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UniProtKB - P45481 (CBP_MOUSE)

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Protein

CREB-binding protein

Gene

Crebbp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers. Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER).By similarity4 Publications

Catalytic activityi

Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi362Zinc 11
Metal bindingi366Zinc 11
Metal bindingi379Zinc 11
Metal bindingi384Zinc 11
Metal bindingi393Zinc 21
Metal bindingi397Zinc 21
Metal bindingi403Zinc 21
Metal bindingi408Zinc 21
Metal bindingi417Zinc 31
Metal bindingi421Zinc 31
Metal bindingi426Zinc 31
Metal bindingi429Zinc 31
Binding sitei1494Acetyl-CoA; via carbonyl oxygenBy similarity1
Binding sitei1499Acetyl-CoABy similarity1
Binding sitei1503Acetyl-CoABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri346 – 432TAZ-type 1PROSITE-ProRule annotationAdd BLAST87
Zinc fingeri1702 – 1745ZZ-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri1766 – 1847TAZ-type 2PROSITE-ProRule annotationAdd BLAST82

GO - Molecular functioni

  • acetyltransferase activity Source: MGI
  • cAMP response element binding protein binding Source: CAFA
  • chromatin binding Source: MGI
  • core promoter proximal region sequence-specific DNA binding Source: MGI
  • damaged DNA binding Source: UniProtKB
  • disordered domain specific binding Source: CAFA
  • DNA binding Source: MGI
  • histone acetyltransferase activity Source: MGI
  • MRF binding Source: UniProtKB
  • p53 binding Source: MGI
  • protein domain specific binding Source: CAFA
  • protein heterodimerization activity Source: CAFA
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
  • RNA polymerase II transcription coactivator activity Source: MGI
  • RNA polymerase II transcription factor binding Source: MGI
  • TFIIB-class transcription factor binding Source: MGI
  • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: MGI
  • transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: MGI
  • transcriptional repressor activity, RNA polymerase II transcription factor binding Source: MGI
  • transcription coactivator activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • zinc ion binding Source: CAFA
Complete GO annotation...

GO - Biological processi

  • cellular response to hepatocyte growth factor stimulus Source: MGI
  • cellular response to UV Source: UniProtKB
  • cellular response to virus Source: CAFA
  • germ-line stem cell population maintenance Source: MGI
  • histone acetylation Source: UniProtKB
  • negative regulation of interferon-beta biosynthetic process Source: CAFA
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • negative regulation of viral process Source: CAFA
  • N-terminal peptidyl-lysine acetylation Source: UniProtKB
  • positive regulation of CREB transcription factor activity Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein acetylation Source: MGI
  • protein destabilization Source: UniProtKB
  • regulation of transcription, DNA-templated Source: MGI
  • rhythmic process Source: UniProtKB-KW
Complete GO annotation...

Keywordsi

Molecular functionActivator, Acyltransferase, Transferase
Biological processBiological rhythms, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1912408. Pre-NOTCH Transcription and Translation.
R-MMU-3214847. HATs acetylate histones.
R-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
CREB-binding protein (EC:2.3.1.48By similarity)
Gene namesi
Name:Crebbp
Synonyms:Cbp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1098280. Crebbp.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus

    • 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

  • condensed chromosome outer kinetochore Source: MGI
  • cytoplasm Source: MGI
  • histone acetyltransferase complex Source: MGI
  • nuclear body Source: MGI
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • PML body Source: MGI
  • protein complex Source: CAFA
  • RNA polymerase II transcription factor complex Source: MGI
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi600R → N: Abolishes binding to CREB. 1 Publication1
Mutagenesisi999K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcriptional activity; when associated with R-1034 and R-1057. 1 Publication1
Mutagenesisi1015K → R: No change in sumoylation. 1 Publication1
Mutagenesisi1034K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcriptional activity; when associated with R-999 and R-1057. 1 Publication1
Mutagenesisi1043K → R: No change in sumoylation. 1 Publication1
Mutagenesisi1053K → R: No change in sumoylation. 1 Publication1
Mutagenesisi1057K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcriptional activity; when associated with R-999 and R-1034. 1 Publication1
Mutagenesisi1061K → R: No change in sumoylation. 1 Publication1
Mutagenesisi1087K → R: No change in sumoylation. 1
Mutagenesisi1690 – 1691LC → KL: Abolishes histone acetyltransferase activity. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002111912 – 2441CREB-binding proteinAdd BLAST2440

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei120PhosphoserineCombined sources1
Modified residuei219Omega-N-methylarginineBy similarity1
Modified residuei600Omega-N-methylated arginine1 Publication1
Modified residuei624Omega-N-methylated arginine1 Publication1
Modified residuei656N6-acetyllysineCombined sources1
Cross-linki999Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Modified residuei1015N6-acetyllysineBy similarity1
Modified residuei1031PhosphoserineBy similarity1
Cross-linki1034Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Cross-linki1057Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Modified residuei1077PhosphoserineBy similarity1
Modified residuei1217N6-acetyllysineCombined sources1
Modified residuei1383Phosphoserine; by IKKABy similarity1
Modified residuei1387Phosphoserine; by IKKABy similarity1
Modified residuei1584N6-acetyllysineBy similarity1
Modified residuei1592N6-acetyllysineBy similarity1
Modified residuei1593N6-acetyllysineBy similarity1
Modified residuei1596N6-acetyllysineCombined sources1
Modified residuei1598N6-acetyllysineCombined sources1
Modified residuei1742N6-acetyllysineBy similarity1
Modified residuei1745N6-acetyllysineCombined sources1
Modified residuei1764PhosphoserineBy similarity1
Modified residuei2064PhosphoserineCombined sources1
Modified residuei2077PhosphoserineBy similarity1
Modified residuei2080PhosphoserineBy similarity1
Modified residuei2350PhosphoserineCombined sources1

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.1 Publication
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.1 Publication
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

EPDiP45481.
MaxQBiP45481.
PaxDbiP45481.
PRIDEiP45481.

PTM databases

iPTMnetiP45481.
PhosphoSitePlusiP45481.

Expressioni

Gene expression databases

CleanExiMM_CREBBP.

Interactioni

Subunit structurei

Interacts (via transactivation domain and C-terminus) with PCNA; the interaction occurs on chromatin in UV-irradiated damaged cells (By similarity). Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex with HIF1A and EP300. The TAZ-type 1 domain interacts with HIF1A. Interacts with SRCAP, ELF3, MLLT7/FOXO4, N4BP2, NCOA6, PCAF, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB and TRERF1. Interacts with KLF1; the interaction results in acetylation and enhancement of transcriptional activity of KLF1. 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). Interacts with FOXO1; the interaction acetylates FOXO1 and inhibits its transcriptional activity. Interacts with MECOM and MTDH. Interacts with ASF1A and ASF1B; this promotes histone acetylation. Interacts with acetylated TP53/p53 and with the acetylated histones H3 and H4 (By similarity). Interacts with CITED1 (via C-terminus). Interacts with GATA1; the interaction results in acetylation and enhancement of transcriptional activity of GATA1. Interacts with MAF, CARM1. NCOA3, ZCCHC12, DDX17, DDX5 AND CITED4 (C-terminal region). Interacts with phosphorylated CREB1. 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 NPAS2, CLOCK and ARNTL/BMAL1.By similarity14 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cAMP response element binding protein binding Source: CAFA
  • disordered domain specific binding Source: CAFA
  • MRF binding Source: UniProtKB
  • p53 binding Source: MGI
  • protein domain specific binding Source: CAFA
  • protein heterodimerization activity Source: CAFA
  • RNA polymerase II transcription factor binding Source: MGI
  • TFIIB-class transcription factor binding Source: MGI
  • transcription factor binding Source: UniProtKB
Complete GO annotation...

Protein-protein interaction databases

DIPiDIP-5974N.
IntActiP45481. 26 interactors.
MINTiMINT-203452.
STRINGi10090.ENSMUSP00000023165.

Structurei

Secondary structure

12441
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni343 – 345Combined sources3
Helixi347 – 372Combined sources26
Beta strandi374 – 376Combined sources3
Helixi384 – 396Combined sources13
Helixi400 – 402Combined sources3
Helixi406 – 420Combined sources15
Turni423 – 425Combined sources3
Helixi429 – 433Combined sources5
Helixi436 – 438Combined sources3
Helixi590 – 594Combined sources5
Helixi597 – 611Combined sources15
Turni617 – 619Combined sources3
Helixi622 – 642Combined sources21
Helixi646 – 664Combined sources19
Turni667 – 671Combined sources5
Turni1709 – 1711Combined sources3
Beta strandi1713 – 1726Combined sources14
Helixi1731 – 1737Combined sources7
Beta strandi1741 – 1746Combined sources6
Helixi1765 – 1785Combined sources21
Helixi1794 – 1808Combined sources15
Helixi1812 – 1815Combined sources4
Helixi1818 – 1833Combined sources16
Beta strandi1840 – 1843Combined sources4
Helixi1844 – 1849Combined sources6
Helixi1877 – 1880Combined sources4
Turni1881 – 1883Combined sources3
Helixi1919 – 1928Combined sources10
Helixi1942 – 1944Combined sources3
Helixi1970 – 1972Combined sources3
Helixi1977 – 1983Combined sources7
Beta strandi2061 – 2064Combined sources4
Helixi2068 – 2075Combined sources8
Beta strandi2076 – 2079Combined sources4
Helixi2088 – 2091Combined sources4
Helixi2097 – 2100Combined sources4
Helixi2102 – 2104Combined sources3
Beta strandi2106 – 2108Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F81NMR-A1764-1850[»]
1JJSNMR-A2067-2112[»]
1KBHNMR-B2059-2117[»]
1KDXNMR-A586-666[»]
1L8CNMR-A345-439[»]
1R8UNMR-B340-439[»]
1SB0NMR-A586-672[»]
1TOTNMR-A1700-1751[»]
1U2NNMR-A340-439[»]
2AGHNMR-B586-672[»]
2C52NMR-A2059-2117[»]
2KA4NMR-A340-439[»]
2KA6NMR-A1764-1855[»]
2KKJNMR-A2059-2117[»]
2L14NMR-A2059-2117[»]
2LQHNMR-A586-672[»]
2LQINMR-A586-672[»]
2LWWNMR-A340-439[»]
4I9OX-ray2.00A586-672[»]
5HOUNMR-A340-439[»]
5HP0NMR-A1764-1857[»]
5HPDNMR-A1764-1855[»]
5U4KNMR-A586-672[»]
DisProtiDP00348.
ProteinModelPortaliP45481.
SMRiP45481.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45481.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini586 – 665KIXPROSITE-ProRule annotationAdd BLAST80
Domaini1104 – 1176BromoPROSITE-ProRule annotationAdd BLAST73
Domaini1324 – 1701CBP/p300-type HATPROSITE-ProRule annotationAdd BLAST378

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni226 – 409Interaction with SRCAPBy similarityAdd BLAST184
Regioni1125 – 1171Interaction with histoneBy similarityAdd BLAST47
Regioni1163 – 1181Interaction with ASF1ABy similarityAdd BLAST19
Regioni1434 – 1436Interaction with histoneBy similarity3
Regioni1435 – 1437Acetyl-CoA bindingBy similarity3
Regioni1447 – 1448Acetyl-CoA bindingBy similarity2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1062 – 1065Poly-Glu4
Compositional biasi1556 – 1563Poly-Glu8
Compositional biasi1944 – 1949Poly-Pro6
Compositional biasi1968 – 1971Poly-Gln4
Compositional biasi2082 – 2086Poly-Gln5
Compositional biasi2200 – 2216Poly-GlnAdd BLAST17
Compositional biasi2296 – 2299Poly-Gln4

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri346 – 432TAZ-type 1PROSITE-ProRule annotationAdd BLAST87
Zinc fingeri1702 – 1745ZZ-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri1766 – 1847TAZ-type 2PROSITE-ProRule annotationAdd BLAST82

Keywords - Domaini

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1778. Eukaryota.
COG5076. LUCA.
HOGENOMiHOG000111353.
HOVERGENiHBG000185.
InParanoidiP45481.

Family and domain databases

CDDicd15802. RING_CBP-p300. 1 hit.
Gene3Di1.10.1630.10. 1 hit.
1.20.1020.10. 3 hits.
1.20.920.10. 1 hit.
InterProiView protein in InterPro
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR031162. CBP_P300_HAT.
IPR013178. Histone_AcTrfase_Rtt109/CBP.
IPR003101. KIX_dom.
IPR009110. Nuc_rcpt_coact.
IPR014744. Nuc_rcpt_coact_CREBbp.
IPR010303. RING_CBP-p300.
IPR000197. Znf_TAZ.
IPR000433. Znf_ZZ.
PfamiView protein in Pfam
PF00439. Bromodomain. 1 hit.
PF09030. Creb_binding. 1 hit.
PF06001. DUF902. 1 hit.
PF08214. HAT_KAT11. 1 hit.
PF02172. KIX. 1 hit.
PF02135. zf-TAZ. 2 hits.
PF00569. ZZ. 1 hit.
PRINTSiPR00503. BROMODOMAIN.
SMARTiView protein in SMART
SM00297. BROMO. 1 hit.
SM01250. KAT11. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
SUPFAMiSSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEiView protein in PROSITE
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.

Sequencei

Sequence statusi: Complete.

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

P45481-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAENLLDGPP NPKRAKLSSP GFSANDNTDF GSLFDLENDL PDELIPNGEL 
        60         70         80         90        100
SLLNSGNLVP DAASKHKQLS ELLRGGSGSS INPGIGNVSA SSPVQQGLGG 
       110        120        130        140        150
QAQGQPNSTN MASLGAMGKS PLNQGDSSTP NLPKQAASTS 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 TTSPFGQPFS QTGGQQMGAT GVNPQLASKQ 
       310        320        330        340        350
SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPTQAIA 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 MNDGSNSGNI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR 
       610        620        630        640        650
SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY 
       660        670        680        690        700
HLLAEKIYKI QKELEEKRRS RLHKQGILGN QPALPASGAQ PPVIPPAQSV 
       710        720        730        740        750
RPPNGPLPLP VNRMQVSQGM NSFNPMSLGN VQLPQAPMGP RAASPMNHSV 
       760        770        780        790        800
QMNSMASVPG MAISPSRMPQ PPNMMGTHAN NIMAQAPTQN QFLPQNQFPS 
       810        820        830        840        850
SSGAMSVNSV GMGQPAAQAG VSQGQVPGAA LPNPLNMLAP QASQLPCPPV 
       860        870        880        890        900
TQSPLHPTPP PASTAAGMPS LQHPTAPGMT 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
EVQTDDAEPE PTESKGEPRS EMMEEDLQGS SQVKEETDTT EQKSEPMEVE 
      1060       1070       1080       1090       1100
EKKPEVKVEA KEEEENSSND 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 FGMHVQNTAL IAPHQIQGRV 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 GFPNVARTQP PTIVSAGKPT NQVPAPPPPA 
      1960       1970       1980       1990       2000
QPPPAAVEAA RQIEREAQQQ QHLYRANINN GMPPGRAGMG TPGSQMTPVG 
      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
PRPGVPPPQP AMGGLNPQGQ ALNIMNPGHN PNMTNMNPQY REMVRRQLLQ 
      2210       2220       2230       2240       2250
HQQQQQQQQQ QQQQQQNSAS LAGGMAGHSQ FQQPQGPGGY APAMQQQRMQ 
      2260       2270       2280       2290       2300
QHLPIQGSSM GQMAAPMGQL GQMGQPGLGA DSTPNIQQAL QQRILQQQQM 
      2310       2320       2330       2340       2350
KQQIGSPGQP NPMSPQQHML SGQPQASHLP GQQIATSLSN QVRSPAPVQS 
      2360       2370       2380       2390       2400
PRPQSQPPHS SPSPRIQPQP SPHHVSPQTG SPHPGLAVTM ASSMDQGHLG 
      2410       2420       2430       2440 
NPEQSAMLPQ LNTPNRSALS SELSLVGDTT GDTLEKFVEG L
Length:2,441
Mass (Da):265,494
Last modified:July 27, 2011 - v3
Checksum:iD89AF52B7BD33347
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti400G → P in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti530I → V in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti670S → T in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti826V → E in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti978S → T in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1159W → R in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1239E → G in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1417N → D in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1429R → C in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1466G → V in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1470G → A in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1850 – 1851KL → NV in AAB28651 (PubMed:8413673).Curated2
Sequence conflicti1859R → C in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti1987A → D in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti2060P → N in AAB28651 (PubMed:8413673).Curated1
Sequence conflicti2381S → T in AAB28651 (PubMed:8413673).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S66385 mRNA. Translation: AAB28651.1.
AC132380 Genomic DNA. No translation available.
CCDSiCCDS27915.1.
PIRiS39161.
UniGeneiMm.132238.
Mm.392384.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiCBP_MOUSE
AccessioniPrimary (citable) accession number: P45481
Secondary accession number(s): E9QPH4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 27, 2011
Last modified: June 7, 2017
This is version 189 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references