Search Results

Overview

Uniprot IDQ8N5C6
Protein NameS1 RNA-binding domain-containing protein 1
Gene NameSRBD1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
104 ALEDRKNKLDTVQTL
112 LDTVQTLKTAKTKQK
132 HTVRRTKKLKVEEET
134 VRRTKKLKVEEETSK
183 FGQSALKKIKTETYP
393 FIRNLCQKRHVCIQS
69 KRMPRVKKNAPQISD
9 SSLPRRAKVQVQDVV

Function

DNA- and histone-binding protein that localizes to the central axes of mitotic chromosomes (PubMed:39955279, PubMed:40106440). Promotes chromosome segregation by facilitating TOP2A recruitment to mitotic chromosomes, thereby preventing anaphase failure (PubMed:39955279). During prophase, safeguards the decatenation process to avoid the formation of difficult-to-resolve DNA structures, preventing chromosome missegregation (PubMed:40106440). Also contributes to the regulation of nucleus pulposus cell senescence (PubMed:38169523)

Protein Sequence

10 MSSLPRRAKV 20 QVQDVVLKDE 30 FSSFSELSSA 40 SEEDDKEDSA 50 WEPQKKVPRS 60 RKQPPPKESK 70 PKRMPRVKKN 80 APQISDGSEV 90 VVVKEELNSS 100 VAIADTALED 110 RKNKLDTVQT 120 LKTAKTKQKC 130 AAQPHTVRRT 140 KKLKVEEETS 150 KASNLEGESN 160 SSETPSTSTV 170 WGGTCKKEEN 180 DDDFTFGQSA 190 LKKIKTETYP 200 QGQPVKFPAN 210 ANSTKEEVEM 220 NWDMVQVLSE 230 RTNIEPWVCA 240 NIIRLFNDDN 250 TIPFIIRYRK 260 ELINNLDADS 270 LREVQQTLEE 280 LRAVAKKVHS 290 TIQKIKKEGK 300 MSECLLKAML 310 NCKTFEELEH 320 VSAPYKTGSK 330 GTKAQRARQL 340 GLEGAARALL 350 EKPGELSLLS 360 YIRPDVKGLS 370 TLQDIEIGVQ 380 HILADMIAKD 390 KDTLDFIRNL 400 CQKRHVCIQS 410 SLAKVSSKKV 420 NEKDVDKFLL 430 YQHFSCNIRN 440 IHHHQILAIN 450 RGENLKVLTV 460 KVNISDGVKD 470 EFCRWCIQNR 480 WRPRSFARPE 490 LMKILYNSLN 500 DSFKRLIYPL 510 LCREFRAKLT 520 SDAEKESVMM 530 FGRNLRQLLL 540 TSPVPGRTLM 550 GVDPGYKHGC 560 KLAIISPTSQ 570 ILHTDVVYLH 580 CGQGFREAEK 590 IKTLLLNFNC 600 STVVIGNGTA 610 CRETEAYFAD 620 LIMKNYFAPL 630 DVVYCIVSEA 640 GASIYSVSPE 650 ANKEMPGLDP 660 NLRSAVSIAR 670 RVQDPLAELV 680 KIEPKHIGVG 690 MYQHDVSQTL 700 LKATLDSVVE 710 ECVSFVGVDI 720 NICSEVLLRH 730 IAGLNANRAK 740 NIIEWREKNG 750 PFINREQLKK 760 VKGLGPKSFQ 770 QCAGFIRINQ 780 DYIRTFCSQQ 790 TETSGQIQGV 800 AVTSSADVEV 810 TNEKQGKKKS 820 KTAVNVLLKP 830 NPLDQTCIHP 840 ESYDIAMRFL 850 SSIGGTLYEV 860 GKPEMQQKIN 870 SFLEKEGMEK 880 IAERLQTTVH 890 TLQVIIDGLS 900 QPESFDFRTD 910 FDKPDFKRSI 920 VCLEDLQIGT 930 VLTGKVENAT 940 LFGIFVDIGV 950 GKSGLIPIRN 960 VTEAKLSKTK 970 KRRSLGLGPG 980 ERVEVQVLNI 990 DIPRSRITLD LIRVL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005694 chromosome
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005730 nucleolus
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003735 structural constituent of ribosome
Biological Process GO:0006139 nucleobase-containing compound metabolic process
Biological Process GO:0006412 translation

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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[3] 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.

[4] 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.

[5] 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.