SMRD1_HUMAN - dbPTM
SMRD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMRD1_HUMAN
UniProt AC Q96GM5
Protein Name SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
Gene Name SMARCD1 {ECO:0000312|EMBL:AAD23390.1}
Organism Homo sapiens (Human).
Sequence Length 515
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. [PubMed: 8804307 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 Has a strong influence on vitamin D-mediated transcriptional activity from an enhancer vitamin D receptor element (VDRE May be a link between mammalian SWI-SNF-like chromatin remodeling complexes and the vitamin D receptor (VDR) heterodimer]
Protein Sequence MAARAGFQSVAPSGGAGASGGAGAAAALGPGGTPGPPVRMGPAPGQGLYRSPMPGAAYPRPGMLPGSRMTPQGPSMGPPGYGGNPSVRPGLAQSGMDQSRKRPAPQQIQQVQQQAVQNRNHNAKKKKMADKILPQRIRELVPESQAYMDLLAFERKLDQTIMRKRLDIQEALKRPIKQKRKLRIFISNTFNPAKSDAEDGEGTVASWELRVEGRLLEDSALSKYDATKQKRKFSSFFKSLVIELDKDLYGPDNHLVEWHRTATTQETDGFQVKRPGDVNVRCTVLLMLDYQPPQFKLDPRLARLLGIHTQTRPVIIQALWQYIKTHKLQDPHEREFVICDKYLQQIFESQRMKFSEIPQRLHALLMPPEPIIINHVISVDPNDQKKTACYDIDVEVDDTLKTQMNSFLLSTASQQEIATLDNKIHETIETINQLKTQREFMLSFARDPQGFINDWLQSQCRDLKTMTDVVGNPEEERRAEFYFQPWAQEAVCRYFYSKVQQRRQELEQALGIRNT
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
4Methylation----MAARAGFQSVA
----CCCCCCCCCCC		26.21115388065
13PhosphorylationGFQSVAPSGGAGASG
CCCCCCCCCCCCCCC		39.8728555341
33PhosphorylationAALGPGGTPGPPVRM
HHCCCCCCCCCCCCC		30.8728555341
39MethylationGTPGPPVRMGPAPGQ
CCCCCCCCCCCCCCC		30.07115917209
49PhosphorylationPAPGQGLYRSPMPGA
CCCCCCCCCCCCCCC		18.8323663014
51PhosphorylationPGQGLYRSPMPGAAY
CCCCCCCCCCCCCCC		16.4023663014
58PhosphorylationSPMPGAAYPRPGMLP
CCCCCCCCCCCCCCC		10.1523663014
60MethylationMPGAAYPRPGMLPGS
CCCCCCCCCCCCCCC		27.94115917213
67PhosphorylationRPGMLPGSRMTPQGP
CCCCCCCCCCCCCCC		19.5528851738
68MethylationPGMLPGSRMTPQGPS
CCCCCCCCCCCCCCC		38.62-
70PhosphorylationMLPGSRMTPQGPSMG
CCCCCCCCCCCCCCC		16.0229978859
75PhosphorylationRMTPQGPSMGPPGYG
CCCCCCCCCCCCCCC		43.1028851738
81PhosphorylationPSMGPPGYGGNPSVR
CCCCCCCCCCCCCCC		27.8629978859
86PhosphorylationPGYGGNPSVRPGLAQ
CCCCCCCCCCCCCHH		34.4629978859
88Asymmetric dimethylarginineYGGNPSVRPGLAQSG
CCCCCCCCCCCHHCC		24.73-
88MethylationYGGNPSVRPGLAQSG
CCCCCCCCCCCHHCC		24.7352717223
100MethylationQSGMDQSRKRPAPQQ
HCCCCCCCCCCCHHH		33.1154548849
101UbiquitinationSGMDQSRKRPAPQQI
CCCCCCCCCCCHHHH		68.9029967540
101SumoylationSGMDQSRKRPAPQQI
CCCCCCCCCCCHHHH		68.9028112733
101MethylationSGMDQSRKRPAPQQI
CCCCCCCCCCCHHHH		68.9082990985
131AcetylationKKKKMADKILPQRIR
HHHHHHHHHHHHHHH		36.2826051181
131UbiquitinationKKKKMADKILPQRIR
HHHHHHHHHHHHHHH		36.2824816145
147PhosphorylationLVPESQAYMDLLAFE
HCCHHHHHHHHHHHH		5.41-
156UbiquitinationDLLAFERKLDQTIMR
HHHHHHHHHHHHHHH		49.5724816145
173UbiquitinationLDIQEALKRPIKQKR
CCHHHHHHCHHHHHC		64.2829967540
194UbiquitinationSNTFNPAKSDAEDGE
ECCCCCCCCCCCCCC		50.56-
195PhosphorylationNTFNPAKSDAEDGEG
CCCCCCCCCCCCCCC		44.1328348404
203PhosphorylationDAEDGEGTVASWELR
CCCCCCCCEEEEEEE		14.48-
206PhosphorylationDGEGTVASWELRVEG
CCCCCEEEEEEEEEC		19.4224719451
219O-linked_GlycosylationEGRLLEDSALSKYDA
ECEECCHHHHHCCCC		23.0228510447
223AcetylationLEDSALSKYDATKQK
CCHHHHHCCCCHHHH		48.2625953088
223 (in isoform 2)Ubiquitination-48.2621890473
223 (in isoform 1)Ubiquitination-48.2621890473
223UbiquitinationLEDSALSKYDATKQK
CCHHHHHCCCCHHHH		48.2632015554
2232-HydroxyisobutyrylationLEDSALSKYDATKQK
CCHHHHHCCCCHHHH		48.26-
228UbiquitinationLSKYDATKQKRKFSS
HHCCCCHHHHHHHHH		56.3933845483
232UbiquitinationDATKQKRKFSSFFKS
CCHHHHHHHHHHHHH		57.54-
246UbiquitinationSLVIELDKDLYGPDN
HHHHHHCHHHHCCCC		63.3629967540
273AcetylationETDGFQVKRPGDVNV
CCCCCEECCCCCCCC		41.9326051181
273 (in isoform 1)Ubiquitination-41.9321890473
273 (in isoform 2)Ubiquitination-41.9321890473
273UbiquitinationETDGFQVKRPGDVNV
CCCCCEECCCCCCCC		41.9321906983
300UbiquitinationPQFKLDPRLARLLGI
CCCCCCHHHHHHHCC		40.4221963094
312UbiquitinationLGIHTQTRPVIIQAL
HCCCCCCHHHHHHHH		17.4224816145
341UbiquitinationREFVICDKYLQQIFE
CCEEEEHHHHHHHHH		43.3721963094
353UbiquitinationIFESQRMKFSEIPQR
HHHHCCCCHHHCCHH		48.1824816145
385UbiquitinationSVDPNDQKKTACYDI
EECCCCCCCCEEEEE		55.76-
386 (in isoform 1)Ubiquitination-35.4021890473
386 (in isoform 2)Ubiquitination-35.4021890473
386UbiquitinationVDPNDQKKTACYDID
ECCCCCCCCEEEEEE		35.4021906983
423UbiquitinationEIATLDNKIHETIET
HHHHHCHHHHHHHHH		45.1423000965
435 (in isoform 1)Ubiquitination-32.6121890473
435UbiquitinationIETINQLKTQREFML
HHHHHHHHHHHHHHH		32.6121906983
436PhosphorylationETINQLKTQREFMLS
HHHHHHHHHHHHHHH		41.2620068231
457UbiquitinationGFINDWLQSQCRDLK
HHHHHHHHHHHCCCC		27.4822505724
464AcetylationQSQCRDLKTMTDVVG
HHHHCCCCHHHHCCC		40.3125953088
464 (in isoform 1)Ubiquitination-40.3121890473
464UbiquitinationQSQCRDLKTMTDVVG
HHHHCCCCHHHHCCC		40.3123000965
466SulfoxidationQCRDLKTMTDVVGNP
HHCCCCHHHHCCCCH		2.6221406390
498AcetylationVCRYFYSKVQQRRQE
HHHHHHHHHHHHHHH		32.4625953088
498UbiquitinationVCRYFYSKVQQRRQE
HHHHHHHHHHHHHHH		32.4622505724
515PhosphorylationQALGIRNT-------
HHHCCCCC-------		30.0929214152
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
-KUbiquitinationE3 ubiquitin ligaseCHFRQ96EP1
PMID:22285184
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMRD1_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 SMRD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC85B_HUMANCCDC85Bphysical
16189514
USBP1_HUMANUSHBP1physical
16189514
CACO2_HUMANCALCOCO2physical
16189514
LDOC1_HUMANLDOC1physical
16189514
SMCA4_HUMANSMARCA4physical
12917342
SMRC2_HUMANSMARCC2physical
12917342
SMRC1_HUMANSMARCC1physical
12917342
GCR_HUMANNR3C1physical
12917342
ESR1_HUMANESR1physical
12917342
NR1H4_HUMANNR1H4physical
12917342
PRGR_HUMANPGRphysical
12917342
FEZ1_HUMANFEZ1physical
16484223
NONO_HUMANNONOphysical
18042045
SFPQ_HUMANSFPQphysical
18042045
SMCA4_HUMANSMARCA4physical
18042045
SMCA2_HUMANSMARCA2physical
18042045
SNF5_HUMANSMARCB1physical
18042045
ACTS_HUMANACTA1physical
20305087
ACL6A_HUMANACTL6Aphysical
20305087
ARI1A_HUMANARID1Aphysical
20305087
ARI1B_HUMANARID1Bphysical
20305087
ARID2_HUMANARID2physical
20305087
BRD7_HUMANBRD7physical
20305087
REQU_HUMANDPF2physical
20305087
IMA1_HUMANKPNA2physical
20305087
PB1_HUMANPBRM1physical
20305087
PHF10_HUMANPHF10physical
20305087
SMCA2_HUMANSMARCA2physical
20305087
SMCA4_HUMANSMARCA4physical
20305087
SNF5_HUMANSMARCB1physical
20305087
SMRC1_HUMANSMARCC1physical
20305087
SMRC2_HUMANSMARCC2physical
20305087
SMRD2_HUMANSMARCD2physical
20305087
SMCE1_HUMANSMARCE1physical
20305087
SSXT_HUMANSS18physical
20305087
SMCA4_HUMANSMARCA4physical
18303029
SMRC1_HUMANSMARCC1physical
18303029
P53_HUMANTP53physical
18303029
CHFR_HUMANCHFRphysical
22285184
TNIP2_HUMANTNIP2physical
12753905
SNF5_HUMANSMARCB1physical
22939629
SMRD2_HUMANSMARCD2physical
22939629
KMT5B_HUMANSUV420H1physical
21988832
1433G_HUMANYWHAGphysical
21988832
KDM1A_HUMANKDM1Aphysical
23455924
ANM6_HUMANPRMT6physical
23455924
MED4_HUMANMED4physical
25416956
VP37B_HUMANVPS37Bphysical
25416956
ARI1B_HUMANARID1Bphysical
26186194
ARI1A_HUMANARID1Aphysical
26186194
PHF10_HUMANPHF10physical
26186194
SMRC2_HUMANSMARCC2physical
26186194
SMRC1_HUMANSMARCC1physical
26186194
BICRA_HUMANGLTSCR1physical
26186194
SMCA2_HUMANSMARCA2physical
26186194
SMCA4_HUMANSMARCA4physical
26186194
ARID2_HUMANARID2physical
26186194
DPF1_HUMANDPF1physical
26186194
PB1_HUMANPBRM1physical
26186194
SMRD3_HUMANSMARCD3physical
26186194
SMRD2_HUMANSMARCD2physical
26186194
SNF5_HUMANSMARCB1physical
26186194
BRD7_HUMANBRD7physical
26186194
IF1AX_HUMANEIF1AXphysical
26186194
BRCC3_HUMANBRCC3physical
26186194
BCL7A_HUMANBCL7Aphysical
26186194
BCL7C_HUMANBCL7Cphysical
26186194
BCL7B_HUMANBCL7Bphysical
26186194
ACL6B_HUMANACTL6Bphysical
26186194
BRD9_HUMANBRD9physical
26186194
SBP1_HUMANSELENBP1physical
26186194
DUS14_HUMANDUSP14physical
26186194
CREST_HUMANSS18L1physical
26186194
KC1E_HUMANCSNK1Ephysical
26186194
LRC15_HUMANLRRC15physical
26186194
PKP3_HUMANPKP3physical
26186194
DSG4_HUMANDSG4physical
26186194
BICRL_HUMANGLTSCR1Lphysical
26186194
PADI3_HUMANPADI3physical
26186194
PLCD1_HUMANPLCD1physical
26186194
PA24B_HUMANJMJD7-PLA2G4Bphysical
26186194
ACL6A_HUMANACTL6Aphysical
26344197
ARI1A_HUMANARID1Aphysical
26344197
ARI1B_HUMANARID1Bphysical
26344197
BCL7A_HUMANBCL7Aphysical
26344197
BCL7B_HUMANBCL7Bphysical
26344197
BCL7C_HUMANBCL7Cphysical
26344197
REQU_HUMANDPF2physical
26344197
HMGB1_HUMANHMGB1physical
26344197
MDC1_HUMANMDC1physical
26344197
MED4_HUMANMED4physical
26344197
RPB4_HUMANPOLR2Dphysical
26344197
RPAB5_HUMANPOLR2Lphysical
26344197
SMCA2_HUMANSMARCA2physical
26344197
SMCA4_HUMANSMARCA4physical
26344197
SMRD2_HUMANSMARCD2physical
26344197
SMCE1_HUMANSMARCE1physical
26344197
SSXT_HUMANSS18physical
26344197
TBL1X_HUMANTBL1Xphysical
26344197
TBL1R_HUMANTBL1XR1physical
26344197
RENT2_HUMANUPF2physical
26344197
VP37B_HUMANVPS37Bphysical
21516116
SMRC2_HUMANSMARCC2physical
28514442
BICRA_HUMANGLTSCR1physical
28514442
BRD7_HUMANBRD7physical
28514442
BRD9_HUMANBRD9physical
28514442
DPF1_HUMANDPF1physical
28514442
ARI1B_HUMANARID1Bphysical
28514442
BICRL_HUMANGLTSCR1Lphysical
28514442
CREST_HUMANSS18L1physical
28514442
SMRD3_HUMANSMARCD3physical
28514442
ARID2_HUMANARID2physical
28514442
SMCA2_HUMANSMARCA2physical
28514442
SMRD2_HUMANSMARCD2physical
28514442
PHF10_HUMANPHF10physical
28514442
BCL7B_HUMANBCL7Bphysical
28514442
SMCA4_HUMANSMARCA4physical
28514442
SNF5_HUMANSMARCB1physical
28514442
PB1_HUMANPBRM1physical
28514442
DUS14_HUMANDUSP14physical
28514442
ARI1A_HUMANARID1Aphysical
28514442
SMRC1_HUMANSMARCC1physical
28514442
ACL6B_HUMANACTL6Bphysical
28514442
DSG4_HUMANDSG4physical
28514442
PLCD1_HUMANPLCD1physical
28514442
PKP3_HUMANPKP3physical
28514442
LRC15_HUMANLRRC15physical
28514442
PADI3_HUMANPADI3physical
28514442
PA24B_HUMANJMJD7-PLA2G4Bphysical
28514442
SBP1_HUMANSELENBP1physical
28514442
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 SMRD1_HUMAN

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