Search Results

Overview

Uniprot ID	Q9UQE7
Protein Name	Structural maintenance of chromosomes protein 3
Gene Name	SMC3
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
106	RRVIGAKKDQYFLDK
143	YYIVKQGKINQMATA
592	VTFLPLNKLDVRDTA

Function

Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex also plays an important role in spindle pole assembly during mitosis and in chromosomes movement

Protein Sequence

10 MYIKQVIIQG 20 FRSYRDQTIV 30 DPFSSKHNVI 40 VGRNGSGKSN 50 FFYAIQFVLS 60 DEFSHLRPEQ 70 RLALLHEGTG 80 PRVISAFVEI 90 IFDNSDNRLP 100 IDKEEVSLRR 110 VIGAKKDQYF 120 LDKKMVTKND 130 VMNLLESAGF 140 SRSNPYYIVK 150 QGKINQMATA 160 PDSQRLKLLR 170 EVAGTRVYDE 180 RKEESISLMK 190 ETEGKREKIN 200 ELLKYIEERL 210 HTLEEEKEEL 220 AQYQKWDKMR 230 RALEYTIYNQ 240 ELNETRAKLD 250 ELSAKRETSG 260 EKSRQLRDAQ 270 QDARDKMEDI 280 ERQVRELKTK 290 ISAMKEEKEQ 300 LSAERQEQIK 310 QRTKLELKAK 320 DLQDELAGNS 330 EQRKRLLKER 340 QKLLEKIEEK 350 QKELAETEPK 360 FNSVKEKEER 370 GIARLAQATQ 380 ERTDLYAKQG 390 RGSQFTSKEE 400 RDKWIKKELK 410 SLDQAINDKK 420 RQIAAIHKDL 430 EDTEANKEKN 440 LEQYNKLDQD 450 LNEVKARVEE 460 LDRKYYEVKN 470 KKDELQSERN 480 YLWREENAEQ 490 QALAAKREDL 500 EKKQQLLRAA 510 TGKAILNGID 520 SINKVLDHFR 530 RKGINQHVQN 540 GYHGIVMNNF 550 ECEPAFYTCV 560 EVTAGNRLFY 570 HIVDSDEVST 580 KILMEFNKMN 590 LPGEVTFLPL 600 NKLDVRDTAY 610 PETNDAIPMI 620 SKLRYNPRFD 630 KAFKHVFGKT 640 LICRSMEVST 650 QLARAFTMDC 660 ITLEGDQVSH 670 RGALTGGYYD 680 TRKSRLELQK 690 DVRKAEEELG 700 ELEAKLNENL 710 RRNIERINNE 720 IDQLMNQMQQ 730 IETQQRKFKA 740 SRDSILSEMK 750 MLKEKRQQSE 760 KTFMPKQRSL 770 QSLEASLHAM 780 ESTRESLKAE 790 LGTDLLSQLS 800 LEDQKRVDAL 810 NDEIRQLQQE 820 NRQLLNERIK 830 LEGIITRVET 840 YLNENLRKRL 850 DQVEQELNEL 860 RETEGGTVLT 870 ATTSELEAIN 880 KRVKDTMARS 890 EDLDNSIDKT 900 EAGIKELQKS 910 MERWKNMEKE 920 HMDAINHDTK 930 ELEKMTNRQG 940 MLLKKKEECM 950 KKIRELGSLP 960 QEAFEKYQTL 970 SLKQLFRKLE 980 QCNTELKKYS 990 HVNKKALDQF 1000 VNFSEQKEKL 1010 IKRQEELDRG 1020 YKSIMELMNV 1030 LELRKYEAIQ 1040 LTFKQVSKNF 1050 SEVFQKLVPG 1060 GKATLVMKKG 1070 DVEGSQSQDE 1080 GEGSGESERG 1090 SGSQSSVPSV 1100 DQFTGVGIRV 1110 SFTGKQGEMR 1120 EMQQLSGGQK 1130 SLVALALIFA 1140 IQKCDPAPFY 1150 LFDEIDQALD 1160 AQHRKAVSDM 1170 IMELAVHAQF 1180 ITTTFRPELL 1190 ESADKFYGVK 1200 FRNKVSHIDV 1210 ITAEMAKDFV EDDTTHG

Gene Ontology

Classification	GO ID	Description
Biological Process	GO:0006281	DNA repair
Cellular Component	GO:0000785	chromatin
Cellular Component	GO:0005694	chromosome
Cellular Component	GO:0000775	chromosome, centromeric region
Cellular Component	GO:0008278	cohesin complex
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0000800	lateral element
Cellular Component	GO:0030893	meiotic cohesin complex
Cellular Component	GO:0030892	mitotic cohesin complex
Cellular Component	GO:0097431	mitotic spindle pole
Cellular Component	GO:0016363	nuclear matrix
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0016887	ATP hydrolysis activity
Molecular Function	GO:0048487	beta-tubulin binding
Molecular Function	GO:0003682	chromatin binding
Molecular Function	GO:0000987	cis-regulatory region sequence-specific DNA binding
Molecular Function	GO:0003690	double-stranded DNA binding
Molecular Function	GO:0070840	dynein complex binding
Molecular Function	GO:0036033	mediator complex binding
Molecular Function	GO:0003777	microtubule motor activity
Molecular Function	GO:0046982	protein heterodimerization activity
Biological Process	GO:0051301	cell division
Biological Process	GO:0034089	establishment of meiotic sister chromatid cohesion
Biological Process	GO:0034087	establishment of mitotic sister chromatid cohesion
Biological Process	GO:0051321	meiotic cell cycle
Biological Process	GO:0000278	mitotic cell cycle
Biological Process	GO:0007064	mitotic sister chromatid cohesion
Biological Process	GO:0090307	mitotic spindle assembly
Biological Process	GO:0006275	regulation of DNA replication
Biological Process	GO:0007062	sister chromatid cohesion

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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] 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.

[6] 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.

[7] 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.

[8] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[9] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[10] 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.

[11] 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.