dbPTM

BAZ2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BAZ2A_HUMAN
UniProt AC	Q9UIF9
Protein Name	Bromodomain adjacent to zinc finger domain protein 2A
Gene Name	BAZ2A
Organism	Homo sapiens (Human).
Sequence Length	1905
Subcellular Localization	Nucleus, nucleolus. Colocalizes with the basal RNA polymerase I transcription factor UBF in the nucleolus..
Protein Description	Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription. Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac. Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA-binding is required for heterochromatin formation and rDNA silencing (By similarity)..
Protein Sequence	MEMEANDHFNFTGLPPAPAASGLKPSPSSGEGLYTNGSPMNFPQQGKSLNGDVNVNGLSTVSHTTTSGILNSAPHSSSTSHLHHPSVAYDCLWNYSQYPSANPGSNLKDPPLLSQFSGGQYPLNGILGGSRQPSSPSHNTNLRAGSQEFWANGTQSPMGLNFDSQELYDSFPDQNFEVMPNGPPSFFTSPQTSPMLGSSIQTFAPSQEVGSGIHPDEAAEKEMTSVVAENGTGLVGSLELEEEQPELKMCGYNGSVPSVESLHQEVSVLVPDPTVSCLDDPSHLPDQLEDTPILSEDSLEPFNSLAPEPVSGGLYGIDDTELMGAEDKLPLEDSPVISALDCPSLNNATAFSLLADDSQTSTSIFASPTSPPVLGESVLQDNSFDLNNGSDAEQEEMETQSSDFPPSLTQPAPDQSSTIQLHPATSPAVSPTTSPAVSLVVSPAASPEISPEVCPAASTVVSPAVFSVVSPASSAVLPAVSLEVPLTASVTSPKASPVTSPAAAFPTASPANKDVSSFLETTADVEEITGEGLTASGSGDVMRRRIATPEEVRLPLQHGWRREVRIKKGSHRWQGETWYYGPCGKRMKQFPEVIKYLSRNVVHSVRREHFSFSPRMPVGDFFEERDTPEGLQWVQLSAEEIPSRIQAITGKRGRPRNTEKAKTKEVPKVKRGRGRPPKVKITELLNKTDNRPLKKLEAQETLNEEDKAKIAKSKKKMRQKVQRGECQTTIQGQARNKRKQETKSLKQKEAKKKSKAEKEKGKTKQEKLKEKVKREKKEKVKMKEKEEVTKAKPACKADKTLATQRRLEERQRQQMILEEMKKPTEDMCLTDHQPLPDFSRVPGLTLPSGAFSDCLTIVEFLHSFGKVLGFDPAKDVPSLGVLQEGLLCQGDSLGEVQDLLVRLLKAALHDPGFPSYCQSLKILGEKVSEIPLTRDNVSEILRCFLMAYGVEPALCDRLRTQPFQAQPPQQKAAVLAFLVHELNGSTLIINEIDKTLESMSSYRKNKWIVEGRLRRLKTVLAKRTGRSEVEMEGPEECLGRRRSSRIMEETSGMEEEEEEESIAAVPGRRGRRDGEVDATASSIPELERQIEKLSKRQLFFRKKLLHSSQMLRAVSLGQDRYRRRYWVLPYLAGIFVEGTEGNLVPEEVIKKETDSLKVAAHASLNPALFSMKMELAGSNTTASSPARARGRPRKTKPGSMQPRHLKSPVRGQDSEQPQAQLQPEAQLHAPAQPQPQLQLQLQSHKGFLEQEGSPLSLGQSQHDLSQSAFLSWLSQTQSHSSLLSSSVLTPDSSPGKLDPAPSQPPEEPEPDEAESSPDPQALWFNISAQMPCNAAPTPPPAVSEDQPTPSPQQLASSKPMNRPSAANPCSPVQFSSTPLAGLAPKRRAGDPGEMPQSPTGLGQPKRRGRPPSKFFKQMEQRYLTQLTAQPVPPEMCSGWWWIRDPEMLDAMLKALHPRGIREKALHKHLNKHRDFLQEVCLRPSADPIFEPRQLPAFQEGIMSWSPKEKTYETDLAVLQWVEELEQRVIMSDLQIRGWTCPSPDSTREDLAYCEHLSDSQEDITWRGRGREGLAPQRKTTNPLDLAVMRLAALEQNVERRYLREPLWPTHEVVLEKALLSTPNGAPEGTTTEISYEITPRIRVWRQTLERCRSAAQVCLCLGQLERSIAWEKSVNKVTCLVCRKGDNDEFLLLCDGCDRGCHIYCHRPKMEAVPEGDWFCTVCLAQQVEGEFTQKPGFPKRGQKRKSGYSLNFSEGDGRRRRVLLRGRESPAAGPRYSEEGLSPSKRRRLSMRNHHSDLTFCEIILMEMESHDAAWPFLEPVNPRLVSGYRRIIKNPMDFSTMRERLLRGGYTSSEEFAADALLVFDNCQTFNEDDSEVGKAGHIMRRFFESRWEEFYQGKQANL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Phosphorylation	LPPAPAASGLKPSPS CCCCCCCCCCCCCCC	46.92	26074081
26	Phosphorylation	AASGLKPSPSSGEGL CCCCCCCCCCCCCCC	35.51	26074081
28	Phosphorylation	SGLKPSPSSGEGLYT CCCCCCCCCCCCCCC	56.14	26074081
29	Phosphorylation	GLKPSPSSGEGLYTN CCCCCCCCCCCCCCC	44.22	26074081
34	Phosphorylation	PSSGEGLYTNGSPMN CCCCCCCCCCCCCCC	14.71	26074081
35	Phosphorylation	SSGEGLYTNGSPMNF CCCCCCCCCCCCCCC	37.84	25627689
38	Phosphorylation	EGLYTNGSPMNFPQQ CCCCCCCCCCCCCCC	24.05	25159151
67	Phosphorylation	TVSHTTTSGILNSAP ECEEECCCCHHHCCC	23.03	-
114	Phosphorylation	LKDPPLLSQFSGGQY CCCCCHHHHCCCCCC	36.54	23090842
117	Phosphorylation	PPLLSQFSGGQYPLN CCHHHHCCCCCCCCC	34.08	23090842
121	Phosphorylation	SQFSGGQYPLNGILG HHCCCCCCCCCCCCC	16.98	23090842
130	Phosphorylation	LNGILGGSRQPSSPS CCCCCCCCCCCCCCC	26.41	23090842
134	Phosphorylation	LGGSRQPSSPSHNTN CCCCCCCCCCCCCCC	46.68	30266825
135	Phosphorylation	GGSRQPSSPSHNTNL CCCCCCCCCCCCCCC	36.79	23401153
137	Phosphorylation	SRQPSSPSHNTNLRA CCCCCCCCCCCCCCC	31.17	30266825
137 (in isoform 2)	Phosphorylation	-	31.17	21406692
138 (in isoform 2)	Phosphorylation	-	48.82	21406692
140	Phosphorylation	PSSPSHNTNLRAGSQ CCCCCCCCCCCCCCC	30.15	23403867
154	Phosphorylation	QEFWANGTQSPMGLN CCHHHCCCCCCCCCC	26.19	26074081
156	Phosphorylation	FWANGTQSPMGLNFD HHHCCCCCCCCCCCC	19.38	26074081
311	Phosphorylation	SLAPEPVSGGLYGID HCCCCCCCCCCCCCC	37.55	26074081
315	Phosphorylation	EPVSGGLYGIDDTEL CCCCCCCCCCCHHHC	18.47	26074081
352	Phosphorylation	LNNATAFSLLADDSQ CCCHHHHHHHCCCCC	21.73	26074081
358	Phosphorylation	FSLLADDSQTSTSIF HHHHCCCCCCCCCEE	35.59	26074081
360	Phosphorylation	LLADDSQTSTSIFAS HHCCCCCCCCCEECC	37.61	26074081
361	Phosphorylation	LADDSQTSTSIFASP HCCCCCCCCCEECCC	16.72	26074081
367	Phosphorylation	TSTSIFASPTSPPVL CCCCEECCCCCCCCC	20.26	26074081
369	Phosphorylation	TSIFASPTSPPVLGE CCEECCCCCCCCCCC	51.90	26074081
370	Phosphorylation	SIFASPTSPPVLGES CEECCCCCCCCCCCC	30.50	26074081
469	Phosphorylation	SPAVFSVVSPASSAV CCHHHCCCCCCCCCC	5.70	15302935
473 (in isoform 2)	Phosphorylation	-	23.39	21406692
480 (in isoform 2)	Phosphorylation	-	6.74	21406692
482 (in isoform 2)	Phosphorylation	-	6.55	21406692
487	Phosphorylation	VSLEVPLTASVTSPK EEEEEEEEEEECCCC	15.71	26074081
489	Phosphorylation	LEVPLTASVTSPKAS EEEEEEEEECCCCCC	22.23	26074081
491	Phosphorylation	VPLTASVTSPKASPV EEEEEEECCCCCCCC	36.50	26074081
492	Phosphorylation	PLTASVTSPKASPVT EEEEEECCCCCCCCC	23.42	26074081
494	Phosphorylation	TASVTSPKASPVTSP EEEECCCCCCCCCCC	62.35	18669648
496	Phosphorylation	SVTSPKASPVTSPAA EECCCCCCCCCCCCH	26.48	30266825
499	Phosphorylation	SPKASPVTSPAAAFP CCCCCCCCCCCHHCC	32.17	30266825
500	O-linked_Glycosylation	PKASPVTSPAAAFPT CCCCCCCCCCHHCCC	16.87	30379171
500	Phosphorylation	PKASPVTSPAAAFPT CCCCCCCCCCHHCCC	16.87	30266825
507	Phosphorylation	SPAAAFPTASPANKD CCCHHCCCCCCCCCC	33.06	30266825
509	Phosphorylation	AAAFPTASPANKDVS CHHCCCCCCCCCCHH	27.33	30266825
513	Acetylation	PTASPANKDVSSFLE CCCCCCCCCHHHHHH	62.71	26051181
516	Phosphorylation	SPANKDVSSFLETTA CCCCCCHHHHHHHCC	26.04	26074081
517	Phosphorylation	PANKDVSSFLETTAD CCCCCHHHHHHHCCC	33.43	26074081
521	Phosphorylation	DVSSFLETTADVEEI CHHHHHHHCCCHHHH	29.45	18669648
548	O-linked_Glycosylation	VMRRRIATPEEVRLP HHHCCCCCHHHCCCC	28.94	30379171
548	Phosphorylation	VMRRRIATPEEVRLP HHHCCCCCHHHCCCC	28.94	30266825
568	Ubiquitination	RREVRIKKGSHRWQG EEEEEEECCCCCCCC	64.37	-
585	Acetylation	WYYGPCGKRMKQFPE EEECCCCHHHHHHHH	56.91	26051181
585	Methylation	WYYGPCGKRMKQFPE EEECCCCHHHHHHHH	56.91	-
595	Ubiquitination	KQFPEVIKYLSRNVV HHHHHHHHHHHHHHH	45.36	21906983
604	Phosphorylation	LSRNVVHSVRREHFS HHHHHHHHHHHHHCC	13.00	-
611	Phosphorylation	SVRREHFSFSPRMPV HHHHHHCCCCCCCCC	27.07	22617229
613	Phosphorylation	RREHFSFSPRMPVGD HHHHCCCCCCCCCHH	15.48	26055452
649	Phosphorylation	PSRIQAITGKRGRPR CHHHHHHHCCCCCCC	39.40	-
651	Acetylation	RIQAITGKRGRPRNT HHHHHHCCCCCCCCC	42.92	25953088
680	Acetylation	RGRPPKVKITELLNK CCCCCCCCHHHHCCC	50.46	19578370
687	Acetylation	KITELLNKTDNRPLK CHHHHCCCCCCCCCH	58.17	23236377
688	Phosphorylation	ITELLNKTDNRPLKK HHHHCCCCCCCCCHH	37.12	28555341
695	Sumoylation	TDNRPLKKLEAQETL CCCCCCHHHHHHHHC	60.28	-
695	Sumoylation	TDNRPLKKLEAQETL CCCCCCHHHHHHHHC	60.28	-
701	Phosphorylation	KKLEAQETLNEEDKA HHHHHHHHCCHHHHH	23.85	24173317
707	Acetylation	ETLNEEDKAKIAKSK HHCCHHHHHHHHHHH	55.66	23236377
737	Acetylation	IQGQARNKRKQETKS HHHHHHHHHHHHHHH	56.25	7367297
739	Acetylation	GQARNKRKQETKSLK HHHHHHHHHHHHHHH	54.84	7367309
742	O-linked_Glycosylation	RNKRKQETKSLKQKE HHHHHHHHHHHHHHH	24.36	30379171
767	Acetylation	KGKTKQEKLKEKVKR HCCHHHHHHHHHHHH	63.47	7258197
799	Acetylation	KPACKADKTLATQRR CHHCHHCHHHHHHHH	50.74	25953088
800	Phosphorylation	PACKADKTLATQRRL HHCHHCHHHHHHHHH	23.36	29759185
803	Phosphorylation	KADKTLATQRRLEER HHCHHHHHHHHHHHH	26.22	29759185
866	Sumoylation	EFLHSFGKVLGFDPA HHHHHHHHHHCCCCC	32.07	28112733
921	Acetylation	PSYCQSLKILGEKVS HHHHHHHHHHCCCCC	40.92	26051181
928	Phosphorylation	KILGEKVSEIPLTRD HHHCCCCCCCCCCCC	40.66	21406692
995	Phosphorylation	IINEIDKTLESMSSY EEHHHHHHHHHHHHH	31.82	-
1006	Acetylation	MSSYRKNKWIVEGRL HHHHHCCCHHHHHHH	41.13	25953088
1023 (in isoform 2)	Phosphorylation	-	36.48	21406692
1024	Phosphorylation	KTVLAKRTGRSEVEM HHHHHHHHCCCCCEE	35.92	21712546
1024 (in isoform 2)	Phosphorylation	-	35.92	21406692
1027	Phosphorylation	LAKRTGRSEVEMEGP HHHHHCCCCCEECCH	47.54	21712546
1043	Phosphorylation	ECLGRRRSSRIMEET HHHCCHHHHHHHHHC	23.35	-
1044	Phosphorylation	CLGRRRSSRIMEETS HHCCHHHHHHHHHCC	24.82	-
1050	Phosphorylation	SSRIMEETSGMEEEE HHHHHHHCCCCCHHH	19.78	30266825
1051	Phosphorylation	SRIMEETSGMEEEEE HHHHHHCCCCCHHHH	39.15	23401153
1061	Phosphorylation	EEEEEEESIAAVPGR CHHHHHHHHCCCCCC	22.32	30278072
1125	Phosphorylation	QDRYRRRYWVLPYLA CHHHHHHHCHHHHHE	9.69	21118733
1130	Phosphorylation	RRYWVLPYLAGIFVE HHHCHHHHHEEEEEE	12.67	21118733
1150	Sumoylation	LVPEEVIKKETDSLK CCCHHHHHHCCCCHH	50.13	28112733
1163	Phosphorylation	LKVAAHASLNPALFS HHHHHHHHCCHHHHH	20.86	28111955
1170	Phosphorylation	SLNPALFSMKMELAG HCCHHHHHHHEECCC	20.53	24719451
1172	Sumoylation	NPALFSMKMELAGSN CHHHHHHHEECCCCC	28.20	-
1172	Sumoylation	NPALFSMKMELAGSN CHHHHHHHEECCCCC	28.20	28112733
1178	Phosphorylation	MKMELAGSNTTASSP HHEECCCCCCCCCCC	25.95	23403867
1180	Phosphorylation	MELAGSNTTASSPAR EECCCCCCCCCCCHH	25.99	23403867
1180 (in isoform 2)	Phosphorylation	-	25.99	21406692
1181	Phosphorylation	ELAGSNTTASSPARA ECCCCCCCCCCCHHH	28.88	23403867
1183	Phosphorylation	AGSNTTASSPARARG CCCCCCCCCCHHHCC	34.46	30266825
1184	Phosphorylation	GSNTTASSPARARGR CCCCCCCCCHHHCCC	21.81	30266825
1195	Phosphorylation	ARGRPRKTKPGSMQP HCCCCCCCCCCCCCC	43.69	23828894
1207	Phosphorylation	MQPRHLKSPVRGQDS CCCCCCCCCCCCCCC	34.68	30266825
1210	Methylation	RHLKSPVRGQDSEQP CCCCCCCCCCCCCCC	40.20	-
1214	Phosphorylation	SPVRGQDSEQPQAQL CCCCCCCCCCCCHHC	30.18	30576142
1243	Phosphorylation	QLQLQLQSHKGFLEQ CHHHHHHHHCCHHHC	35.44	24144214
1343	Phosphorylation	PTPPPAVSEDQPTPS CCCCCCCCCCCCCCC	37.25	18669648
1350	Phosphorylation	SEDQPTPSPQQLASS CCCCCCCCHHHHHCC	37.51	26657352
1364	Phosphorylation	SKPMNRPSAANPCSP CCCCCCCCCCCCCCC	36.45	30576142
1370	Phosphorylation	PSAANPCSPVQFSST CCCCCCCCCCCCCCC	29.39	25159151
1370 (in isoform 2)	Phosphorylation	-	29.39	21406692
1372 (in isoform 2)	Phosphorylation	-	5.29	21406692
1375	Phosphorylation	PCSPVQFSSTPLAGL CCCCCCCCCCCCCCC	19.06	22199227
1376	Phosphorylation	CSPVQFSSTPLAGLA CCCCCCCCCCCCCCC	35.02	22199227
1377	Phosphorylation	SPVQFSSTPLAGLAP CCCCCCCCCCCCCCC	22.56	30576142
1397	Phosphorylation	DPGEMPQSPTGLGQP CCCCCCCCCCCCCCC	20.68	29255136
1399	Phosphorylation	GEMPQSPTGLGQPKR CCCCCCCCCCCCCCC	50.73	29255136
1467	Ubiquitination	IREKALHKHLNKHRD HHHHHHHHHHHHCHH	51.11	-
1503	Phosphorylation	AFQEGIMSWSPKEKT HHHHCCCCCCCCCCC	23.60	28348404
1505	Phosphorylation	QEGIMSWSPKEKTYE HHCCCCCCCCCCCHH	20.84	27050516
1531	Phosphorylation	LEQRVIMSDLQIRGW HHHHHHHCCCEECCE	24.84	20068231
1532	Phosphorylation	EQRVIMSDLQIRGWT HHHHHHCCCEECCEE	25.80	17525332
1539	Phosphorylation	DLQIRGWTCPSPDST CCEECCEECCCCCCC	19.84	30266825
1542	Phosphorylation	IRGWTCPSPDSTRED ECCEECCCCCCCHHH	43.41	30266825
1545	Phosphorylation	WTCPSPDSTREDLAY EECCCCCCCHHHHHH	32.52	23663014
1546	Phosphorylation	TCPSPDSTREDLAYC ECCCCCCCHHHHHHC	45.52	23663014
1552	Phosphorylation	STREDLAYCEHLSDS CCHHHHHHCCCCCCC	12.98	30266825
1557	Phosphorylation	LAYCEHLSDSQEDIT HHHCCCCCCCCCCCC	36.80	30266825
1559	Phosphorylation	YCEHLSDSQEDITWR HCCCCCCCCCCCCCC	31.90	17525332
1564	Phosphorylation	SDSQEDITWRGRGRE CCCCCCCCCCCCCCC	22.79	30108239
1579	Phosphorylation	GLAPQRKTTNPLDLA CCCCCCCCCCHHHHH	33.71	20068231
1580	Phosphorylation	LAPQRKTTNPLDLAV CCCCCCCCCHHHHHH	37.56	20068231
1620	Phosphorylation	VLEKALLSTPNGAPE HHHHHHHCCCCCCCC	42.54	27050516
1621	Phosphorylation	LEKALLSTPNGAPEG HHHHHHCCCCCCCCC	22.27	22199227
1629	Phosphorylation	PNGAPEGTTTEISYE CCCCCCCCCEEEEEE	28.96	22199227
1630	Phosphorylation	NGAPEGTTTEISYEI CCCCCCCCEEEEEEE	33.03	22199227
1631	Phosphorylation	GAPEGTTTEISYEIT CCCCCCCEEEEEEEC	31.03	26714015
1634	Phosphorylation	EGTTTEISYEITPRI CCCCEEEEEEECHHH	15.52	20068231
1635	Phosphorylation	GTTTEISYEITPRIR CCCEEEEEEECHHHH	19.60	20068231
1672	Ubiquitination	ERSIAWEKSVNKVTC HHHHHHHHCCCEEEE	49.34	-
1672 (in isoform 3)	Ubiquitination	-	49.34	21890473
1676	Sumoylation	AWEKSVNKVTCLVCR HHHHCCCEEEEEEEE	36.44	28112733
1676	Ubiquitination	AWEKSVNKVTCLVCR HHHHCCCEEEEEEEE	36.44	21890473
1676 (in isoform 1)	Ubiquitination	-	36.44	21890473
1709	Sumoylation	HIYCHRPKMEAVPEG EEEECCCCCCCCCCC	49.70	28112733
1746	Acetylation	PKRGQKRKSGYSLNF CCCCCCCCCCEECCC	56.09	20167786
1747	Phosphorylation	KRGQKRKSGYSLNFS CCCCCCCCCEECCCC	47.17	25159151
1749	Phosphorylation	GQKRKSGYSLNFSEG CCCCCCCEECCCCCC	19.64	22199227
1750	Phosphorylation	QKRKSGYSLNFSEGD CCCCCCEECCCCCCC	21.99	25159151
1754	Phosphorylation	SGYSLNFSEGDGRRR CCEECCCCCCCCCCE	39.33	23403867
1756 (in isoform 2)	Phosphorylation	-	41.28	21406692
1758 (in isoform 2)	Phosphorylation	-	35.53	21406692
1768	Methylation	RRVLLRGRESPAAGP EEEEECCCCCCCCCC	34.48	-
1770	Phosphorylation	VLLRGRESPAAGPRY EEECCCCCCCCCCCC	20.62	30266825
1776	Methylation	ESPAAGPRYSEEGLS CCCCCCCCCCCCCCC	46.84	-
1777	Phosphorylation	SPAAGPRYSEEGLSP CCCCCCCCCCCCCCH	24.46	23927012
1778	Phosphorylation	PAAGPRYSEEGLSPS CCCCCCCCCCCCCHH	30.37	23927012
1783	Phosphorylation	RYSEEGLSPSKRRRL CCCCCCCCHHHHHHH	37.67	29255136
1785	Phosphorylation	SEEGLSPSKRRRLSM CCCCCCHHHHHHHHC	35.10	30266825
1786	Acetylation	EEGLSPSKRRRLSMR CCCCCHHHHHHHHCC	53.99	25953088
1786	Ubiquitination	EEGLSPSKRRRLSMR CCCCCHHHHHHHHCC	53.99	-
1787	Methylation	EGLSPSKRRRLSMRN CCCCHHHHHHHHCCH	33.03	-
1841	Phosphorylation	IKNPMDFSTMRERLL HCCCCCHHHHHHHHH	19.61	23403867
1842	Phosphorylation	KNPMDFSTMRERLLR CCCCCHHHHHHHHHC	21.90	23403867
1901	Ubiquitination	WEEFYQGKQANL--- HHHHHCHHHCCC---	30.61	21906983

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
509	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
680	K	Acetylation		19578370
Acetylation at Lys-680 by KAT8/MOF promotes its dissociation from pRNA, affecting heterochromatin formation, nucleosome positioning and rDNA silencing.

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 BAZ2A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMCA5_HUMAN	SMARCA5	physical	11532953
KAT8_HUMAN	KAT8	physical	19578370
SMCA5_HUMAN	SMARCA5	physical	19578370
HDAC1_HUMAN	HDAC1	physical	16085498
DNMT1_HUMAN	DNMT1	physical	16085498
DNM3B_HUMAN	DNMT3B	physical	16085498
SMCA5_HUMAN	SMARCA5	physical	16085498
BEND3_HUMAN	BEND3	physical	26100909
UBP21_HUMAN	USP21	physical	26100909

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of BAZ2A_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Reversible acetylation of the chromatin remodelling complex NoRC isrequired for non-coding RNA-dependent silencing."; Zhou Y., Schmitz K.M., Mayer C., Yuan X., Akhtar A., Grummt I.; Nat. Cell Biol. 11:1010-1016(2009). Cited for: ACETYLATION AT LYS-680.	19578370 [Abstract]
Phosphorylation
Reference	PubMed
"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 THR-1050; SER-1051; SER-1397AND SER-1783, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-509; SER-1184; SER-1397AND SER-1783, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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 THR-548; SER-1747; SER-1770;SER-1778 AND SER-1783, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1397, AND MASSSPECTROMETRY.	18691976 [Abstract]
"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 THR-548 AND SER-1747, ANDMASS SPECTROMETRY.	19007248 [Abstract]
"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-1559, AND MASSSPECTROMETRY.	17525332 [Abstract]
"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-1397, AND MASSSPECTROMETRY.	17081983 [Abstract]
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