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Q6JHU9

- CBP_RAT

UniProt

Q6JHU9 - CBP_RAT

Protein

CREB-binding protein

Gene

Crebbp

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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.By similarity

    Catalytic activityi

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

    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

    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. protein binding Source: UniProtKB
    7. SMAD binding Source: RGD
    8. transcription coactivator activity Source: RGD
    9. 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. rhythmic process Source: UniProtKB-KW
    8. transcription, DNA-templated Source: UniProtKB-KW

    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:2.3.1.48)
    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.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. histone acetyltransferase complex Source: InterPro
    3. nucleus Source: RGD
    4. protein complex Source: RGD
    5. transcription factor complex Source: RGD

    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

    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 By similarity.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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni226 – 409184Interaction with SRCAPBy similarityAdd
    BLAST

    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 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.

    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.
    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.

    Q6JHU9-1 [UniParc]FASTAAdd to Basket

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    MAENLLDGPP NPKRAKLSSP GFSANDSTDF GSLFDLENDL PDELIPNGEL     50
    SLLNSGNLVP DAASKHKQLS ELLRGGSGSS ITPGIGNVSA SSPVQQGLGG 100
    QAQGQPNSTS MASLGAMGKS PLNPGDSSTP SLPKQAASTS GPTPPASQAL 150
    NPQAQKQVGL VTSSPATSQT GPGICMNANF NQTHPGLLNS NSGHSLMNQA 200
    QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE TLTQVSPQMA 250
    GHAGLNTAQA GGMTKMGMTG NTSPFGQPFS QTGGQPMGAT GVNPQLASKQ 300
    SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPAQGIA TGPTADPEKR 350
    KLIQQQLVLL LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAG 400
    KACQVAHCAS SRQIISHWKN CTRHDCPVCL PLKNASDKRN QQTILGSPAS 450
    GIQNTIGSVG AGQQNATSLS NPNPIDPSSM QRAYAALGLP YMNQPQTQLQ 500
    PQVPGQQPAQ PPAHQQMRTL NALGNNPMSI PAGGITTDQQ PPNLISESAL 550
    PTSLGATNPL MNDGSNSDSI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR 600
    SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY 650
    HLLAEKIYKI QKELEEKRRS RLHKQGILGN QPALPAPGAQ PPVIPPTQSV 700
    RPPNGPLSLP VNRVQVSQGM NSFNPMSLGN VQLPQAPMGP RAASPMNHSV 750
    QMNSMASVPG MAISPSRMPQ PPNMMGTHAN NIMAQAPTQN QFLPQNQFPS 800
    SSGAMSVNSV GMGQPATQAG VSQGQVPGGT LPNPLNMLAP QTSQLPCPPV 850
    TQSPLHPTPP PASTAAGMPS LQHPTPPGMT PPQPAAPTQP STPVSSGQTP 900
    TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP 950
    TPVHTQPPGT PLSQAAASID NRVPTPSSVT SAETSSQQPG PDVPMLEMKT 1000
    EVQTDDAEPD PAESKGEPRS EMMEEDLQGS SQVKEETDTT EQKSEPMEVE 1050
    EKKPEVKVEA KEEEENSANG TASQSTSPSQ PRKKIFKPEE LRQALMPTLE 1100
    ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK RKLDTGQYQE 1150
    PWQYVDDVWL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC 1200
    CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCEK CFTEIQGENV 1250
    TLGDDPSQPQ TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD 1300
    IIWPSGFVCD NCLKKTGRPR KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ 1350
    NHPEAGEVFV RVVASSDKTV EVKPGMKSRF VDSGEMSESF PYRTKALFAF 1400
    EEIDGVDVCF FGMHVQEYGS DCPPPNTRRV YISYLDSIHF FRPRCLRTAV 1450
    YHEILIGYLE YVKKLGYVTG HIWACPPSEG DDYIFHCHPP DQKIPKPKRL 1500
    QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL 1550
    EESIKELEQE EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS 1600
    ISRANKKKPS MPNVSNDLSQ KLYATMEKHK EVFFVIHLHA GPVISTQPPI 1650
    VDPDPLLSCD LMDGRDAFLT LARDKHWEFS SLRRSKWSTL CMLVELHTQG 1700
    QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT HKMVKWGLGL 1750
    DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK 1800
    RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHK 1850
    LRQQQIQHRL QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST 1900
    PQTPQPPAQP QPSPVNMSPA GFPSVARTQP PTIVSAGKPT NQVPAPPPPA 1950
    QPPPAAVEAA RQIEREGQQQ QHLYRANINN GMPPGRAGMG TPGSQMAPVG 2000
    LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV MSMQAQAAVA 2050
    GPRMPNVQPP RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA 2100
    FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV 2150
    PRPGVPPPQQ AMGGLNPQGQ ALNIMNPGHN PNMANMNPQY REMVRRQLLQ 2200
    HQQQQQQQQQ QQQQQQQSSA SLAGGMAGHS QFQQPQGPGG YAPAMQQQRM 2250
    QQHLPIQGSS MGQMAAPMGQ LGQMGQPGLG ADSTPNIQQA LQQRILQQQQ 2300
    MKQQIGSPGQ PNPMSPQQHM LSGQPQASHL PGQQIATSLS NQVRSPAPVQ 2350
    SPRPQSQPPH SSPSPRIQPQ PSPHHVSPQT GSPHPGLAVT MASSMDQGHL 2400
    GNPEQSAMLP QLNTPNRSAL SSELSLVGDT TGDTLEKFVE GL 2442
    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.

    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.
    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 1, 2014
    This is version 88 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