Overview
| Uniprot ID | F1S8K5 |
| Protein Name | FACT complex subunit |
| Gene Name | SUPT16H |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 192 |
SWNDCLNKEGFDKID |
| 259 |
KLAESVEKAIEEKKY |
| 316 |
CAMGIRFKSYCSNLV |
| 462 |
TSVKKKVKNVGIFLK |
| 515 |
EKRRAHQKELAAQLN |
| 540 |
KGEQQIQKARKSNVS |
| 662 |
QNAFRIIKEVQKRYK |
| 732 |
FTSVRGDKVDILYNN |
| 817 |
HKLKTAFKNFIEKVE |
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)
Protein Sequence
10
MLPGHWESAG
20
FRGRERVAEP
30
GPRVILGTRG
40
GAASVAMAVT
50
LDKDAYYRRV
60
KRLYSNWRKG
70
EDEYANVDAI
80
VVSVGVDEEI
90
VYAKSTALQT
100
WLFGYELTDT
110
IMVFCDDKII
120
FMASKKKVEF
130
LKQIANTKGN
140
ENANGAPAIT
150
LLIREKNESN
160
KSSFDKMIEA
170
IKESKNGKKI
180
GVFSKDKFPG
190
EFMKSWNDCL
200
NKEGFDKIDI
210
SAVVAYTIAV
220
KEDGELNLMK
230
KAASITSEVF
240
NKFFKERVME
250
IVDADEKVRH
260
SKLAESVEKA
270
IEEKKYLAGA
280
DPSTVEMCYP
290
PIIQSGGNYN
300
LKFSVVSDKN
310
HMHFGAITCA
320
MGIRFKSYCS
330
NLVRTLMVDP
340
SQEVQENYNF
350
LLQLQEELLK
360
ELRHGVKICD
370
VYNAVMDVVK
380
KQKPELLNKI
390
TKNLGFGMGI
400
EFREGSLVIN
410
SKNQYKLKKG
420
MVFSINLGFS
430
DLTNKEGKKP
440
EEKTYALFIG
450
DTVLVDEDGP
460
ATVLTSVKKK
470
VKNVGIFLKN
480
EDEEEEEEEK
490
DEAEDLLGRG
500
SRAALLTERT
510
RNEMTAEEKR
520
RAHQKELAAQ
530
LNEEAKRRLT
540
EQKGEQQIQK
550
ARKSNVSYKN
560
PSLMPKEPHI
570
REMKIYIDKK
580
YETVIMPVFG
590
IATPFHIATI
600
KNISMSVEGD
610
YTYLRINFYC
620
PGSALGRNEG
630
NIFPNPEATF
640
VKEITYRASN
650
MKAPGEQTVP
660
ALNLQNAFRI
670
IKEVQKRYKT
680
REAEEKEKEG
690
IVKQDSLVIN
700
LNRSNPKLKD
710
LYIRPNIAQK
720
RMQGSLEAHV
730
NGFRFTSVRG
740
DKVDILYNNI
750
KHALFQPCDG
760
EMIIVLHFHL
770
KNAIMFGKKR
780
HTDVQFYTEV
790
GEITTDLGKH
800
QHMHDRDDLY
810
AEQMEREMRH
820
KLKTAFKNFI
830
EKVEALTKEE
840
LEFEVPFRDL
850
GFNGAPYRST
860
CLLQPTSSAL
870
VNATEWPPFV
880
VTLDEVELIH
890
FERVQFHLKN
900
FDMVIVYKDY
910
SKKVTMINAI
920
PVASLDPIKE
930
WLNSCDLKYT
940
EGVQSLNWTK
950
IMKTIVDDPE
960
GFFEQGGWSF
970
LEPEGEGSDA
980
EEGDSESEIE
990
DETFNPSEDD
1000
YEEEEEDSDE
1010
DYSSEAEESD
1020
YSKESLGSEE
1030
ESGKDWDELE
1040
EEARKADRES
1050
RYEEEEEQSR
1060
SMSRKRKASV
1070
HSSGRGSNRG
1080
SRHSSAPPKK
KRK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0035101 |
FACT complex |
| Molecular Function |
GO:0031491 |
nucleosome binding |
| Biological Process |
GO:0006281 |
DNA repair |
| Biological Process |
GO:0006260 |
DNA replication |
| Biological Process |
GO:0006351 |
DNA-templated transcription |
| Biological Process |
GO:0006337 |
nucleosome disassembly |
| Biological Process |
GO:0032786 |
positive regulation of DNA-templated transcription, elongation |
| Biological Process |
GO:0032784 |
regulation of DNA-templated transcription elongation |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.