UniProt Accession

 SSRP1_HUMAN; Q08945; Q5BJG8 

Genbank Protein ID

 M86737; BC005116; BC091486 

Genbank Nucleotide ID

 AAA58660.1; AAH05116.1; AAH91486.1 

Protein Name

 FACT complex subunit SSRP1 

Protein Synonyms/Alias

 Chromatin-specific transcription elongation factor 80 kDa subunit; Facilitates chromatin transcription complex 80 kDa subunit; FACT 80 kDa subunit; FACTp80; Facilitates chromatin transcription complex subunit SSRP1; Recombination signal sequence recognition protein 1; Structure-specific recognition protein 1; hSSRP1; T160 

Gene Name

 SSRP1 

Gene Synonyms/Alias

 FACT80 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
15	NDVYQEVKGSMNDGR	ubiquitination	[1, 2, 3, 4, 5]
33	SRQGIIFKNSKTGKV	acetylation	[6]
33	SRQGIIFKNSKTGKV	ubiquitination	[3]
36	GIIFKNSKTGKVDNI	ubiquitination	[3]
39	FKNSKTGKVDNIQAG	ubiquitination	[3, 5, 7]
63	VALGHGLKLLTKNGH	ubiquitination	[1, 3, 4, 5, 8]
67	HGLKLLTKNGHVYKY	ubiquitination	[3, 5]
73	TKNGHVYKYDGFRES	ubiquitination	[5]
84	FRESEFEKLSDFFKT	ubiquitination	[1, 3, 4, 5, 7]
90	EKLSDFFKTHYRLEL	acetylation	[6]
90	EKLSDFFKTHYRLEL	ubiquitination	[1, 3, 4, 5]
100	YRLELMEKDLCVKGW	ubiquitination	[3, 5, 8]
105	MEKDLCVKGWNWGTV	ubiquitination	[2, 3, 8]
228	TFLHLHGKTFDYKIP	ubiquitination	[1, 4]
233	HGKTFDYKIPYTTVL	acetylation	[6]
233	HGKTFDYKIPYTTVL	ubiquitination	[1, 3, 4, 7, 8]
304	RFEGRLTKNMSGSLY	ubiquitination	[1, 3, 4, 5, 7, 8]
319	EMVSRVMKALVNRKI	ubiquitination	[1, 3, 4]
325	MKALVNRKITVPGNF	ubiquitination	[3, 5]
364	RGFIYVHKPPVHIRF	acetylation	[5]
364	RGFIYVHKPPVHIRF	ubiquitination	[3]
413	IEREEYGKLFDFVNA	acetylation	[6]
413	IEREEYGKLFDFVNA	ubiquitination	[5, 8]
421	LFDFVNAKKLNIKNR	ubiquitination	[3]
542	PVEVKKGKDPNAPKR	acetylation	[5, 6]
548	GKDPNAPKRPMSAYM	acetylation	[6]
566	NASREKIKSDHPGIS	ubiquitination	[1, 4, 5]
661	RQLSESFKSKEFVSS	acetylation	[5]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 

Functional 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. 

Sequence Annotation

 DNA_BIND 547 615 HMG box.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 170 170 Phosphothreonine.
 MOD_RES 233 233 N6-acetyllysine.
 MOD_RES 413 413 N6-acetyllysine.
 MOD_RES 437 437 Phosphoserine.
 MOD_RES 441 441 Phosphotyrosine (By similarity).
 MOD_RES 444 444 Phosphoserine.
 MOD_RES 510 510 Phosphoserine; by CK2 (Probable).
 MOD_RES 657 657 Phosphoserine.
 MOD_RES 659 659 Phosphoserine.
 MOD_RES 667 667 Phosphoserine.
 MOD_RES 668 668 Phosphoserine.
 MOD_RES 671 671 Phosphoserine.
 MOD_RES 672 672 Phosphoserine.
 MOD_RES 673 673 Phosphoserine.
 MOD_RES 688 688 Phosphoserine; by CK2 (Probable).  

Keyword

 Acetylation; Chromosome; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA replication; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 709 AA 

Protein Sequence

Gene Ontology

 GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
 GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
 GO:0022415; P:viral reproductive process; TAS:Reactome. 

Interpro

 IPR013719; DUF1747.
 IPR009071; HMG_box_dom.
 IPR011993; PH_like_dom.
 IPR000969; SSrcognition.
 IPR024954; SSRP1_dom. 

Pfam

 PF00505; HMG_box
 PF08512; Rtt106
 PF03531; SSrecog 

SMART

 SM00398; HMG 

PROSITE

 PS50118; HMG_BOX_2 

PRINTS

 PR00887; SSRCOGNITION.