BRWD3_HUMAN - dbPTM
BRWD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRWD3_HUMAN
UniProt AC Q6RI45
Protein Name Bromodomain and WD repeat-containing protein 3
Gene Name BRWD3
Organism Homo sapiens (Human).
Sequence Length 1802
Subcellular Localization
Protein Description Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape..
Protein Sequence MAAAPTQIEAELYYLIARFLQSGPCNKSAQVLVQELEEHQLIPRRLDWEGKEHRRSFEDLVAANAHIPPDYLLKICERIGPLLDKEIPQSVPGVQTLLGVGRQSLLRDAKDCKSTLWNGSAFAALHRGRPPELPVNYVKPPNVVNITSARQLTGCSRFGHIFPSSAYQHIKMHKRILGHLSSVYCVAFDRSGRRIFTGSDDCLVKIWATDDGRLLATLRGHSAEISDMAVNYENTLIAAGSCDKVVRVWCLRTCAPVAVLQGHSASITSIQFCPSTKGTNRYLTSTGADGTICFWQWHVKTMKFRDRPVKFTERSRPGVQISCSSFSSGGMFITTGSTDHVIRIYYLGSEVPEKIAELESHTDKVVAVQFCNNGDSLRFVSGSRDGTARIWQYQQQEWKSIVLDMATKMTGNNLPSGEDKITKLKVTMVAWDRYDTTVITAVNNFLLKVWNSITGQLLHTLSGHDDEVFVLEAHPFDQRIILSAGHDGNIFIWDLDRGTKIRNYFNMIEGQGHGAVFDCKFSPDGNHFACTDSHGHLLLFGFGCSKYYEKIPDQMFFHTDYRPLIRDANNYVLDEQTQQAPHLMPPPFLVDVDGNPHPTKFQRLVPGRENCKDEQLIPQLGYVANGDGEVVEQVIGQQTNDQDESILDGIIRELQREQDLRLINEGDVPHLPVNRAYSVNGALRSPNMDISSSPNIRLRRHSSQIEGVRQMHNNAPRSQMATERDLMAWSRRVVVNELNNGVSRVQEECRTAKGDIEISLYTVEKKKKPSYTTQRNDYEPSCGRSLRRTQRKRQHTYQTRSNIEHNSQASCQNSGVQEDSDSSSEEDETVGTSDASVEDPVVEWQSESSSSDSSSEYSDWTADAGINLQPPKRQTRQTTRKICSSSDEENLKSLEERQKKPKQTRKKKGGLVSIAGEPNEEWFAPQWILDTIPRRSPFVPQMGDELIYFRQGHEAYVRAVRKSKIYSVNLQKQPWNKMDLREQEFVKIVGIKYEVGPPTLCCLKLAFLDPISGKMTGESFSIKYHDMPDVIDFLVLHQFYNEAKERNWQIGDRFRSIIDDAWWFGTVESQQPFQPEYPDSSFQCYSVHWDNNEREKMSPWDMEPIPEGTAFPDEVGAGVPVSQEELTALLYKPQEGEWGAHSRDEECERVIQGINHLLSLDFASPFAVPVDLSAYPLYCTVVAYPTDLNTIRRRLENRFYRRISALMWEVRYIEHNARTFNEPDSPIVKAAKIVTDVLLRFIGDQSCTDILDTYNKIKAEERNSTDAEEDTEIVDLDSDGPGTSSGRKVKCRGRRQSLKCNPDAWKKQCKELLSLIYEREDSEPFRQPADLLSYPGHQEQEGESSESVVPERQQDSSLSEDYQDVIDTPVDFSTVKETLEAGNYGSPLEFYKDVRQIFNNSKAYTSNKKSRIYSMMLRLSALFESHIKNIISEYKSAIQSQKRRRPRYRKRLRSSSSSLSSSGAPSPKGKQKQMKLQPKNDQNTSVSHARTSSPFSSPVSDAAEGLSLYLLDDEPDGPFSSSSFGGYSRSGNSHDPGKAKSFRNRVLPVKQDHSLDGPLTNGDGREPRTGIKRKLLSASEEDENMGGEDKEKKETKEKSHLSTSESGELGSSLSSESTCGSDSDSESTSRTDQDYVDGDHDYSKFIQTRPKRKLRKQHGNGKRNWKTRGTGGRGRWGRWGRWSRGGRGRGGRGRGSRGRGGGGTRGRGRGRGGRGASRGATRAKRARIADDEFDTMFSGRFSRLPRIKTRNQGRRTVLYNDDSDNDNFVSTEDPLNLGTSRSGRVRKMTEKARVSHLMGWNY
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
6Phosphorylation--MAAAPTQIEAELY
--CCCCCCHHHHHHH		37.14-
13PhosphorylationTQIEAELYYLIARFL
CHHHHHHHHHHHHHH		6.4227422710
14PhosphorylationQIEAELYYLIARFLQ
HHHHHHHHHHHHHHH		12.3127422710
104PhosphorylationLLGVGRQSLLRDAKD
HHCCCHHHHHHCHHH		28.1924719451
171AcetylationSSAYQHIKMHKRILG
CHHHHHHHHHHHHHH		32.5925953088
268PhosphorylationQGHSASITSIQFCPS
CCCCCEEEEEEECCC		19.7920058876
312PhosphorylationRDRPVKFTERSRPGV
CCCCCCCCCCCCCCC		25.4430576142
315PhosphorylationPVKFTERSRPGVQIS
CCCCCCCCCCCCEEE		36.2730576142
334PhosphorylationSSGGMFITTGSTDHV
CCCCEEEECCCCCCE		17.5328450419
335PhosphorylationSGGMFITTGSTDHVI
CCCEEEECCCCCCEE		25.0728450419
337PhosphorylationGMFITTGSTDHVIRI
CEEEECCCCCCEEEE		28.6828450419
338PhosphorylationMFITTGSTDHVIRIY
EEEECCCCCCEEEEE		31.3128450419
360PhosphorylationEKIAELESHTDKVVA
HHHHHHHHCCCCEEE		44.2930576142
362PhosphorylationIAELESHTDKVVAVQ
HHHHHHCCCCEEEEE		46.9630576142
546AcetylationLFGFGCSKYYEKIPD
EEECCCHHHHHHCCC		56.8025953088
577PhosphorylationNYVLDEQTQQAPHLM
CCCCCCCCCCCCCCC		22.17-
583UbiquitinationQTQQAPHLMPPPFLV
CCCCCCCCCCCCEEE		5.5521890473
583UbiquitinationQTQQAPHLMPPPFLV
CCCCCCCCCCCCEEE		5.5521890473
583 (in isoform 3)Ubiquitination-5.5521890473
588UbiquitinationPHLMPPPFLVDVDGN
CCCCCCCEEEECCCC		14.8422817900
677PhosphorylationHLPVNRAYSVNGALR
CCCCCCEEEECCCCC		15.2023186163
678PhosphorylationLPVNRAYSVNGALRS
CCCCCEEEECCCCCC		14.2327067055
685PhosphorylationSVNGALRSPNMDISS
EECCCCCCCCCCCCC		22.8323403867
691PhosphorylationRSPNMDISSSPNIRL
CCCCCCCCCCCCHHH		22.0923403867
692PhosphorylationSPNMDISSSPNIRLR
CCCCCCCCCCCHHHH		50.5823403867
693PhosphorylationPNMDISSSPNIRLRR
CCCCCCCCCCHHHHH		18.3823403867
702PhosphorylationNIRLRRHSSQIEGVR
CHHHHHCHHHHHHHH		23.3330266825
703PhosphorylationIRLRRHSSQIEGVRQ
HHHHHCHHHHHHHHH		29.1117525332
816 (in isoform 4)Ubiquitination-5.9021890473
816 (in isoform 2)Ubiquitination-5.9021890473
816UbiquitinationASCQNSGVQEDSDSS
HHHCCCCCCCCCCCC		5.9021890473
884PhosphorylationQTTRKICSSSDEENL
HHHHHHHCCCCHHHH		36.0323663014
885PhosphorylationTTRKICSSSDEENLK
HHHHHHCCCCHHHHH		37.0823663014
886PhosphorylationTRKICSSSDEENLKS
HHHHHCCCCHHHHHH		32.5223663014
893PhosphorylationSDEENLKSLEERQKK
CCHHHHHHHHHHHHC		44.1528787133
937UbiquitinationDTIPRRSPFVPQMGD
HCCCCCCCCCCCCCC		32.2321890473
942UbiquitinationRSPFVPQMGDELIYF
CCCCCCCCCCEEEEE		6.3022817900
948PhosphorylationQMGDELIYFRQGHEA
CCCCEEEEEECCHHH		12.82-
964UbiquitinationVRAVRKSKIYSVNLQ
HHHHHHHCEEEEECC		49.0129967540
987 (in isoform 1)Ubiquitination-36.6721890473
987UbiquitinationLREQEFVKIVGIKYE
CCHHHHHEEECEEEE		36.6722817900
987 (in isoform 5)Ubiquitination-36.6721890473
992UbiquitinationFVKIVGIKYEVGPPT
HHEEECEEEEECCCC		29.4522817900
1019PhosphorylationSGKMTGESFSIKYHD
CCCCCCCCEEEEECC		26.1624719451
1021PhosphorylationKMTGESFSIKYHDMP
CCCCCCEEEEECCCC		27.7024719451
1024PhosphorylationGESFSIKYHDMPDVI
CCCEEEEECCCCCHH		11.03-
1040PhosphorylationFLVLHQFYNEAKERN
HHHHHHHHHHHHHHC		12.91-
1225PhosphorylationRTFNEPDSPIVKAAK
CCCCCCCCHHHHHHH		27.5224719451
1246PhosphorylationLRFIGDQSCTDILDT
HHHHCCCCHHHHHHH		24.5923828894
1253PhosphorylationSCTDILDTYNKIKAE
CHHHHHHHHHHHHHH		26.0823828894
1254PhosphorylationCTDILDTYNKIKAEE
HHHHHHHHHHHHHHH		17.7123828894
1256UbiquitinationDILDTYNKIKAEERN
HHHHHHHHHHHHHHC		34.8629967540
1264PhosphorylationIKAEERNSTDAEEDT
HHHHHHCCCCCCCCC		33.6121406692
1265PhosphorylationKAEERNSTDAEEDTE
HHHHHCCCCCCCCCE		42.6621406692
1271PhosphorylationSTDAEEDTEIVDLDS
CCCCCCCCEEEECCC		30.7821406692
1278PhosphorylationTEIVDLDSDGPGTSS
CEEEECCCCCCCCCC		52.3321406692
1283PhosphorylationLDSDGPGTSSGRKVK
CCCCCCCCCCCCEEE		23.8921406692
1284PhosphorylationDSDGPGTSSGRKVKC
CCCCCCCCCCCEEEE		36.3921406692
1285PhosphorylationSDGPGTSSGRKVKCR
CCCCCCCCCCEEEEC		42.3221406692
1386PhosphorylationLEAGNYGSPLEFYKD
HHCCCCCCCHHHHHH		18.8925159151
1402MethylationRQIFNNSKAYTSNKK
HHHHHCCCCCCCCCH		47.76-
1402"N6,N6-dimethyllysine"RQIFNNSKAYTSNKK
HHHHHCCCCCCCCCH		47.76-
1404PhosphorylationIFNNSKAYTSNKKSR
HHHCCCCCCCCCHHH		17.90-
1405PhosphorylationFNNSKAYTSNKKSRI
HHCCCCCCCCCHHHH		30.59-
1406PhosphorylationNNSKAYTSNKKSRIY
HCCCCCCCCCHHHHH		33.69-
1410PhosphorylationAYTSNKKSRIYSMML
CCCCCCHHHHHHHHH		26.0627174698
1413PhosphorylationSNKKSRIYSMMLRLS
CCCHHHHHHHHHHHH		6.87-
1414PhosphorylationNKKSRIYSMMLRLSA
CCHHHHHHHHHHHHH		8.7127174698
1450UbiquitinationRRRPRYRKRLRSSSS
HCCHHHHHHHHHCCC		47.02-
1454PhosphorylationRYRKRLRSSSSSLSS
HHHHHHHHCCCCCCC		38.8820068231
1455PhosphorylationYRKRLRSSSSSLSSS
HHHHHHHCCCCCCCC		28.0120068231
1456PhosphorylationRKRLRSSSSSLSSSG
HHHHHHCCCCCCCCC		25.7820068231
1457PhosphorylationKRLRSSSSSLSSSGA
HHHHHCCCCCCCCCC		36.9320068231
1458PhosphorylationRLRSSSSSLSSSGAP
HHHHCCCCCCCCCCC		33.9320068231
1460PhosphorylationRSSSSSLSSSGAPSP
HHCCCCCCCCCCCCC		25.1420068231
1461PhosphorylationSSSSSLSSSGAPSPK
HCCCCCCCCCCCCCC		37.7820068231
1462PhosphorylationSSSSLSSSGAPSPKG
CCCCCCCCCCCCCCC		35.2820068231
1466PhosphorylationLSSSGAPSPKGKQKQ
CCCCCCCCCCCCCCC		38.4220068231
1491PhosphorylationTSVSHARTSSPFSSP
CCCHHCCCCCCCCCC		34.0528348404
1492PhosphorylationSVSHARTSSPFSSPV
CCHHCCCCCCCCCCC		30.3828348404
1493PhosphorylationVSHARTSSPFSSPVS
CHHCCCCCCCCCCCC		29.3828348404
1569PhosphorylationGDGREPRTGIKRKLL
CCCCCCCCCHHHHHH		54.7117081983
1577PhosphorylationGIKRKLLSASEEDEN
CHHHHHHCCCHHHHC		39.9425159151
1579PhosphorylationKRKLLSASEEDENMG
HHHHHCCCHHHHCCC		37.8425159151
1599PhosphorylationKKETKEKSHLSTSES
HHHHHHHHCCCCCCC		30.65-
1603PhosphorylationKEKSHLSTSESGELG
HHHHCCCCCCCCCCC		42.76-
1606PhosphorylationSHLSTSESGELGSSL
HCCCCCCCCCCCCCC		37.02-
1611PhosphorylationSESGELGSSLSSEST
CCCCCCCCCCCCCCC		40.50-
1612PhosphorylationESGELGSSLSSESTC
CCCCCCCCCCCCCCC		30.39-
1740MethylationFDTMFSGRFSRLPRI
HHHHHCCCCCCCCCE		25.76-
1743MethylationMFSGRFSRLPRIKTR
HHCCCCCCCCCEECC		46.10-
1756PhosphorylationTRNQGRRTVLYNDDS
CCCCCCCEEEECCCC		17.3223663014
1759PhosphorylationQGRRTVLYNDDSDND
CCCCEEEECCCCCCC		16.5323663014
1763PhosphorylationTVLYNDDSDNDNFVS
EEEECCCCCCCCCCC		40.9730175587
1770PhosphorylationSDNDNFVSTEDPLNL
CCCCCCCCCCCCCCC		23.1827251275
1771PhosphorylationDNDNFVSTEDPLNLG
CCCCCCCCCCCCCCC		38.8227251275
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 BRWD3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRWD3_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 BRWD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of BRWD3_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=A chromosomal aberration involving BRWD3 can be found in patients with B-cell chronic lymphocytic leukemia (B-CLL). Translocation t(X
11)(q21
q23) with ARHGAP20 does not result in fusion transcripts but disrupts both genes.
300659
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BRWD3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1455 AND SER-1466, 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 THR-1569, AND MASSSPECTROMETRY.

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