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Overview

Uniprot IDQ08945
Protein NameFACT complex subunit SSRP1
Gene NameSSRP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
228 TFLHLHGKTFDYKIP
364 RGFIYVHKPPVHIRF
421 LFDFVNAKKLNIKNR
422 FDFVNAKKLNIKNRG
533 AKDRKSRKKPVEVKK
579 ISITDLSKKAGEIWK
580 SITDLSKKAGEIWKG
623 GGRGESSKRDKSKKK
661 RQLSESFKSKEFVSS

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

Protein Sequence

10 MAETLEFNDV 20 YQEVKGSMND 30 GRLRLSRQGI 40 IFKNSKTGKV 50 DNIQAGELTE 60 GIWRRVALGH 70 GLKLLTKNGH 80 VYKYDGFRES 90 EFEKLSDFFK 100 THYRLELMEK 110 DLCVKGWNWG 120 TVKFGGQLLS 130 FDIGDQPVFE 140 IPLSNVSQCT 150 TGKNEVTLEF 160 HQNDDAEVSL 170 MEVRFYVPPT 180 QEDGVDPVEA 190 FAQNVLSKAD 200 VIQATGDAIC 210 IFRELQCLTP 220 RGRYDIRIYP 230 TFLHLHGKTF 240 DYKIPYTTVL 250 RLFLLPHKDQ 260 RQMFFVISLD 270 PPIKQGQTRY 280 HFLILLFSKD 290 EDISLTLNMN 300 EEEVEKRFEG 310 RLTKNMSGSL 320 YEMVSRVMKA 330 LVNRKITVPG 340 NFQGHSGAQC 350 ITCSYKASSG 360 LLYPLERGFI 370 YVHKPPVHIR 380 FDEISFVNFA 390 RGTTTTRSFD 400 FEIETKQGTQ 410 YTFSSIEREE 420 YGKLFDFVNA 430 KKLNIKNRGL 440 KEGMNPSYDE 450 YADSDEDQHD 460 AYLERMKEEG 470 KIREENANDS 480 SDDSGEETDE 490 SFNPGEEEED 500 VAEEFDSNAS 510 ASSSSNEGDS 520 DRDEKKRKQL 530 KKAKMAKDRK 540 SRKKPVEVKK 550 GKDPNAPKRP 560 MSAYMLWLNA 570 SREKIKSDHP 580 GISITDLSKK 590 AGEIWKGMSK 600 EKKEEWDRKA 610 EDARRDYEKA 620 MKEYEGGRGE 630 SSKRDKSKKK 640 KKVKVKMEKK 650 STPSRGSSSK 660 SSSRQLSESF 670 KSKEFVSSDE 680 SSSGENKSKK 690 KRRRSEDSEE 700 EELASTPPSS EDSASGSDE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0035101 FACT complex
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0042393 histone binding
Molecular Function GO:0031491 nucleosome binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006281 DNA repair
Biological Process GO:0006260 DNA replication
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006334 nucleosome assembly
Biological Process GO:0006337 nucleosome disassembly
Biological Process GO:1902275 regulation of chromatin organization

Reference

[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[2] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.