dbPTM

SMCA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SMCA2_HUMAN
UniProt AC	P51531
Protein Name	Probable global transcription activator SNF2L2
Gene Name	SMARCA2 {ECO:0000312\|HGNC:HGNC:11098}
Organism	Homo sapiens (Human).
Sequence Length	1590
Subcellular Localization	Nucleus.
Protein Description	Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Binds DNA non-specifically. [PubMed: 22952240]
Protein Sequence	MSTPTDPGAMPHPGPSPGPGPSPGPILGPSPGPGPSPGSVHSMMGPSPGPPSVSHPMPTMGSTDFPQEGMHQMHKPIDGIHDKGIVEDIHCGSMKGTGMRPPHPGMGPPQSPMDQHSQGYMSPHPSPLGAPEHVSSPMSGGGPTPPQMPPSQPGALIPGDPQAMSQPNRGPSPFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQGKRTLPGLQQQQQQQQQQQQQQQQQQQQQQQPQQQPPQPQTQQQQQPALVNYNRPSGPGPELSGPSTPQKLPVPAPGGRPSPAPPAAAQPPAAAVPGPSVPQPAPGQPSPVLQLQQKQSRISPIQKPQGLDPVEILQEREYRLQARIAHRIQELENLPGSLPPDLRTKATVELKALRLLNFQRQLRQEVVACMRRDTTLETALNSKAYKRSKRQTLREARMTEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMAEDEEGYRKLIDQKKDRRLAYLLQQTDEYVANLTNLVWEHKQAQAAKEKKKRRRRKKKAEENAEGGESALGPDGEPIDESSQMSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPRSDSEESDSDYEEEDEEEESSRQETEEKILLDPNSEEVSEKDAKQIIETAKQDVDDEYSMQYSARGSQSYYTVAHAISERVEKQSALLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHKVLRPFLLRRLKKEVESQLPEKVEYVIKCDMSALQKILYRHMQAKGILLTDGSEKDKKGKGGAKTLMNTIMQLRKICNHPYMFQHIEESFAEHLGYSNGVINGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPGSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEENEEEDEVPDDETLNQMIARREEEFDLFMRMDMDRRREDARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKIFGRGSRQRRDVDYSDALTEKQWLRAIEDGNLEEMEEEVRLKKRKRRRNVDKDPAKEDVEKAKKRRGRPPAEKLSPNPPKLTKQMNAIIDTVINYKDRCNVEKVPSNSQLEIEGNSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKIAKEEESEDESNEEEEEEDEEESESEAKSVKVKIKLNKKDDKGRDKGKGKKRPNRGKAKPVVSDFDSDEEQDEREQSEGSGTDDE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
93	Phosphorylation	VEDIHCGSMKGTGMR EEEEECCCCCCCCCC	23.79	23401153
172	Phosphorylation	SQPNRGPSPFSPVQL CCCCCCCCCCCHHHH	41.21	30266825
175	Phosphorylation	NRGPSPFSPVQLHQL CCCCCCCCHHHHHHH	27.78	30266825
190	Acetylation	RAQILAYKMLARGQP HHHHHHHHHHHCCCC	23.10	26051181
194	Methylation	LAYKMLARGQPLPET HHHHHHHCCCCCCHH	40.08	115917169
263	Phosphorylation	LVNYNRPSGPGPELS EECCCCCCCCCCCCC	55.15	23312004
270	Phosphorylation	SGPGPELSGPSTPQK CCCCCCCCCCCCCCC	47.17	29255136
273	Phosphorylation	GPELSGPSTPQKLPV CCCCCCCCCCCCCCC	57.13	29255136
274	Phosphorylation	PELSGPSTPQKLPVP CCCCCCCCCCCCCCC	32.64	29255136
288	Phosphorylation	PAPGGRPSPAPPAAA CCCCCCCCCCCCHHH	32.12	28348404
316	Phosphorylation	QPAPGQPSPVLQLQQ CCCCCCCCCCHHHHH	21.54	27067055
322	Phosphorylation	PSPVLQLQQKQSRIS CCCCHHHHHHHHCCC	35.15	17081983
325	Phosphorylation	VLQLQQKQSRISPIQ CHHHHHHHHCCCCCC	33.34	17081983
326	Phosphorylation	LQLQQKQSRISPIQK HHHHHHHHCCCCCCC	38.32	23401153
329	Phosphorylation	QQKQSRISPIQKPQG HHHHHCCCCCCCCCC	18.16	29255136
333	Acetylation	SRISPIQKPQGLDPV HCCCCCCCCCCCCHH	39.77	26051181
333	Ubiquitination	SRISPIQKPQGLDPV HCCCCCCCCCCCCHH	39.77	-
381	Ubiquitination	TKATVELKALRLLNF CCHHHHHHHHHHHHH	31.69	-
408	Phosphorylation	RRDTTLETALNSKAY HCCCHHHHHHCCHHH	39.29	-
413	Acetylation	LETALNSKAYKRSKR HHHHHCCHHHHHHHH	55.45	26051181
413	Ubiquitination	LETALNSKAYKRSKR HHHHHCCHHHHHHHH	55.45	21890473
413 (in isoform 1)	Ubiquitination	-	55.45	21890473
413 (in isoform 2)	Ubiquitination	-	55.45	21890473
415	Phosphorylation	TALNSKAYKRSKRQT HHHCCHHHHHHHHHH	15.63	-
416	Acetylation	ALNSKAYKRSKRQTL HHCCHHHHHHHHHHH	55.87	26051181
431	Acetylation	REARMTEKLEKQQKI HHHHHHHHHHHHHHH	53.43	26051181
437	Acetylation	EKLEKQQKIEQERKR HHHHHHHHHHHHHHH	45.80	23749302
447	Acetylation	QERKRRQKHQEYLNS HHHHHHHHHHHHHHH	45.50	26051181
447	Ubiquitination	QERKRRQKHQEYLNS HHHHHHHHHHHHHHH	45.50	-
460	Acetylation	NSILQHAKDFKEYHR HHHHHHHHHHHHHHH	62.67	25953088
463	Ubiquitination	LQHAKDFKEYHRSVA HHHHHHHHHHHHHHH	68.45	-
472	Ubiquitination	YHRSVAGKIQKLSKA HHHHHHHHHHHHHHH	32.02	-
505	Methylation	IEKERMRRLMAEDEE HHHHHHHHHHHCCHH	21.33	-
514	Phosphorylation	MAEDEEGYRKLIDQK HHCCHHHHHHHHHHH	14.09	21406692
541	Phosphorylation	DEYVANLTNLVWEHK HHHHHHHHHHHHHHH	26.72	-
575	Phosphorylation	ENAEGGESALGPDGE HHCCCCCCCCCCCCC	31.88	23403867
587	Phosphorylation	DGEPIDESSQMSDLP CCCCCCCCCCCCCCC	23.32	23401153
588	Phosphorylation	GEPIDESSQMSDLPV CCCCCCCCCCCCCCC	28.05	30266825
591	Phosphorylation	IDESSQMSDLPVKVT CCCCCCCCCCCCEEE	28.49	23927012
604	Acetylation	VTHTETGKVLFGPEA EEECCCCCEEECCCC	43.09	23954790
604	Ubiquitination	VTHTETGKVLFGPEA EEECCCCCEEECCCC	43.09	21890473
604 (in isoform 1)	Ubiquitination	-	43.09	21890473
604 (in isoform 2)	Ubiquitination	-	43.09	21890473
611	Phosphorylation	KVLFGPEAPKASQLD CEEECCCCCCHHHHH	17.64	17081983
615	Phosphorylation	GPEAPKASQLDAWLE CCCCCCHHHHHHHHH	37.08	17081983
627	Phosphorylation	WLEMNPGYEVAPRSD HHHCCCCCCCCCCCC	14.42	17081983
633	Phosphorylation	GYEVAPRSDSEESDS CCCCCCCCCCCCCCC	44.42	22817900
638	Phosphorylation	PRSDSEESDSDYEEE CCCCCCCCCCCCCCC	38.06	17081983
640	Phosphorylation	SDSEESDSDYEEEDE CCCCCCCCCCCCCHH	51.91	17081983
642	Phosphorylation	SEESDSDYEEEDEEE CCCCCCCCCCCHHHH	29.23	17081983
651	Phosphorylation	EEDEEEESSRQETEE CCHHHHHHHHHHHHH	33.82	17081983
652	Phosphorylation	EDEEEESSRQETEEK CHHHHHHHHHHHHHH	41.06	17081983
666	Phosphorylation	KILLDPNSEEVSEKD HHHCCCCCHHCCHHH	40.29	30266825
670	Phosphorylation	DPNSEEVSEKDAKQI CCCCHHCCHHHHHHH	42.06	30266825
672	Acetylation	NSEEVSEKDAKQIIE CCHHCCHHHHHHHHH	56.32	23236377
680	Phosphorylation	DAKQIIETAKQDVDD HHHHHHHHHHHCCCC	28.84	28985074
689	Phosphorylation	KQDVDDEYSMQYSAR HHCCCCHHHHCHHCC	19.21	24043423
690	Phosphorylation	QDVDDEYSMQYSARG HCCCCHHHHCHHCCC	9.43	24043423
693	Phosphorylation	DDEYSMQYSARGSQS CCHHHHCHHCCCCCH	8.82	24043423
694	Phosphorylation	DEYSMQYSARGSQSY CHHHHCHHCCCCCHH	8.46	24043423
698	Phosphorylation	MQYSARGSQSYYTVA HCHHCCCCCHHHHHH	15.48	25849741
700	Phosphorylation	YSARGSQSYYTVAHA HHCCCCCHHHHHHHH	23.08	27080861
701	Phosphorylation	SARGSQSYYTVAHAI HCCCCCHHHHHHHHH	8.77	28985074
756	Phosphorylation	DEMGLGKTIQTIALI HCCCCCHHHHHHHHH	19.27	21406692
759	Phosphorylation	GLGKTIQTIALITYL CCCHHHHHHHHHHHH	12.36	21406692
764	Phosphorylation	IQTIALITYLMEHKR HHHHHHHHHHHHHCC	16.08	21406692
765	Phosphorylation	QTIALITYLMEHKRL HHHHHHHHHHHHCCC	9.32	21406692
803	Phosphorylation	APSVVKISYKGTPAM CCCEEEEEECCCHHH	18.31	27174698
804	Phosphorylation	PSVVKISYKGTPAMR CCEEEEEECCCHHHH	19.53	27174698
807	Phosphorylation	VKISYKGTPAMRRSL EEEEECCCHHHHHHH	12.06	27174698
820	Phosphorylation	SLVPQLRSGKFNVLL HHHHHHHCCCCCEEE	55.73	29083192
828	Phosphorylation	GKFNVLLTTYEYIIK CCCCEEEEEHHHHHC	24.15	25954137
829	Phosphorylation	KFNVLLTTYEYIIKD CCCEEEEEHHHHHCC	17.83	24719451
830	Phosphorylation	FNVLLTTYEYIIKDK CCEEEEEHHHHHCCC	11.08	24719451
832	Phosphorylation	VLLTTYEYIIKDKHI EEEEEHHHHHCCCHH	9.49	25954137
842	Ubiquitination	KDKHILAKIRWKYMI CCCHHHHEEEEEEEE	29.38	-
862	Acetylation	RMKNHHCKLTQVLNT HHCCCCCCCHHHHCC	50.65	25953088
880	Phosphorylation	APRRILLTGTPLQNK CCCEEECCCCCHHHC	35.25	20068231
882	Phosphorylation	RRILLTGTPLQNKLP CEEECCCCCHHHCHH	18.65	20068231
931	Phosphorylation	VDLNEEETILIIRRL CCCCHHHHHHHHHHH	25.10	28555341
940	Acetylation	LIIRRLHKVLRPFLL HHHHHHHHHHHHHHH	47.78	26051181
956	Phosphorylation	RLKKEVESQLPEKVE HHHHHHHHCCCHHHH	42.04	17081983
961	Acetylation	VESQLPEKVEYVIKC HHHCCCHHHHHHHCC	38.13	26051181
961	Ubiquitination	VESQLPEKVEYVIKC HHHCCCHHHHHHHCC	38.13	-
967	Acetylation	EKVEYVIKCDMSALQ HHHHHHHCCCHHHHH	17.71	26051181
967	Ubiquitination	EKVEYVIKCDMSALQ HHHHHHHCCCHHHHH	17.71	-
971	Phosphorylation	YVIKCDMSALQKILY HHHCCCHHHHHHHHH	16.75	-
978	Phosphorylation	SALQKILYRHMQAKG HHHHHHHHHHHHHCC	11.27	18083107
996	Acetylation	TDGSEKDKKGKGGAK CCCCCCCCCCCCHHH	74.60	68845
997	Acetylation	DGSEKDKKGKGGAKT CCCCCCCCCCCHHHH	75.81	19608861
999	Acetylation	SEKDKKGKGGAKTLM CCCCCCCCCHHHHHH	64.15	19608861
1003	Acetylation	KKGKGGAKTLMNTIM CCCCCHHHHHHHHHH	45.53	68857
1004	Phosphorylation	KGKGGAKTLMNTIMQ CCCCHHHHHHHHHHH	30.61	-
1008	Phosphorylation	GAKTLMNTIMQLRKI HHHHHHHHHHHHHHH	12.12	-
1020	Phosphorylation	RKICNHPYMFQHIEE HHHCCCHHHHHHHHH	11.74	-
1035	Phosphorylation	SFAEHLGYSNGVING HHHHHHCCCCCCCCH	12.81	-
1046	Phosphorylation	VINGAELYRASGKFE CCCHHHHHHHCCCHH	8.81	-
1051	Acetylation	ELYRASGKFELLDRI HHHHHCCCHHHHHHH	32.92	26051181
1051	Ubiquitination	ELYRASGKFELLDRI HHHHHCCCHHHHHHH	32.92	21890473
1051 (in isoform 1)	Ubiquitination	-	32.92	21890473
1051 (in isoform 2)	Ubiquitination	-	32.92	21890473
1057	Methylation	GKFELLDRILPKLRA CCHHHHHHHHHHHHH	32.11	-
1102	Phosphorylation	RLDGTTKSEDRAALL EECCCCCCHHHHHHH	42.51	28258704
1183	Acetylation	TVNSVEEKILAAAKY ECCCHHHHHHHHHHH	29.52	26051181
1183	Ubiquitination	TVNSVEEKILAAAKY ECCCHHHHHHHHHHH	29.52	-
1189	Acetylation	EKILAAAKYKLNVDQ HHHHHHHHHCCCCCH	37.89	25953088
1189	Ubiquitination	EKILAAAKYKLNVDQ HHHHHHHHHCCCCCH	37.89	-
1190	Phosphorylation	KILAAAKYKLNVDQK HHHHHHHHCCCCCHH	18.91	-
1191	Ubiquitination	ILAAAKYKLNVDQKV HHHHHHHCCCCCHHH	32.64	-
1197	Sumoylation	YKLNVDQKVIQAGMF HCCCCCHHHHHHCCC	36.52	-
1197	Sumoylation	YKLNVDQKVIQAGMF HCCCCCHHHHHHCCC	36.52	-
1197	Ubiquitination	YKLNVDQKVIQAGMF HCCCCCHHHHHHCCC	36.52	-
1203	Sulfoxidation	QKVIQAGMFDQKSSS HHHHHHCCCCCCCCH	3.62	21406390
1207	Acetylation	QAGMFDQKSSSHERR HHCCCCCCCCHHHHH	54.90	25953088
1207	Ubiquitination	QAGMFDQKSSSHERR HHCCCCCCCCHHHHH	54.90	-
1208	Phosphorylation	AGMFDQKSSSHERRA HCCCCCCCCHHHHHH	31.29	21406692
1209	Phosphorylation	GMFDQKSSSHERRAF CCCCCCCCHHHHHHH	42.63	21406692
1210	Phosphorylation	MFDQKSSSHERRAFL CCCCCCCHHHHHHHH	36.14	21406692
1271	Acetylation	DARNPKRKPRLMEED HHCCCCCCCCCCCCC	40.39	12429859
1282	Phosphorylation	MEEDELPSWIIKDDA CCCCCCCCEEECCHH	43.46	22199227
1286	Sumoylation	ELPSWIIKDDAEVER CCCCEEECCHHHHEE	40.18	-
1286	Ubiquitination	ELPSWIIKDDAEVER CCCCEEECCHHHHEE	40.18	21906983
1286 (in isoform 1)	Ubiquitination	-	40.18	21890473
1286 (in isoform 2)	Ubiquitination	-	40.18	21890473
1295	Phosphorylation	DAEVERLTCEEEEEK HHHHEEECCHHHHHH	24.88	25159151
1302	Acetylation	TCEEEEEKIFGRGSR CCHHHHHHHCCCCCC	46.76	27452117
1302	Ubiquitination	TCEEEEEKIFGRGSR CCHHHHHHHCCCCCC	46.76	-
1308	Phosphorylation	EKIFGRGSRQRRDVD HHHCCCCCCCCCCCC	24.71	27251275
1316	Phosphorylation	RQRRDVDYSDALTEK CCCCCCCHHHHCCHH	14.32	27642862
1323	Ubiquitination	YSDALTEKQWLRAIE HHHHCCHHHHHHHHH	41.35	21890473
1323 (in isoform 1)	Ubiquitination	-	41.35	21890473
1323 (in isoform 2)	Ubiquitination	-	41.35	21890473
1337	Sulfoxidation	EDGNLEEMEEEVRLK HCCCHHHHHHHHHHH	6.00	21406390
1373	Phosphorylation	KRRGRPPAEKLSPNP HHCCCCCHHHCCCCC	29.28	17081983
1377	Phosphorylation	RPPAEKLSPNPPKLT CCCHHHCCCCCCHHH	33.43	22167270
1384	Phosphorylation	SPNPPKLTKQMNAII CCCCCHHHHHHHHHH	25.92	23403867
1393 (in isoform 2)	Phosphorylation	-	16.93	27251275
1400 (in isoform 2)	Phosphorylation	-	15.12	17081983
1401 (in isoform 2)	Phosphorylation	-	10.83	17081983
1406	Phosphorylation	DRCNVEKVPSNSQLE HHCCCEECCCCCCEE	3.88	17525332
1406 (in isoform 2)	Phosphorylation	-	3.88	27251275
1408	Phosphorylation	CNVEKVPSNSQLEIE CCCEECCCCCCEEEE	52.69	-
1410	Phosphorylation	VEKVPSNSQLEIEGN CEECCCCCCEEEECC	40.24	26657352
1414 (in isoform 2)	Phosphorylation	-	12.81	27251275
1418	Phosphorylation	QLEIEGNSSGRQLSE CEEEECCCCCCCCEE	45.05	17081983
1419	Phosphorylation	LEIEGNSSGRQLSEV EEEECCCCCCCCEEE	41.83	17081983
1432	Phosphorylation	EVFIQLPSRKELPEY EEEEECCCCCCCHHH	65.66	-
1434	Acetylation	FIQLPSRKELPEYYE EEECCCCCCCHHHHH	68.86	26051181
1434	Ubiquitination	FIQLPSRKELPEYYE EEECCCCCCCHHHHH	68.86	-
1439	Phosphorylation	SRKELPEYYELIRKP CCCCCHHHHHHHHCC	10.57	-
1508	Phosphorylation	SARQKIAKEEESEDE HHHHHHHHHHHCCCC	69.96	18669648
1512	Phosphorylation	KIAKEEESEDESNEE HHHHHHHCCCCCCHH	54.34	20164059
1516	Phosphorylation	EEESEDESNEEEEEE HHHCCCCCCHHHHHH	62.96	20164059
1528	Phosphorylation	EEEDEEESESEAKSV HHHHHHHCHHHHHHH	50.10	30278072
1530	Phosphorylation	EDEEESESEAKSVKV HHHHHCHHHHHHHEE	52.73	23927012
1537	Acetylation	SEAKSVKVKIKLNKK HHHHHHEEEEECCCC	7.90	14657023
1538	Acetylation	EAKSVKVKIKLNKKD HHHHHEEEEECCCCC	28.53	14657023
1544	Acetylation	VKIKLNKKDDKGRDK EEEECCCCCCCCCCC	70.82	14657023
1546	Acetylation	IKLNKKDDKGRDKGK EECCCCCCCCCCCCC	65.28	14657023
1547	Acetylation	KLNKKDDKGRDKGKG ECCCCCCCCCCCCCC	67.01	88949
1551	Acetylation	KDDKGRDKGKGKKRP CCCCCCCCCCCCCCC	62.25	19666589
1553	Acetylation	DKGRDKGKGKKRPNR CCCCCCCCCCCCCCC	73.61	16916647
1555	Acetylation	GRDKGKGKKRPNRGK CCCCCCCCCCCCCCC	49.44	16916647
1556	Acetylation	RDKGKGKKRPNRGKA CCCCCCCCCCCCCCC	80.09	14657023
1562	Acetylation	KKRPNRGKAKPVVSD CCCCCCCCCCCCCCC	50.42	14657023
1564	Acetylation	RPNRGKAKPVVSDFD CCCCCCCCCCCCCCC	41.66	14657023
1564	Phosphorylation	RPNRGKAKPVVSDFD CCCCCCCCCCCCCCC	41.66	18669648
1568	Phosphorylation	GKAKPVVSDFDSDEE CCCCCCCCCCCCHHH	32.56	29255136
1572	Phosphorylation	PVVSDFDSDEEQDER CCCCCCCCHHHHHHH	47.09	29255136
1582	Phosphorylation	EQDEREQSEGSGTDD HHHHHHHHCCCCCCC	38.89	18669648
1585	Phosphorylation	EREQSEGSGTDDE-- HHHHHCCCCCCCC--	34.17	18669648
1587	Phosphorylation	EQSEGSGTDDE---- HHHCCCCCCCC----	41.81	25849741

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 SMCA2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SMCA2_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 SMCA2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SSXT_HUMAN	SS18	physical	14603256
SMRC1_HUMAN	SMARCC1	physical	11238380
RPB1_HUMAN	POLR2A	physical	11238380
SIN3A_HUMAN	SIN3A	physical	11238380
HDAC1_HUMAN	HDAC1	physical	11238380
HDAC2_HUMAN	HDAC2	physical	11238380
RBBP4_HUMAN	RBBP4	physical	11238380
ESR1_HUMAN	ESR1	physical	9099865
PHB_HUMAN	PHB	physical	12065415
ARI1A_HUMAN	ARID1A	physical	8895581
SMRC2_HUMAN	SMARCC2	physical	8895581
SMRC1_HUMAN	SMARCC1	physical	8895581
RPB1_HUMAN	POLR2A	physical	8895581
SMCE1_HUMAN	SMARCE1	physical	8895581
ACL6A_HUMAN	ACTL6A	physical	8895581
SNF5_HUMAN	SMARCB1	physical	8895581
ARI1B_HUMAN	ARID1B	physical	12200431
ACL6B_MOUSE	Actl6b	physical	12437990
ACL6B_HUMAN	ACTL6B	physical	12437990
RUVB1_HUMAN	RUVBL1	physical	11839798
ACL6A_HUMAN	ACTL6A	physical	11839798
ACL6A_MOUSE	Actl6a	physical	12437990
ACL6A_HUMAN	ACTL6A	physical	12437990
CEBPB_HUMAN	CEBPB	physical	10619021
MYB_HUMAN	MYB	physical	10619021
MECP2_HUMAN	MECP2	physical	15696166
ARI1A_HUMAN	ARID1A	physical	16940996
SMRC2_HUMAN	SMARCC2	physical	16940996
SMRC1_HUMAN	SMARCC1	physical	16940996
SMRC1_HUMAN	SMARCC1	physical	16452305
CDX2_HUMAN	CDX2	physical	19371634
ARI1A_HUMAN	ARID1A	physical	14559996
SMRC2_HUMAN	SMARCC2	physical	14559996
SMRC1_HUMAN	SMARCC1	physical	14559996
ANM5_HUMAN	PRMT5	physical	14559996
SMRD1_HUMAN	SMARCD1	physical	14559996
SMRD2_HUMAN	SMARCD2	physical	14559996
SMCE1_HUMAN	SMARCE1	physical	14559996
ACL6A_HUMAN	ACTL6A	physical	14559996
SNF5_HUMAN	SMARCB1	physical	14559996
SMCA4_HUMAN	SMARCA4	physical	14559996
SIN3A_HUMAN	SIN3A	physical	14559996
HDAC2_HUMAN	HDAC2	physical	14559996
PRP6_HUMAN	PRPF6	physical	16341228
KHDR1_HUMAN	KHDRBS1	physical	16341228
RPB1_HUMAN	POLR2A	physical	16341228
TAF1_HUMAN	TAF1	physical	12453419
CHD3_HUMAN	CHD3	physical	12453419
SIN3A_HUMAN	SIN3A	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
SIN3A_HUMAN	SIN3A	physical	15314177
NR0B2_HUMAN	NR0B2	physical	15314177
PHB_HUMAN	PHB	physical	15141164
NONO_HUMAN	NONO	physical	18042045
SFPQ_HUMAN	SFPQ	physical	18042045
SMCA4_HUMAN	SMARCA4	physical	18042045
SNF5_HUMAN	SMARCB1	physical	18042045
REQU_HUMAN	DPF2	physical	20460684
SMRC1_HUMAN	SMARCC1	physical	20460684
SMRC2_HUMAN	SMARCC2	physical	20460684
SMRD1_HUMAN	SMARCD1	physical	20460684
ACL6A_HUMAN	ACTL6A	physical	20460684
SMCE1_HUMAN	SMARCE1	physical	20460684
ZMAT3_HUMAN	ZMAT3	physical	20460684
BCL7A_HUMAN	BCL7A	physical	20460684
GEMI_HUMAN	GMNN	physical	17261582
CEBPB_HUMAN	CEBPB	physical	17257825
MECP2_HUMAN	MECP2	physical	20093853
CBX5_HUMAN	CBX5	physical	20011120
H33_BOVIN	H3F3A	physical	20011120
H31_HUMAN	HIST1H3A	physical	20011120
EP300_HUMAN	EP300	physical	21079652
CBP_HUMAN	CREBBP	physical	21079652
KAT2B_HUMAN	KAT2B	physical	21079652
NR0B2_HUMAN	NR0B2	physical	21566081
SMRC1_HUMAN	SMARCC1	physical	22939629
SMRC2_HUMAN	SMARCC2	physical	22939629
SMRD1_HUMAN	SMARCD1	physical	22939629
SNF5_HUMAN	SMARCB1	physical	22939629
SMCA4_HUMAN	SMARCA4	physical	22939629
SMCE1_HUMAN	SMARCE1	physical	22939629
SMRD3_HUMAN	SMARCD3	physical	22939629
SMRD2_HUMAN	SMARCD2	physical	22939629
TOP2B_HUMAN	TOP2B	physical	22939629
ARI1A_HUMAN	ARID1A	physical	11318604
TAT_HV1H2	tat	physical	16601680
BEND7_HUMAN	BEND7	physical	25416956
ACL6A_HUMAN	ACTL6A	physical	26344197
BCL7A_HUMAN	BCL7A	physical	26344197
BCL7B_HUMAN	BCL7B	physical	26344197
BCL7C_HUMAN	BCL7C	physical	26344197
REQU_HUMAN	DPF2	physical	26344197
DPF3_HUMAN	DPF3	physical	26344197
FUBP1_HUMAN	FUBP1	physical	26344197
HMGB1_HUMAN	HMGB1	physical	26344197
FUBP2_HUMAN	KHSRP	physical	26344197
RPAC1_HUMAN	POLR1C	physical	26344197
SIN3A_HUMAN	SIN3A	physical	26344197
SNF5_HUMAN	SMARCB1	physical	26344197
SMRC1_HUMAN	SMARCC1	physical	26344197
SMRC2_HUMAN	SMARCC2	physical	26344197
SMRD2_HUMAN	SMARCD2	physical	26344197
SMRD3_HUMAN	SMARCD3	physical	26344197
SSXT_HUMAN	SS18	physical	26344197
BRCA1_HUMAN	BRCA1	physical	27591253
BARD1_HUMAN	BARD1	physical	27591253
SPTA1_HUMAN	SPTA1	physical	16889989

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
601358	Nicolaides-Baraitser syndrome (NCBRS)
181500	Schizophrenia (SCZD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SMCA2_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-604; LYS-997 AND LYS-999,AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1551; LYS-1553 AND LYS-1555,AND MASS SPECTROMETRY.	16916647 [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-329; SER-1512 ANDSER-1516, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1568 AND SER-1572, ANDMASS SPECTROMETRY.	18318008 [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-175; SER-329; SER-1512;SER-1516; SER-1528; SER-1568; SER-1572; SER-1582; SER-1585 ANDTHR-1587, AND MASS SPECTROMETRY.	18669648 [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-1410, 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-329; SER-956; SER-1377;SER-1418; SER-1419; SER-1568 AND SER-1572, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1568 AND SER-1572, ANDMASS SPECTROMETRY.	16097034 [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-591, AND MASSSPECTROMETRY.	15302935 [Abstract]