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Protein

Protein cbp-1

Gene

cbp-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Acetyltransferase enzyme. Acetylates histones, giving a specific tag for transcriptional activation (By similarity). May prevent DNA damage-induced apoptosis by inhibiting cep-1-dependent transcription activation of the programmed cell death activator egl-1 (PubMed:19521535).1 PublicationBy similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei1284Acetyl-CoA; via carbonyl oxygenBy similarity1
Binding sitei1289Acetyl-CoABy similarity1
Binding sitei1293Acetyl-CoABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri399 – 505TAZ-type 1PROSITE-ProRule annotationAdd BLAST107
Zinc fingeri1493 – 1534ZZ-typePROSITE-ProRule annotationAdd BLAST42
Zinc fingeri1550 – 1631TAZ-type 2PROSITE-ProRule annotationAdd BLAST82

GO - Molecular functioni

  • histone acetyltransferase activity Source: WormBase
  • lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: WormBase
  • peptide-lysine-N-acetyltransferase activity Source: WormBase
  • RNA polymerase II sequence-specific DNA binding transcription factor binding Source: WormBase
  • transcription cofactor activity Source: WormBase
  • transcription factor binding Source: WormBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • embryo development ending in birth or egg hatching Source: WormBase
  • histone acetylation Source: WormBase
  • internal peptidyl-lysine acetylation Source: WormBase
  • positive regulation of apoptotic process Source: WormBase
  • positive regulation of transcription by RNA polymerase II Source: WormBase
  • regulation of neuron projection development Source: WormBase
  • regulation of transcription, DNA-templated Source: WormBase
  • spermatogenesis Source: WormBase
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionActivator, Acyltransferase, Chromatin regulator, Transferase
Biological processApoptosis, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-CEL-1234158 Regulation of gene expression by Hypoxia-inducible Factor
R-CEL-3214847 HATs acetylate histones
R-CEL-6781823 Formation of TC-NER Pre-Incision Complex
R-CEL-6782135 Dual incision in TC-NER
R-CEL-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-CEL-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
SignaLinkiP34545

Names & Taxonomyi

Protein namesi
Recommended name:
Protein cbp-1 (EC:2.3.1.48By similarity)
Gene namesi
Name:cbp-1
ORF Names:R10E11.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiR10E11.1a ; CE47039 ; WBGene00000366 ; cbp-1
R10E11.1b ; CE46860 ; WBGene00000366 ; cbp-1
R10E11.1c ; CE46909 ; WBGene00000366 ; cbp-1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi234R → A: Loss of methylation by prmt-5. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002111891 – 2017Protein cbp-1Add BLAST2017

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei234Symmetric dimethylarginine; by PRMT5; in vitro1 Publication1

Post-translational modificationi

Methylation by prmt-5 may repress the capacity of cbp-1 to enhance cep-1-dependent transcription of egl-1.1 Publication

Keywords - PTMi

Methylation

Proteomic databases

EPDiP34545
PaxDbiP34545
PeptideAtlasiP34545

PTM databases

iPTMnetiP34545

Expressioni

Gene expression databases

BgeeiWBGene00000366

Interactioni

Subunit structurei

Interacts (via N-terminus domain and HAT domain) with prmt-5; the interaction results in methylation of cbp-1 (PubMed:19521535). Interacts (via HAT domain) with cep-1; cep-1 transcriptional activity may be inhibited by interaction with methylated cbp-1 (PubMed:19521535). Component of a complex that contains prmt-5 and cbp-1 (PubMed:19521535).1 Publication1 Publication

GO - Molecular functioni

  • RNA polymerase II sequence-specific DNA binding transcription factor binding Source: WormBase
  • transcription factor binding Source: WormBase

Protein-protein interaction databases

BioGridi41575, 5 interactors
STRINGi6239.R10E11.1b

Structurei

3D structure databases

ProteinModelPortaliP34545
SMRiP34545
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini593 – 672KIXPROSITE-ProRule annotationAdd BLAST80
Domaini881 – 953BromoPROSITE-ProRule annotationAdd BLAST73
Domaini1112 – 1492CBP/p300-type HATPROSITE-ProRule annotationAdd BLAST381

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni902 – 948Interaction with histoneBy similarityAdd BLAST47
Regioni1224 – 1226Interaction with histoneBy similarity3
Regioni1225 – 1227Acetyl-CoA bindingBy similarity3
Regioni1237 – 1238Acetyl-CoA bindingBy similarity2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1687 – 2008Gln/Gly-richAdd BLAST322

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri399 – 505TAZ-type 1PROSITE-ProRule annotationAdd BLAST107
Zinc fingeri1493 – 1534ZZ-typePROSITE-ProRule annotationAdd BLAST42
Zinc fingeri1550 – 1631TAZ-type 2PROSITE-ProRule annotationAdd BLAST82

Keywords - Domaini

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1778 Eukaryota
COG5076 LUCA
GeneTreeiENSGT00760000119206
HOGENOMiHOG000019113
InParanoidiP34545
KOiK04498
OMAiMCTIARE
OrthoDBiEOG091G0L04

Family and domain databases

CDDicd15802 RING_CBP-p300, 1 hit
Gene3Di1.20.1020.10, 2 hits
1.20.920.10, 1 hit
2.10.110.40, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR018359 Bromodomain_CS
IPR031162 CBP_P300_HAT
IPR013178 Histone_AcTrfase_Rtt109/CBP
IPR003101 KIX_dom
IPR036529 KIX_dom_sf
IPR010303 RING_CBP-p300
IPR038547 RING_CBP-p300_sf
IPR035898 TAZ_dom_sf
IPR013083 Znf_RING/FYVE/PHD
IPR000197 Znf_TAZ
IPR000433 Znf_ZZ
PfamiView protein in Pfam
PF00439 Bromodomain, 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
PROSITEiView protein in PROSITE
PS00633 BROMODOMAIN_1, 1 hit
PS50014 BROMODOMAIN_2, 1 hit
PS51727 CBP_P300_HAT, 1 hit
PS50952 KIX, 1 hit
PS01359 ZF_PHD_1, 1 hit
PS50134 ZF_TAZ, 2 hits
PS01357 ZF_ZZ_1, 1 hit
PS50135 ZF_ZZ_2, 1 hit

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform b (identifier: P34545-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDEPPSKKSR ADSDYDSGLD ALSALESLEA FPTSSKDTDV DNNPSTSAGG
60 70 80 90 100
SGGPSGSTPH PQGTPQPAPS NNGGFNLQPG QSQPQQPPQN MGGGVNGSVL
110 120 130 140 150
QELLMNPSQT SNNSPRPQAY PPGQQNAFNR SPMMPNGTPN MMSPPSMGRV
160 170 180 190 200
PGPSPGGPQP PGPGQPQMRP GQPGMFQGDQ QQQMMMGAQG QQFPGMMHRY
210 220 230 240 250
PYAQGGPPPG AQGMPQGYPG VSRGGPTPGQ PMGRGAMMNG AMPRSGPMPT
260 270 280 290 300
QGRPGIPPNQ QAMMQPMMTD RQFMQHGQYG QQRPEFMQQY GRPGGYPMMH
310 320 330 340 350
QGMMMDSNGQ PIRGPNQMMM MSNGHPGMSH GPPNGQPGPQ AAAAQHAAQQ
360 370 380 390 400
QAAAQAQAQA AAQQQQQQQR EQEAAAAAQR NGAGRATTPG SSMLATHQDP
410 420 430 440 450
EKRKLIQQQL VLLLHAHKCS QREKENRDFA AKNQPPPHAA CTLPHCSTMK
460 470 480 490 500
EVLTHMTSCN VGRLCHSDTT QTTKKCSVAH CASSRQIIAH WKNCSREDCP
510 520 530 540 550
VCKPLKRIQD TPLQFSLPDL ANLIGVNGNS NGSAEGDGLH QFGSPAMRTG
560 570 580 590 600
NITNSLFEGF NGNPFQNGPN RGGPRPPGGN GEIPNLPPPD MPDCTKEWHH
610 620 630 640 650
QVTKDLRNHL VGKLVKAIFP EPNQEAMNDN RLKDLIAYAR KVEKEMFESA
660 670 680 690 700
NDREEYYHLL AEKIYKIQKE LQEKKNSRLN QGAAAHDQYA IPPSNELAQM
710 720 730 740 750
LGVEGGRSDV HSEGSSMAVA PSQQNQPWGG APNSNMHQQI PPNGQVPQVN
760 770 780 790 800
NSSTFPSSGN STPNIGASST VSAMLQPKTE PMDDQNTDSL SSRPPTAIGF
810 820 830 840 850
GGSSSSTPAP IMNGIVKKEE DPEESSNQAP PSVKDTKDGV AESKPKEQQA
860 870 880 890 900
KREPTPPPTE DTVFSQEDLI KFLLPVWEKL DKSEDAAPFR VPVDAKLLNI
910 920 930 940 950
PDYHEIIKRP MDLETVHKKL YAGQYQNAGQ FCDDIWLMLD NAWLYNRKNS
960 970 980 990 1000
KVYKYGLKLS EMFVSEMDPV MKSMGYCCAK KLAFTPLSLF CYGAAMCTIA
1010 1020 1030 1040 1050
REQQYWVFEQ SSTQYNVTVT ERYTYCQKCF DALPPEGISL SENPNDRNNM
1060 1070 1080 1090 1100
APKTSFTEQK NSVIDYEPFE RCKYCMRKWH RICALHDKKV YPEGFICECC
1110 1120 1130 1140 1150
RTAKKYQKPD NKYLASKLPH NKLSTFLEDR VNGFIKKQLQ AEAHKYPVII
1160 1170 1180 1190 1200
RTLCVQDKEA EVKAQMKQKY VESNQFPEKF PYRTKAVFAF EIIDGVEVCF
1210 1220 1230 1240 1250
FGLHVQEYGS ACPAPNARRV YIAYLDSVHF FQPRELRTDV YHELLLGYLD
1260 1270 1280 1290 1300
YAKMLGYTMA HIWACPPSEG DDYIFHCHPP EQKIPKPKRL QDWYKKMLEK
1310 1320 1330 1340 1350
GVQEGSVVEF KDIYKQARDD NLTTPTQLPY FEGDFWPNVI EDCIREASNE
1360 1370 1380 1390 1400
EAQRKVKEDD DDGEDADGGL GGGDSGKKKS SKNKKNNLKK NAKMNKKKAG
1410 1420 1430 1440 1450
SITGNEVADK LYSQFEKHKE VFFTIRLVSL QNEPAVLAKP ISDPDGLMQS
1460 1470 1480 1490 1500
DMMDGRDTFL TKAREEHWEF SSLRRAKYST LCLAYSLHET DSKGMEYTCN
1510 1520 1530 1540 1550
KCSSPAVWHC QSCDDFDLCD GCKPTTQHPH EMEKIKSLIG GGEAGDSAAG
1560 1570 1580 1590 1600
GTRYESIQRC IASLVHACQC RDANCRRMSC HKMKRVVQHT KMCKKRINGT
1610 1620 1630 1640 1650
CPVCKQLIAL CCYHAKHCTR DACTVPFCMN IRQKLAEQKR SQQRRADMMM
1660 1670 1680 1690 1700
RRRMEGLQSH VGGAAPTPST VSNGTPSNAP TPPVSAGPGP AVKGGGVGQV
1710 1720 1730 1740 1750
QMQQHQGSHV GGSGPAGMGQ PMNSFGGMPG MGLGPNAQNG PGLPGMNPQM
1760 1770 1780 1790 1800
NANQSRYMPN GPGLGQSGAP GQQQQPMYSS GMPMQRPGGL GGMNPQQQPQ
1810 1820 1830 1840 1850
QQQGHPGLQN PGGRPGGVHG MGQNQPVRNN QDMVMNMQMQ NQHQQPPPFD
1860 1870 1880 1890 1900
STLQPQIMKI NSRLKAAKTE EERETVFSDL KKTPHLFHAW LRMRENQNLV
1910 1920 1930 1940 1950
PNRMQGYSQM SMGSSNLQNL QQQQLQQQQA GAMRGGGGFA PGQNNSQPRA
1960 1970 1980 1990 2000
PSGQFASMNP SMQQQYPQQQ QGWPQQRQQN PGGMQQNANP YNQFQNRQNM
2010
MMMPQQQQPH PSNAGGQ
Length:2,017
Mass (Da):222,415
Last modified:October 3, 2012 - v6
Checksum:iAAA0D2A7962DF163
GO
Isoform a (identifier: P34545-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     467-478: SDTTQTTKKCSV → F

Note: No experimental confirmation available.
Show »
Length:2,006
Mass (Da):221,281
Checksum:i86C92757AE478BFE
GO
Isoform c (identifier: P34545-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     467-478: SDTTQTTKKCSV → F
     1893-1921: Missing.

Note: No experimental confirmation available.
Show »
Length:1,977
Mass (Da):217,943
Checksum:i6483CE231C65A663
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000557467 – 478SDTTQ…KKCSV → F in isoform a and isoform c. CuratedAdd BLAST12
Alternative sequenceiVSP_0441491893 – 1921Missing in isoform c. CuratedAdd BLAST29

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z29095 Genomic DNA Translation: CAA82353.3
Z29095 Genomic DNA Translation: CAD18875.2
Z29095 Genomic DNA Translation: CAP72377.2
PIRiG88564
S60123
RefSeqiNP_001122711.2, NM_001129239.2 [P34545-3]
NP_499160.2, NM_066759.3 [P34545-1]
NP_499161.2, NM_066760.5 [P34545-2]
UniGeneiCel.22950

Genome annotation databases

EnsemblMetazoaiR10E11.1b; R10E11.1b; WBGene00000366 [P34545-1]
GeneIDi176380
KEGGicel:CELE_R10E11.1
UCSCiR10E11.1c c. elegans [P34545-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiCBP1_CAEEL
AccessioniPrimary (citable) accession number: P34545
Secondary accession number(s): B0M0M3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 3, 2012
Last modified: March 28, 2018
This is version 146 of the entry and version 6 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health