UniProt ID | SSRP1_RAT | |
---|---|---|
UniProt AC | Q04931 | |
Protein Name | FACT complex subunit SSRP1 | |
Gene Name | Ssrp1 | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 709 | |
Subcellular Localization | Nucleus . Chromosome . Nucleus, nucleolus . Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. | |
Protein Description | Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63.. | |
Protein Sequence | MAETLEFNDIFQEVKGSMNDGRLRLSRQGIIFKNSKTGKVDNIQAGELTEGIWRRVALGHGLKLLTKNGHVYKYDGFRESEFEKLSDFFKTHYRLELMEKDLCVKGWNWGTVKFGGQLLSFDIGDQPVFEIPLSNVSQCTTGKNEVTLEFHQNDDAEVSLMEVRFYVPPTQEDGVDPVEAFAQNVLSKADVIQATGDAICIFRELQCLTPRGRYDIRIYPTFLHLHGKTFDYKIPYTTVLRLFLLPHKDQRQMFFVISLDPPIKQGQTRYHFLILLFSKDEDISLTLNMNEEEVEKRFEGRLTKNMSGSLYEMVSRVMKALVNRKITVPGNFQGHSGAQCITCSYKASSGLLYPLERGFIYVHKPPVHIRFDEISFVNFARGTTTTRSFDFEIETKQGTQYTFSSIEREEYGKLFDFVNAKKLNIKNRGLKEGINPGYDDYADSDEDQHDAYLERMKEEGKIREENANDSSDDSGEETDESFNPGEEEEDVAEEFDSNASASSSSNEGDSDREEKKRKQLKRAKMAKDRKSRKKSSEGKKGKDPNAPKRPMSAYMLWLNASREKIKSDHPGISITDLSKKAGEIWKGMSKEKKEEWDRKAEDARREYEKAMKEYEGGRGDSSKRDKSKKKKKVKAKLEKKSTPSRGSSSKSSSRQLSDSFKSKEFVSSDESSSGENKSKKKRRRSEDSDEEELASTPPSSEDSASGSDE | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAETLEFND ------CCCEECHHH | 20.62 | - | |
84 | Ubiquitination | FRESEFEKLSDFFKT CCHHHHHHHHHHHHH | 59.62 | - | |
100 | Ubiquitination | YRLELMEKDLCVKGW HHHHHHHHCEEECCC | 41.87 | - | |
105 | Ubiquitination | MEKDLCVKGWNWGTV HHHCEEECCCCCEEE | 58.15 | - | |
111 | Phosphorylation | VKGWNWGTVKFGGQL ECCCCCEEEEECCEE | 16.49 | 23984901 | |
170 | Phosphorylation | VRFYVPPTQEDGVDP EEEECCCCCCCCCCH | 38.22 | - | |
233 | Acetylation | HGKTFDYKIPYTTVL CCCCCCCCCCCHHHE | 38.76 | 22902405 | |
413 | Acetylation | IEREEYGKLFDFVNA EEHHHHHHHHHHHCH | 45.11 | - | |
438 | Phosphorylation | KEGINPGYDDYADSD CCCCCCCCCCCCCCC | 13.60 | 25403869 | |
441 | Phosphorylation | INPGYDDYADSDEDQ CCCCCCCCCCCCHHH | 14.92 | 27097102 | |
444 | Phosphorylation | GYDDYADSDEDQHDA CCCCCCCCCHHHHHH | 34.43 | 23712012 | |
452 | Phosphorylation | DEDQHDAYLERMKEE CHHHHHHHHHHHHHH | 18.36 | 27097102 | |
471 | Phosphorylation | EENANDSSDDSGEET CCCCCCCCCCCCCCC | 48.58 | - | |
510 | Phosphorylation | SSSNEGDSDREEKKR CCCCCCCCHHHHHHH | 49.80 | - | |
536 | Phosphorylation | RKSRKKSSEGKKGKD HHHHHHCCCCCCCCC | 60.28 | 25532521 | |
542 | Acetylation | SSEGKKGKDPNAPKR CCCCCCCCCCCCCCC | 78.04 | - | |
657 | Phosphorylation | KSSSRQLSDSFKSKE CHHHCHHCHHHHCHH | 23.91 | 22108457 | |
659 | Phosphorylation | SSRQLSDSFKSKEFV HHCHHCHHHHCHHHH | 31.06 | 22108457 | |
661 | Acetylation | RQLSDSFKSKEFVSS CHHCHHHHCHHHHCC | 65.65 | 22902405 | |
662 | Phosphorylation | QLSDSFKSKEFVSSD HHCHHHHCHHHHCCC | 35.09 | 28432305 | |
667 | Phosphorylation | FKSKEFVSSDESSSG HHCHHHHCCCCCCCC | 37.08 | 28432305 | |
668 | Phosphorylation | KSKEFVSSDESSSGE HCHHHHCCCCCCCCC | 39.84 | 28432305 | |
671 | Phosphorylation | EFVSSDESSSGENKS HHHCCCCCCCCCCHH | 34.49 | 28432305 | |
672 | Phosphorylation | FVSSDESSSGENKSK HHCCCCCCCCCCHHH | 40.07 | 21630457 | |
673 | Phosphorylation | VSSDESSSGENKSKK HCCCCCCCCCCHHHH | 60.45 | 28432305 | |
688 | Phosphorylation | KRRRSEDSDEEELAS CCCCCCCCCHHHHHC | 42.76 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
510 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
657 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
688 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SSRP1_RAT !! |
* 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 SSRP1_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of SSRP1_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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