Q6PJP8 · DCR1A_HUMAN
- ProteinDNA cross-link repair 1A protein
- GeneDCLRE1A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1040 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
Exhibits no activity towards other beta-lactam antibiotic classes including cephalosporins (cefotaxime) and carbapenems (imipenem) (PubMed:31434986).
Catalytic activity
- a beta-lactam + H2O = a substituted beta-amino acid
Activity regulation
Beta-lactamase activity is inhibited by sulbactam.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | fibrillar center | |
Cellular Component | nucleoplasm | |
Molecular Function | 5'-3' DNA exonuclease activity | |
Molecular Function | beta-lactamase activity | |
Molecular Function | damaged DNA binding | |
Molecular Function | metal ion binding | |
Biological Process | cell division | |
Biological Process | double-strand break repair via nonhomologous end joining | |
Biological Process | interstrand cross-link repair |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA cross-link repair 1A protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6PJP8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_023286 | 58 | in dbSNP:rs17235066 | |||
Sequence: K → E | ||||||
Natural variant | VAR_023287 | 59 | in dbSNP:rs17228665 | |||
Sequence: E → D | ||||||
Natural variant | VAR_023288 | 71 | in dbSNP:rs17228672 | |||
Sequence: G → D | ||||||
Natural variant | VAR_023289 | 287 | in dbSNP:rs17235094 | |||
Sequence: P → L | ||||||
Natural variant | VAR_023290 | 317 | in dbSNP:rs3750898 | |||
Sequence: D → H | ||||||
Natural variant | VAR_030574 | 582 | in dbSNP:rs17855759 | |||
Sequence: G → W | ||||||
Mutagenesis | 838 | Impaired nuclear focus formation, reduced interaction with PIAS and increased sensitivity to cisplatin. | ||||
Sequence: D → N | ||||||
Natural variant | VAR_023291 | 859 | in dbSNP:rs11196530 | |||
Sequence: I → F | ||||||
Mutagenesis | 994 | Impaired nuclear focus formation, reduced interaction with PIAS and increased sensitivity to cisplatin. | ||||
Sequence: H → A |
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.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, cross-link, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000209116 | 1-1040 | UniProt | DNA cross-link repair 1A protein | |||
Sequence: MLEDISEEDIWEYKSKRKPKRVDPNNGSKNILKSVEKATDGKYQSKRSRNRKRAAEAKEVKDHEVPLGNAGCQTSVASSQNSSCGDGIQQTQDKETTPGKLCRTQKSQHVSPKIRPVYDGYCPNCQMPFSSLIGQTPRWHVFECLDSPPRSETECPDGLLCTSTIPFHYKRYTHFLLAQSRAGDHPFSSPSPASGGSFSETKSGVLCSLEERWSSYQNQTDNSVSNDPLLMTQYFKKSPSLTEASEKISTHIQTSQQALQFTDFVENDKLVGVALRLANNSEHINLPLPENDFSDCEISYSPLQSDEDTHDIDEKPDDSQEQLFFTESSKDGSLEEDDDSCGFFKKRHGPLLKDQDESCPKVNSFLTRDKYDEGLYRFNSLNDLSQPISQNNESTLPYDLACTGGDFVLFPPALAGKLAASVHQATKAKPDEPEFHSAQSNKQKQVIEESSVYNQVSLPLVKSLMLKPFESQVEGYLSSQPTQNTIRKLSSENLNAKNNTNSACFCRKALEGVPVGKATILNTENLSSTPAPKYLKILPSGLKYNARHPSTKVMKQMDIGVYFGLPPKRKEEKLLGESALEGINLNPVPSPNQKRSSQCKRKAEKSLSDLEFDASTLHESQLSVELSSERSQRQKKRCRKSNSLQEGACQKRSDHLINTESEAVNLSKVKVFTKSAHGGLQRGNKKIPESSNVGGSRKKTCPFYKKIPGTGFTVDAFQYGVVEGCTAYFLTHFHSDHYAGLSKHFTFPVYCSEITGNLLKNKLHVQEQYIHPLPLDTECIVNGVKVVLLDANHCPGAVMILFYLPNGTVILHTGDFRADPSMERSLLADQKVHMLYLDTTYCSPEYTFPSQQEVIRFAINTAFEAVTLNPHALVVCGTYSIGKEKVFLAIADVLGSKVGMSQEKYKTLQCLNIPEINSLITTDMCSSLVHLLPMMQINFKGLQSHLKKCGGKYNQILAFRPTGWTHSNKFTRIADVIPQTKGNISIYGIPYSEHSSYLEMKRFVQWLKPQKIIPTVNVGTWKSRSTMEKYFREWKLEAGY | |||||||
Cross-link | 202 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 236 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 238 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 240 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 269 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 333 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 340 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 353 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 361 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 429 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 488 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 490 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 508 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 517 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 529 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 533 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 536 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 590 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 590 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 641 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 643 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 668 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 670 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 674 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
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
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-190 | Nuclear localization region | ||||
Sequence: MLEDISEEDIWEYKSKRKPKRVDPNNGSKNILKSVEKATDGKYQSKRSRNRKRAAEAKEVKDHEVPLGNAGCQTSVASSQNSSCGDGIQQTQDKETTPGKLCRTQKSQHVSPKIRPVYDGYCPNCQMPFSSLIGQTPRWHVFECLDSPPRSETECPDGLLCTSTIPFHYKRYTHFLLAQSRAGDHPFSSP | ||||||
Region | 15-76 | Disordered | ||||
Sequence: SKRKPKRVDPNNGSKNILKSVEKATDGKYQSKRSRNRKRAAEAKEVKDHEVPLGNAGCQTSV | ||||||
Compositional bias | 35-65 | Basic and acidic residues | ||||
Sequence: VEKATDGKYQSKRSRNRKRAAEAKEVKDHEV | ||||||
Zinc finger | 119-149 | UBZ4-type | ||||
Sequence: DGYCPNCQMPFSSLIGQTPRWHVFECLDSPP | ||||||
Region | 396-614 | Nuclear focus formation | ||||
Sequence: LPYDLACTGGDFVLFPPALAGKLAASVHQATKAKPDEPEFHSAQSNKQKQVIEESSVYNQVSLPLVKSLMLKPFESQVEGYLSSQPTQNTIRKLSSENLNAKNNTNSACFCRKALEGVPVGKATILNTENLSSTPAPKYLKILPSGLKYNARHPSTKVMKQMDIGVYFGLPPKRKEEKLLGESALEGINLNPVPSPNQKRSSQCKRKAEKSLSDLEFDA | ||||||
Region | 582-602 | Disordered | ||||
Sequence: GINLNPVPSPNQKRSSQCKRK | ||||||
Region | 623-651 | Disordered | ||||
Sequence: SVELSSERSQRQKKRCRKSNSLQEGACQK |
Sequence similarities
Belongs to the DNA repair metallo-beta-lactamase (DRMBL) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,040
- Mass (Da)116,400
- Last updated2010-11-02 v3
- Checksum708FFA1F75451803
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 35-65 | Basic and acidic residues | ||||
Sequence: VEKATDGKYQSKRSRNRKRAAEAKEVKDHEV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |