SSRP1_MOUSE - dbPTM
SSRP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSRP1_MOUSE
UniProt AC Q08943
Protein Name FACT complex subunit SSRP1
Gene Name Ssrp1
Organism Mus musculus (Mouse).
Sequence Length 708
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. Also acts as a transcriptional coactivator for p63/TP63..
Protein Sequence MAETLEFNDIFQEVKGSMNDGRLRLSRQGIIFKNSKTGKVDNIQAGELTEGIWRRVALGHGLKLLTKNGHVYKYDGFRESEFEKLSDFFKTHYRLELMEKDLCVKGWNWGTVKFGGQLLSFDIGDQPVFEIPLSNVSQCTTGKNEVTLEFHQNDDAEVSLMEVRFYVPPTQEDGVDPVEAFAQNVLSKADVIQATGDAICIFRELQCLTPRGRYDIRIYPTFLHLHGKTFDYKIPYTTVLRLFLLPHKDQRQMFFVISLDPPIKQGQTRYHFLILLFSKDEDISLTLNMNEEEVEKRFEGRLTKNMSGSLYEMVSRVMKALVNRKITVPGNFQGHSGAQCITCSYKASSGLLYPLERGFIYVHKPPVHIRFDEISFVNFARGTTTTRSFDFEIETKQGTQYTFSSIEREEYGKLFDFVNAKKLNIKNRGLKEGINPGYDDYADSDEDQHDAYLERMKEEGKIREENANDSSDDSGEETDESFNPGEEEEDVAEEFDSNASASSSSNEGDSDREEKKREQLKRAKMAKDRKSRRKSSEAKKGKDPNAPKRPMSAYMLWLNASREKIKSDHPGISITDLSKKAGEIWKGMSKEKKEEWDRKAEDARREYEKAMKEYEGGRGDSSKRDKSKKKKKVKAKMEKKSTPSRGSSSKSSSRQLSDSFKSKEFVSSDESSSGENKSKKKRRRSEDSEEELASTPPSSEDSASGSDE
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-
39UbiquitinationFKNSKTGKVDNIQAG
EECCCCCCCCCEECC		52.20-
84UbiquitinationFRESEFEKLSDFFKT
CCHHHHHHHHHHHHH		59.62-
84AcetylationFRESEFEKLSDFFKT
CCHHHHHHHHHHHHH		59.6222826441
100UbiquitinationYRLELMEKDLCVKGW
HHHHHHHHCEEECCC		41.87-
105UbiquitinationMEKDLCVKGWNWGTV
HHHCEEECCCCCEEE		58.15-
111PhosphorylationVKGWNWGTVKFGGQL
ECCCCCEEEEECCEE		16.4927600695
120PhosphorylationKFGGQLLSFDIGDQP
EECCEEEEEECCCCE		29.4826643407
170PhosphorylationVRFYVPPTQEDGVDP
EEEECCCCCCCCCCH		38.22-
233AcetylationHGKTFDYKIPYTTVL
CCCCCCCCCCCHHHE		38.7623236377
311PhosphorylationKNMSGSLYEMVSRVM
CCCCCHHHHHHHHHH		12.04-
319MalonylationEMVSRVMKALVNRKI
HHHHHHHHHHHCCCE		35.3926320211
401PhosphorylationETKQGTQYTFSSIER
EECCCCEEEEEEEEH		15.0227566939
413AcetylationIEREEYGKLFDFVNA
EEHHHHHHHHHHHCH		45.1122826441
438PhosphorylationKEGINPGYDDYADSD
CCCCCCCCCCCCCCC		13.6024925903
441PhosphorylationINPGYDDYADSDEDQ
CCCCCCCCCCCCHHH		14.9224925903
444 (in isoform 2)Phosphorylation-34.4319144319
444PhosphorylationGYDDYADSDEDQHDA
CCCCCCCCCHHHHHH		34.4324925903
452PhosphorylationDEDQHDAYLERMKEE
CHHHHHHHHHHHHHH		18.3625521595
471PhosphorylationEENANDSSDDSGEET
CCCCCCCCCCCCCCC		48.58-
510PhosphorylationSSSNEGDSDREEKKR
CCCCCCCCHHHHHHH		49.80-
524AcetylationREQLKRAKMAKDRKS
HHHHHHHHHHHHHHH		43.347627701
535PhosphorylationDRKSRRKSSEAKKGK
HHHHHHHHHHHHCCC		31.44-
536PhosphorylationRKSRRKSSEAKKGKD
HHHHHHHHHHHCCCC		44.61-
539AcetylationRRKSSEAKKGKDPNA
HHHHHHHHCCCCCCC		58.996566397
542AcetylationSSEAKKGKDPNAPKR
HHHHHCCCCCCCCCC		78.0423806337
548AcetylationGKDPNAPKRPMSAYM
CCCCCCCCCCHHHHH		67.726568849
549MethylationKDPNAPKRPMSAYML
CCCCCCCCCHHHHHH		30.9718967765
621PhosphorylationYEGGRGDSSKRDKSK
HCCCCCCCCCCHHHH		40.3526824392
622PhosphorylationEGGRGDSSKRDKSKK
CCCCCCCCCCHHHHH		36.1329550500
651PhosphorylationSRGSSSKSSSRQLSD
CCCCCCCHHHCHHCH		35.1829550500
652PhosphorylationRGSSSKSSSRQLSDS
CCCCCCHHHCHHCHH		33.0229550500
653PhosphorylationGSSSKSSSRQLSDSF
CCCCCHHHCHHCHHH		31.0129550500
657PhosphorylationKSSSRQLSDSFKSKE
CHHHCHHCHHHHCHH		23.9122942356
659PhosphorylationSSRQLSDSFKSKEFV
HHCHHCHHHHCHHHH		31.0626824392
662PhosphorylationQLSDSFKSKEFVSSD
HHCHHHHCHHHHCCC		35.0925159016
667PhosphorylationFKSKEFVSSDESSSG
HHCHHHHCCCCCCCC		37.0827087446
668PhosphorylationKSKEFVSSDESSSGE
HCHHHHCCCCCCCCC		39.8427087446
671PhosphorylationEFVSSDESSSGENKS
HHHCCCCCCCCCCHH		34.4923684622
672PhosphorylationFVSSDESSSGENKSK
HHCCCCCCCCCCHHH		40.0727087446
673PhosphorylationVSSDESSSGENKSKK
HCCCCCCCCCCHHHH		60.4527087446
678PhosphorylationSSSGENKSKKKRRRS
CCCCCCHHHHCCCCC		62.3825159016
685PhosphorylationSKKKRRRSEDSEEEL
HHHCCCCCCCCHHHH		43.9025338131
688PhosphorylationKRRRSEDSEEELAST
CCCCCCCCHHHHHCC		42.7425338131
695PhosphorylationSEEELASTPPSSEDS
CHHHHHCCCCCCCCC		33.3424719451
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_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SSRP1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SSRP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444; SER-667 ANDSER-668, AND MASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667; SER-668; SER-671;SER-672 AND SER-673, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-441, AND MASSSPECTROMETRY.

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