BRD9_MOUSE - dbPTM
BRD9_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRD9_MOUSE
UniProt AC Q3UQU0
Protein Name Bromodomain-containing protein 9
Gene Name Brd9
Organism Mus musculus (Mouse).
Sequence Length 596
Subcellular Localization
Protein Description Plays a role in chromatin remodeling and regulation of transcription. Acts as a chromatin reader that recognizes and binds acylated histones: binds histones that are acetylated and/or butyrylated..
Protein Sequence MGKKHKKHKAEWRSSYEDYTDTPLEKPLKLVLKVGGSEVTELSGSGHDSSYYDDRSDHERERHREKKKKKKKKSEKEKHLDEEERRKRKEEKKRKREKEHCDSEGEADAFDPGKKVEVEPPPDRPVRACRTQPAENESTPIQRLLEHFLRQLQRKDPHGFFAFPVTDAIAPGYSMIIKHPMDFGTMKDKIVANEYKSVTEFKADFKLMCDNAMTYNRPDTVYYKLAKKILHAGFKMMSKAALLGSEDPAAEEPVPEVVPVQVETTKKSKKPSREVISCMFEPEGNACSLTDSTAEEHVLALVEHAADEARDRINRFLPGGKMGYLKKLGDGSLLYSVVNAPEPDADEEETHPVDLSSLSSKLLPGFTTLGFKDERRNKVTFLSSASTALSMQNNSVFGDLKSDEMELLYSAYGDETGVQCALSLQEFVKDAGSYSKKMVDDLLDQITGGDHSRMIFQLKQRRSIPMRPADEMKVGDPLGESGGPVLDFMSMKQYPDVSLDVSMLSSLGKVKKELDHEDSHLNLDETARLLQDLHEAQAERGGSRPSSNLSSLSTASEREHPPPGSPSRLSVGEQPDVAHDPYEFLQSPEPAAPAKN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
14PhosphorylationKHKAEWRSSYEDYTD
HCCCHHHHCCCCCCC
38.0425338131
15PhosphorylationHKAEWRSSYEDYTDT
CCCHHHHCCCCCCCC
24.7824704852
37PhosphorylationLVLKVGGSEVTELSG
EEEEECCCEEEECCC
23.9825777480
40PhosphorylationKVGGSEVTELSGSGH
EECCCEEEECCCCCC
27.4525777480
43PhosphorylationGSEVTELSGSGHDSS
CCEEEECCCCCCCCC
25.3625159016
45PhosphorylationEVTELSGSGHDSSYY
EEEECCCCCCCCCCC
29.5825159016
49PhosphorylationLSGSGHDSSYYDDRS
CCCCCCCCCCCCCCC
17.9925159016
50PhosphorylationSGSGHDSSYYDDRSD
CCCCCCCCCCCCCCH
33.5028066266
51PhosphorylationGSGHDSSYYDDRSDH
CCCCCCCCCCCCCHH
18.1825159016
52PhosphorylationSGHDSSYYDDRSDHE
CCCCCCCCCCCCHHH
17.2025777480
56PhosphorylationSSYYDDRSDHERERH
CCCCCCCCHHHHHHH
50.7621082442
103PhosphorylationREKEHCDSEGEADAF
HHHHHCCCCCCCCCC
53.5525521595
321AcetylationNRFLPGGKMGYLKKL
HHHCCCCCCCCEEEC
34.7619861903
326MalonylationGGKMGYLKKLGDGSL
CCCCCCEEECCCCCE
37.1526073543
372AcetylationGFTTLGFKDERRNKV
CCCCCCCCCCCCCCE
57.81-
395PhosphorylationALSMQNNSVFGDLKS
HHHHCCCCCCCCCCH
26.7728576409
494PhosphorylationDFMSMKQYPDVSLDV
CHHCCCCCCCCEEEH
8.90-
502PhosphorylationPDVSLDVSMLSSLGK
CCCEEEHHHHHHHHH
17.42-
519PhosphorylationKELDHEDSHLNLDET
HHCCCCCCCCCHHHH
27.2125521595
551PhosphorylationRPSSNLSSLSTASER
CCCCCHHHCCCCCCC
29.5225195567
565PhosphorylationREHPPPGSPSRLSVG
CCCCCCCCCCCCCCC
26.0226824392
567PhosphorylationHPPPGSPSRLSVGEQ
CCCCCCCCCCCCCCC
47.7729899451
570PhosphorylationPGSPSRLSVGEQPDV
CCCCCCCCCCCCCCC
27.2825619855
582PhosphorylationPDVAHDPYEFLQSPE
CCCCCCHHHHHHCCC
25.9325619855
587PhosphorylationDPYEFLQSPEPAAPA
CHHHHHHCCCCCCCC
33.1227087446
588PhosphorylationPYEFLQSPEPAAPAK
HHHHHHCCCCCCCCC
38.3324719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of BRD9_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRD9_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of BRD9_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of BRD9_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BRD9_MOUSE

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Related Literatures of Post-Translational Modification

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