dbPTM

SMRD3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SMRD3_HUMAN
UniProt AC	Q6STE5
Protein Name	SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3
Gene Name	SMARCD3
Organism	Homo sapiens (Human).
Sequence Length	483
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. Stimulates nuclear receptor mediated transcription. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity)..
Protein Sequence	MAADEVAGGARKATKSKLFEFLVHGVRPGMPSGARMPHQGAPMGPPGSPYMGSPAVRPGLAPAGMEPARKRAAPPPGQSQAQSQGQPVPTAPARSRSAKRRKMADKILPQRIRELVPESQAYMDLLAFERKLDQTIMRKRVDIQEALKRPMKQKRKLRLYISNTFNPAKPDAEDSDGSIASWELRVEGKLLDDPSKQKRKFSSFFKSLVIELDKDLYGPDNHLVEWHRTPTTQETDGFQVKRPGDLSVRCTLLLMLDYQPPQFKLDPRLARLLGLHTQSRSAIVQALWQYVKTNRLQDSHDKEYINGDKYFQQIFDCPRLKFSEIPQRLTALLLPPDPIVINHVISVDPSDQKKTACYDIDVEVEEPLKGQMSSFLLSTANQQEISALDSKIHETIESINQLKIQRDFMLSFSRDPKGYVQDLLRSQSRDLKVMTDVAGNPEEERRAEFYHQPWSQEAVSRYFYCKIQQRRQELEQSLVVRNT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAADEVAGG ------CCHHHHCCC	24.50	22814378
48	Phosphorylation	APMGPPGSPYMGSPA CCCCCCCCCCCCCCC	20.73	22210691
71	Methylation	GMEPARKRAAPPPGQ CCCHHHHHCCCCCCC	30.35	115917225
90	Phosphorylation	SQGQPVPTAPARSRS HCCCCCCCCCCCCCH	45.57	-
95	Phosphorylation	VPTAPARSRSAKRRK CCCCCCCCCHHHHHH	32.47	28555341
106	Ubiquitination	KRRKMADKILPQRIR HHHHHHHHHHHHHHH	36.28	-
106	Acetylation	KRRKMADKILPQRIR HHHHHHHHHHHHHHH	36.28	25953088
122	Phosphorylation	LVPESQAYMDLLAFE HCCHHHHHHHHHHHH	5.41	-
131	Ubiquitination	DLLAFERKLDQTIMR HHHHHHHHHHHHHHH	49.57	-
160	Phosphorylation	QKRKLRLYISNTFNP HHCCCEEEEECCCCC	8.89	20068231
162	Phosphorylation	RKLRLYISNTFNPAK CCCEEEEECCCCCCC	19.09	20068231
164	Phosphorylation	LRLYISNTFNPAKPD CEEEEECCCCCCCCC	20.28	20068231
175	Phosphorylation	AKPDAEDSDGSIASW CCCCCCCCCCCEEEE	35.06	22617229
176 (in isoform 2)	Ubiquitination	-	68.15	21906983
178	Phosphorylation	DAEDSDGSIASWELR CCCCCCCCEEEEEEE	21.70	28102081
181	Phosphorylation	DSDGSIASWELRVEG CCCCCEEEEEEEEEC	21.29	23927012
183 (in isoform 2)	Ubiquitination	-	24.97	21906983
189	Ubiquitination	WELRVEGKLLDDPSK EEEEEECEECCCHHH	32.16	21906983
189 (in isoform 1)	Ubiquitination	-	32.16	21906983
189	Acetylation	WELRVEGKLLDDPSK EEEEEECEECCCHHH	32.16	25953088
196	Ubiquitination	KLLDDPSKQKRKFSS EECCCHHHHHHHHHH	66.29	21906983
196 (in isoform 1)	Ubiquitination	-	66.29	21906983
200	Ubiquitination	DPSKQKRKFSSFFKS CHHHHHHHHHHHHHH	57.54	-
200	Acetylation	DPSKQKRKFSSFFKS CHHHHHHHHHHHHHH	57.54	25953088
214	Ubiquitination	SLVIELDKDLYGPDN HHHHHHCHHHHCCCC	63.36	-
247	Phosphorylation	VKRPGDLSVRCTLLL ECCCCCHHHEEEEEE	16.56	28509920
277	Phosphorylation	ARLLGLHTQSRSAIV HHHHCCHHHCHHHHH	33.03	-
386	Phosphorylation	TANQQEISALDSKIH HCCHHHHHHHHHHHH	23.25	22210691
411	Phosphorylation	IQRDFMLSFSRDPKG HCHHHHHHCCCCCCH	14.91	-
413	Phosphorylation	RDFMLSFSRDPKGYV HHHHHHCCCCCCHHH	32.19	20068231
419	Phosphorylation	FSRDPKGYVQDLLRS CCCCCCHHHHHHHHH	10.89	20068231
426	Phosphorylation	YVQDLLRSQSRDLKV HHHHHHHHCCCCCCC	32.26	20068231
428	Phosphorylation	QDLLRSQSRDLKVMT HHHHHHCCCCCCCEE	29.07	20068231
434	Sulfoxidation	QSRDLKVMTDVAGNP CCCCCCCEECCCCCH	2.24	21406390
477	Phosphorylation	RRQELEQSLVVRNT- HHHHHHHHHHCCCC-	17.47	28555341
483	Phosphorylation	QSLVVRNT------- HHHHCCCC-------	29.44	21712546

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
247	S	Phosphorylation	Kinase	PRKCI	P41743	GPS
247	S	Phosphorylation	Kinase	PRKCZ	Q05513	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SMRD3_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 SMRD3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RARA_HUMAN	RARA	physical	17363140
MYOD1_HUMAN	MYOD1	physical	22068056
SMCA4_HUMAN	SMARCA4	physical	22068056
SNF5_HUMAN	SMARCB1	physical	22939629
PPARG_HUMAN	PPARG	physical	14701856
SMCA4_HUMAN	SMARCA4	physical	14701856
ERR1_HUMAN	ESRRA	physical	14701856
NR1H4_HUMAN	NR1H4	physical	14701856
RORA_HUMAN	RORA	physical	14701856
SRBP1_HUMAN	SREBF1	physical	14701856
JUN_HUMAN	JUN	physical	14701856
PBX1_HUMAN	PBX1	physical	14701856
ACL6A_HUMAN	ACTL6A	physical	26344197
ARI1A_HUMAN	ARID1A	physical	26344197
ARI1B_HUMAN	ARID1B	physical	26344197
BCL7A_HUMAN	BCL7A	physical	26344197
BCL7B_HUMAN	BCL7B	physical	26344197
BCL7C_HUMAN	BCL7C	physical	26344197
REQU_HUMAN	DPF2	physical	26344197
HMGB1_HUMAN	HMGB1	physical	26344197
RPB4_HUMAN	POLR2D	physical	26344197
SMCA4_HUMAN	SMARCA4	physical	26344197
TBL1X_HUMAN	TBL1X	physical	26344197
TBL1R_HUMAN	TBL1XR1	physical	26344197
RENT2_HUMAN	UPF2	physical	26344197
ESR1_HUMAN	ESR1	physical	17363140
RARG_HUMAN	RARG	physical	17363140
RARB_HUMAN	RARB	physical	17363140
RXRA_HUMAN	RXRA	physical	17363140

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 SMRD3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-178, AND MASSSPECTROMETRY.	17081983 [Abstract]