dbPTM

SMCA5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SMCA5_MOUSE
UniProt AC	Q91ZW3
Protein Name	SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5
Gene Name	Smarca5
Organism	Mus musculus (Mouse).
Sequence Length	1051
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	MSSAVEPPPPPPPESAPSKPSAAGAGGSSSGNKGGPEGGAAPAAPCAAGSGPADTEMEEVFDHGSPGKQKEIQEPDPTYEEKMQTDRANRFEYLLKQTELFAHFIQPAAQKTPTSPLKMKPGRPRVKKDEKQNLLSVGDYRHRRTEQEEDEELLTESSKATNVCTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKKWVPTLRSVCLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPKKEVKIYVGLSKMQREWYTRILMKDIDILNSAGKMDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDMHLVTNSGKMVVLDKLLPKLKEQGSRVLIFSQMTRVLDILEDYCMWRNYEYCRLDGQTPHDERQDSINAYNEPNSTKFVFMLSTRAGGLGINLATADVVILYDSDWNPQVDLQAMDRAHRIGQTKTVRVFRFITDNTVEERIVERAEMKLRLDSIVIQQGRLVDQNLNKIGKDEMLQMIRHGATHVFASKESEITDEDIDGILERGAKKTAEMNEKLSKMGESSLRNFTMDTESSVYNFEGEDYREKQKIAFTEWIEPPKRERKANYAVDAYFREALRVSEPKAPKAPRPPKQPNVQDFQFFPPRLFELLEKEILYYRKTIGYKVPRSPDLPNAAQAQKEEQLKIDEAEPLNDEELEEKEKLLTQGFTNWNKRDFNQFIKANEKWGRDDIENIAREVEGKTPEEVIEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDTKIGRYKAPFHQLRISYGTNKGKNYTEEEDRFLICMLHKLGFDKENVYDELRQCIRNSPQFRFDWFLKSRTAMELQRRCNTLITLIERENMELEEKEKAEKKKRGPKPSTQKRKMDGAPDGRGRKKKLKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSAVEPPP ------CCCCCCCCC	38.01	-
3	Phosphorylation	-----MSSAVEPPPP -----CCCCCCCCCC	48.47	25619855
15	Phosphorylation	PPPPPPESAPSKPSA CCCCCCCCCCCCCCC	51.78	25619855
18	Phosphorylation	PPPESAPSKPSAAGA CCCCCCCCCCCCCCC	57.84	25619855
50	Phosphorylation	AAPCAAGSGPADTEM CCCCCCCCCCCCCCH	36.56	24925903
55	Phosphorylation	AGSGPADTEMEEVFD CCCCCCCCCHHHHHC	39.06	25521595
57	Oxidation	SGPADTEMEEVFDHG CCCCCCCHHHHHCCC	6.05	17242355
65	Phosphorylation	EEVFDHGSPGKQKEI HHHHCCCCCCCCCCC	27.36	24925903
78	Phosphorylation	EIQEPDPTYEEKMQT CCCCCCCCHHHHHHH	51.44	25159016
79	Phosphorylation	IQEPDPTYEEKMQTD CCCCCCCHHHHHHHH	27.72	25159016
98	Phosphorylation	FEYLLKQTELFAHFI HHHHHHHHHHHHHHH	32.82	24068923
112	Phosphorylation	IQPAAQKTPTSPLKM HHHHHHCCCCCCCCC	21.51	27149854
114	Phosphorylation	PAAQKTPTSPLKMKP HHHHCCCCCCCCCCC	48.48	22942356
115	Phosphorylation	AAQKTPTSPLKMKPG HHHCCCCCCCCCCCC	29.46	22942356
136	Phosphorylation	DEKQNLLSVGDYRHR HHHCCCCCHHCCCCC	27.50	22942356
170	Phosphorylation	VCTRFEDSPSYVKWG CCCCCCCCCCHHCCC	14.46	-
402	Phosphorylation	IKADVEKSLPPKKEV HHHHHHHCCCCCCCE	32.38	18779572
439	Acetylation	DILNSAGKMDKMRLL HHHHCCCCCCHHHHH	43.58	23806337
489	Acetylation	GKMVVLDKLLPKLKE CCEEEHHHHHHHHHH	48.00	22826441
608	Phosphorylation	VRVFRFITDNTVEER EEEEEEECCCCHHHH	22.08	29895711
611	Phosphorylation	FRFITDNTVEERIVE EEEECCCCHHHHHHH	31.91	29895711
646	Acetylation	QNLNKIGKDEMLQMI CCHHHCCHHHHHHHH	54.72	23806337
664	Ubiquitination	ATHVFASKESEITDE CCEEEECCCCCCCHH	62.93	-
709	Phosphorylation	FTMDTESSVYNFEGE CCCCCCCCCCCCCCC	23.53	29514104
754	Phosphorylation	FREALRVSEPKAPKA HHHHHHCCCCCCCCC	41.57	22817900
802	Phosphorylation	IGYKVPRSPDLPNAA CCCCCCCCCCCCCHH	19.39	26824392
835	Ubiquitination	EELEEKEKLLTQGFT HHHHHHHHHHHHCCC	60.92	22790023
965	Acetylation	LHKLGFDKENVYDEL HHHCCCCHHHHHHHH	49.26	22826441
992	Phosphorylation	DWFLKSRTAMELQRR HHHHHCHHHHHHHHH	37.13	22802335
1000	Glutathionylation	AMELQRRCNTLITLI HHHHHHHHHHHHHHH	5.06	24333276
1028	Acetylation	EKKKRGPKPSTQKRK HHHHCCCCCCHHHCC	55.19	15613399
1033	Acetylation	GPKPSTQKRKMDGAP CCCCCHHHCCCCCCC	54.82	15613407
1035	Acetylation	KPSTQKRKMDGAPDG CCCHHHCCCCCCCCC	48.67	15620243

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 SMCA5_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SMCA5_MOUSE !!

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 SMCA5_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
BAZ1B_MOUSE	Baz1b	physical	11980720

Drug and Disease Associations

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

Regulatory Network of SMCA5_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55 AND SER-65, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND MASSSPECTROMETRY.	14729942 [Abstract]