Overview
| Uniprot ID | Q2KHR3 |
| Protein Name | Glutamine and serine-rich protein 1 |
| Gene Name | QSER1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 1091 |
EEDNSNQKQLKRPAQ |
| 1130 |
DGYQHQEKMRQKIKE |
| 1259 |
TLDATSDKKKKTEAL |
| 1260 |
LDATSDKKKKTEALQ |
| 1388 |
PAIWKVQKALLQKFV |
| 1466 |
AKPSSSSKTSDPLAS |
| 1474 |
TSDPLASKTTTTKAP |
| 1479 |
ASKTTTTKAPSVKPK |
| 1486 |
KAPSVKPKVKQPKVK |
| 1493 |
KVKQPKVKAEPPPKK |
| 1625 |
ITRDSKAKSGGTAIS |
| 1654 |
RTSKTTTKSAQEFAV |
| 368 |
YRSSKVEKLPPLYKT |
| 674 |
PQIRLNTKDLKQQHP |
| 812 |
LQQHLTTKGHFSETN |
| 978 |
EQSSGPFKKQSATNL |
| 979 |
QSSGPFKKQSATNLE |
Function
Plays an essential role in the protection and maintenance of transcriptional and developmental programs. Protects many bivalent promoters and poised enhancers from hypermethylation, showing a marked preference for these regulatory elements over other types of promoters or enhancers. Mechanistically, cooperates with TET1 and binds to DNA in a common complex to inhibit the binding of DNMT3A/3B and therefore de novo methylation
Protein Sequence
10
MNFLSTAESR
20
TAQAAASGTT
30
LLPQFRAPSW
40
QTGMHSSAAT
50
ELFATGPLPS
60
TGTLPPSLSA
70
YQHPTTFSNR
80
NFATTSPLVL
90
QDSTFNTTSN
100
GILSHHDPLL
110
QIKTSQGTVP
120
TALAFERLGS
130
SVLSNSIPPQ
140
SSTYRSAQES
150
APHLLQPQFS
160
LLPSALGGSQ
170
QTPQAYSSTL
180
FTSSTASIER
190
ALLRECSVIK
200
HHQRPSGTQS
210
IQAQLTGSQH
220
SLHSYLSNSS
230
VVNFQETTRQ
240
SSLSCSPIGD
250
STQVSNGGLQ
260
QKTSQVSVEL
270
AQSYSSAIPS
280
SGYPPSTTKI
290
KSCSTEQPLT
300
STKTPKPQSI
310
IPPVQTLSYS
320
KPLHNQSSVI
330
SGQAQIYSTA
340
QLPSLLSVSQ
350
SQNYGLVQPH
360
NVPSIVHSQV
370
YRSSKVEKLP
380
PLYKTLTFSG
390
SSQTVTPENQ
400
TLNYSSNQQE
410
VLSSVTNENY
420
PAQTRDLSSV
430
SQSQSYSSGH
440
SQGLSPVSQT
450
QVSYSSQSQV
460
LSVVSLSESY
470
ASGESLTLTA
480
PSLSYSSASR
490
AQNLPDSSPT
500
QNYISMHSSQ
510
NVQTQESSSP
520
QSQKFLPAVQ
530
SSSFASSTHC
540
QTLQNNITSP
550
DPKSYAERKL
560
DSDVYPSSKQ
570
EDGFPMQELQ
580
VLQPQASLES
590
STQRLSDGEI
600
NAQESTYKVS
610
KADDRYSQSV
620
IRSNSRLEDQ
630
VIGVALQASK
640
KEESVVGSVT
650
QLNQQIGQVN
660
NAATLDLKNS
670
TNLIQTPQIR
680
LNTKDLKQQH
690
PLILKVHESK
700
VQEQHDQIIN
710
ASSQIQIPNH
720
ALGHGHQASL
730
PNTQVLLDSA
740
CDLQILQQSI
750
LQAGLGQVKA
760
SLQAQRVQSP
770
QQIVHPFLQM
780
EGHVIQSNGD
790
HSQQQLHPQN
800
SEVMKMDLSE
810
SSKPLQQHLT
820
TKGHFSETNQ
830
HDSKNQFVSL
840
GSMCFPEAVL
850
LSDERNILSN
860
VDDILAATAA
870
ACGVTPTDFS
880
KSTSNETMQA
890
VEDGDSKSHF
900
QQSLDVRHVT
910
SDFNSMTATV
920
GKPQNINDTS
930
LNGNQVTVNL
940
SPVPALQSKM
950
TLDQQHIETP
960
GQNIPTKVTS
970
AVVGPSHEVQ
980
EQSSGPFKKQ
990
SATNLESEED
1000
SEAPVDSTLN
1010
NNRNQEFVSS
1020
SRSISGENAT
1030
SESEFTLGGD
1040
DSGVSMNPAR
1050
SALALLAMAQ
1060
SGDAVSVKIE
1070
EENQDLMHFN
1080
LQKKRAKGKG
1090
QVKEEDNSNQ
1100
KQLKRPAQGK
1110
RQNPRGTDIY
1120
LPYTPPSSES
1130
CHDGYQHQEK
1140
MRQKIKEVEE
1150
KQPEVKTGFI
1160
ASFLDFLKSG
1170
PKQQFSTLAV
1180
RMPNRTRRPG
1190
TQMVRTFCPP
1200
PLPKPSSTTP
1210
TPLVSETGGN
1220
SPSDKVDNEL
1230
KNLEHLSSFS
1240
SDEDDPGYSQ
1250
DAYKSVSTPL
1260
TTLDATSDKK
1270
KKTEALQVAT
1280
TSPTANTTGT
1290
ATTSSTTVGA
1300
VKQEPLHSTS
1310
YAVNILENIS
1320
SSESSKPIEL
1330
DGLPSDQFAK
1340
GQDTVAIEGF
1350
TDEEDTESGG
1360
EGQYRERDEF
1370
VVKIEDIETF
1380
KEALKTGKEP
1390
PAIWKVQKAL
1400
LQKFVPEIRD
1410
GQREFAATNS
1420
YLGYFGDAKS
1430
KYKRIYVKFI
1440
ENANKKEYVR
1450
VCSKKPRNKP
1460
SQTIRTVQAK
1470
PSSSSKTSDP
1480
LASKTTTTKA
1490
PSVKPKVKQP
1500
KVKAEPPPKK
1510
RKKWKEEFSS
1520
SQSDSSPEIH
1530
TSSSDDEEFE
1540
PPAPFVTRFL
1550
NTRAMKETFK
1560
SYMELLVSIA
1570
LDPDTMQALE
1580
KSNDELLLPH
1590
MKKIDGMLND
1600
NRKRLLLNLH
1610
LDQSFKNALE
1620
SFPELTIITR
1630
DSKAKSGGTA
1640
ISKIKMNGKA
1650
YNKKTLRTSK
1660
TTTKSAQEFA
1670
VDPEKIQLYS
1680
LYHSLHHYKY
1690
HVYLICKDEI
1700
SSVQKKNEDL
1710
GQEEIVQLCM
1720
KNVKWVEDLF
1730
EKFGELLNHV
QQKCS
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005694 |
chromosome |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] 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.
[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.