dbPTM

BRM_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BRM_ARATH
UniProt AC	Q6EVK6
Protein Name	ATP-dependent helicase BRM {ECO:0000303\|PubMed:15371304}
Gene Name	BRM {ECO:0000303\|PubMed:15371304}
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	2193
Subcellular Localization	Nucleus .
Protein Description	ATPase subunit of a multiprotein complex equivalent of the SWI/SNF complex that acts by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. Represses embryonic genes in leaves and controls shoot development and flowering. Activates flower homeotic genes. The association of BRM with its target genes requires REF6. [PubMed: 27111034 Necessary to acquire heat stress (HS) memory, by globally binding to HS memory genes]
Protein Sequence	MQSGGSGGGPARNPAMGPAGRTASTSSAASPSSSSSSVQQQQQQQQQQQQQQQLASRQQQQQHRNSDTNENMFAYQPGGVQGMMGGGNFASSPGSMQMPQQSRNFFESPQQQQQQQQQGSSTQEGQQNFNPMQQAYIQFAMQAQHQKAQQQARMGMVGSSSVGKDQDARMGMLNMQDLNPSSQPQASSSKPSGDQFARGERQTESSSQQRNETKSHPQQQVGTGQLMPGNMIRPMQAPQAQQLVNNMGNNQLAFAQQWQAMQAWARERNIDLSHPANASQMAHILQARMAAQQKAGEGNVASQSPSIPISSQPASSSVVPGENSPHANSASDISGQSGSAKARHALSTGSFASTSSPRMVNPAMNPFSGQGRENPMYPRHLVQPTNGMPSGNPLQTSANETPVLDQNASTKKSLGPAEHLQMQQPRQLNTPTPNLVAPSDTGPLSNSSLQSGQGTQQAQQRSGFTKQQLHVLKAQILAFRRLKKGEGSLPPELLQAISPPPLELQTQRQISPAIGKVQDRSSDKTGEDQARSLECGKESQAAASSNGPIFSKEEDNVGDTEVALTTGHSQLFQNLGKEATSTDVATKEEQQTDVFPVKSDQGADSSTQKNPRSDSTADKGKAVASDGSQSKVPPQANSPQPPKDTASARKYYGPLFDFPFFTRKLDSYGSATANANNNLTLAYDIKDLICEEGAEFLSKKRTDSLKKINGLLAKNLERKRIRPDLVLRLQIEEKKLRLSDLQSRVREEVDRQQQEIMSMPDRPYRKFVRLCERQRLEMNRQVLANQKAVREKQLKTIFQWRKKLLEAHWAIRDARTARNRGVAKYHEKMLREFSKRKDDGRNKRMEALKNNDVERYREMLLEQQTNMPGDAAERYAVLSSFLTQTEDYLHKLGGKITATKNQQEVEEAANAAAVAARLQGLSEEEVRAAATCAREEVVIRNRFTEMNAPKENSSVNKYYTLAHAVNEVVVRQPSMLQAGTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSCIYYVGTKDQRSKLFSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGPAHNIEDDWLETEKKVIVIHRLHQILEPFMLRRRVEDVEGSLPAKVSVVLRCRMSAIQSAVYDWIKATGTLRVDPDDEKLRAQKNPIYQAKIYRTLNNRCMELRKACNHPLLNYPYFNDFSKDFLVRSCGKLWILDRILIKLQRTGHRVLLFSTMTKLLDILEEYLQWRRLVYRRIDGTTSLEDRESAIVDFNDPDTDCFIFLLSIRAAGRGLNLQTADTVVIYDPDPNPKNEEQAVARAHRIGQTREVKVIYMEAVVEKLSSHQKEDELRSGGSVDLEDDMAGKDRYIGSIEGLIRNNIQQYKIDMADEVINAGRFDQRTTHEERRMTLETLLHDEERYQETVHDVPSLHEVNRMIARSEEEVELFDQMDEEFDWTEEMTNHEQVPKWLRASTREVNATVADLSKKPSKNMLSSSNLIVQPGGPGGERKRGRPKSKKINYKEIEDDIAGYSEESSEERNIDSGNEEEGDIRQFDDDELTGALGDHQTNKGEFDGENPVCGYDYPPGSGSYKKNPPRDDAGSSGSSPESHRSKEMASPVSSQKFGSLSALDTRPGSVSKRLLDDLEEGEIAASGDSHIDLQRSGSWAHDRDEGDEEQVLQPTIKRKRSIRLRPRQTAERVDGSEMPAAQPLQVDRSYRSKLRTVVDSHSSRQDQSDSSSRLRSVPAKKVASTSKLHVSSPKSGRLNATQLTVEDNAEASRETWDGTSPISSSNAGARMSHIIQKRCKIVISKLQRRIDKEGQQIVPMLTNLWKRIQNGYAAGGVNNLLELREIDHRVERLEYAGVMELASDVQLMLRGAMQFYGFSHEVRSEAKKVHNLFFDLLKMSFPDTDFREARNALSFSGSAPTLVSTPTPRGAGISQGKRQKLVNEPETEPSSPQRSQQRENSRIRVQIPQKETKLGGTTSHTDESPILAHPGELVICKKKRKDREKSGPKTRTGGSSSPVSPPPAMIGRGLRSPVSGGVPRETRLAQQQRWPNQPTHPNNSGAAGDSVGWANPVKRLRTDSGKRRPSHL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MQSGGSGG -------CCCCCCCC	33.46	22223895
25	Phosphorylation	PAGRTASTSSAASPS CCCCCCCCCCCCCCC	25.00	30407730
26	Phosphorylation	AGRTASTSSAASPSS CCCCCCCCCCCCCCC	18.58	30407730
27	Phosphorylation	GRTASTSSAASPSSS CCCCCCCCCCCCCCC	28.13	30407730
30	Phosphorylation	ASTSSAASPSSSSSS CCCCCCCCCCCCCHH	25.65	30407730
32	Phosphorylation	TSSAASPSSSSSSVQ CCCCCCCCCCCHHHH	40.12	30407730
33	Phosphorylation	SSAASPSSSSSSVQQ CCCCCCCCCCHHHHH	37.31	30407730
34	Phosphorylation	SAASPSSSSSSVQQQ CCCCCCCCCHHHHHH	38.28	30407730
347	Phosphorylation	AKARHALSTGSFAST HHHHHHHHCCCCCCC	31.35	23776212
348	Phosphorylation	KARHALSTGSFASTS HHHHHHHCCCCCCCC	37.38	23776212
350	Phosphorylation	RHALSTGSFASTSSP HHHHHCCCCCCCCCC	20.09	23776212
353	Phosphorylation	LSTGSFASTSSPRMV HHCCCCCCCCCCCCC	27.15	23776212
354	Phosphorylation	STGSFASTSSPRMVN HCCCCCCCCCCCCCC	29.78	23776212
355	Phosphorylation	TGSFASTSSPRMVNP CCCCCCCCCCCCCCC	35.53	23776212
356	Phosphorylation	GSFASTSSPRMVNPA CCCCCCCCCCCCCCC	19.33	23776212
511	Phosphorylation	LQTQRQISPAIGKVQ HHCCCCCCCCCCCCC	10.43	25561503
539	Phosphorylation	SLECGKESQAAASSN HHHCCHHHHHHHHCC	28.71	25561503
544	Phosphorylation	KESQAAASSNGPIFS HHHHHHHHCCCCCCC	21.43	25561503
545	Phosphorylation	ESQAAASSNGPIFSK HHHHHHHCCCCCCCC	40.87	25561503
581	Phosphorylation	NLGKEATSTDVATKE HHCCCCCCCCCCCHH	29.65	25561503
592	Phosphorylation	ATKEEQQTDVFPVKS CCHHHHCCCEEECCC	33.55	30407730
599	Phosphorylation	TDVFPVKSDQGADSS CCEEECCCCCCCCCC	35.09	30407730
605	Phosphorylation	KSDQGADSSTQKNPR CCCCCCCCCCCCCCC	34.45	30407730
606	Phosphorylation	SDQGADSSTQKNPRS CCCCCCCCCCCCCCC	35.09	30407730
607	Phosphorylation	DQGADSSTQKNPRSD CCCCCCCCCCCCCCC	47.73	30407730
628	Phosphorylation	KAVASDGSQSKVPPQ CCCCCCCCCCCCCCC	35.95	25561503
638	Phosphorylation	KVPPQANSPQPPKDT CCCCCCCCCCCCCCC	28.11	30291188
1331	Phosphorylation	GHRVLLFSTMTKLLD CCCHHHHHHHHHHHH	19.76	19880383
1332	Phosphorylation	HRVLLFSTMTKLLDI CCHHHHHHHHHHHHH	22.86	19880383
1450	Phosphorylation	QKEDELRSGGSVDLE CCHHHHHCCCCCCCC	61.19	25561503
1453	Phosphorylation	DELRSGGSVDLEDDM HHHHCCCCCCCCCCC	18.91	30407730
1594	Phosphorylation	SKNMLSSSNLIVQPG CCCCCCCCCEEECCC	32.07	19880383
1629	Phosphorylation	IEDDIAGYSEESSEE HCCHHCCCCHHCCCC	12.14	19880383
1630	Phosphorylation	EDDIAGYSEESSEER CCHHCCCCHHCCCCC	33.69	27531888
1633	Phosphorylation	IAGYSEESSEERNID HCCCCHHCCCCCCCC	38.71	27531888
1634	Phosphorylation	AGYSEESSEERNIDS CCCCHHCCCCCCCCC	46.91	27531888
1641	Phosphorylation	SEERNIDSGNEEEGD CCCCCCCCCCCCCCC	39.46	30291188
1658	Phosphorylation	QFDDDELTGALGDHQ ECCHHHCCCCCCCCC	20.54	25561503
1701	Phosphorylation	PRDDAGSSGSSPESH CCCCCCCCCCCCHHH	41.60	29654922
1704	Phosphorylation	DAGSSGSSPESHRSK CCCCCCCCCHHHHCH	35.89	29654922
1715	Phosphorylation	HRSKEMASPVSSQKF HHCHHCCCCCHHHHH	25.23	30407730
1718	Phosphorylation	KEMASPVSSQKFGSL HHCCCCCHHHHHCCC	30.36	30407730
1719	Phosphorylation	EMASPVSSQKFGSLS HCCCCCHHHHHCCCC	37.31	30407730
1724	Phosphorylation	VSSQKFGSLSALDTR CHHHHHCCCCCCCCC	23.45	30291188
1726	Phosphorylation	SQKFGSLSALDTRPG HHHHCCCCCCCCCCC	28.60	25561503
1730	Phosphorylation	GSLSALDTRPGSVSK CCCCCCCCCCCCHHH	39.34	28295753
1734	Phosphorylation	ALDTRPGSVSKRLLD CCCCCCCCHHHHHHH	26.37	30291188
1736	Phosphorylation	DTRPGSVSKRLLDDL CCCCCCHHHHHHHHH	17.47	30407730
1754	Phosphorylation	EIAASGDSHIDLQRS CCCCCCCCCEECCCC	26.35	30291188
1761	Phosphorylation	SHIDLQRSGSWAHDR CCEECCCCCCCCCCC	24.99	23776212
1763	Phosphorylation	IDLQRSGSWAHDRDE EECCCCCCCCCCCCC	23.49	23776212
1880	Phosphorylation	NAEASRETWDGTSPI CHHHCCCCCCCCCCC	27.96	23776212
1884	Phosphorylation	SRETWDGTSPISSSN CCCCCCCCCCCCCCC	28.93	23776212
1885	Phosphorylation	RETWDGTSPISSSNA CCCCCCCCCCCCCCH	26.26	30291188
1888	Phosphorylation	WDGTSPISSSNAGAR CCCCCCCCCCCHHHH	30.97	23776212
1889	Phosphorylation	DGTSPISSSNAGARM CCCCCCCCCCHHHHH	28.47	23776212
1890	Phosphorylation	GTSPISSSNAGARMS CCCCCCCCCHHHHHH	24.73	23776212
2019	Phosphorylation	REARNALSFSGSAPT HHHHHHHHCCCCCCE	18.24	30291188
2029	Phosphorylation	GSAPTLVSTPTPRGA CCCCEEECCCCCCCC	31.61	23328941
2030	Phosphorylation	SAPTLVSTPTPRGAG CCCEEECCCCCCCCC	24.57	23328941
2052	Phosphorylation	KLVNEPETEPSSPQR HHCCCCCCCCCCCCH	65.00	23776212
2055	Phosphorylation	NEPETEPSSPQRSQQ CCCCCCCCCCCHHHH	48.71	19880383
2056	Phosphorylation	EPETEPSSPQRSQQR CCCCCCCCCCHHHHH	35.45	30291188
2060	Phosphorylation	EPSSPQRSQQRENSR CCCCCCHHHHHHHCC	25.97	19376835
2089	Phosphorylation	TTSHTDESPILAHPG CCCCCCCCCCCCCCC	21.76	23111157
2117	Phosphorylation	KSGPKTRTGGSSSPV HCCCCCCCCCCCCCC	51.64	23776212
2120	Phosphorylation	PKTRTGGSSSPVSPP CCCCCCCCCCCCCCC	29.05	23776212
2121	Phosphorylation	KTRTGGSSSPVSPPP CCCCCCCCCCCCCCC	41.77	23776212
2122	Phosphorylation	TRTGGSSSPVSPPPA CCCCCCCCCCCCCCH	30.90	23776212
2125	Phosphorylation	GGSSSPVSPPPAMIG CCCCCCCCCCCHHCC	34.76	23776212
2137	Phosphorylation	MIGRGLRSPVSGGVP HCCCCCCCCCCCCCC	34.39	30291188
2140	Phosphorylation	RGLRSPVSGGVPRET CCCCCCCCCCCCHHH	32.96	23776212

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 BRM_ARATH !!

Functions of PTM Sites

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

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 BRM_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SWI3C_ARATH	SWI3C	physical	15371304
SWI3C_ARATH	SWI3C	physical	16845477
SWI3B_ARATH	SWI3B	physical	16845477
COL2_ARATH	COL2	physical	23449474
COL5_ARATH	COL5	physical	23449474
COL15_ARATH	AT1G28050	physical	23449474
COL11_ARATH	AT4G15250	physical	23449474
COL7_ARATH	AT1G73870	physical	23449474
GBF3_ARATH	GBF3	physical	23449474
AI5L4_ARATH	ABF1	physical	23449474
TGA7_ARATH	AT1G77920	physical	23449474
TGA3_ARATH	TGA3	physical	23449474
TGA4_ARATH	TGA4	physical	23449474
TGA5_ARATH	OBF5	physical	23449474
AI5L6_ARATH	ABF3	physical	23449474
DRE2H_ARATH	AT2G40350	physical	23449474
ERF53_ARATH	AT2G20880	physical	23449474
RAP21_ARATH	RAP2.1	physical	23449474
RAP22_ARATH	RAP2.2	physical	23449474
ERF56_ARATH	AT2G22200	physical	23449474
SHN2_ARATH	SHN3	physical	23449474
DRE1D_ARATH	CBF4	physical	23449474
EF102_ARATH	ERF5	physical	23449474
ERF77_ARATH	ERF10	physical	23449474
CRF6_ARATH	CRF6	physical	23449474
ERF24_ARATH	HRD	physical	23449474
BBM_ARATH	BBM	physical	23449474
RA211_ARATH	RAP2.11	physical	23449474
TOE2_ARATH	TOE2	physical	23449474
MYB12_ARATH	MYB12	physical	23449474
MYB46_ARATH	MYB46	physical	23449474
MY122_ARATH	MYB122	physical	23449474
AS1_ARATH	AS1	physical	23449474
RADL6_ARATH	RL6	physical	23449474
MYB86_ARATH	MYB86	physical	23449474
Y1385_ARATH	AT1G63850	physical	23449474
GTE11_ARATH	BET10	physical	23449474
Y3272_ARATH	AT3G27220	physical	23449474
WRKY6_ARATH	WRKY6	physical	23449474
WRK31_ARATH	WRKY31	physical	23449474
WRK61_ARATH	WRKY61	physical	23449474
WRK46_ARATH	WRKY46	physical	23449474
WRK53_ARATH	WRKY53	physical	23449474
BH085_ARATH	RSL2	physical	23449474
BH054_ARATH	RSL4	physical	23449474
BH139_ARATH	AT5G43175	physical	23449474
BH086_ARATH	RSL1	physical	23449474
UNE12_ARATH	UNE12	physical	23449474
BH007_ARATH	AT1G03040	physical	23449474
HEC2_ARATH	HEC2	physical	23449474
HEC1_ARATH	HEC1	physical	23449474
BH080_ARATH	AT1G35460	physical	23449474
BH130_ARATH	AT2G42280	physical	23449474
SPT_ARATH	SPT	physical	23449474
BH049_ARATH	AT1G68920	physical	23449474
BH062_ARATH	AT3G07340	physical	23449474
BH010_ARATH	AT2G31220	physical	23449474
BH148_ARATH	AT3G06590	physical	23449474
BH089_ARATH	AT1G06170	physical	23449474
BH047_ARATH	PYE	physical	23449474
MYC2_ARATH	MYC2	physical	23449474
DEGP4_ARATH	DegP4	physical	23449474
TT8_ARATH	TT8	physical	23449474
BH095_ARATH	RGE1	physical	23449474
BH014_ARATH	AT4G00870	physical	23449474
BH003_ARATH	AT4G16430	physical	23449474
BH067_ARATH	AT3G61950	physical	23449474
BH057_ARATH	AT4G01460	physical	23449474
BH094_ARATH	AT1G22490	physical	23449474
BH096_ARATH	AT1G72210	physical	23449474
BIM1_ARATH	BIM1	physical	23449474
NAC55_ARATH	NAC3	physical	23449474
HAT5_ARATH	HB-1	physical	23449474
ATB40_ARATH	HB40	physical	23449474
ATB20_ARATH	HB20	physical	23449474
ATB53_ARATH	HB53	physical	23449474
ATB21_ARATH	HB21	physical	23449474
KNAT3_ARATH	KNAT3	physical	23449474
AGL92_ARATH	AGL92	physical	23449474
ZFP7_ARATH	ZFP7	physical	23449474
STOP1_ARATH	STOP1	physical	23449474
AZF2_ARATH	ZF2	physical	23449474
SINA4_ARATH	AT4G27880	physical	23449474
NFYB8_ARATH	NF-YB8	physical	23449474
ARR11_ARATH	ARR11	physical	23449474
ARR10_ARATH	RR10	physical	23449474
GLK1_ARATH	GPRI1	physical	23449474
PCL1_ARATH	PCL1	physical	23449474
PHL1_ARATH	AT5G29000	physical	23449474
DMC1_ARATH	DMC1	physical	23449474
HSFA3_ARATH	HSFA3	physical	23449474
HFA6A_ARATH	HSFA6A	physical	23449474
SCL15_ARATH	AT4G36710	physical	23449474
TGT3A_ARATH	AT5G01380	physical	23449474
FAF1_ARATH	AT4G02810	physical	23449474
TCP3_ARATH	TCP3	physical	23449474
TCP8_ARATH	AT1G58100	physical	23449474
TCP22_ARATH	AT1G72010	physical	23449474
TCP4_ARATH	TCP4	physical	23449474
TCP20_ARATH	TCP20	physical	23449474
TCP16_ARATH	TCP16	physical	23449474
TCP19_ARATH	AT5G51910	physical	23449474
TCP5_ARATH	TCP5	physical	23449474
TCP1_ARATH	TCP1	physical	23449474
IAA11_ARATH	IAA11	physical	23449474
E2FA_ARATH	E2F3	physical	23449474
VAL1_ARATH	HSI2	physical	23449474
ABI3_ARATH	ABI3	physical	23449474
NGA2_ARATH	NGA2	physical	23449474
NGA4_ARATH	NGA4	physical	23449474
ARFC_ARATH	ETT	physical	23449474
ARFR_ARATH	ARF18	physical	23449474
LBD1_ARATH	LBD1	physical	23449474
LBD10_ARATH	LBD10	physical	23449474
LBD39_ARATH	LBD39	physical	23449474
LBD35_ARATH	LBD35	physical	23449474
KNAT1_ARATH	KNAT1	physical	25822547
PLT2_ARATH	PMT2	genetic	25991732

Drug and Disease Associations

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

Regulatory Network of BRM_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1641; SER-2056 ANDSER-2137, AND MASS SPECTROMETRY.	19376835 [Abstract]
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2137, SUBCELLULARLOCATION, AND MASS SPECTROMETRY.	19245862 [Abstract]
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis."; de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.; J. Proteome Res. 7:2458-2470(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1641, AND MASSSPECTROMETRY.	18433157 [Abstract]