dbPTM

SIN3A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SIN3A_HUMAN
UniProt AC	Q96ST3
Protein Name	Paired amphipathic helix protein Sin3a
Gene Name	SIN3A {ECO:0000312\|HGNC:HGNC:19353}
Organism	Homo sapiens (Human).
Sequence Length	1273
Subcellular Localization	Nucleus . Nucleus, nucleolus . Recruited to the nucleolus by SAP30L.
Protein Description	Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Involved in he control of the circadian rhythms. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. Cooperates with FOXK1 to regulate cell cycle progression probably by repressing cell cycle inhibitor genes expression (By similarity)..
Protein Sequence	MKRRLDDQESPVYAAQQRRIPGSTEAFPHQHRVLAPAPPVYEAVSETMQSATGIQYSVTPSYQVSAMPQSSGSHGPAIAAVHSSHHHPTAVQPHGGQVVQSHAHPAPPVAPVQGQQQFQRLKVEDALSYLDQVKLQFGSQPQVYNDFLDIMKEFKSQSIDTPGVISRVSQLFKGHPDLIMGFNTFLPPGYKIEVQTNDMVNVTTPGQVHQIPTHGIQPQPQPPPQHPSQPSAQSAPAPAQPAPQPPPAKVSKPSQLQAHTPASQQTPPLPPYASPRSPPVQPHTPVTISLGTAPSLQNNQPVEFNHAINYVNKIKNRFQGQPDIYKAFLEILHTYQKEQRNAKEAGGNYTPALTEQEVYAQVARLFKNQEDLLSEFGQFLPDANSSVLLSKTTAEKVDSVRNDHGGTVKKPQLNNKPQRPSQNGCQIRRHPTGTTPPVKKKPKLLNLKDSSMADASKHGGGTESLFFDKVRKALRSAEAYENFLRCLVIFNQEVISRAELVQLVSPFLGKFPELFNWFKNFLGYKESVHLETYPKERATEGIAMEIDYASCKRLGSSYRALPKSYQQPKCTGRTPLCKEVLNDTWVSFPSWSEDSTFVSSKKTQYEEHIYRCEDERFELDVVLETNLATIRVLEAIQKKLSRLSAEEQAKFRLDNTLGGTSEVIHRKALQRIYADKAADIIDGLRKNPSIAVPIVLKRLKMKEEEWREAQRGFNKVWREQNEKYYLKSLDHQGINFKQNDTKVLRSKSLLNEIESIYDERQEQATEENAGVPVGPHLSLAYEDKQILEDAAALIIHHVKRQTGIQKEDKYKIKQIMHHFIPDLLFAQRGDLSDVEEEEEEEMDVDEATGAVKKHNGVGGSPPKSKLLFSNTAAQKLRGMDEVYNLFYVNNNWYIFMRLHQILCLRLLRICSQAERQIEEENREREWEREVLGIKRDKSDSPAIQLRLKEPMDVDVEDYYPAFLDMVRSLLDGNIDSSQYEDSLREMFTIHAYIAFTMDKLIQSIVRQLQHIVSDEICVQVTDLYLAENNNGATGGQLNTQNSRSLLESTYQRKAEQLMSDENCFKLMFIQSQGQVQLTIELLDTEEENSDDPVEAERWSDYVERYMNSDTTSPELREHLAQKPVFLPRNLRRIRKCQRGREQQEKEGKEGNSKKTMENVDSLDKLECRFKLNSYKMVYVIKSEDYMYRRTALLRAHQSHERVSKRLHQRFQAWVDKWTKEHVPREMAAETSKWLMGEGLEGLVPCTTTCDTETLHFVSINKYRVKYGTVFKAP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	RRLDDQESPVYAAQQ CCCCCCCCHHHHHHH	17.65	25159151
13	Phosphorylation	DDQESPVYAAQQRRI CCCCCHHHHHHHCCC	10.29	21945579
23	Phosphorylation	QQRRIPGSTEAFPHQ HHCCCCCCCCCCCCC	20.09	25159151
24	Phosphorylation	QRRIPGSTEAFPHQH HCCCCCCCCCCCCCC	36.93	28985074
41	Phosphorylation	LAPAPPVYEAVSETM CCCCCCHHHHHHHHH	12.16	-
122	Acetylation	QQQFQRLKVEDALSY HHHHHHCCHHHHHHH	45.85	26051181
122	Sumoylation	QQQFQRLKVEDALSY HHHHHHCCHHHHHHH	45.85	28112733
122	Ubiquitination	QQQFQRLKVEDALSY HHHHHHCCHHHHHHH	45.85	21906983
134	Sumoylation	LSYLDQVKLQFGSQP HHHHHHHCHHCCCCC	30.82	28112733
139	Phosphorylation	QVKLQFGSQPQVYND HHCHHCCCCCHHHHH	39.72	28348404
155	Ubiquitination	LDIMKEFKSQSIDTP HHHHHHHHHCCCCCC	48.99	29967540
158	Phosphorylation	MKEFKSQSIDTPGVI HHHHHHCCCCCCHHH	29.53	23532336
161	Phosphorylation	FKSQSIDTPGVISRV HHHCCCCCCHHHHHH	21.92	21406692
166	Phosphorylation	IDTPGVISRVSQLFK CCCCHHHHHHHHHHC	24.99	21406692
169	Phosphorylation	PGVISRVSQLFKGHP CHHHHHHHHHHCCCC	21.76	23532336
228	Phosphorylation	QPPPQHPSQPSAQSA CCCCCCCCCCCCCCC	53.23	26714015
231	Phosphorylation	PQHPSQPSAQSAPAP CCCCCCCCCCCCCCC	31.16	26714015
234	Phosphorylation	PSQPSAQSAPAPAQP CCCCCCCCCCCCCCC	35.62	26714015
251	O-linked_Glycosylation	QPPPAKVSKPSQLQA CCCCCCCCCHHHCCC	37.84	30059200
251	Phosphorylation	QPPPAKVSKPSQLQA CCCCCCCCCHHHCCC	37.84	28152594
254	Phosphorylation	PAKVSKPSQLQAHTP CCCCCCHHHCCCCCC	47.46	28152594
260	Phosphorylation	PSQLQAHTPASQQTP HHHCCCCCCHHHCCC	24.46	30266825
263	O-linked_Glycosylation	LQAHTPASQQTPPLP CCCCCCHHHCCCCCC	24.83	30059200
263	Phosphorylation	LQAHTPASQQTPPLP CCCCCCHHHCCCCCC	24.83	30266825
266	Phosphorylation	HTPASQQTPPLPPYA CCCHHHCCCCCCCCC	21.16	30266825
272	Phosphorylation	QTPPLPPYASPRSPP CCCCCCCCCCCCCCC	20.12	30266825
274	Phosphorylation	PPLPPYASPRSPPVQ CCCCCCCCCCCCCCC	18.27	30266825
277	Phosphorylation	PPYASPRSPPVQPHT CCCCCCCCCCCCCCC	36.62	30266825
284	O-linked_Glycosylation	SPPVQPHTPVTISLG CCCCCCCCCEEEEEC	26.57	30059200
284	Phosphorylation	SPPVQPHTPVTISLG CCCCCCCCCEEEEEC	26.57	30266825
287	O-linked_Glycosylation	VQPHTPVTISLGTAP CCCCCCEEEEECCCC	13.17	30059200
287	Phosphorylation	VQPHTPVTISLGTAP CCCCCCEEEEECCCC	13.17	23927012
289	O-linked_Glycosylation	PHTPVTISLGTAPSL CCCCEEEEECCCCCC	16.04	30059200
289	Phosphorylation	PHTPVTISLGTAPSL CCCCEEEEECCCCCC	16.04	23927012
292	O-linked_Glycosylation	PVTISLGTAPSLQNN CEEEEECCCCCCCCC	40.46	30059200
292	Phosphorylation	PVTISLGTAPSLQNN CEEEEECCCCCCCCC	40.46	23927012
295	O-linked_Glycosylation	ISLGTAPSLQNNQPV EEECCCCCCCCCCCC	39.87	30059200
295	Phosphorylation	ISLGTAPSLQNNQPV EEECCCCCCCCCCCC	39.87	23927012
310	Phosphorylation	EFNHAINYVNKIKNR CHHHHHHHHHHHHHH	10.17	20873877
337	Ubiquitination	EILHTYQKEQRNAKE HHHHHHHHHHHHHHH	45.46	33845483
343	Ubiquitination	QKEQRNAKEAGGNYT HHHHHHHHHCCCCCC	52.20	32015554
350	Phosphorylation	KEAGGNYTPALTEQE HHCCCCCCCCCCHHH	13.19	26714015
391	Ubiquitination	NSSVLLSKTTAEKVD CCCEEEECCCHHHHH	50.27	29967540
396	Acetylation	LSKTTAEKVDSVRND EECCCHHHHHHCCCC	49.21	25953088
421	Phosphorylation	NNKPQRPSQNGCQIR CCCCCCCCCCCCCCC	38.17	25159151
432	Phosphorylation	CQIRRHPTGTTPPVK CCCCCCCCCCCCCCC	40.82	30266825
434	Phosphorylation	IRRHPTGTTPPVKKK CCCCCCCCCCCCCCC	38.31	30266825
435	Phosphorylation	RRHPTGTTPPVKKKP CCCCCCCCCCCCCCC	27.26	30266825
439	Acetylation	TGTTPPVKKKPKLLN CCCCCCCCCCCCCCC	61.93	25953088
450	Phosphorylation	KLLNLKDSSMADASK CCCCCCCCHHHHHHH	22.04	25159151
451	Phosphorylation	LLNLKDSSMADASKH CCCCCCCHHHHHHHC	28.29	23312004
456	Phosphorylation	DSSMADASKHGGGTE CCHHHHHHHCCCCHH	26.23	27251275
457	Ubiquitination	SSMADASKHGGGTES CHHHHHHHCCCCHHH	48.25	32015554
469	Acetylation	TESLFFDKVRKALRS HHHHHHHHHHHHHHH	38.49	19608861
505	Phosphorylation	AELVQLVSPFLGKFP HHHHHHHHHHHCCCH	20.66	-
524	Phosphorylation	WFKNFLGYKESVHLE HHHHHHCCCCCEECC	17.46	-
539	Phosphorylation	TYPKERATEGIAMEI CCCHHHCCCCCEEEE	40.75	-
558	Phosphorylation	CKRLGSSYRALPKSY HHHCCCCCCCCCHHH	11.12	25884760
563	Sumoylation	SSYRALPKSYQQPKC CCCCCCCHHHCCCCC	63.75	28112733
563	Ubiquitination	SSYRALPKSYQQPKC CCCCCCCHHHCCCCC	63.75	32142685
565	Phosphorylation	YRALPKSYQQPKCTG CCCCCHHHCCCCCCC	19.79	25884760
574	Phosphorylation	QPKCTGRTPLCKEVL CCCCCCCCCCHHHHH	23.20	-
584	Phosphorylation	CKEVLNDTWVSFPSW HHHHHCCCCCCCCCC	27.05	-
601	Acetylation	DSTFVSSKKTQYEEH CCCCCCCCCCHHEEE	52.94	30592395
601	Ubiquitination	DSTFVSSKKTQYEEH CCCCCCCCCCHHEEE	52.94	-
603	Phosphorylation	TFVSSKKTQYEEHIY CCCCCCCCHHEEEEE	39.87	28152594
605	Phosphorylation	VSSKKTQYEEHIYRC CCCCCCHHEEEEEEC	28.63	28152594
610	Phosphorylation	TQYEEHIYRCEDERF CHHEEEEEECCCCCE	15.89	-
638	Acetylation	RVLEAIQKKLSRLSA HHHHHHHHHHHCCCH	49.95	25953088
638	Ubiquitination	RVLEAIQKKLSRLSA HHHHHHHHHHHCCCH	49.95	33845483
639	Ubiquitination	VLEAIQKKLSRLSAE HHHHHHHHHHCCCHH	35.01	-
641	Phosphorylation	EAIQKKLSRLSAEEQ HHHHHHHHCCCHHHH	39.80	-
650	2-Hydroxyisobutyrylation	LSAEEQAKFRLDNTL CCHHHHHHHCCCCCC	30.61	-
650	Acetylation	LSAEEQAKFRLDNTL CCHHHHHHHCCCCCC	30.61	25953088
650	Ubiquitination	LSAEEQAKFRLDNTL CCHHHHHHHCCCCCC	30.61	33845483
673	Phosphorylation	RKALQRIYADKAADI HHHHHHHHHHHHHHH	15.78	22817900
676	Ubiquitination	LQRIYADKAADIIDG HHHHHHHHHHHHHHH	36.98	29967540
686	Ubiquitination	DIIDGLRKNPSIAVP HHHHHHHHCHHCHHH	77.56	33845483
697	Ubiquitination	IAVPIVLKRLKMKEE CHHHHHHHHHCCCHH	44.80	32015554
715	Ubiquitination	EAQRGFNKVWREQNE HHHHCHHHHHHHHHH	40.70	29967540
723	Acetylation	VWREQNEKYYLKSLD HHHHHHHHHCCCCCC	46.90	19608861
723	Ubiquitination	VWREQNEKYYLKSLD HHHHHHHHHCCCCCC	46.90	22817900
727	Acetylation	QNEKYYLKSLDHQGI HHHHHCCCCCCCCCC	32.62	19608861
727	Ubiquitination	QNEKYYLKSLDHQGI HHHHHCCCCCCCCCC	32.62	22817900
737	Acetylation	DHQGINFKQNDTKVL CCCCCCCCCCCHHHH	43.64	25953088
737	Methylation	DHQGINFKQNDTKVL CCCCCCCCCCCHHHH	43.64	115981205
742	Acetylation	NFKQNDTKVLRSKSL CCCCCCHHHHHCHHH	41.98	25953088
742	Ubiquitination	NFKQNDTKVLRSKSL CCCCCCHHHHHCHHH	41.98	22817900
746	Phosphorylation	NDTKVLRSKSLLNEI CCHHHHHCHHHHHHH	23.57	18669648
747	Ubiquitination	DTKVLRSKSLLNEIE CHHHHHCHHHHHHHH	38.39	21906983
748	Phosphorylation	TKVLRSKSLLNEIES HHHHHCHHHHHHHHH	39.06	20873877
755	Phosphorylation	SLLNEIESIYDERQE HHHHHHHHHHHHHHH	31.91	20873877
757	Phosphorylation	LNEIESIYDERQEQA HHHHHHHHHHHHHHH	22.49	-
799	2-Hydroxyisobutyrylation	ALIIHHVKRQTGIQK HHHHHHHHHHHCCCC	34.14	-
802	Phosphorylation	IHHVKRQTGIQKEDK HHHHHHHHCCCCHHH	40.04	-
806	Acetylation	KRQTGIQKEDKYKIK HHHHCCCCHHHHHHH	66.99	21339330
832	Phosphorylation	FAQRGDLSDVEEEEE HHCCCCCHHCCHHHH	44.33	19664994
848	Phosphorylation	EMDVDEATGAVKKHN CCCHHHHHCCHHHCC	24.51	23403867
860	Phosphorylation	KHNGVGGSPPKSKLL HCCCCCCCCCCHHHC	31.91	23401153
864	Phosphorylation	VGGSPPKSKLLFSNT CCCCCCCHHHCCCHH	34.02	23312004
865	Acetylation	GGSPPKSKLLFSNTA CCCCCCHHHCCCHHH	56.17	23954790
865	Ubiquitination	GGSPPKSKLLFSNTA CCCCCCHHHCCCHHH	56.17	29967540
869	Phosphorylation	PKSKLLFSNTAAQKL CCHHHCCCHHHHHHH	32.99	28555341
875	Acetylation	FSNTAAQKLRGMDEV CCHHHHHHHCCCCHH	35.11	23954790
875	Ubiquitination	FSNTAAQKLRGMDEV CCHHHHHHHCCCCHH	35.11	23000965
911	Phosphorylation	LRLLRICSQAERQIE HHHHHHHHHHHHHHH	30.01	28634298
934	Acetylation	EREVLGIKRDKSDSP HHHHHCCCCCCCCCC	53.39	19608861
934	Ubiquitination	EREVLGIKRDKSDSP HHHHHCCCCCCCCCC	53.39	33845483
937	Ubiquitination	VLGIKRDKSDSPAIQ HHCCCCCCCCCCCEE	61.26	24816145
938	Phosphorylation	LGIKRDKSDSPAIQL HCCCCCCCCCCCEEC	47.84	23401153
940	Phosphorylation	IKRDKSDSPAIQLRL CCCCCCCCCCEECCC	24.27	29255136
958	Phosphorylation	MDVDVEDYYPAFLDM CCCCHHHHHHHHHHH	9.61	-
959	Phosphorylation	DVDVEDYYPAFLDMV CCCHHHHHHHHHHHH	10.62	-
1003	Phosphorylation	TMDKLIQSIVRQLQH HHHHHHHHHHHHHHH	18.96	20068231
1044	Phosphorylation	LNTQNSRSLLESTYQ CCHHHHHHHHHHHHH	36.81	27732954
1048	Phosphorylation	NSRSLLESTYQRKAE HHHHHHHHHHHHHHH	32.17	27732954
1049	Phosphorylation	SRSLLESTYQRKAEQ HHHHHHHHHHHHHHH	17.82	27732954
1050	Phosphorylation	RSLLESTYQRKAEQL HHHHHHHHHHHHHHH	18.66	27732954
1053	Ubiquitination	LESTYQRKAEQLMSD HHHHHHHHHHHHCCC	40.53	-
1084	Phosphorylation	LTIELLDTEEENSDD EEEEECCCCCCCCCC	45.31	26657352
1089	Phosphorylation	LDTEEENSDDPVEAE CCCCCCCCCCCCHHH	46.82	26657352
1099	Phosphorylation	PVEAERWSDYVERYM CCHHHHHHHHHHHHH	25.86	21815630
1101	Phosphorylation	EAERWSDYVERYMNS HHHHHHHHHHHHHCC	9.93	27794612
1105	Phosphorylation	WSDYVERYMNSDTTS HHHHHHHHHCCCCCC	6.27	23927012
1106	Sulfoxidation	SDYVERYMNSDTTSP HHHHHHHHCCCCCCH	4.92	21406390
1108	Phosphorylation	YVERYMNSDTTSPEL HHHHHHCCCCCCHHH	21.58	22167270
1110	Phosphorylation	ERYMNSDTTSPELRE HHHHCCCCCCHHHHH	29.06	22167270
1111	Phosphorylation	RYMNSDTTSPELREH HHHCCCCCCHHHHHH	47.47	29255136
1112	Phosphorylation	YMNSDTTSPELREHL HHCCCCCCHHHHHHH	20.61	19664994
1122	Acetylation	LREHLAQKPVFLPRN HHHHHHCCCCCCCHH	37.23	25953088
1122	Ubiquitination	LREHLAQKPVFLPRN HHHHHHCCCCCCCHH	37.23	22817900
1152	Phosphorylation	KEGKEGNSKKTMENV HCCCCCCCHHHHCCH	46.52	26074081
1154	Ubiquitination	GKEGNSKKTMENVDS CCCCCCHHHHCCHHH	53.58	-
1155	Phosphorylation	KEGNSKKTMENVDSL CCCCCHHHHCCHHHH	33.19	26074081
1161	Phosphorylation	KTMENVDSLDKLECR HHHCCHHHHHHHEEE	33.90	25849741
1164	Acetylation	ENVDSLDKLECRFKL CCHHHHHHHEEEEEE	52.02	26051181
1164	Ubiquitination	ENVDSLDKLECRFKL CCHHHHHHHEEEEEE	52.02	29967540
1170	Acetylation	DKLECRFKLNSYKMV HHHEEEEEECCEEEE	27.66	25953088
1170	Ubiquitination	DKLECRFKLNSYKMV HHHEEEEEECCEEEE	27.66	29967540
1173	Phosphorylation	ECRFKLNSYKMVYVI EEEEEECCEEEEEEE	36.24	20068231
1174	Phosphorylation	CRFKLNSYKMVYVIK EEEEECCEEEEEEEE	11.30	20068231
1178	Phosphorylation	LNSYKMVYVIKSEDY ECCEEEEEEEECCHH	7.92	25219547
1182	Phosphorylation	KMVYVIKSEDYMYRR EEEEEEECCHHHHHH	25.28	25219547
1185	Phosphorylation	YVIKSEDYMYRRTAL EEEECCHHHHHHHHH	7.62	25219547
1187	Phosphorylation	IKSEDYMYRRTALLR EECCHHHHHHHHHHH	7.24	25219547
1218	Phosphorylation	QAWVDKWTKEHVPRE HHHHHHHHHHHCCHH	32.09	22210691
1219	Ubiquitination	AWVDKWTKEHVPREM HHHHHHHHHHCCHHH	44.71	29967540
1230	Phosphorylation	PREMAAETSKWLMGE CHHHHHHHHHHHHCC	30.77	22210691
1231	O-linked_Glycosylation	REMAAETSKWLMGEG HHHHHHHHHHHHCCC	17.22	30059200
1231	Phosphorylation	REMAAETSKWLMGEG HHHHHHHHHHHHCCC	17.22	22210691
1232	Ubiquitination	EMAAETSKWLMGEGL HHHHHHHHHHHCCCC	52.33	29967540
1271	Ubiquitination	VKYGTVFKAP----- EEEEEEEECC-----	56.25	29967540

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
434	T	Phosphorylation	Kinase	CHEK1	O14757	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SIN3A_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 SIN3A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC9_HUMAN	HDAC9	physical	11959865
IKZF1_HUMAN	IKZF1	physical	11959865
ARI4B_HUMAN	ARID4B	physical	12724404
HDAC1_HUMAN	HDAC1	physical	12724404
HDAC2_HUMAN	HDAC2	physical	12724404
SDS3_HUMAN	SUDS3	physical	12724404
SAP30_HUMAN	SAP30	physical	12724404
SP130_HUMAN	SAP130	physical	12724404
HCFC1_HUMAN	HCFC1	physical	12670868
SETB1_HUMAN	SETDB1	physical	12398767
HDAC1_HUMAN	HDAC1	physical	12398767
HDAC2_HUMAN	HDAC2	physical	12398767
HDAC1_HUMAN	HDAC1	physical	11931768
PML_HUMAN	PML	physical	11430826
SKI_HUMAN	SKI	physical	11430826
SMCA2_HUMAN	SMARCA2	physical	11238380
SMRC1_HUMAN	SMARCC1	physical	11238380
SMCA4_HUMAN	SMARCA4	physical	11238380
PHB_HUMAN	PHB	physical	12466959
RBBP4_HUMAN	RBBP4	physical	9150133
SAP30_HUMAN	SAP30	physical	9651585
HBP1_HUMAN	HBP1	physical	15235594
MAD1_HUMAN	MXD1	physical	15235594
IKZF1_HUMAN	IKZF1	physical	10357820
HDAC1_HUMAN	HDAC1	physical	9804427
HDAC2_HUMAN	HDAC2	physical	9804427
ZBT16_HUMAN	ZBTB16	physical	9627120
CABIN_HUMAN	CABIN1	physical	10933397
PHF12_HUMAN	PHF12	physical	11390640
IKZF1_HUMAN	IKZF1	physical	12015313
HDAC1_HUMAN	HDAC1	physical	10640275
MAD1_HUMAN	MXD1	physical	11106735
SMCA4_HUMAN	SMARCA4	physical	11784859
SMRC1_HUMAN	SMARCC1	physical	11784859
HDAC1_HUMAN	HDAC1	physical	11784859
RBBP7_HUMAN	RBBP7	physical	11784859
ING1_HUMAN	ING1	physical	11784859
SAP30_HUMAN	SAP30	physical	11784859
RNF12_HUMAN	RLIM	physical	10431247
MNT_HUMAN	MNT	physical	9184233
MAD3_HUMAN	MXD3	physical	9184233
OGT1_HUMAN	OGT	physical	12150998
MECP2_HUMAN	MECP2	physical	9620779
MECP2_HUMAN	MECP2	physical	14593184
HDAC1_HUMAN	HDAC1	physical	14593184
MBD4_HUMAN	MBD4	physical	15899845
NSD2_HUMAN	WHSC1	physical	18156491
GPS2_HUMAN	GPS2	physical	17210713
TBL1X_HUMAN	TBL1X	physical	17210713
NCOR1_HUMAN	NCOR1	physical	17210713
HDAC4_HUMAN	HDAC4	physical	17210713
HS90A_HUMAN	HSP90AA1	physical	17210713
NR0B2_HUMAN	NR0B2	physical	17210713
SMCA4_HUMAN	SMARCA4	physical	19081374
ESR1_HUMAN	ESR1	physical	19620290
SP30L_HUMAN	SAP30L	physical	16820529
ID2_HUMAN	ID2	physical	16776654
OGA_HUMAN	MGEA5	physical	16505006
OGT1_HUMAN	OGT	physical	16505006
SAP25_HUMAN	SAP25	physical	16449650
ANM5_HUMAN	PRMT5	physical	14559996
SMCA4_HUMAN	SMARCA4	physical	14559996
SMCA2_HUMAN	SMARCA2	physical	14559996
SMCE1_HUMAN	SMARCE1	physical	14559996
SNF5_HUMAN	SMARCB1	physical	14559996
PA2G4_HUMAN	PA2G4	physical	16254079
HDAC2_HUMAN	HDAC2	physical	16254079
NFX1_HUMAN	NFX1	physical	18505829
MTG8_HUMAN	RUNX1T1	physical	16227606
MTG8R_HUMAN	CBFA2T2	physical	16227606
TAF1_HUMAN	TAF1	physical	12453419
CHD3_HUMAN	CHD3	physical	12453419
SMCA2_HUMAN	SMARCA2	physical	12453419
SMRC2_HUMAN	SMARCC2	physical	12453419
SMRC1_HUMAN	SMARCC1	physical	12453419
TAF6_HUMAN	TAF6	physical	12453419
HDAC1_HUMAN	HDAC1	physical	12453419
HDAC2_HUMAN	HDAC2	physical	12453419
RBBP4_HUMAN	RBBP4	physical	12453419
RBBP7_HUMAN	RBBP7	physical	12453419
SNF5_HUMAN	SMARCB1	physical	12453419
TBP_HUMAN	TBP	physical	12453419
MBD3_HUMAN	MBD3	physical	12453419
TAF9_HUMAN	TAF9	physical	12453419
SAP30_HUMAN	SAP30	physical	12453419
RAN_HUMAN	RAN	physical	12453419
TGIF1_HUMAN	TGIF1	physical	11682623
MTA2_HUMAN	MTA2	physical	11602581
RBBP4_HUMAN	RBBP4	physical	11602581
HDAC1_HUMAN	HDAC1	physical	11602581
ARI4A_HUMAN	ARID4A	physical	11283269
ING1_HUMAN	ING1	physical	11118440
SAP30_HUMAN	SAP30	physical	11118440
HDAC1_HUMAN	HDAC1	physical	11118440
RBBP4_HUMAN	RBBP4	physical	11118440
SMCA2_HUMAN	SMARCA2	physical	15314177
CSN2_HUMAN	COPS2	physical	15173382
P53_HUMAN	TP53	physical	10521394
HDAC2_HUMAN	HDAC2	physical	18059533
HDAC1_HUMAN	HDAC1	physical	18059533
BCL6_HUMAN	BCL6	physical	9753732
MYB_HUMAN	MYB	physical	14761981
SMN_HUMAN	SMN1	physical	14749338
SFPQ_HUMAN	SFPQ	physical	17452459
RUNX1_HUMAN	RUNX1	physical	14729951
HDAC2_HUMAN	HDAC2	physical	17827154
HDAC1_HUMAN	HDAC1	physical	17827154
CSK21_HUMAN	CSNK2A1	physical	17827154
PHF12_HUMAN	PHF12	physical	21440557
MAD1_HUMAN	MXD1	physical	20547842
IRF5_HUMAN	IRF5	physical	20935208
NR0B2_HUMAN	NR0B2	physical	21566081
LTOR5_HUMAN	LAMTOR5	physical	21706058
SAP30_HUMAN	SAP30	physical	21676866
TAB2_HUMAN	TAB2	physical	16469706
SYUA_HUMAN	SNCA	genetic	16959795
TM1L2_HUMAN	TOM1L2	physical	22939629
THADA_HUMAN	THADA	physical	22939629
TTL12_HUMAN	TTLL12	physical	22939629
P53_HUMAN	TP53	physical	11359905
HDAC1_HUMAN	HDAC1	physical	21258344
RBBP4_HUMAN	RBBP4	physical	21258344
SP30L_HUMAN	SAP30L	physical	21258344
SAP30_HUMAN	SAP30	physical	21258344
BRMS1_HUMAN	BRMS1	physical	21258344
STAT3_HUMAN	STAT3	physical	22783022
CUL4B_HUMAN	CUL4B	physical	25189618
DDB1_HUMAN	DDB1	physical	25189618
BRMS1_HUMAN	BRMS1	physical	23390556
BRMS1_HUMAN	BRMS1	physical	14581478
LOXL2_HUMAN	LOXL2	physical	22483618
T2EB_HUMAN	GTF2E2	physical	26344197
SNAI1_HUMAN	SNAI1	physical	25314079
HDAC1_HUMAN	HDAC1	physical	25314079
HDAC2_HUMAN	HDAC2	physical	25314079

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 SIN3A_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-469; LYS-723; LYS-727 ANDLYS-934, AND MASS SPECTROMETRY.	19608861 [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 SER-10; SER-277; SER-289;SER-832 AND SER-1112, 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-10; SER-1108 ANDSER-1112, 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 SER-10; SER-277; SER-832;SER-940 AND SER-1112, 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-10, AND MASSSPECTROMETRY.	18691976 [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-860, AND MASSSPECTROMETRY.	17081983 [Abstract]
"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-832; SER-860 ANDSER-1112, AND MASS SPECTROMETRY.	15302935 [Abstract]