UniProt Accession

 SSRP1_RAT; Q04931; Q5XIT2 

Genbank Protein ID

 BC083588; L08814 

Genbank Nucleotide ID

 AAH83588.1; AAA40927.1 

Protein Name

 FACT complex subunit SSRP1 

Protein Synonyms/Alias

 Facilitates chromatin transcription complex subunit SSRP1; Recombination signal sequence recognition protein 1; Structure-specific recognition protein 1; T160 

Gene Name

 Ssrp1 

Gene Synonyms/Alias

 Ciidbp 

Created Date

 July 27, 2013 

Organism

 Rattus norvegicus (Rat) 

NCBI Taxa ID

 10116 

Lysine Modification

Position	Peptide	Type	References
84	FRESEFEKLSDFFKT	ubiquitination	[1]
100	YRLELMEKDLCVKGW	ubiquitination	[1]
105	MEKDLCVKGWNWGTV	ubiquitination	[1]
233	HGKTFDYKIPYTTVL	acetylation	[2]
661	RQLSDSFKSKEFVSS	acetylation	[2]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 

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. Also acts as a transcriptional coactivator for p63/TP63 (By similarity). 

Sequence Annotation

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

Keyword

 Acetylation; Chromosome; Complete proteome; DNA damage; DNA repair; DNA replication; DNA-binding; Nucleus; Phosphoprotein; 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; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; NAS:RGD.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

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.