{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8R1M0","uniProtkbId":"HMCES_MOUSE","entryAudit":{"firstPublicDate":"2006-01-24","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2002-06-01","entryVersion":133,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Mus musculus","commonName":"Mouse","taxonId":10090,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Abasic site processing protein HMCES"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96FZ2"}],"value":"4.-.-.-"}]},"alternativeNames":[{"fullName":{"value":"Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein"},"shortNames":[{"value":"ES cell-specific 5hmC-binding protein"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Peptidase HMCES"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29020633"}],"value":"3.4.-.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29020633"}],"value":"SRAP domain-containing protein 1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31806351"},{"evidenceCode":"ECO:0000312","source":"MGI","id":"MGI:1914053"}],"value":"Hmces"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29020633"}],"value":"Srap1"},{"evidences":[{"evidenceCode":"ECO:0000312","source":"MGI","id":"MGI:1914053"}],"value":"Srapd1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96FZ2"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29020633"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31806351"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35450882"}],"value":"Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites (By similarity). 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 (By similarity). 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 (By similarity). The HMCES DNA-protein cross-link is then either reversed or degraded (By similarity). 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 (By similarity). The HMCES DNA-protein cross-link can also be degraded by the SPRTN metalloprotease following unfolding by the BRIP1/FANCJ helicase (By similarity). Has preference for ssDNA, but can also accommodate double-stranded DNA with 3' or 5' overhang (dsDNA), and dsDNA-ssDNA 3' junction (By similarity). 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 (PubMed:31806351). Acts as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (PubMed:29020633)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96FZ2"}],"value":"Formation and reversal of DNA-protein cross-link depends on DNA context. Catalyzes formation of the thiazolidine linkage in presence of abasic sites in single-stranded DNA. Mediates the reversal of the thiazolidine cross-link in presence of double stranded DNA"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96FZ2"}],"value":"Interacts (via PIP-box motif) with PCNA"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96FZ2"}],"value":"Recruited to chromatin following DNA damage. Localizes to replication forks"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96FZ2"}],"value":"Chromosome","id":"SL-0468"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29020633"}],"value":"Expressed in embryonic stem cells"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P76318"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96FZ2"}],"value":"The N-terminal catalytic Cys-2 residue forms a thiazolidine linkage to a ring-opened DNA abasic site. Glu-127 catalyzes reversal of the thiazolidine linkage; self-reversal is favoured by duplex DNA formation (By similarity). Glu-127 is also involved in sensing abasic sites in single-stranded DNA (ssDNA). His-209 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":"29020633"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31806351"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35450882"}],"value":"Embryonic sublethality and altered DNA methylation, possibly caused by accumulation of 5-hydroxymethylcytosine (5hmC) in genomic DNA (PubMed:29020633). Mice do not show defects in hematopoiesis and no alterations in global 5hmC levels in bone marrow cells (PubMed:31806351). In contrast, mice display a decrease in class switch recombination (CSR) in mature activated B-cells (PubMed:31806351). Increased deletions in germinal center B-cells (PubMed:35450882)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the SOS response-associated peptidase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23434322"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29020633"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31806351"}],"value":"Was initially reported to specifically bind 5-hydroxymethylcytosine (5hmC)-containing DNA in stem cells (PubMed:23434322). It was later suggested to act as an endonuclease that specifically cleaves 5hmC-containing DNA (PubMed:29020633). However, recent studies question this activity: no alterations in global 5hmC levels are observed in bone marrow cells from knockout mice (PubMed:31806351)"}],"commentType":"CAUTION"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29020633"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"Abasic site processing protein 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