Search Results

Overview

Uniprot IDQ04837
Protein NameSingle-stranded DNA-binding protein, mitochondrial
Gene NameSSBP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
103 DVAYQYVKKGSRIYL
104 VAYQYVKKGSRIYLE
122 DYGEYMDKNNVRRQA
81 QLGDVSQKTTWHRIS

Function

Binds preferentially and cooperatively to pyrimidine rich single-stranded DNA (ss-DNA) (PubMed:21953457, PubMed:23290262, PubMed:31550240). In vitro, required to maintain the copy number of mitochondrial DNA (mtDNA) and plays a crucial role during mtDNA replication by stimulating the activity of the replisome components POLG and TWNK at the replication fork (PubMed:12975372, PubMed:15167897, PubMed:21953457, PubMed:26446790, PubMed:31550240). Promotes the activity of the gamma complex polymerase POLG, largely by organizing the template DNA and eliminating secondary structures to favor ss-DNA conformations that facilitate POLG activity (PubMed:21953457, PubMed:26446790, PubMed:31550240). In addition it is able to promote the 5'-3' unwinding activity of the mtDNA helicase TWNK (PubMed:12975372). May also function in mtDNA repair (PubMed:23290262)

Protein Sequence

10 MFRRPVLQVL 20 RQFVRHESET 30 TTSLVLERSL 40 NRVHLLGRVG 50 QDPVLRQVEG 60 KNPVTIFSLA 70 TNEMWRSGDS 80 EVYQLGDVSQ 90 KTTWHRISVF 100 RPGLRDVAYQ 110 YVKKGSRIYL 120 EGKIDYGEYM 130 DKNNVRRQAT 140 TIIADNIIFL SDQTKEKE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0042645 mitochondrial nucleoid
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0008047 enzyme activator activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003697 single-stranded DNA binding
Biological Process GO:0006260 DNA replication
Biological Process GO:0006264 mitochondrial DNA replication
Biological Process GO:0051096 positive regulation of helicase activity
Biological Process GO:0090297 positive regulation of mitochondrial DNA replication
Biological Process GO:0051289 protein homotetramerization

Reference

[1] 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.

[2] 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.

[3] 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.

[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.