SMCA5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SMCA5_HUMAN
• UniProt AC: O60264
• Protein Name: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5
• Gene Name: SMARCA5
• Organism: Homo sapiens (Human).
• Sequence Length: 1052
• Subcellular Localization: Nucleus .
• Protein Description: Helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity. Complexes containing SMARCA5 are capable of forming ordered nucleosome arrays on chromatin; this may require intact histone H4 tails. Also required for replication of pericentric heterochromatin in S-phase specifically in conjunction with BAZ1A. Probably plays a role in repression of polI dependent transcription of the rDNA locus, through the recruitment of the SIN3/HDAC1 corepressor complex to the rDNA promoter. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. 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..
• Protein Sequence: MSSAAEPPPPPPPESAPSKPAASIASGGSNSSNKGGPEGVAAQAVASAASAGPADAEMEEIFDDASPGKQKEIQEPDPTYEEKMQTDRANRFEYLLKQTELFAHFIQPAAQKTPTSPLKMKPGRPRIKKDEKQNLLSVGDYRHRRTEQEEDEELLTESSKATNVCTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVCLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPKKEVKIYVGLSKMQREWYTRILMKDIDILNSAGKMDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDMHLVTNSGKMVVLDKLLPKLKEQGSRVLIFSQMTRVLDILEDYCMWRNYEYCRLDGQTPHDERQDSINAYNEPNSTKFVFMLSTRAGGLGINLATADVVILYDSDWNPQVDLQAMDRAHRIGQTKTVRVFRFITDNTVEERIVERAEMKLRLDSIVIQQGRLVDQNLNKIGKDEMLQMIRHGATHVFASKESEITDEDIDGILERGAKKTAEMNEKLSKMGESSLRNFTMDTESSVYNFEGEDYREKQKIAFTEWIEPPKRERKANYAVDAYFREALRVSEPKAPKAPRPPKQPNVQDFQFFPPRLFELLEKEILFYRKTIGYKVPRNPELPNAAQAQKEEQLKIDEAESLNDEELEEKEKLLTQGFTNWNKRDFNQFIKANEKWGRDDIENIAREVEGKTPEEVIEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDTKIGRYKAPFHQLRISYGTNKGKNYTEEEDRFLICMLHKLGFDKENVYDELRQCIRNSPQFRFDWFLKSRTAMELQRRCNTLITLIERENMELEEKEKAEKKKRGPKPSTQKRKMDGAPDGRGRKKKLKL

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
2	Acetylation	------MSSAAEPPP ------CCCCCCCCC	39.73	18491316
2	Phosphorylation	------MSSAAEPPP ------CCCCCCCCC	39.73	29116813
3	Phosphorylation	-----MSSAAEPPPP -----CCCCCCCCCC	43.27	29116813
23	Phosphorylation	APSKPAASIASGGSN CCCCCCCCCCCCCCC	22.31	25159151
26	Phosphorylation	KPAASIASGGSNSSN CCCCCCCCCCCCCCC	41.85	25159151
29	Phosphorylation	ASIASGGSNSSNKGG CCCCCCCCCCCCCCC	36.74	25849741
31	Phosphorylation	IASGGSNSSNKGGPE CCCCCCCCCCCCCCH	36.66	30576142
32	Phosphorylation	ASGGSNSSNKGGPEG CCCCCCCCCCCCCHH	46.97	30576142
47	Phosphorylation	VAAQAVASAASAGPA HHHHHHHHHHHCCCC	20.12	23401153
50	Phosphorylation	QAVASAASAGPADAE HHHHHHHHCCCCCHH	33.21	30278072
66	Phosphorylation	EEIFDDASPGKQKEI HHHHCCCCCCCCCCC	40.97	29255136
71	Acetylation	DASPGKQKEIQEPDP CCCCCCCCCCCCCCC	61.34	26051181
71	Ubiquitination	DASPGKQKEIQEPDP CCCCCCCCCCCCCCC	61.34	33845483
79	Phosphorylation	EIQEPDPTYEEKMQT CCCCCCCCHHHHHHH	51.44	22210691
80	Phosphorylation	IQEPDPTYEEKMQTD CCCCCCCHHHHHHHH	27.72	28796482
83	Sumoylation	PDPTYEEKMQTDRAN CCCCHHHHHHHHHHH	25.11	-
83	Sumoylation	PDPTYEEKMQTDRAN CCCCHHHHHHHHHHH	25.11	28112733
83	Ubiquitination	PDPTYEEKMQTDRAN CCCCHHHHHHHHHHH	25.11	21906983
86	Phosphorylation	TYEEKMQTDRANRFE CHHHHHHHHHHHHHH	24.77	29978859
94	Phosphorylation	DRANRFEYLLKQTEL HHHHHHHHHHHHHHH	18.02	28152594
97	Ubiquitination	NRFEYLLKQTELFAH HHHHHHHHHHHHHHH	53.21	23503661
99	Phosphorylation	FEYLLKQTELFAHFI HHHHHHHHHHHHHHH	32.82	28176443
112	Acetylation	FIQPAAQKTPTSPLK HHHHHHHCCCCCCCC	52.31	25953088
113	Phosphorylation	IQPAAQKTPTSPLKM HHHHHHCCCCCCCCC	21.51	22167270
115	Phosphorylation	PAAQKTPTSPLKMKP HHHHCCCCCCCCCCC	48.48	29255136
116	Phosphorylation	AAQKTPTSPLKMKPG HHHCCCCCCCCCCCC	29.46	29255136
128	Ubiquitination	KPGRPRIKKDEKQNL CCCCCCCCHHHHCCC	56.29	22817900
129	Acetylation	PGRPRIKKDEKQNLL CCCCCCCHHHHCCCC	69.61	25953088
129	Ubiquitination	PGRPRIKKDEKQNLL CCCCCCCHHHHCCCC	69.61	22817900
132	Acetylation	PRIKKDEKQNLLSVG CCCCHHHHCCCCCHH	55.40	7298799
132	Ubiquitination	PRIKKDEKQNLLSVG CCCCHHHHCCCCCHH	55.40	22817900
137	Phosphorylation	DEKQNLLSVGDYRHR HHHCCCCCHHCCCCC	27.50	28355574
141	Phosphorylation	NLLSVGDYRHRRTEQ CCCCHHCCCCCCCCH	11.46	23403867
146	Phosphorylation	GDYRHRRTEQEEDEE HCCCCCCCCHHHHHH	41.81	28555341
156	Phosphorylation	EEDEELLTESSKATN HHHHHHHHHHHHCCC	46.58	30108239
158	Phosphorylation	DEELLTESSKATNVC HHHHHHHHHHCCCCC	31.72	23312004
159	Phosphorylation	EELLTESSKATNVCT HHHHHHHHHCCCCCC	21.78	21130716
160	Acetylation	ELLTESSKATNVCTR HHHHHHHHCCCCCCC	69.39	25953088
160	Ubiquitination	ELLTESSKATNVCTR HHHHHHHHCCCCCCC	69.39	21906983
162	Phosphorylation	LTESSKATNVCTRFE HHHHHHCCCCCCCCC	31.74	30108239
166	Phosphorylation	SKATNVCTRFEDSPS HHCCCCCCCCCCCCC	33.82	30108239
171	Phosphorylation	VCTRFEDSPSYVKWG CCCCCCCCCCHHCCC	14.46	21815630
176	Acetylation	EDSPSYVKWGKLRDY CCCCCHHCCCCCCCC	41.83	25953088
176	Ubiquitination	EDSPSYVKWGKLRDY CCCCCHHCCCCCCCC	41.83	23000965
179	Ubiquitination	PSYVKWGKLRDYQVR CCHHCCCCCCCCCCC	38.95	23000965
212	Phosphorylation	DEMGLGKTLQTISLL HCCCCCHHHHHHHHH	23.46	20068231
223	Acetylation	ISLLGYMKHYRNIPG HHHHHHHHHHCCCCC	29.06	26051181
238	Acetylation	PHMVLVPKSTLHNWM CCEEEEEHHHHHHHH	48.90	26051181
249	Acetylation	HNWMSEFKRWVPTLR HHHHHHHHHHHHHHH	41.10	25825284
254	Phosphorylation	EFKRWVPTLRSVCLI HHHHHHHHHHHHHCC	25.78	20068231
257	Phosphorylation	RWVPTLRSVCLIGDK HHHHHHHHHHCCCCH	21.94	20068231
264	Acetylation	SVCLIGDKEQRAAFV HHHCCCCHHHHHHHH	51.00	23749302
264	Ubiquitination	SVCLIGDKEQRAAFV HHHCCCCHHHHHHHH	51.00	24816145
319	Acetylation	RIKNEKSKLSEIVRE HHHCCHHHHHHHHHH	68.08	25953088
319	Malonylation	RIKNEKSKLSEIVRE HHHCCHHHHHHHHHH	68.08	26320211
319	Ubiquitination	RIKNEKSKLSEIVRE HHHCCHHHHHHHHHH	68.08	24816145
397	Acetylation	PFLLRRIKADVEKSL HHHHHHHHHHHHHCC	36.40	7297737
402	Acetylation	RIKADVEKSLPPKKE HHHHHHHHCCCCCCC	58.08	7297747
418	Ubiquitination	KIYVGLSKMQREWYT EEEEECHHHHHHHHH	44.06	23000965
430	Acetylation	WYTRILMKDIDILNS HHHHHHHHHHHHHHC	48.35	25825284
430	Ubiquitination	WYTRILMKDIDILNS HHHHHHHHHHHHHHC	48.35	21890473
437	Phosphorylation	KDIDILNSAGKMDKM HHHHHHHCCCCCCHH	34.65	21815630
440	Acetylation	DILNSAGKMDKMRLL HHHHCCCCCCHHHHH	43.58	19608861
440	Ubiquitination	DILNSAGKMDKMRLL HHHHCCCCCCHHHHH	43.58	32015554
455	Ubiquitination	NILMQLRKCCNHPYL HHHHHHHHHCCCCCC	52.29	23503661
490	Ubiquitination	GKMVVLDKLLPKLKE CCEEEHHHHHHHHHH	48.00	29967540
506	Phosphorylation	GSRVLIFSQMTRVLD CCEEEEEECHHHHHH	16.43	20068231
509	Phosphorylation	VLIFSQMTRVLDILE EEEEECHHHHHHHHH	15.25	20068231
519	Glutathionylation	LDILEDYCMWRNYEY HHHHHHHHHHCCCCC	3.05	22555962
558	Phosphorylation	TKFVFMLSTRAGGLG CEEEEEEECCCCCCC	12.22	24719451
600	Acetylation	AHRIGQTKTVRVFRF HHHHCCCCEEEEEEE	36.82	23749302
600	Ubiquitination	AHRIGQTKTVRVFRF HHHHCCCCEEEEEEE	36.82	-
644	Sumoylation	LVDQNLNKIGKDEML HHCCCHHHCCHHHHH	56.87	28112733
644	Ubiquitination	LVDQNLNKIGKDEML HHCCCHHHCCHHHHH	56.87	23000965
647	Sumoylation	QNLNKIGKDEMLQMI CCHHHCCHHHHHHHH	54.72	-
647	Acetylation	QNLNKIGKDEMLQMI CCHHHCCHHHHHHHH	54.72	26051181
647	Sumoylation	QNLNKIGKDEMLQMI CCHHHCCHHHHHHHH	54.72	28112733
647	Ubiquitination	QNLNKIGKDEMLQMI CCHHHCCHHHHHHHH	54.72	23000965
665	Acetylation	ATHVFASKESEITDE CCEEEECCCCCCCHH	62.93	25953088
665	Ubiquitination	ATHVFASKESEITDE CCEEEECCCCCCCHH	62.93	32015554
667	Phosphorylation	HVFASKESEITDEDI EEEECCCCCCCHHHH	37.73	22617229
670	Phosphorylation	ASKESEITDEDIDGI ECCCCCCCHHHHHHH	29.32	20873877
683	Acetylation	GILERGAKKTAEMNE HHHHHHHHHHHHHHH	54.18	7704113
683	Ubiquitination	GILERGAKKTAEMNE HHHHHHHHHHHHHHH	54.18	29967540
685	Phosphorylation	LERGAKKTAEMNEKL HHHHHHHHHHHHHHH	27.43	25278378
691	Acetylation	KTAEMNEKLSKMGES HHHHHHHHHHHHCHH	53.72	25953088
691	Ubiquitination	KTAEMNEKLSKMGES HHHHHHHHHHHHCHH	53.72	24816145
693	Phosphorylation	AEMNEKLSKMGESSL HHHHHHHHHHCHHHH	31.50	25278378
694	Sumoylation	EMNEKLSKMGESSLR HHHHHHHHHCHHHHH	62.45	-
694	Acetylation	EMNEKLSKMGESSLR HHHHHHHHHCHHHHH	62.45	25953088
694	Sumoylation	EMNEKLSKMGESSLR HHHHHHHHHCHHHHH	62.45	28112733
694	Ubiquitination	EMNEKLSKMGESSLR HHHHHHHHHCHHHHH	62.45	29967540
698	Phosphorylation	KLSKMGESSLRNFTM HHHHHCHHHHHCCCC	29.01	18669648
699	Phosphorylation	LSKMGESSLRNFTMD HHHHCHHHHHCCCCC	27.35	21815630
704	Phosphorylation	ESSLRNFTMDTESSV HHHHHCCCCCCCCCC	20.07	29214152
707	Phosphorylation	LRNFTMDTESSVYNF HHCCCCCCCCCCCCC	27.26	27251275
709	Phosphorylation	NFTMDTESSVYNFEG CCCCCCCCCCCCCCC	27.48	27690223
710	Phosphorylation	FTMDTESSVYNFEGE CCCCCCCCCCCCCCC	23.53	27251275
712	Phosphorylation	MDTESSVYNFEGEDY CCCCCCCCCCCCCCH	18.97	27251275
719	Phosphorylation	YNFEGEDYREKQKIA CCCCCCCHHHHHEEE	19.17	-
722	Sumoylation	EGEDYREKQKIAFTE CCCCHHHHHEEEEEC	48.14	28112733
722	Ubiquitination	EGEDYREKQKIAFTE CCCCHHHHHEEEEEC	48.14	22817900
724	Ubiquitination	EDYREKQKIAFTEWI CCHHHHHEEEEECCC	47.25	21906983
735	Acetylation	TEWIEPPKRERKANY ECCCCCCHHHHHHHH	77.07	26051181
735	Sumoylation	TEWIEPPKRERKANY ECCCCCCHHHHHHHH	77.07	28112733
735	Ubiquitination	TEWIEPPKRERKANY ECCCCCCHHHHHHHH	77.07	23000965
739	Sumoylation	EPPKRERKANYAVDA CCCHHHHHHHHHHHH	35.91	-
739	Sumoylation	EPPKRERKANYAVDA CCCHHHHHHHHHHHH	35.91	-
739	Ubiquitination	EPPKRERKANYAVDA CCCHHHHHHHHHHHH	35.91	23000965
742	Phosphorylation	KRERKANYAVDAYFR HHHHHHHHHHHHHHH	16.92	28152594
747	Phosphorylation	ANYAVDAYFREALRV HHHHHHHHHHHHHHC	9.94	21406692
755	Phosphorylation	FREALRVSEPKAPKA HHHHHHCCCCCCCCC	41.57	25159151
767	Acetylation	PKAPRPPKQPNVQDF CCCCCCCCCCCCCCC	79.61	26051181
798	Phosphorylation	FYRKTIGYKVPRNPE HHHCCCCCCCCCCCC	12.64	-
799	Acetylation	YRKTIGYKVPRNPEL HHCCCCCCCCCCCCC	40.32	25953088
799	Ubiquitination	YRKTIGYKVPRNPEL HHCCCCCCCCCCCCC	40.32	29967540
814	Acetylation	PNAAQAQKEEQLKID CCHHHHHHHHHHCHH	67.26	26051181
814	Ubiquitination	PNAAQAQKEEQLKID CCHHHHHHHHHHCHH	67.26	21906983
819	Acetylation	AQKEEQLKIDEAESL HHHHHHHCHHHHHHC	48.05	26051181
819	Ubiquitination	AQKEEQLKIDEAESL HHHHHHHCHHHHHHC	48.05	22817900
825	Phosphorylation	LKIDEAESLNDEELE HCHHHHHHCCHHHHH	39.25	29255136
834	Acetylation	NDEELEEKEKLLTQG CHHHHHHHHHHHHHC	51.26	26051181
834	Sumoylation	NDEELEEKEKLLTQG CHHHHHHHHHHHHHC	51.26	-
834	Ubiquitination	NDEELEEKEKLLTQG CHHHHHHHHHHHHHC	51.26	23000965
836	Ubiquitination	EELEEKEKLLTQGFT HHHHHHHHHHHHCCC	60.92	23000965
847	Acetylation	QGFTNWNKRDFNQFI HCCCCCCHHHHHHHH	44.98	25953088
847	Ubiquitination	QGFTNWNKRDFNQFI HCCCCCCHHHHHHHH	44.98	22817900
855	Acetylation	RDFNQFIKANEKWGR HHHHHHHHHCHHHCH	46.58	25953088
855	Ubiquitination	RDFNQFIKANEKWGR HHHHHHHHHCHHHCH	46.58	29967540
859	Acetylation	QFIKANEKWGRDDIE HHHHHCHHHCHHHHH	55.55	26051181
901	Sulfoxidation	LQDIEKIMAQIERGE HHHHHHHHHHHHHHH	3.13	21406390
916	Phosphorylation	ARIQRRISIKKALDT HHHHHHHCHHHHHHC	26.92	20068231
923	Phosphorylation	SIKKALDTKIGRYKA CHHHHHHCCCCCCCC	25.97	20068231
924	Ubiquitination	IKKALDTKIGRYKAP HHHHHHCCCCCCCCC	42.71	22817900
928	Phosphorylation	LDTKIGRYKAPFHQL HHCCCCCCCCCCHHE	13.29	28152594
929	Sumoylation	DTKIGRYKAPFHQLR HCCCCCCCCCCHHEE	48.50	-
929	Acetylation	DTKIGRYKAPFHQLR HCCCCCCCCCCHHEE	48.50	26051181
929	Sumoylation	DTKIGRYKAPFHQLR HCCCCCCCCCCHHEE	48.50	-
929	Ubiquitination	DTKIGRYKAPFHQLR HCCCCCCCCCCHHEE	48.50	22817900
945	Acetylation	SYGTNKGKNYTEEED EECCCCCCCCCHHHH	48.68	26051181
945	Ubiquitination	SYGTNKGKNYTEEED EECCCCCCCCCHHHH	48.68	-
947	Phosphorylation	GTNKGKNYTEEEDRF CCCCCCCCCHHHHHH	21.00	-
961	Ubiquitination	FLICMLHKLGFDKEN HHHHHHHHCCCCHHH	46.47	29967540
966	Acetylation	LHKLGFDKENVYDEL HHHCCCCHHHHHHHH	49.26	26051181
966	Sumoylation	LHKLGFDKENVYDEL HHHCCCCHHHHHHHH	49.26	28112733
970	Phosphorylation	GFDKENVYDELRQCI CCCHHHHHHHHHHHH	18.45	28152594
974	Methylation	ENVYDELRQCIRNSP HHHHHHHHHHHHCCC	27.55	115917189
990	Acetylation	FRFDWFLKSRTAMEL CCHHHHHHCHHHHHH	28.55	26051181
1003	Phosphorylation	ELQRRCNTLITLIER HHHHHHHHHHHHHHH	24.14	21406692
1006	Phosphorylation	RRCNTLITLIERENM HHHHHHHHHHHHHCC	25.46	21406692
1018	Ubiquitination	ENMELEEKEKAEKKK HCCCHHHHHHHHHHH	55.96	-
1025	Ubiquitination	KEKAEKKKRGPKPST HHHHHHHHCCCCCCH	73.91	24816145
1031	Phosphorylation	KKRGPKPSTQKRKMD HHCCCCCCHHHCCCC	49.98	24719451
1044	Methylation	MDGAPDGRGRKKKLK CCCCCCCCCCCCCCC	49.47	80701415
1049	Acetylation	DGRGRKKKLKL---- CCCCCCCCCCC----	54.62	7266247

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SMCA5_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SMCA5_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SMCA5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BAZ1A_HUMAN	BAZ1A	physical	10655480
BAZ1A_HUMAN	BAZ1A	physical	10880450
DPOE3_HUMAN	POLE3	physical	10880450
CHRC1_HUMAN	CHRAC1	physical	10880450
BAZ1A_HUMAN	BAZ1A	physical	11980720
BAZ1B_HUMAN	BAZ1B	physical	11980720
BAZ1A_HUMAN	BAZ1A	physical	12374985
SATB1_HUMAN	SATB1	physical	12374985
BAZ1A_HUMAN	BAZ1A	physical	12198550
RAD21_HUMAN	RAD21	physical	12198550
HDAC2_HUMAN	HDAC2	physical	12198550
RBBP4_HUMAN	RBBP4	physical	12198550
CHD3_HUMAN	CHD3	physical	12198550
SMC1A_HUMAN	SMC1A	physical	12198550
SMC3_HUMAN	SMC3	physical	12198550
MAF_HUMAN	MAF	physical	16675956
CREB1_HUMAN	CREB1	physical	16675956
MYO1C_HUMAN	MYO1C	physical	16514417
SIN3A_HUMAN	SIN3A	physical	18535655
HDAC2_HUMAN	HDAC2	physical	15775975
MCM3_HUMAN	MCM3	physical	15775975
H2A2B_HUMAN	HIST2H2AB	physical	11691835
H31_HUMAN	HIST1H3A	physical	11691835
DNMT1_HUMAN	DNMT1	physical	15313181
DNM3B_HUMAN	DNMT3B	physical	15120635
CECR2_HUMAN	CECR2	physical	22154806
CDT1_HUMAN	CDT1	physical	21937426
CEBPB_HUMAN	CEBPB	physical	22242598
SMRC2_HUMAN	SMARCC2	physical	22939629
SMRC1_HUMAN	SMARCC1	physical	22939629
RN168_HUMAN	RNF168	physical	23264744
RSF1_HUMAN	RSF1	physical	12972596
BAZ1A_HUMAN	BAZ1A	physical	10747848
RSF1_HUMAN	RSF1	physical	10747848
SMCA5_HUMAN	SMARCA5	physical	10747848
CHRC1_HUMAN	CHRAC1	physical	26344197
CSN3_HUMAN	COPS3	physical	26344197
HDAC2_HUMAN	HDAC2	physical	26344197
INO80_HUMAN	INO80	physical	26344197
IPO9_HUMAN	IPO9	physical	26344197
DPOE3_HUMAN	POLE3	physical	26344197
RPAC1_HUMAN	POLR1C	physical	26344197
RPC1_HUMAN	POLR3A	physical	26344197
RBBP4_HUMAN	RBBP4	physical	26344197
RUVB1_HUMAN	RUVBL1	physical	26344197
BAZ1A_HUMAN	BAZ1A	physical	25533843
BEND3_HUMAN	BEND3	physical	26100909
BAZ1B_HUMAN	BAZ1B	physical	23555303
MYO1C_HUMAN	MYO1C	physical	23555303
RSF1_HUMAN	RSF1	physical	26666816

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.

Related Literatures of Post-Translational Modification

Acetylation

"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-440, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-66, AND MASSSPECTROMETRY.
PubMed: 19690332

"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-116, AND MASSSPECTROMETRY.
PubMed: 19413330

"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 SER-66; THR-113; SER-116 ANDSER-137, AND MASS SPECTROMETRY.
PubMed: 18669648

"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-66; THR-113 AND SER-116,AND MASS SPECTROMETRY.
PubMed: 18691976

"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 SER-66; THR-115; SER-116;SER-699 AND SER-755, AND MASS SPECTROMETRY.
PubMed: 19007248

"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASSSPECTROMETRY.
PubMed: 17693683

"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; THR-113 AND SER-755,AND MASS SPECTROMETRY.
PubMed: 16565220

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASSSPECTROMETRY.
PubMed: 16964243

"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-66; THR-113 AND SER-116,AND MASS SPECTROMETRY.
PubMed: 17081983

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASSSPECTROMETRY.
PubMed: 15302935