BRD7_HUMAN - dbPTM
BRD7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRD7_HUMAN
UniProt AC Q9NPI1
Protein Name Bromodomain-containing protein 7
Gene Name BRD7
Organism Homo sapiens (Human).
Sequence Length 651
Subcellular Localization Isoform 2: Nucleus.
Protein Description Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. Activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. Induces dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional activation by AR (By similarity). Transcriptional corepressor that down-regulates the expression of target genes. Binds to target promoters, leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter. Coactivator for TP53-mediated activation of transcription of a set of target genes. Required for TP53-mediated cell-cycle arrest in response to oncogene activation. Promotes acetylation of TP53 at 'Lys-382', and thereby promotes efficient recruitment of TP53 to target promoters. Inhibits cell cycle progression from G1 to S phase..
Protein Sequence MGKKHKKHKSDKHLYEEYVEKPLKLVLKVGGNEVTELSTGSSGHDSSLFEDKNDHDKHKDRKRKKRKKGEKQIPGEEKGRKRRRVKEDKKKRDRDRVENEAEKDLQCHAPVRLDLPPEKPLTSSLAKQEEVEQTPLQEALNQLMRQLQRKDPSAFFSFPVTDFIAPGYSMIIKHPMDFSTMKEKIKNNDYQSIEELKDNFKLMCTNAMIYNKPETIYYKAAKKLLHSGMKILSQERIQSLKQSIDFMADLQKTRKQKDGTDTSQSGEDGGCWQREREDSGDAEAHAFKSPSKENKKKDKDMLEDKFKSNNLEREQEQLDRIVKESGGKLTRRLVNSQCEFERRKPDGTTTLGLLHPVDPIVGEPGYCPVRLGMTTGRLQSGVNTLQGFKEDKRNKVTPVLYLNYGPYSSYAPHYDSTFANISKDDSDLIYSTYGEDSDLPSDFSIHEFLATCQDYPYVMADSLLDVLTKGGHSRTLQEMEMSLPEDEGHTRTLDTAKEMEITEVEPPGRLDSSTQDRLIALKAVTNFGVPVEVFDSEEAEIFQKKLDETTRLLRELQEAQNERLSTRPPPNMICLLGPSYREMHLAEQVTNNLKELAQQVTPGDIVSTYGVRKAMGISIPSPVMENNFVDLTEDTEEPKKTDVAECGPGGS
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
7Acetylation-MGKKHKKHKSDKHL
-CCCCCCCCCCCHHH		56.8618586841
15PhosphorylationHKSDKHLYEEYVEKP
CCCCHHHHHHHHHCC		13.3628796482
15 (in isoform 2)Phosphorylation-13.3627642862
18PhosphorylationDKHLYEEYVEKPLKL
CHHHHHHHHHCCEEE		11.2829978859
18 (in isoform 2)Phosphorylation-11.2827642862
21SumoylationLYEEYVEKPLKLVLK
HHHHHHHCCEEEEEE		45.68-
21AcetylationLYEEYVEKPLKLVLK
HHHHHHHCCEEEEEE		45.6823236377
21SumoylationLYEEYVEKPLKLVLK
HHHHHHHCCEEEEEE		45.6828112733
21UbiquitinationLYEEYVEKPLKLVLK
HHHHHHHCCEEEEEE		45.6821890473
21 (in isoform 1)Ubiquitination-45.6821890473
21 (in isoform 2)Ubiquitination-45.6821890473
24UbiquitinationEYVEKPLKLVLKVGG
HHHHCCEEEEEEECC		45.1122817900
35PhosphorylationKVGGNEVTELSTGSS
EECCCEEEEECCCCC		25.6522496350
38PhosphorylationGNEVTELSTGSSGHD
CCEEEEECCCCCCCC		25.2122496350
38 (in isoform 2)Phosphorylation-25.2121406692
39PhosphorylationNEVTELSTGSSGHDS
CEEEEECCCCCCCCC		54.4220363803
39 (in isoform 2)Phosphorylation-54.4221406692
41PhosphorylationVTELSTGSSGHDSSL
EEEECCCCCCCCCCC		32.9822496350
41 (in isoform 2)Phosphorylation-32.9821406692
42PhosphorylationTELSTGSSGHDSSLF
EEECCCCCCCCCCCC		41.3025159151
46PhosphorylationTGSSGHDSSLFEDKN
CCCCCCCCCCCCCCC		24.2230576142
47PhosphorylationGSSGHDSSLFEDKND
CCCCCCCCCCCCCCC		43.0430576142
47 (in isoform 2)Phosphorylation-43.0421406692
52SumoylationDSSLFEDKNDHDKHK
CCCCCCCCCCCCHHH		58.0128112733
78AcetylationKQIPGEEKGRKRRRV
CCCCCCHHHHHHHHH		60.767824251
90UbiquitinationRRVKEDKKKRDRDRV
HHHHHHHHHHHHHHH		66.4224816145
103AcetylationRVENEAEKDLQCHAP
HHHHHHHHHHCCCCC		71.4427452117
103UbiquitinationRVENEAEKDLQCHAP
HHHHHHHHHHCCCCC		71.4421890473
105UbiquitinationENEAEKDLQCHAPVR
HHHHHHHHCCCCCEE		9.6622817900
127SumoylationPLTSSLAKQEEVEQT
CCCHHHHCHHHHHCC		64.6328112733
153PhosphorylationQLQRKDPSAFFSFPV
HHHHCCHHHHHCCCH		48.09-
157PhosphorylationKDPSAFFSFPVTDFI
CCHHHHHCCCHHHCC		23.37-
182UbiquitinationPMDFSTMKEKIKNND
CCCHHHHHHHHHCCC		56.8122817900
184UbiquitinationDFSTMKEKIKNNDYQ
CHHHHHHHHHCCCCC		54.1622817900
186SumoylationSTMKEKIKNNDYQSI
HHHHHHHHCCCCCCH		61.8528112733
186UbiquitinationSTMKEKIKNNDYQSI
HHHHHHHHCCCCCCH		61.8522817900
186 (in isoform 1)Ubiquitination-61.8521890473
186 (in isoform 2)Ubiquitination-61.8521890473
190PhosphorylationEKIKNNDYQSIEELK
HHHHCCCCCCHHHHH		13.29-
190 (in isoform 2)Phosphorylation-13.2927642862
197AcetylationYQSIEELKDNFKLMC
CCCHHHHHHHHEEEE		54.6426051181
197SumoylationYQSIEELKDNFKLMC
CCCHHHHHHHHEEEE		54.6428112733
197UbiquitinationYQSIEELKDNFKLMC
CCCHHHHHHHHEEEE		54.6429967540
199UbiquitinationSIEELKDNFKLMCTN
CHHHHHHHHEEEECC		34.0722817900
201SumoylationEELKDNFKLMCTNAM
HHHHHHHEEEECCCH		41.3828112733
201UbiquitinationEELKDNFKLMCTNAM
HHHHHHHEEEECCCH		41.3822817900
203UbiquitinationLKDNFKLMCTNAMIY
HHHHHEEEECCCHHC		2.4621890473
210PhosphorylationMCTNAMIYNKPETIY
EECCCHHCCCCCHHH		12.2124275748
212SumoylationTNAMIYNKPETIYYK
CCCHHCCCCCHHHHH		27.5328112733
217PhosphorylationYNKPETIYYKAAKKL
CCCCCHHHHHHHHHH		13.3118083107
227PhosphorylationAAKKLLHSGMKILSQ
HHHHHHHHHCHHCCH		40.3221406692
230UbiquitinationKLLHSGMKILSQERI
HHHHHHCHHCCHHHH		43.9829967540
233PhosphorylationHSGMKILSQERIQSL
HHHCHHCCHHHHHHH		33.2121406692
233 (in isoform 2)Phosphorylation-33.2121406692
239PhosphorylationLSQERIQSLKQSIDF
CCHHHHHHHHHHHHH		34.8522210691
241SumoylationQERIQSLKQSIDFMA
HHHHHHHHHHHHHHH		47.4428112733
260PhosphorylationTRKQKDGTDTSQSGE
HHCCCCCCCCCCCCC		46.3628450419
262PhosphorylationKQKDGTDTSQSGEDG
CCCCCCCCCCCCCCC		28.6228450419
262 (in isoform 2)Phosphorylation-28.6224719451
263PhosphorylationQKDGTDTSQSGEDGG
CCCCCCCCCCCCCCC		25.7625159151
263 (in isoform 2)Phosphorylation-25.7624719451
265PhosphorylationDGTDTSQSGEDGGCW
CCCCCCCCCCCCCCC		43.8728450419
265 (in isoform 2)Phosphorylation-43.8727251275
279PhosphorylationWQREREDSGDAEAHA
CCCCCCCCCCCHHHH		33.5429255136
279 (in isoform 2)Phosphorylation-33.5424719451
289PhosphorylationAEAHAFKSPSKENKK
CHHHHHCCCCHHCHH		28.1429255136
289 (in isoform 2)Phosphorylation-28.1424719451
291PhosphorylationAHAFKSPSKENKKKD
HHHHCCCCHHCHHHH		60.7429255136
295UbiquitinationKSPSKENKKKDKDML
CCCCHHCHHHHHHHH		63.3924816145
299AcetylationKENKKKDKDMLEDKF
HHCHHHHHHHHHHHH		54.6526051181
305SumoylationDKDMLEDKFKSNNLE
HHHHHHHHHHHCCHH		45.3728112733
305UbiquitinationDKDMLEDKFKSNNLE
HHHHHHHHHHHCCHH		45.3722817900
305 (in isoform 1)Ubiquitination-45.3721890473
305 (in isoform 2)Ubiquitination-45.3721890473
307SumoylationDMLEDKFKSNNLERE
HHHHHHHHHCCHHHH		59.0028112733
307UbiquitinationDMLEDKFKSNNLERE
HHHHHHHHHCCHHHH		59.0022817900
308PhosphorylationMLEDKFKSNNLEREQ
HHHHHHHHCCHHHHH		33.8022210691
322UbiquitinationQEQLDRIVKESGGKL
HHHHHHHHHHHCCHH		6.1521890473
324UbiquitinationQLDRIVKESGGKLTR
HHHHHHHHHCCHHHH		43.6622817900
325PhosphorylationLDRIVKESGGKLTRR
HHHHHHHHCCHHHHH		47.32-
328AcetylationIVKESGGKLTRRLVN
HHHHHCCHHHHHHHH		50.6523749302
344SumoylationQCEFERRKPDGTTTL
CCCEEECCCCCCEEE		54.4028112733
374PhosphorylationCPVRLGMTTGRLQSG
CCCHHCCCCCCCCCC		25.0522210691
375PhosphorylationPVRLGMTTGRLQSGV
CCHHCCCCCCCCCCC		16.0622210691
380PhosphorylationMTTGRLQSGVNTLQG
CCCCCCCCCCCCHHC		49.6623186163
380 (in isoform 2)Phosphorylation-49.6624719451
389SumoylationVNTLQGFKEDKRNKV
CCCHHCCCHHHCCCC		72.3528112733
389UbiquitinationVNTLQGFKEDKRNKV
CCCHHCCCHHHCCCC		72.3533845483
461UbiquitinationDYPYVMADSLLDVLT
CCCHHHHHHHHHHHH		23.0124816145
475PhosphorylationTKGGHSRTLQEMEMS
HCCCCCCCHHHHHHC		35.4929214152
478UbiquitinationGHSRTLQEMEMSLPE
CCCCCHHHHHHCCCC		39.9824816145
482PhosphorylationTLQEMEMSLPEDEGH
CHHHHHHCCCCCCCC		27.7129214152
497UbiquitinationTRTLDTAKEMEITEV
CCCCHHHHHCEEEEC		60.7424816145
499SulfoxidationTLDTAKEMEITEVEP
CCHHHHHCEEEECCC		4.4421406390
502PhosphorylationTAKEMEITEVEPPGR
HHHHCEEEECCCCCC		22.2220068231
512PhosphorylationEPPGRLDSSTQDRLI
CCCCCCCCCHHHHHH		39.62-
513PhosphorylationPPGRLDSSTQDRLIA
CCCCCCCCHHHHHHH		29.7429214152
514PhosphorylationPGRLDSSTQDRLIAL
CCCCCCCHHHHHHHH		38.1423186163
514UbiquitinationPGRLDSSTQDRLIAL
CCCCCCCHHHHHHHH		38.1424816145
517MethylationLDSSTQDRLIALKAV
CCCCHHHHHHHHHHH		20.41-
565PhosphorylationEAQNERLSTRPPPNM
HHHHHHHCCCCCCCE		28.7024532841
566PhosphorylationAQNERLSTRPPPNMI
HHHHHHCCCCCCCEE		52.3524532841
580PhosphorylationICLLGPSYREMHLAE
EEEECHHHHHHHHHH		17.4624532841
590PhosphorylationMHLAEQVTNNLKELA
HHHHHHHHHHHHHHH		20.3424532841
618PhosphorylationVRKAMGISIPSPVME
HHHHHCCCCCCCCCC		23.7930266825
621PhosphorylationAMGISIPSPVMENNF
HHCCCCCCCCCCCCC		28.5830266825
622 (in isoform 2)Phosphorylation-24.9127251275
632PhosphorylationENNFVDLTEDTEEPK
CCCCCCCCCCCCCCC		27.6130266825
635PhosphorylationFVDLTEDTEEPKKTD
CCCCCCCCCCCCCCC		35.7027080861
641PhosphorylationDTEEPKKTDVAECGP
CCCCCCCCCCCCCCC		41.6628985074
651PhosphorylationAECGPGGS-------
CCCCCCCC-------		42.8525627689
652 (in isoform 2)Phosphorylation-27251275
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 BRD7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRD7_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 BRD7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HNRL1_HUMANHNRNPUL1physical
12489984
BRCA1_HUMANBRCA1physical
20215511
ARID2_HUMANARID2physical
18809673
SMCA4_HUMANSMARCA4physical
18809673
SMRC1_HUMANSMARCC1physical
18809673
TIF1A_HUMANTRIM24physical
19909775
HAP1_HUMANHAP1physical
15383276
LRIF1_HUMANLRIF1physical
15383276
BRD2_HUMANBRD2physical
16786191
DVL1_MOUSEDvl1physical
12941796
H32_HUMANHIST2H3Cphysical
16265664
P53_HUMANTP53physical
20228809
EP300_HUMANEP300physical
20228809
ARID2_HUMANARID2physical
26344197
PB1_HUMANPBRM1physical
26344197
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 BRD7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-279, AND MASSSPECTROMETRY.

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