Search Results

Overview

Uniprot IDQ8IY18
Protein NameStructural maintenance of chromosomes protein 5
Gene NameSMC5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
17 TPSPQPSKRALPRDP
31 PSSEVPSKRKNSAPQ

Function

Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression; the function seems to be independent of SMC6. SMC5-SMC6 complex may prevent transcription of episomal DNA, such as circular viral DNA genome (PubMed:26983541)

Protein Sequence

10 MATPSKKTST 20 PSPQPSKRAL 30 PRDPSSEVPS 40 KRKNSAPQLP 50 LLQSSGPFVE 60 GSIVRISMEN 70 FLTYDICEVS 80 PGPHLNMIVG 90 ANGTGKSSIV 100 CAICLGLAGK 110 PAFMGRADKV 120 GFFVKRGCSR 130 GMVEIELFRA 140 SGNLVITREI 150 DVAKNQSFWF 160 INKKSTTQKI 170 VEEKVAALNI 180 QVGNLCQFLP 190 QDKVGEFAKL 200 SKIELLEATE 210 KSIGPPEMHK 220 YHCELKNLRE 230 KEKQLETSCK 240 EKTEYLQKMV 250 QRNERYKQDV 260 ERFYERKRHL 270 DLIEMLEAKR 280 PWVEYENVRQ 290 EYEEVKLVRD 300 RVKEEVRKLK 310 EGQIPVTCRI 320 EEMENERHNL 330 EARIKEKATD 340 IKEASQKCKQ 350 KQDVIERKDK 360 HIEELQQALI 370 VKQNEELDRQ 380 RRIGNTRKMI 390 EDLQNELKTT 400 ENCENLQPQI 410 DAITNDLRRI 420 QDEKALCEGE 430 IIDKRRERET 440 LEKEKKSVDD 450 HIVRFDNLMN 460 QKEDKLRQRF 470 RDTYDAVLWL 480 RNNRDKFKQR 490 VCEPIMLTIN 500 MKDNKNAKYI 510 ENHIPSNDLR 520 AFVFESQEDM 530 EVFLKEVRDN 540 KKLRVNAVIA 550 PKSSYADKAP 560 SRSLNELKQY 570 GFFSYLRELF 580 DAPDPVMSYL 590 CCQYHIHEVP 600 VGTEKTRERI 610 ERVIQETRLK 620 QIYTAEEKYV 630 VKTSFYSNKV 640 ISSNTSLKVA 650 QFLTVTVDLE 660 QRRHLEEQLK 670 EIHRKLQAVD 680 SGLIALRETS 690 KHLEHKDNEL 700 RQKKKELLER 710 KTKKRQLEQK 720 ISSKLGSLKL 730 MEQDTCNLEE 740 EERKASTKIK 750 EINVQKAKLV 760 TELTNLIKIC 770 TSLHIQKVDL 780 ILQNTTVISE 790 KNKLESDYMA 800 ASSQLRLTEQ 810 HFIELDENRQ 820 RLLQKCKELM 830 KRARQVCNLG 840 AEQTLPQEYQ 850 TQVPTIPNGH 860 NSSLPMVFQD 870 LPNTLDEIDA 880 LLTEERSRAS 890 CFTGLNPTIV 900 QEYTKREEEI 910 EQLTEELKGK 920 KVELDQYREN 930 ISQVKERWLN 940 PLKELVEKIN 950 EKFSNFFSSM 960 QCAGEVDLHT 970 ENEEDYDKYG 980 IRIRVKFRSS 990 TQLHELTPHH 1000 QSGGERSVST 1010 MLYLMALQEL 1020 NRCPFRVVDE 1030 INQGMDPINE 1040 RRVFEMVVNT 1050 ACKENTSQYF 1060 FITPKLLQNL 1070 PYSEKMTVLF 1080 VYNGPHMLEP 1090 NTWNLKAFQR 1100 RRRRITFTQP S

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000775 chromosome, centromeric region
Biological Process GO:0090398 cellular senescence
Biological Process GO:0140588 chromatin looping
Biological Process GO:0006974 DNA damage response
Biological Process GO:0000724 double-strand break repair via homologous recombination
Biological Process GO:0044828 host-mediated suppression of viral genome replication
Biological Process GO:0051984 positive regulation of chromosome segregation
Biological Process GO:0034184 positive regulation of maintenance of mitotic sister chromatid cohesion
Biological Process GO:0016925 protein sumoylation
Biological Process GO:0032204 regulation of telomere maintenance
Biological Process GO:0000722 telomere maintenance via recombination
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0035061 interchromatin granule
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0016605 PML body
Cellular Component GO:0000803 sex chromosome
Cellular Component GO:0035861 site of double-strand break
Cellular Component GO:0030915 Smc5-Smc6 complex
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0000217 DNA secondary structure binding
Molecular Function GO:0003697 single-stranded DNA binding
Biological Process GO:0051301 cell division

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] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[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] 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.

[5] 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.