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Acts as an enzyme that recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA: forms a stable thiazolidine linkage between a ring-opened abasic site and the alpha-amino and sulfhydryl substituents of its N-terminal catalytic cysteine residue (PubMed:30554877, PubMed:31235913). Promotes error-free repair by protecting abasic sites from translesion synthesis (TLS) polymerases and endonucleases that are error-prone and would generate mutations and double-strand breaks (PubMed:30554877). The HMCES DNA-protein cross-link is then either reversed or degraded (PubMed:30554877, PubMed:36608669, PubMed:37519246, PubMed:37950866). HMCES is able to catalyze the reversal of its thiazolidine cross-link and cycle between a cross-link and a non-cross-linked state depending on DNA context: mediates self-reversal of the thiazolidine cross-link in double stranded DNA, allowing APEX1 to initiate downstream repair of abasic sites (PubMed:37519246, PubMed:37950866). The HMCES DNA-protein cross-link can also be degraded by the SPRTN metalloprotease following unfolding by the BRIP1/FANCJ helicase (PubMed:36608669). Has preference for ssDNA, but can also accommodate double-stranded DNA with 3' or 5' overhang (dsDNA), and dsDNA-ssDNA 3' junction (PubMed:31235915, PubMed:31806351). Plays a protective role during somatic hypermutation of immunoglobulin genes in B-cells: acts via its ability to form covalent cross-links with abasic sites, thereby limiting the accumulation of deletions in somatic hypermutation target regions (PubMed:35450882). Also involved in class switch recombination (CSR) in B-cells independently of the formation of a DNA-protein cross-link: acts by binding and protecting ssDNA overhangs to promote DNA double-strand break repair through the microhomology-mediated alternative-end-joining (Alt-EJ) pathway (By similarity). Acts as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30554877"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31235913"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37519246"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37950866"}],"value":"Formation and reversal of DNA-protein cross-link depends on DNA context (PubMed:37519246, PubMed:37950866). Catalyzes formation of the thiazolidine linkage in presence of abasic sites in single-stranded DNA (PubMed:30554877, PubMed:31235913). Mediates the reversal of the thiazolidine cross-link in presence of double stranded DNA (PubMed:37519246, PubMed:37950866)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30554877"}],"value":"Interacts (via PIP-box motif) with PCNA"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30554877"}],"value":"Recruited to chromatin following DNA damage (PubMed:30554877). Localizes to replication forks (PubMed:30554877)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30554877"}],"value":"Chromosome","id":"SL-0468"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30554877"}],"value":"Expressed at higher level in S-phase than in quiescent cells"}],"commentType":"DEVELOPMENTAL STAGE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P76318"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31235913"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37519246"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37950866"}],"value":"The N-terminal catalytic Cys-2 residue forms a thiazolidine linkage to a ring-opened DNA abasic site (PubMed:31235913). Glu-127 catalyzes reversal of the thiazolidine linkage; self-reversal is favoured by duplex DNA formation (PubMed:37519246, PubMed:37950866). Glu-127 is also involved in sensing abasic sites in single-stranded DNA (ssDNA) (By similarity). His-210 stabilizes the abasic sites by forming a hydrogen bond with the O4' hydroxyl group (By similarity)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30554877"}],"value":"Ubiquitinated; the covalent HMCES DNA-protein cross-link is ubiquitinated, leading to its degradation by the proteasome"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the SOS response-associated peptidase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8R1M0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30554877"}],"value":"Was initially reported to specifically bind 5-hydroxymethylcytosine (5hmC)-containing DNA in stem cells (By similarity). It was later suggested to act as an endonuclease that specifically cleaves 5hmC-containing DNA (By similarity). However, the endonuclease activity on 5hmC-containing DNA could not be confirmed by another report (PubMed:30554877)"}],"commentType":"CAUTION"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"AAF86870.1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"WEB RESOURCE","resourceName":"Protein Spotlight","resourceUrl":"https://www.proteinspotlight.org/back_issues/226/","ftp":false,"note":"Integrity - Issue 226 of June 2020"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8R1M0"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"Abasic site processing protein 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