SSRP1_RAT - dbPTM
SSRP1_RAT - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAETLEFND
------CCCEECHHH
20.62-
84UbiquitinationFRESEFEKLSDFFKT
CCHHHHHHHHHHHHH
59.62-
100UbiquitinationYRLELMEKDLCVKGW
HHHHHHHHCEEECCC
41.87-
105UbiquitinationMEKDLCVKGWNWGTV
HHHCEEECCCCCEEE
58.15-
111PhosphorylationVKGWNWGTVKFGGQL
ECCCCCEEEEECCEE
16.4923984901
170PhosphorylationVRFYVPPTQEDGVDP
EEEECCCCCCCCCCH
38.22-
233AcetylationHGKTFDYKIPYTTVL
CCCCCCCCCCCHHHE
38.7622902405
413AcetylationIEREEYGKLFDFVNA
EEHHHHHHHHHHHCH
45.11-
438PhosphorylationKEGINPGYDDYADSD
CCCCCCCCCCCCCCC
13.6025403869
441PhosphorylationINPGYDDYADSDEDQ
CCCCCCCCCCCCHHH
14.9227097102
444PhosphorylationGYDDYADSDEDQHDA
CCCCCCCCCHHHHHH
34.4323712012
452PhosphorylationDEDQHDAYLERMKEE
CHHHHHHHHHHHHHH
18.3627097102
471PhosphorylationEENANDSSDDSGEET
CCCCCCCCCCCCCCC
48.58-
510PhosphorylationSSSNEGDSDREEKKR
CCCCCCCCHHHHHHH
49.80-
536PhosphorylationRKSRKKSSEGKKGKD
HHHHHHCCCCCCCCC
60.2825532521
542AcetylationSSEGKKGKDPNAPKR
CCCCCCCCCCCCCCC
78.04-
657PhosphorylationKSSSRQLSDSFKSKE
CHHHCHHCHHHHCHH
23.9122108457
659PhosphorylationSSRQLSDSFKSKEFV
HHCHHCHHHHCHHHH
31.0622108457
661AcetylationRQLSDSFKSKEFVSS
CHHCHHHHCHHHHCC
65.6522902405
662PhosphorylationQLSDSFKSKEFVSSD
HHCHHHHCHHHHCCC
35.0928432305
667PhosphorylationFKSKEFVSSDESSSG
HHCHHHHCCCCCCCC
37.0828432305
668PhosphorylationKSKEFVSSDESSSGE
HCHHHHCCCCCCCCC
39.8428432305
671PhosphorylationEFVSSDESSSGENKS
HHHCCCCCCCCCCHH
34.4928432305
672PhosphorylationFVSSDESSSGENKSK
HHCCCCCCCCCCHHH
40.0721630457
673PhosphorylationVSSDESSSGENKSKK
HCCCCCCCCCCHHHH
60.4528432305
688PhosphorylationKRRRSEDSDEEELAS
CCCCCCCCCHHHHHC
42.76-

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
510SPhosphorylationKinaseCK2-Uniprot
657SPhosphorylationKinaseCK2-Uniprot
688SPhosphorylationKinaseCK2-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSRP1_RAT !!

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 SSRP1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SSRP1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SSRP1_RAT

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Related Literatures of Post-Translational Modification

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