Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Bromodomain-containing protein 1  

UniProtKB / Swiss-Prot ID :  BRD1_HUMAN

Gene Name (Synonyms) : 
BRD1, BRL, BRPF2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. 

Protein Sequence MRRKGRCHRGSAARHPSSPCSVKHSPTRETLTYAQAQRMVEIEIEGRLHRISIFDPLEIILEDDLTAQEM...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHCEEEEEEECCCCCCCCCCCCHHHHHHHCCCHHHC...
Protein Variant
LocationDescription
38R -> G (in dbSNP:rs11549978). VAR_048424
321A -> S (in dbSNP:rs12157714). VAR_048425
730A -> T (in dbSNP:rs35331092). VAR_048426
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
18PhosphoserineRHPSSPCSV
CCCCCCCCC
34.08HPRD
Link-
25PhosphoserineSVKHSPTRE
CCCCCCCCC
23.42HPRD
Link-
25PhosphoserineSVKHSPTRE
CCCCCCCCC
23.42PhosphoELM
Link-
25PhosphoserineSVKHSPTRE
CCCCCCCCC
23.42SysPTM
Link-
25Phosphoserine.SVKHSPTRE
CCCCCCCCC
23.42UniProtKB
Link-
127PhosphotyrosineRIVEYSPPS
ECCCCCCCC
18.64HPRD
Link-
127PhosphotyrosineRIVEYSPPS
ECCCCCCCC
18.64PhosphoELM
Link-
127PhosphotyrosineRIVEYSPPS
ECCCCCCCC
18.64Phosphositeplus
Link-
128PhosphoserineIVEYSPPSA
CCCCCCCCC
19.48HPRD
Link-
128PhosphoserineIVEYSPPSA
CCCCCCCCC
19.48PhosphoELM
Link-
128PhosphoserineIVEYSPPSA
CCCCCCCCC
19.48Phosphositeplus
Link-
128PhosphoserineIVEYSPPSA
CCCCCCCCC
19.48SysPTM
Link-
128Phosphoserine.IVEYSPPSA
CCCCCCCCC
19.48UniProtKB
Link-
131PhosphoserineYSPPSAPRR
CCCCCCCCC
55.05HPRD
Link-
368Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MEPVKELTG
EHHHHHCCC
58.69Phosphositeplus
Link-
368N6-acetyllysineMEPVKELTG
EHHHHHCCC
58.69HPRD
Link-
368N6-acetyllysineMEPVKELTG
EHHHHHCCC
58.69Phosphositeplus
Link-
368N6-acetyllysine.MEPVKELTG
EHHHHHCCC
58.69UniProtKB
Link-
418N6-acetyllysineESSVKTVRS
CCCCCCCCC
43.16HPRD
Link-
418N6-acetyllysineESSVKTVRS
CCCCCCCCC
43.16Phosphositeplus
Link-
418N6-acetyllysine.ESSVKTVRS
CCCCCCCCC
43.16UniProtKB
Link-
486PhosphoserineLKRLSRNGA
HHHHHHCCC
27.94HPRD
Link-
516N6-acetyllysineDEEMKAAKE
HHHHHHHHH
48.77HPRD
Link-
516N6-acetyllysineDEEMKAAKE
HHHHHHHHH
48.77Phosphositeplus
Link-
516N6-acetyllysine.DEEMKAAKE
HHHHHHHHH
48.77UniProtKB
Link-
519N6-acetyllysineMKAAKEKLK
HHHHHHHHH
61.31HPRD
Link-
519N6-acetyllysineMKAAKEKLK
HHHHHHHHH
61.31Phosphositeplus
Link-
519N6-acetyllysine.MKAAKEKLK
HHHHHHHHH
61.31UniProtKB
Link-
523N6-acetyllysineKEKLKYWQR
HHHHHHHCC
56.35HPRD
Link-
523N6-acetyllysineKEKLKYWQR
HHHHHHHCC
56.35Phosphositeplus
Link-
523N6-acetyllysine.KEKLKYWQR
HHHHHHHCC
56.35UniProtKB
Link-
801PhosphoserinePRKRSRSTC
CCCCCCCCC
33.35Phosphositeplus
Link-
803PhosphoserineKRSRSTCGD
CCCCCCCCC
29.33Phosphositeplus
Link-
804PhosphothreonineRSRSTCGDS
CCCCCCCCC
21.28Phosphositeplus
Link-
808PhosphoserineTCGDSEVEE
CCCCCCCCC
28.91Phosphositeplus
Link-
814PhosphoserineVEEESPGKR
CCCCCCHHH
42.08HPRD
Link-
814PhosphoserineVEEESPGKR
CCCCCCHHH
42.08Phosphositeplus
Link-
852PhosphoserineRRCASESSI
CCCCCCCCC
41.45Phosphositeplus
Link-
854PhosphoserineCASESSISS
CCCCCCCCC
30.40Phosphositeplus
Link-
855PhosphoserineASESSISSS
CCCCCCCCC
23.57Phosphositeplus
Link-
857PhosphoserineESSISSSNS
CCCCCCCCC
29.66Phosphositeplus
Link-
858PhosphoserineSSISSSNSP
CCCCCCCCC
31.69Phosphositeplus
Link-
885PhosphothreonineVRRHTLEDR
EECCCCCCC
29.99Phosphositeplus
Link-
903N6-acetyllysineGNYAKAARI
CCCCHHHHH
32.02HPRD
Link-
903N6-acetyllysineGNYAKAARI
CCCCHHHHH
32.02Phosphositeplus
Link-
903N6-acetyllysine.GNYAKAARI
CCCCHHHHH
32.02UniProtKB
Link-
921Caspase cleavage aspartic acidWISTDAAAS
CCCCCCCCC
27.67Phosphositeplus
Link-
1026PhosphoserineEGRNSSIRK
HCCCHHHHH
26.28Phosphositeplus
Link-
1027PhosphoserineGRNSSIRKA
CCCHHHHHH
29.93Phosphositeplus
Link-
1051PhosphothreonineHGEPTSDLS
CCCCCCCCC
30.48HPRD
Link-
1051PhosphothreonineHGEPTSDLS
CCCCCCCCC
30.48PhosphoELM
Link-
1051PhosphothreonineHGEPTSDLS
CCCCCCCCC
30.48Phosphositeplus
Link-
1051PhosphothreonineHGEPTSDLS
CCCCCCCCC
30.48SysPTM
Link-
1051Phosphothreonine.HGEPTSDLS
CCCCCCCCC
30.48UniProtKB
Link-
1052PhosphoserineGEPTSDLSD
CCCCCCCCC
47.47HPRD
Link-
1052PhosphoserineGEPTSDLSD
CCCCCCCCC
47.47PhosphoELM
Link-
1052PhosphoserineGEPTSDLSD
CCCCCCCCC
47.47Phosphositeplus
Link-
1052PhosphoserineGEPTSDLSD
CCCCCCCCC
47.47SysPTM
Link-
1052PhosphoserineGEPTSDLSD
CCCCCCCCC
47.47SysPTM
Link-
1052Phosphoserine.GEPTSDLSD
CCCCCCCCC
47.47UniProtKB
Link-
1055PhosphoserineTSDLSDID
CCCCCCCC
37.19HPRD
Link-
1055PhosphoserineTSDLSDID
CCCCCCCC
37.19PhosphoELM
Link-
1055PhosphoserineTSDLSDID
CCCCCCCC
37.19Phosphositeplus
Link-
1055PhosphoserineTSDLSDID
CCCCCCCC
37.19SysPTM
Link-
1055PhosphoserineTSDLSDID
CCCCCCCC
37.19SysPTM
Link-
1055Phosphoserine.TSDLSDID
CCCCCCCC
37.19UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
VIME_HUMANphysical interactionEBI-734024
intact16169070
K1377_HUMANphysical interactionEBI-731407
intact16169070
K1377_HUMANyeast 2-hybridHPRD:06848HPRD16169070
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Disease Reference
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-368; LYS-418; LYS-516;LYS-519; LYS-523 AND LYS-903, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1052 AND SER-1055, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; THR-1051 ANDSER-1055, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128 AND SER-1055, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures