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Entry version 163 (07 Oct 2020)
Sequence version 6 (03 Oct 2012)
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Protein

Protein cbp-1

Gene

cbp-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1284Acetyl-CoA; via carbonyl oxygenBy similarity1
Binding sitei1289Acetyl-CoABy similarity1
Binding sitei1293Acetyl-CoABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri399 – 505TAZ-type 1PROSITE-ProRule annotationAdd BLAST107
Zinc fingeri1493 – 1534ZZ-typePROSITE-ProRule annotationAdd BLAST42
Zinc fingeri1550 – 1631TAZ-type 2PROSITE-ProRule annotationAdd BLAST82

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-1234158, Regulation of gene expression by Hypoxia-inducible Factor
R-CEL-201722, Formation of the beta-catenin:TCF transactivating complex
R-CEL-3214847, HATs acetylate histones
R-CEL-3371568, Attenuation phase
R-CEL-3899300, SUMOylation of transcription cofactors
R-CEL-5689901, Metalloprotease DUBs
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
R-CEL-8939243, RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-CEL-8939246, RUNX1 regulates transcription of genes involved in differentiation of myeloid cells
R-CEL-8951936, RUNX3 regulates p14-ARF
R-CEL-9617629, Regulation of FOXO transcriptional activity by acetylation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
P34545

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Protein cbp-1 (EC:2.3.1.48By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cbp-1
ORF Names:R10E11.1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCaenorhabditis elegans
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri6239 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001940 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome III

Organism-specific databases

WormBase

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

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi234R → A: Loss of methylation by prmt-5. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002111891 – 2017Protein cbp-1Add BLAST2017

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei234Symmetric dimethylarginine; by PRMT5; in vitro1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...
EPDi
P34545

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P34545

PeptideAtlas

More...
PeptideAtlasi
P34545

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P34545

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00000366, Expressed in multi-cellular organism and 5 other tissues

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
41575, 8 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1131, Prmt-5-cep-1-cbp-1 complex

STRING: functional protein association networks

More...
STRINGi
6239.R10E11.1b

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P34545

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini593 – 672KIXPROSITE-ProRule annotationAdd BLAST80
Domaini881 – 953BromoPROSITE-ProRule annotationAdd BLAST73
Domaini1112 – 1492CBP/p300-type HATPROSITE-ProRule annotationAdd BLAST381

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1778, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000166210

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P34545

KEGG Orthology (KO)

More...
KOi
K04498

Identification of Orthologs from Complete Genome Data

More...
OMAi
MCTIARE

Database of Orthologous Groups

More...
OrthoDBi
619848at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd15802, RING_CBP-p300, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.246.20, 1 hit
1.20.1020.10, 2 hits
1.20.920.10, 1 hit
2.10.110.40, 1 hit
3.30.40.10, 1 hit
3.30.60.90, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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
IPR043145, Znf_ZZ_sf

Pfam protein domain database

More...
Pfami
View 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

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00503, BROMODOMAIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00297, BROMO, 1 hit
SM01250, KAT11, 1 hit
SM00551, ZnF_TAZ, 2 hits
SM00291, ZnF_ZZ, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47040, SSF47040, 1 hit
SSF47370, SSF47370, 1 hit
SSF57933, SSF57933, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform b (identifier: P34545-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

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.

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Length:1,977
Mass (Da):217,943
Checksum:i6483CE231C65A663
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
Z29095 Genomic DNA Translation: CAA82353.3
Z29095 Genomic DNA Translation: CAD18875.2
Z29095 Genomic DNA Translation: CAP72377.2

Protein sequence database of the Protein Information Resource

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PIRi
G88564
S60123

NCBI Reference Sequences

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RefSeqi
NP_001122711.2, NM_001129239.2 [P34545-3]
NP_499160.2, NM_066759.3 [P34545-1]
NP_499161.2, NM_066760.5 [P34545-2]

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
R10E11.1a.1; R10E11.1a.1; WBGene00000366 [P34545-2]
R10E11.1b.1; R10E11.1b.1; WBGene00000366 [P34545-1]
R10E11.1c.1; R10E11.1c.1; WBGene00000366 [P34545-3]
R10E11.1c.2; R10E11.1c.2; WBGene00000366 [P34545-3]

Database of genes from NCBI RefSeq genomes

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GeneIDi
176380

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cel:CELE_R10E11.1

UCSC genome browser

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UCSCi
R10E11.1c, c. elegans [P34545-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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]

3D structure databases

SMRiP34545
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi41575, 8 interactors
ComplexPortaliCPX-1131, Prmt-5-cep-1-cbp-1 complex
STRINGi6239.R10E11.1b

PTM databases

iPTMnetiP34545

Proteomic databases

EPDiP34545
PaxDbiP34545
PeptideAtlasiP34545

Genome annotation databases

EnsemblMetazoaiR10E11.1a.1; R10E11.1a.1; WBGene00000366 [P34545-2]
R10E11.1b.1; R10E11.1b.1; WBGene00000366 [P34545-1]
R10E11.1c.1; R10E11.1c.1; WBGene00000366 [P34545-3]
R10E11.1c.2; R10E11.1c.2; WBGene00000366 [P34545-3]
GeneIDi176380
KEGGicel:CELE_R10E11.1
UCSCiR10E11.1c, c. elegans [P34545-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
176380
WormBaseiR10E11.1a ; CE47039 ; WBGene00000366 ; cbp-1
R10E11.1b ; CE46860 ; WBGene00000366 ; cbp-1
R10E11.1c ; CE46909 ; WBGene00000366 ; cbp-1

Phylogenomic databases

eggNOGiKOG1778, Eukaryota
GeneTreeiENSGT00940000166210
InParanoidiP34545
KOiK04498
OMAiMCTIARE
OrthoDBi619848at2759

Enzyme and pathway databases

ReactomeiR-CEL-1234158, Regulation of gene expression by Hypoxia-inducible Factor
R-CEL-201722, Formation of the beta-catenin:TCF transactivating complex
R-CEL-3214847, HATs acetylate histones
R-CEL-3371568, Attenuation phase
R-CEL-3899300, SUMOylation of transcription cofactors
R-CEL-5689901, Metalloprotease DUBs
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
R-CEL-8939243, RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-CEL-8939246, RUNX1 regulates transcription of genes involved in differentiation of myeloid cells
R-CEL-8951936, RUNX3 regulates p14-ARF
R-CEL-9617629, Regulation of FOXO transcriptional activity by acetylation
SignaLinkiP34545

Miscellaneous databases

Protein Ontology

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PROi
PR:P34545

Gene expression databases

BgeeiWBGene00000366, Expressed in multi-cellular organism and 5 other tissues

Family and domain databases

CDDicd15802, RING_CBP-p300, 1 hit
Gene3Di1.10.246.20, 1 hit
1.20.1020.10, 2 hits
1.20.920.10, 1 hit
2.10.110.40, 1 hit
3.30.40.10, 1 hit
3.30.60.90, 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
IPR043145, Znf_ZZ_sf
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCBP1_CAEEL
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P34545
Secondary accession number(s): B0M0M3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 3, 2012
Last modified: October 7, 2020
This is version 163 of the entry and version 6 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
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