Q6PJP8 · DCR1A_HUMAN

  • Protein
    DNA cross-link repair 1A protein
  • Gene
    DCLRE1A
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

May be required for DNA interstrand cross-link repair. Also required for checkpoint mediated cell cycle arrest in early prophase in response to mitotic spindle poisons. Possesses beta-lactamase activity, catalyzing the hydrolysis of penicillin G and nitrocefin (PubMed:31434986).
Exhibits no activity towards other beta-lactam antibiotic classes including cephalosporins (cefotaxime) and carbapenems (imipenem) (PubMed:31434986).

Catalytic activity

Activity regulation

Beta-lactamase activity is inhibited by sulbactam.

Features

Showing features for binding site.

110401002003004005006007008009001,000
TypeIDPosition(s)Description
Binding site122Zn2+ (UniProtKB | ChEBI)
Binding site125Zn2+ (UniProtKB | ChEBI)
Binding site140Zn2+ (UniProtKB | ChEBI)
Binding site144Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentfibrillar center
Cellular Componentnucleoplasm
Molecular Function5'-3' DNA exonuclease activity
Molecular Functionbeta-lactamase activity
Molecular Functiondamaged DNA binding
Molecular Functionmetal ion binding
Biological Processcell division
Biological Processdouble-strand break repair via nonhomologous end joining
Biological Processinterstrand cross-link repair

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA cross-link repair 1A protein
  • Alternative names
    • Beta-lactamase DCLRE1A (EC:3.5.2.6
      ) . EC:3.5.2.6 (UniProtKB | ENZYME | Rhea)
    • SNM1 homolog A (hSNM1; hSNM1A)

Gene names

    • Name
      DCLRE1A
    • Synonyms
      KIAA0086, SNM1, SNM1A

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q6PJP8
  • Secondary accessions
    • D3DRC1
    • Q14701
    • Q6P5Y3
    • Q6PKL4

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Note: In some cells it may be found in typically 1 or 2 discrete nuclear aggregates of unknown function which also contain TP53BP1. Also found in multiple discrete nuclear foci which increase in number following treatment with ionizing radiation or interstrand cross-linking agents. These foci overlap with those formed by the MRN complex (composed of MRE11, RAD50 and NBN) and BRCA1.

Keywords

Disease & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_02328658in dbSNP:rs17235066
Natural variantVAR_02328759in dbSNP:rs17228665
Natural variantVAR_02328871in dbSNP:rs17228672
Natural variantVAR_023289287in dbSNP:rs17235094
Natural variantVAR_023290317in dbSNP:rs3750898
Natural variantVAR_030574582in dbSNP:rs17855759
Mutagenesis838Impaired nuclear focus formation, reduced interaction with PIAS and increased sensitivity to cisplatin.
Natural variantVAR_023291859in dbSNP:rs11196530
Mutagenesis994Impaired nuclear focus formation, reduced interaction with PIAS and increased sensitivity to cisplatin.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,212 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain, cross-link, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00002091161-1040UniProt
Cross-link202UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link236UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)238PRIDEPhosphoserine
Modified residue (large scale data)240PRIDEPhosphoserine
Modified residue (large scale data)255PRIDEPhosphoserine
Cross-link269UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)333PRIDEPhosphoserine
Modified residue (large scale data)340PRIDEPhosphoserine
Cross-link353UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link361UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link429UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link488UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)490PRIDEPhosphoserine
Cross-link508UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link517UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)529PRIDEPhosphothreonine
Cross-link533UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link536UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue590UniProtPhosphoserine
Modified residue (large scale data)590PRIDEPhosphoserine
Modified residue (large scale data)641PRIDEPhosphoserine
Modified residue (large scale data)643PRIDEPhosphoserine
Cross-link668UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link670UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link674UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in brain, heart, kidney, liver, pancreas, placenta and skeletal muscle.

Induction

During mitosis. The mRNA encoding this protein contains an internal ribosome entry site (IRES) in its 5'-UTR. This 5'-UTR generally suppresses translation while specifically promoting expression during mitosis, when cap-dependent translation may be impaired.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Binds constitutively to TP53BP1. Binds CDC27, which is itself a component of the anaphase promoting complex (APC). Binds PIAS1.

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, zinc finger.

TypeIDPosition(s)Description
Region1-190Nuclear localization region
Region15-76Disordered
Compositional bias35-65Basic and acidic residues
Zinc finger119-149UBZ4-type
Region396-614Nuclear focus formation
Region582-602Disordered
Region623-651Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,040
  • Mass (Da)
    116,400
  • Last updated
    2010-11-02 v3
  • Checksum
    708FFA1F75451803
MLEDISEEDIWEYKSKRKPKRVDPNNGSKNILKSVEKATDGKYQSKRSRNRKRAAEAKEVKDHEVPLGNAGCQTSVASSQNSSCGDGIQQTQDKETTPGKLCRTQKSQHVSPKIRPVYDGYCPNCQMPFSSLIGQTPRWHVFECLDSPPRSETECPDGLLCTSTIPFHYKRYTHFLLAQSRAGDHPFSSPSPASGGSFSETKSGVLCSLEERWSSYQNQTDNSVSNDPLLMTQYFKKSPSLTEASEKISTHIQTSQQALQFTDFVENDKLVGVALRLANNSEHINLPLPENDFSDCEISYSPLQSDEDTHDIDEKPDDSQEQLFFTESSKDGSLEEDDDSCGFFKKRHGPLLKDQDESCPKVNSFLTRDKYDEGLYRFNSLNDLSQPISQNNESTLPYDLACTGGDFVLFPPALAGKLAASVHQATKAKPDEPEFHSAQSNKQKQVIEESSVYNQVSLPLVKSLMLKPFESQVEGYLSSQPTQNTIRKLSSENLNAKNNTNSACFCRKALEGVPVGKATILNTENLSSTPAPKYLKILPSGLKYNARHPSTKVMKQMDIGVYFGLPPKRKEEKLLGESALEGINLNPVPSPNQKRSSQCKRKAEKSLSDLEFDASTLHESQLSVELSSERSQRQKKRCRKSNSLQEGACQKRSDHLINTESEAVNLSKVKVFTKSAHGGLQRGNKKIPESSNVGGSRKKTCPFYKKIPGTGFTVDAFQYGVVEGCTAYFLTHFHSDHYAGLSKHFTFPVYCSEITGNLLKNKLHVQEQYIHPLPLDTECIVNGVKVVLLDANHCPGAVMILFYLPNGTVILHTGDFRADPSMERSLLADQKVHMLYLDTTYCSPEYTFPSQQEVIRFAINTAFEAVTLNPHALVVCGTYSIGKEKVFLAIADVLGSKVGMSQEKYKTLQCLNIPEINSLITTDMCSSLVHLLPMMQINFKGLQSHLKKCGGKYNQILAFRPTGWTHSNKFTRIADVIPQTKGNISIYGIPYSEHSSYLEMKRFVQWLKPQKIIPTVNVGTWKSRSTMEKYFREWKLEAGY

Sequence caution

The sequence BAA07646.2 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias35-65Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D42045
EMBL· GenBank· DDBJ
BAA07646.2
EMBL· GenBank· DDBJ
mRNA Different initiation
AY607842
EMBL· GenBank· DDBJ
AAT09762.1
EMBL· GenBank· DDBJ
Genomic DNA
AL592546
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471066
EMBL· GenBank· DDBJ
EAW49489.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471066
EMBL· GenBank· DDBJ
EAW49490.1
EMBL· GenBank· DDBJ
Genomic DNA
BC013124
EMBL· GenBank· DDBJ
AAH13124.1
EMBL· GenBank· DDBJ
mRNA
BC062582
EMBL· GenBank· DDBJ
AAH62582.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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