 – 3931Zinc 2By similarity
Metal bindingi397 – 3971Zinc 2By similarity
Metal bindingi403 – 4031Zinc 2By similarity
Metal bindingi408 – 4081Zinc 2By similarity
Metal bindingi417 – 4171Zinc 3By similarity
Metal bindingi421 – 4211Zinc 3By similarity
Metal bindingi426 – 4261Zinc 3By similarity
Metal bindingi429 – 4291Zinc 3By similarity
Binding sitei1494 – 14941Acetyl-CoA; via carbonyl oxygenBy similarity
Binding sitei1499 – 14991Acetyl-CoABy similarity
Binding sitei1503 – 15031Acetyl-CoABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri346 – 43287TAZ-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1702 – 174544ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1766 – 184782TAZ-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. acetyltransferase activity Source: UniProtKB
  2. activating transcription factor binding Source: RGD
  3. histone acetyltransferase activity Source: UniProtKB
  4. MRF binding Source: UniProtKB
  5. peroxisome proliferator activated receptor binding Source: RGD
  6. SMAD binding Source: RGD
  7. transcription coactivator activity Source: RGD
  8. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell proliferation Source: RGD
  2. histone acetylation Source: UniProtKB
  3. positive regulation of G1/S transition of mitotic cell cycle Source: RGD
  4. positive regulation of transcription, DNA-templated Source: UniProtKB
  5. positive regulation of transcription from RNA polymerase II promoter Source: RGD
  6. regulation of transcription, DNA-templated Source: RGD
  7. response to interleukin-1 Source: RGD
  8. rhythmic process Source: UniProtKB-KW
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
CREB-binding protein (EC:2.3.1.48By similarity)
Gene namesi
Name:Crebbp
Synonyms:Cbp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2401. Crebbp.

Subcellular locationi

Cytoplasm By similarity. Nucleus PROSITE-ProRule annotation
Note: Recruited to nuclear bodies by SS18L1/CREST. In the presence of ALX1 relocalizes from the cytoplasm to the nucleus.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. histone acetyltransferase complex Source: InterPro
  3. nuclear body Source: RGD
  4. nucleus Source: RGD
  5. protein complex Source: RGD
  6. transcription factor complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 24422441CREB-binding proteinPRO_0000409385Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei120 – 1201PhosphoserineBy similarity
Modified residuei600 – 6001Omega-N-methylated arginineBy similarity
Modified residuei624 – 6241Omega-N-methylated arginineBy similarity
Modified residuei656 – 6561N6-acetyllysineBy similarity
Cross-linki999 – 999Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)By similarity
Modified residuei1015 – 10151N6-acetyllysineBy similarity
Modified residuei1031 – 10311PhosphoserineBy similarity
Cross-linki1034 – 1034Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)By similarity
Cross-linki1057 – 1057Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)By similarity
Modified residuei1217 – 12171N6-acetyllysineBy similarity
Modified residuei1383 – 13831Phosphoserine; by IKKABy similarity
Modified residuei1387 – 13871Phosphoserine; by IKKABy similarity
Modified residuei1584 – 15841N6-acetyllysineBy similarity
Modified residuei1587 – 15871N6-acetyllysineBy similarity
Modified residuei1592 – 15921N6-acetyllysineBy similarity
Modified residuei1593 – 15931N6-acetyllysineBy similarity
Modified residuei1596 – 15961N6-acetyllysineBy similarity
Modified residuei1598 – 15981N6-acetyllysineBy similarity
Modified residuei1742 – 17421N6-acetyllysineBy similarity
Modified residuei1745 – 17451N6-acetyllysineBy similarity
Modified residuei2064 – 20641PhosphoserineBy similarity
Modified residuei2077 – 20771PhosphoserineBy similarity
Modified residuei2080 – 20801PhosphoserineBy similarity

Post-translational modificationi

Methylation of the KIX domain by CARM1 blocks association with CREB. This results in the blockade of CREB signaling, and in activation of apoptotic response (By similarity).By similarity
Phosphorylated by CHUK/IKKA at Ser-1383 and Ser-1387; these phosphorylations promote cell growth by switching the binding preference of CREBBP from TP53 to NF-kappa-B.By similarity
Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX.By similarity
Autoacetylation is required for binding to protein substrates, such as acetylated histones and acetylated TP53/p53.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ6JHU9.

PTM databases

PhosphoSiteiQ6JHU9.

Expressioni

Tissue specificityi

Expressed in hypothalamus and cortex.1 Publication

Inductioni

Up-regulated by IL-1 treatment.1 Publication

Gene expression databases

GenevestigatoriQ6JHU9.

Interactioni

Subunit structurei

Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex with HIF1A and EP300. Interacts with phosphorylated CREB1. Interacts with the C-terminal region of CITED4. The TAZ-type 1 domain interacts with HIF1A. Interacts with SRCAP, CARM1, ELF3, MLLT7/FOXO4, N4BP2, NCOA1, NCOA3, NCOA6, PCAF, DDX5, DDX17, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB, TRERF1 and ZCCHC12. Interacts with KLF1; the interaction results in acetylation and enhancement of transcriptional activity of KLF1. Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activity via recruitment of HDAC2 to DAXX. Interacts with MAF. Interacts with MTDH. Interacts with MAFG; the interaction acetylates MAFG in the basic region and stimulates NFE2 transcriptional activity through increasing its DNA-binding activity. Interacts with IRF2; the interaction acetylates IRF2 and regulates its activity on the H4 promoter. Interacts (via N-terminus) with SS18L1/CREST (via C-terminus) (By similarity). Interacts with MECOM. Interacts with CITED1 (via C-terminus) Interacts with GATA1; the interaction results in acetylation and enhancement of transcriptional activity of GATA1. Interacts with FOXO1; the interaction acetylates FOXO1 and inhibits its transcriptional activity. Interacts with NPAS2, CLOCK and ARNTL/BMAL1. Interacts with ASF1A and ASF1B; this promotes histone acetylation. Interacts with acetylated TP53/p53 and with the acetylated histones H3 and H4.By similarity

Protein-protein interaction databases

IntActiQ6JHU9. 1 interaction.
MINTiMINT-7292086.

Structurei

3D structure databases

ProteinModelPortaliQ6JHU9.
SMRiQ6JHU9. Positions 340-439, 586-672, 1085-1198, 1324-1751, 1764-1850, 2066-2112.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini586 – 66580KIXPROSITE-ProRule annotationAdd
BLAST
Domaini1104 – 117673BromoPROSITE-ProRule annotationAdd
BLAST
Domaini1324 – 1701378CBP/p300-type HATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni226 – 409184Interaction with SRCAPBy similarityAdd
BLAST
Regioni1125 – 117147Interaction with histoneBy similarityAdd
BLAST
Regioni1163 – 118119Interaction with ASF1ABy similarityAdd
BLAST
Regioni1434 – 14363Interaction with histoneBy similarity
Regioni1435 – 14373Acetyl-CoA bindingBy similarity
Regioni1447 – 14482Acetyl-CoA bindingBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1548 – 157528Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi682 – 961280Pro-richAdd
BLAST
Compositional biasi1556 – 15638Poly-Glu
Compositional biasi1853 – 2370518Gln-richAdd
BLAST
Compositional biasi1879 – 2065187Pro-richAdd
BLAST
Compositional biasi1944 – 19496Poly-Pro
Compositional biasi1968 – 19714Poly-Gln
Compositional biasi2082 – 20865Poly-Gln
Compositional biasi2200 – 221718Poly-GlnAdd
BLAST
Compositional biasi2297 – 23004Poly-Gln

Sequence similaritiesi

Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 CBP/p300-type HAT (histone acetyltransferase) domain.PROSITE-ProRule annotation
Contains 1 KIX domain.PROSITE-ProRule annotation
Contains 2 TAZ-type zinc fingers.PROSITE-ProRule annotation
Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri346 – 43287TAZ-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1702 – 174544ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1766 – 184782TAZ-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5076.
HOGENOMiHOG000111353.
HOVERGENiHBG000185.
InParanoidiQ6JHU9.

Family and domain databases

Gene3Di1.10.1630.10. 1 hit.
1.10.246.20. 1 hit.
1.20.1020.10. 2 hits.
1.20.920.10. 1 hit.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR010303. DUF902_CREBbp.
IPR013178. Histone_H3-K56_AcTrfase_RTT109.
IPR003101. KIX_dom.
IPR009110. Nuc_rcpt_coact.
IPR014744. Nuc_rcpt_coact_CREBbp.
IPR000197. Znf_TAZ.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF09030. Creb_binding. 1 hit.
PF06001. DUF902. 1 hit.
PF08214. KAT11. 1 hit.
PF02172. KIX. 1 hit.
PF02135. zf-TAZ. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51727. CBP_P300_HAT. 1 hit.
PS50952. KIX. 1 hit.
PS50134. ZF_TAZ. 2 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6JHU9 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MAENLLDGPP NPKRAKLSSP GFSANDSTDF GSLFDLENDL PDELIPNGEL
60 70 80 90 100
SLLNSGNLVP DAASKHKQLS ELLRGGSGSS ITPGIGNVSA SSPVQQGLGG
110 120 130 140 150
QAQGQPNSTS MASLGAMGKS PLNPGDSSTP SLPKQAASTS GPTPPASQAL
160 170 180 190 200
NPQAQKQVGL VTSSPATSQT GPGICMNANF NQTHPGLLNS NSGHSLMNQA
210 220 230 240 250
QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE TLTQVSPQMA
260 270 280 290 300
GHAGLNTAQA GGMTKMGMTG NTSPFGQPFS QTGGQPMGAT GVNPQLASKQ
310 320 330 340 350
SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPAQGIA TGPTADPEKR
360 370 380 390 400
KLIQQQLVLL LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAG
410 420 430 440 450
KACQVAHCAS SRQIISHWKN CTRHDCPVCL PLKNASDKRN QQTILGSPAS
460 470 480 490 500
GIQNTIGSVG AGQQNATSLS NPNPIDPSSM QRAYAALGLP YMNQPQTQLQ
510 520 530 540 550
PQVPGQQPAQ PPAHQQMRTL NALGNNPMSI PAGGITTDQQ PPNLISESAL
560 570 580 590 600
PTSLGATNPL MNDGSNSDSI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR
610 620 630 640 650
SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY
660 670 680 690 700
HLLAEKIYKI QKELEEKRRS RLHKQGILGN QPALPAPGAQ PPVIPPTQSV
710 720 730 740 750
RPPNGPLSLP VNRVQVSQGM NSFNPMSLGN VQLPQAPMGP RAASPMNHSV
760 770 780 790 800
QMNSMASVPG MAISPSRMPQ PPNMMGTHAN NIMAQAPTQN QFLPQNQFPS
810 820 830 840 850
SSGAMSVNSV GMGQPATQAG VSQGQVPGGT LPNPLNMLAP QTSQLPCPPV
860 870 880 890 900
TQSPLHPTPP PASTAAGMPS LQHPTPPGMT PPQPAAPTQP STPVSSGQTP
910 920 930 940 950
TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP
960 970 980 990 1000
TPVHTQPPGT PLSQAAASID NRVPTPSSVT SAETSSQQPG PDVPMLEMKT
1010 1020 1030 1040 1050
EVQTDDAEPD PAESKGEPRS EMMEEDLQGS SQVKEETDTT EQKSEPMEVE
1060 1070 1080 1090 1100
EKKPEVKVEA KEEEENSANG TASQSTSPSQ PRKKIFKPEE LRQALMPTLE
1110 1120 1130 1140 1150
ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK RKLDTGQYQE
1160 1170 1180 1190 1200
PWQYVDDVWL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC
1210 1220 1230 1240 1250
CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCEK CFTEIQGENV
1260 1270 1280 1290 1300
TLGDDPSQPQ TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD
1310 1320 1330 1340 1350
IIWPSGFVCD NCLKKTGRPR KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ
1360 1370 1380 1390 1400
NHPEAGEVFV RVVASSDKTV EVKPGMKSRF VDSGEMSESF PYRTKALFAF
1410 1420 1430 1440 1450
EEIDGVDVCF FGMHVQEYGS DCPPPNTRRV YISYLDSIHF FRPRCLRTAV
1460 1470 1480 1490 1500
YHEILIGYLE YVKKLGYVTG HIWACPPSEG DDYIFHCHPP DQKIPKPKRL
1510 1520 1530 1540 1550
QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL
1560 1570 1580 1590 1600
EESIKELEQE EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS
1610 1620 1630 1640 1650
ISRANKKKPS MPNVSNDLSQ KLYATMEKHK EVFFVIHLHA GPVISTQPPI
1660 1670 1680 1690 1700
VDPDPLLSCD LMDGRDAFLT LARDKHWEFS SLRRSKWSTL CMLVELHTQG
1710 1720 1730 1740 1750
QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT HKMVKWGLGL
1760 1770 1780 1790 1800
DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK
1810 1820 1830 1840 1850
RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHK
1860 1870 1880 1890 1900
LRQQQIQHRL QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST
1910 1920 1930 1940 1950
PQTPQPPAQP QPSPVNMSPA GFPSVARTQP PTIVSAGKPT NQVPAPPPPA
1960 1970 1980 1990 2000
QPPPAAVEAA RQIEREGQQQ QHLYRANINN GMPPGRAGMG TPGSQMAPVG
2010 2020 2030 2040 2050
LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV MSMQAQAAVA
2060 2070 2080 2090 2100
GPRMPNVQPP RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA
2110 2120 2130 2140 2150
FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV
2160 2170 2180 2190 2200
PRPGVPPPQQ AMGGLNPQGQ ALNIMNPGHN PNMANMNPQY REMVRRQLLQ
2210 2220 2230 2240 2250
HQQQQQQQQQ QQQQQQQSSA SLAGGMAGHS QFQQPQGPGG YAPAMQQQRM
2260 2270 2280 2290 2300
QQHLPIQGSS MGQMAAPMGQ LGQMGQPGLG ADSTPNIQQA LQQRILQQQQ
2310 2320 2330 2340 2350
MKQQIGSPGQ PNPMSPQQHM LSGQPQASHL PGQQIATSLS NQVRSPAPVQ
2360 2370 2380 2390 2400
SPRPQSQPPH SSPSPRIQPQ PSPHHVSPQT GSPHPGLAVT MASSMDQGHL
2410 2420 2430 2440
GNPEQSAMLP QLNTPNRSAL SSELSLVGDT TGDTLEKFVE GL
Length:2,442
Mass (Da):265,424
Last modified:July 5, 2004 - v1
Checksum:i2E77EF213C72C024
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY462245 mRNA. Translation: AAR23149.1.
UniGeneiRn.12815.

Genome annotation databases

UCSCiRGD:2401. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY462245 mRNA. Translation: AAR23149.1 .
UniGenei Rn.12815.

3D structure databases

ProteinModelPortali Q6JHU9.
SMRi Q6JHU9. Positions 340-439, 586-672, 1085-1198, 1324-1751, 1764-1850, 2066-2112.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q6JHU9. 1 interaction.
MINTi MINT-7292086.

PTM databases

PhosphoSitei Q6JHU9.

Proteomic databases

PaxDbi Q6JHU9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:2401. rat.

Organism-specific databases

RGDi 2401. Crebbp.

Phylogenomic databases

eggNOGi COG5076.
HOGENOMi HOG000111353.
HOVERGENi HBG000185.
InParanoidi Q6JHU9.

Miscellaneous databases

NextBioi 13957143.
PROi Q6JHU9.

Gene expression databases

Genevestigatori Q6JHU9.

Family and domain databases

Gene3Di 1.10.1630.10. 1 hit.
1.10.246.20. 1 hit.
1.20.1020.10. 2 hits.
1.20.920.10. 1 hit.
InterProi IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR010303. DUF902_CREBbp.
IPR013178. Histone_H3-K56_AcTrfase_RTT109.
IPR003101. KIX_dom.
IPR009110. Nuc_rcpt_coact.
IPR014744. Nuc_rcpt_coact_CREBbp.
IPR000197. Znf_TAZ.
IPR000433. Znf_ZZ.
[Graphical view ]
Pfami PF00439. Bromodomain. 1 hit.
PF09030. Creb_binding. 1 hit.
PF06001. DUF902. 1 hit.
PF08214. KAT11. 1 hit.
PF02172. KIX. 1 hit.
PF02135. zf-TAZ. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view ]
SUPFAMi SSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51727. CBP_P300_HAT. 1 hit.
PS50952. KIX. 1 hit.
PS50134. ZF_TAZ. 2 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Interleukin-1beta induces CREB-binding protein (CBP) mRNA in brain and the sequencing of rat CBP."
    Tang C., Sula M.J., Bohnet S., Rehman A., Taishi P., Krueger J.M.
    Brain Res. Mol. Brain Res. 137:213-222(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: Sprague-Dawley.

Entry informationi

Entry nameiCBP_RAT
AccessioniPrimary (citable) accession number: Q6JHU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3