| UniProt ID | SNF5_HUMAN | |
|---|---|---|
| UniProt AC | Q12824 | |
| Protein Name | SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 | |
| Gene Name | SMARCB1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 385 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Core component of the BAF (hSWI/SNF) complex. This ATP-dependent chromatin-remodeling complex plays important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling would be due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures, termed altosomes, each composed of 2 histones octamers. Stimulates in vitro the remodeling activity of SMARCA4/BRG1/BAF190A. Involved in activation of CSF1 promoter. 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). Plays a key role in cell-cycle control and causes cell cycle arrest in G0/G1.. | |
| Protein Sequence | MMMMALSKTFGQKPVKFQLEDDGEFYMIGSEVGNYLRMFRGSLYKRYPSLWRRLATVEERKKIVASSHGKKTKPNTKDHGYTTLATSVTLLKASEVEEILDGNDEKYKAVSISTEPPTYLREQKAKRNSQWVPTLPNSSHHLDAVPCSTTINRNRMGRDKKRTFPLCFDDHDPAVIHENASQPEVLVPIRLDMEIDGQKLRDAFTWNMNEKLMTPEMFSEILCDDLDLNPLTFVPAIASAIRQQIESYPTDSILEDQSDQRVIIKLNIHVGNISLVDQFEWDMSEKENSPEKFALKLCSELGLGGEFVTTIAYSIRGQLSWHQKTYAFSENPLPTVEIAIRNTGDADQWCPLLETLTDAEMEKKIRDQDRNTRRMRRLANTAPAW | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 7 | Phosphorylation | -MMMMALSKTFGQKP -CCCCCCCCHHCCCC | 21.80 | 21406692 | |
| 8 | Ubiquitination | MMMMALSKTFGQKPV CCCCCCCCHHCCCCC | 49.04 | - | |
| 9 | O-linked_Glycosylation | MMMALSKTFGQKPVK CCCCCCCHHCCCCCE | 29.62 | 28510447 | |
| 13 | Ubiquitination | LSKTFGQKPVKFQLE CCCHHCCCCCEEEEC | 52.75 | - | |
| 16 | Ubiquitination | TFGQKPVKFQLEDDG HHCCCCCEEEECCCC | 35.60 | - | |
| 49 | Phosphorylation | SLYKRYPSLWRRLAT CHHHHCHHHHHHHCC | 31.46 | 20044836 | |
| 67 (in isoform 2) | Phosphorylation | - | 26.90 | - | |
| 77 | Acetylation | KKTKPNTKDHGYTTL CCCCCCCCCCCCCCH | 55.13 | 23749302 | |
| 77 | Ubiquitination | KKTKPNTKDHGYTTL CCCCCCCCCCCCCCH | 55.13 | - | |
| 92 | Ubiquitination | ATSVTLLKASEVEEI HHEEEEEEHHHHHHH | 53.64 | - | |
| 94 | Phosphorylation | SVTLLKASEVEEILD EEEEEEHHHHHHHHC | 40.36 | - | |
| 97 (in isoform 2) | Ubiquitination | - | 34.96 | 21890473 | |
| 106 | Ubiquitination | ILDGNDEKYKAVSIS HHCCCCHHEEEEEEE | 55.72 | 21906983 | |
| 106 (in isoform 1) | Ubiquitination | - | 55.72 | 21890473 | |
| 106 | Sumoylation | ILDGNDEKYKAVSIS HHCCCCHHEEEEEEE | 55.72 | 28112733 | |
| 106 | Acetylation | ILDGNDEKYKAVSIS HHCCCCHHEEEEEEE | 55.72 | 26051181 | |
| 108 | Sumoylation | DGNDEKYKAVSISTE CCCCHHEEEEEEECC | 54.07 | 28112733 | |
| 108 | Ubiquitination | DGNDEKYKAVSISTE CCCCHHEEEEEEECC | 54.07 | - | |
| 111 | Phosphorylation | DEKYKAVSISTEPPT CHHEEEEEEECCCCC | 18.71 | 28152594 | |
| 113 | Phosphorylation | KYKAVSISTEPPTYL HEEEEEEECCCCCHH | 21.15 | 28152594 | |
| 114 | Phosphorylation | YKAVSISTEPPTYLR EEEEEEECCCCCHHH | 51.33 | 28152594 | |
| 118 | Phosphorylation | SISTEPPTYLREQKA EEECCCCCHHHHHHH | 46.00 | 28152594 | |
| 119 | Phosphorylation | ISTEPPTYLREQKAK EECCCCCHHHHHHHH | 14.99 | 28152594 | |
| 124 | Ubiquitination | PTYLREQKAKRNSQW CCHHHHHHHHHCCCC | 51.64 | - | |
| 124 | Sumoylation | PTYLREQKAKRNSQW CCHHHHHHHHHCCCC | 51.64 | 28112733 | |
| 129 | Phosphorylation | EQKAKRNSQWVPTLP HHHHHHCCCCCCCCC | 29.47 | 17525332 | |
| 134 | Phosphorylation | RNSQWVPTLPNSSHH HCCCCCCCCCCCCCC | 45.27 | 30108239 | |
| 138 | Phosphorylation | WVPTLPNSSHHLDAV CCCCCCCCCCCCCCC | 29.16 | 30108239 | |
| 139 | Phosphorylation | VPTLPNSSHHLDAVP CCCCCCCCCCCCCCC | 22.90 | 30108239 | |
| 148 | Phosphorylation | HLDAVPCSTTINRNR CCCCCCCCCCCCCCC | 23.63 | 30108239 | |
| 149 | Phosphorylation | LDAVPCSTTINRNRM CCCCCCCCCCCCCCC | 38.11 | 30108239 | |
| 150 | Phosphorylation | DAVPCSTTINRNRMG CCCCCCCCCCCCCCC | 10.44 | 30108239 | |
| 161 | Sumoylation | NRMGRDKKRTFPLCF CCCCCCCCCCCCCCC | 62.04 | 28112733 | |
| 190 (in isoform 2) | Ubiquitination | - | 20.68 | 21890473 | |
| 199 | Ubiquitination | DMEIDGQKLRDAFTW EEEECCEEHHHHHCC | 51.52 | 21906983 | |
| 199 (in isoform 1) | Ubiquitination | - | 51.52 | 21890473 | |
| 250 | Phosphorylation | QQIESYPTDSILEDQ HHHHHCCCCCCCCCC | 33.86 | 28555341 | |
| 283 (in isoform 2) | Ubiquitination | - | 6.13 | 21890473 | |
| 283 | Ubiquitination | VDQFEWDMSEKENSP EEEEECCCCCCCCCH | 6.13 | 21890473 | |
| 292 | Ubiquitination | EKENSPEKFALKLCS CCCCCHHHHHHHHHH | 39.04 | 21890473 | |
| 292 (in isoform 1) | Ubiquitination | - | 39.04 | 21890473 | |
| 314 | Phosphorylation | FVTTIAYSIRGQLSW EEEEEHHHHHCCCCE | 9.22 | 24719451 | |
| 324 | Ubiquitination | GQLSWHQKTYAFSEN CCCCEEECEEEECCC | 30.53 | - | |
| 350 | Glutathionylation | TGDADQWCPLLETLT CCCHHHHHHHHHHHC | 1.09 | 22555962 | |
| 364 | Ubiquitination | TDAEMEKKIRDQDRN CHHHHHHHHHHCCHH | 29.66 | - | |
| 372 | Phosphorylation | IRDQDRNTRRMRRLA HHHCCHHHHHHHHHH | 22.12 | - |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SNF5_HUMAN !! | ||||||
* 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 SNF5_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 609322 | Rhabdoid tumor predisposition syndrome 1 (RTPS1) | |||||
| 162091 | Schwannomatosis 1 (SWNTS1) | |||||
| 614608 | Mental retardation, autosomal dominant 15 (MRD15) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-129, AND MASSSPECTROMETRY. | |
