BRD9_HUMAN - dbPTM
BRD9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRD9_HUMAN
UniProt AC Q9H8M2
Protein Name Bromodomain-containing protein 9
Gene Name BRD9
Organism Homo sapiens (Human).
Sequence Length 597
Subcellular Localization
Protein Description Plays a role in chromatin remodeling and regulation of transcription. [PubMed: 22464331]
Protein Sequence MGKKHKKHKAEWRSSYEDYADKPLEKPLKLVLKVGGSEVTELSGSGHDSSYYDDRSDHERERHKEKKKKKKKKSEKEKHLDDEERRKRKEEKKRKREREHCDTEGEADDFDPGKKVEVEPPPDRPVRACRTQPAENESTPIQQLLEHFLRQLQRKDPHGFFAFPVTDAIAPGYSMIIKHPMDFGTMKDKIVANEYKSVTEFKADFKLMCDNAMTYNRPDTVYYKLAKKILHAGFKMMSKQAALLGNEDTAVEEPVPEVVPVQVETAKKSKKPSREVISCMFEPEGNACSLTDSTAEEHVLALVEHAADEARDRINRFLPGGKMGYLKRNGDGSLLYSVVNTAEPDADEEETHPVDLSSLSSKLLPGFTTLGFKDERRNKVTFLSSATTALSMQNNSVFGDLKSDEMELLYSAYGDETGVQCALSLQEFVKDAGSYSKKVVDDLLDQITGGDHSRTLFQLKQRRNVPMKPPDEAKVGDTLGDSSSSVLEFMSMKSYPDVSVDISMLSSLGKVKKELDPDDSHLNLDETTKLLQDLHEAQAERGGSRPSSNLSSLSNASERDQHHLGSPSRLSVGEQPDVTHDPYEFLQSPEPAASAKT
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
3 (in isoform 6)Phosphorylation-50.8627762562
6 (in isoform 6)Phosphorylation-66.5127762562
14PhosphorylationKHKAEWRSSYEDYAD
HCCHHHHHCHHHHCC		38.0430108239
15PhosphorylationHKAEWRSSYEDYADK
CCHHHHHCHHHHCCC		24.7826657352
16PhosphorylationKAEWRSSYEDYADKP
CHHHHHCHHHHCCCC		17.6730108239
19PhosphorylationWRSSYEDYADKPLEK
HHHCHHHHCCCCCCC		12.5429978859
26AcetylationYADKPLEKPLKLVLK
HCCCCCCCCCEEEEE		64.4323749302
26UbiquitinationYADKPLEKPLKLVLK
HCCCCCCCCCEEEEE		64.43-
37PhosphorylationLVLKVGGSEVTELSG
EEEEECCCEEEECCC		23.9825022875
40PhosphorylationKVGGSEVTELSGSGH
EECCCEEEECCCCCC		27.4530576142
42 (in isoform 6)Phosphorylation-5.26-
43PhosphorylationGSEVTELSGSGHDSS
CCEEEECCCCCCCCC		25.3630576142
44 (in isoform 6)Phosphorylation-50.72-
45PhosphorylationEVTELSGSGHDSSYY
EEEECCCCCCCCCCC		29.5823401153
49PhosphorylationLSGSGHDSSYYDDRS
CCCCCCCCCCCCCCC		17.9930576142
50PhosphorylationSGSGHDSSYYDDRSD
CCCCCCCCCCCCCCH		33.5030576142
51PhosphorylationGSGHDSSYYDDRSDH
CCCCCCCCCCCCCHH		18.1830576142
52PhosphorylationSGHDSSYYDDRSDHE
CCCCCCCCCCCCHHH		17.2030576142
56PhosphorylationSSYYDDRSDHERERH
CCCCCCCCHHHHHHH		50.7623401153
103PhosphorylationREREHCDTEGEADDF
HHHHHCCCCCCCCCC		51.8123401153
131PhosphorylationRPVRACRTQPAENES
CCCCHHCCCCCCCCC		38.5028450419
138PhosphorylationTQPAENESTPIQQLL
CCCCCCCCCHHHHHH		51.5728450419
139PhosphorylationQPAENESTPIQQLLE
CCCCCCCCHHHHHHH		20.4524719451
155UbiquitinationFLRQLQRKDPHGFFA
HHHHHHCCCCCCCEE		63.75-
228AcetylationVYYKLAKKILHAGFK
HHHHHHHHHHHHHHH		44.9118586019
235AcetylationKILHAGFKMMSKQAA
HHHHHHHHHHHHHHH		32.5425953088
322AcetylationNRFLPGGKMGYLKRN
HHHCCCCCCCEEEEC		34.7625953088
322UbiquitinationNRFLPGGKMGYLKRN
HHHCCCCCCCEEEEC		34.76-
327MethylationGGKMGYLKRNGDGSL
CCCCCEEEECCCCCE		35.02-
357PhosphorylationETHPVDLSSLSSKLL
CCCCCCHHHHHCCCC		25.4426437602
358PhosphorylationTHPVDLSSLSSKLLP
CCCCCHHHHHCCCCC		39.3026437602
373AcetylationGFTTLGFKDERRNKV
CCCCCCCCCCCCCCE		57.8119608861
373UbiquitinationGFTTLGFKDERRNKV
CCCCCCCCCCCCCCE		57.8119608861
373SumoylationGFTTLGFKDERRNKV
CCCCCCCCCCCCCCE		57.8128112733
438UbiquitinationDAGSYSKKVVDDLLD
HCCCCCHHHHHHHHH		41.36-
460UbiquitinationSRTLFQLKQRRNVPM
HHHHHHHHHHCCCCC		30.86-
468AcetylationQRRNVPMKPPDEAKV
HHCCCCCCCCCHHCC		47.5325953088
468UbiquitinationQRRNVPMKPPDEAKV
HHCCCCCCCCCHHCC		47.53-
478PhosphorylationDEAKVGDTLGDSSSS
CHHCCCCCCCCCCHH		27.0623186163
482PhosphorylationVGDTLGDSSSSVLEF
CCCCCCCCCHHHHHH		30.2625106551
483PhosphorylationGDTLGDSSSSVLEFM
CCCCCCCCHHHHHHH		31.2230108239
484PhosphorylationDTLGDSSSSVLEFMS
CCCCCCCHHHHHHHH		28.5525106551
485PhosphorylationTLGDSSSSVLEFMSM
CCCCCCHHHHHHHHC		32.4430108239
491PhosphorylationSSVLEFMSMKSYPDV
HHHHHHHHCCCCCCC		28.5124719451
494PhosphorylationLEFMSMKSYPDVSVD
HHHHHCCCCCCCEEE		33.0027251275
510AcetylationSMLSSLGKVKKELDP
HHHHHHCCCCCCCCC		57.0626051181
512UbiquitinationLSSLGKVKKELDPDD
HHHHCCCCCCCCCCC		43.97-
513UbiquitinationSSLGKVKKELDPDDS
HHHCCCCCCCCCCCC		67.51-
520PhosphorylationKELDPDDSHLNLDET
CCCCCCCCCCCHHHH		36.9425849741
527PhosphorylationSHLNLDETTKLLQDL
CCCCHHHHHHHHHHH		28.9719651622
528PhosphorylationHLNLDETTKLLQDLH
CCCHHHHHHHHHHHH		20.0428111955
544PhosphorylationAQAERGGSRPSSNLS
HHHHHCCCCCCCCHH		43.7928985074
547PhosphorylationERGGSRPSSNLSSLS
HHCCCCCCCCHHHHC		30.6523927012
548PhosphorylationRGGSRPSSNLSSLSN
HCCCCCCCCHHHHCC		44.4623927012
551PhosphorylationSRPSSNLSSLSNASE
CCCCCCHHHHCCCCH		33.2223927012
552PhosphorylationRPSSNLSSLSNASER
CCCCCHHHHCCCCHH		38.7023927012
554PhosphorylationSSNLSSLSNASERDQ
CCCHHHHCCCCHHHH		32.0923927012
557PhosphorylationLSSLSNASERDQHHL
HHHHCCCCHHHHCCC		37.1023927012
566PhosphorylationRDQHHLGSPSRLSVG
HHHCCCCCCCCCCCC		26.5129255136
568PhosphorylationQHHLGSPSRLSVGEQ
HCCCCCCCCCCCCCC		47.7729255136
571PhosphorylationLGSPSRLSVGEQPDV
CCCCCCCCCCCCCCC		27.2829255136
579PhosphorylationVGEQPDVTHDPYEFL
CCCCCCCCCCHHHHH		28.1329255136
583PhosphorylationPDVTHDPYEFLQSPE
CCCCCCHHHHHHCCC		25.9330266825
588PhosphorylationDPYEFLQSPEPAASA
CHHHHHHCCCCHHHC		33.1229255136
594PhosphorylationQSPEPAASAKT----
HCCCCHHHCCC----		32.1929255136
597PhosphorylationEPAASAKT-------
CCHHHCCC-------		43.4926074081
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
588SPhosphorylationKinaseMTORP42345
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRD9_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CATIP_HUMANCATIPphysical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BRD9_HUMAN

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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-373, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-588, AND MASSSPECTROMETRY.

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