SSRP1
entrez
6749
canonical
uniprot
Q08945
canonical
ensembl
ENSG00000149136
resolver
ensp
ENSP00000278412
resolver
ensp
ENSP00000527914
resolver
ensp
ENSP00000527915
resolver
ensp
ENSP00000527918
resolver
ensp
ENSP00000610029
resolver
ensp
ENSP00000610035
resolver
ensp
ENSP00000610037
resolver
enst
ENST00000278412
resolver
enst
ENST00000857855
resolver
enst
ENST00000857856
resolver
enst
ENST00000857859
resolver
enst
ENST00000939970
resolver
enst
ENST00000939976
resolver
enst
ENST00000939978
resolver
genesymbol
SSRP1
resolver
genesymbol_syn
FACT80
resolver
hgnc
HGNC:11327
resolver
uniprot
Q5BJG8
resolver
uniprot_entry
SSRP1_HUMAN
resolver
uniprot_sec
Q5BJG8
resolver
amino_acid_sequence
MAETLEFNDVYQEVKGSMNDGRLRLSRQGIIFKNSKTGKVDNIQAGELTEGIWRRVALGHGLKLLTKNGHVYKYDGFRESEFEKLSDFFKTHYRLELMEKDLCVKGWNWGTVKFGGQLLSFDIGDQPVFEIPLSNVSQCTTGKNEVTLEFHQNDDAEVSLMEVRFYVPPTQEDGVDPVEAFAQNVLSKADVIQATGDAICIFRELQCLTPRGRYDIRIYPTFLHLHGKTFDYKIPYTTVLRLFLLPHKDQRQMFFVISLDPPIKQGQTRYHFLILLFSKDEDISLTLNMNEEEVEKRFEGRLTKNMSGSLYEMVSRVMKALVNRKITVPGNFQGHSGAQCITCSYKASSGLLYPLERGFIYVHKPPVHIRFDEISFVNFARGTTTTRSFDFEIETKQGTQYTFSSIEREEYGKLFDFVNAKKLNIKNRGLKEGMNPSYDEYADSDEDQHDAYLERMKEEGKIREENANDSSDDSGEETDESFNPGEEEEDVAEEFDSNASASSSSNEGDSDRDEKKRKQLKKAKMAKDRKSRKKPVEVKKGKDPNAPKRPMSAYMLWLNASREKIKSDHPGISITDLSKKAGEIWKGMSKEKKEEWDRKAEDARRDYEKAMKEYEGGRGESSKRDKSKKKKKVKVKMEKKSTPSRGSSSKSSSRQLSESFKSKEFVSSDESSSGENKSKKKRRRSEDSEEEELASTPPSSEDSASGSDE
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12374749, ECO:0000269|PubMed:12934006, ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:9489704, ECO:0000269|PubMed:9566881, ECO:0000269|PubMed:9836642}.
uniprot
proteins
mass_dalton
81075
uniprot
proteins
mutagenesis
MUTAGEN 450; /note="D->A: Abolishes cleavage by caspase."; /evidence="ECO:0000269|PubMed:16498457"; MUTAGEN 510; /note="S->A: Unable to bind DNA; when associated with A-657 and A-688."; /evidence="ECO:0000269|PubMed:15659405"; MUTAGEN 657; /note="S->A: Unable to bind DNA; when associated with A-510 and A-688. Still able to bind DNA; when associated with A-688."; /evidence="ECO:0000269|PubMed:15659405"; MUTAGEN 688; /note="S->A: Unable to bind DNA; when associated with A-510 and A-657. Still able to bind DNA; when associated with A-657."; /evidence="ECO:0000269|PubMed:15659405
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by CK2 following UV but not gamma irradiation. Phosphorylation inhibits its DNA-binding activity. {ECO:0000269|PubMed:12393879, ECO:0000269|PubMed:15659405}.; PTM: Ubiquitinated. Polyubiquitinated following caspase cleavage resulting in degradation of the N-terminal ubiquitinated part of the cleaved protein. {ECO:0000269|PubMed:16498457}.; PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
uniprot
proteins
protein_family
SSRP1 family
uniprot
proteins
pubmed
10421373
uniprot
proteins
pubmed
10912001
uniprot
proteins
pubmed
11239457
uniprot
proteins
pubmed
11344167
uniprot
proteins
pubmed
11824977
uniprot
proteins
pubmed
12374749
uniprot
proteins
pubmed
12393879
uniprot
proteins
pubmed
12934006
uniprot
proteins
pubmed
1372440
uniprot
proteins
pubmed
14660563
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15561718
uniprot
proteins
pubmed
15659405
uniprot
proteins
pubmed
16498457
uniprot
proteins
pubmed
16713563
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19836239
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22002106
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27499292
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28611249
uniprot
proteins
pubmed
9489704
uniprot
proteins
pubmed
9566881
uniprot
proteins
pubmed
9836642
uniprot
proteins
sequence_length
709
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10421373, ECO:0000269|PubMed:22002106}. Nucleus, nucleolus {ECO:0000269|PubMed:22002106}. Chromosome {ECO:0000269|PubMed:10421373}. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. {ECO:0000250|UniProtKB:Q05344}.
uniprot
proteins