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Q96SD1

- DCR1C_HUMAN

UniProt

Q96SD1 - DCR1C_HUMAN

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Protein

Protein artemis

Gene

DCLRE1C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.11 Publications

GO - Molecular functioni

  1. 5'-3' exonuclease activity Source: MGI
  2. single-stranded DNA endodeoxyribonuclease activity Source: MGI

GO - Biological processi

  1. B cell differentiation Source: Ensembl
  2. DNA catabolic process, endonucleolytic Source: GOC
  3. DNA recombination Source: UniProtKB-KW
  4. double-strand break repair Source: Ensembl
  5. nucleic acid phosphodiester bond hydrolysis Source: GOC
  6. response to ionizing radiation Source: Ensembl
  7. telomere maintenance Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Adaptive immunity, DNA damage, DNA recombination, DNA repair, Immunity

Keywords - Ligandi

Magnesium

Names & Taxonomyi

Protein namesi
Recommended name:
Protein artemis (EC:3.1.-.-)
Alternative name(s):
DNA cross-link repair 1C protein
Protein A-SCID
SNM1 homolog C
Short name:
hSNM1C
SNM1-like protein
Gene namesi
Name:DCLRE1C
Synonyms:ARTEMIS, ASCID, SCIDA, SNM1C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:17642. DCLRE1C.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-negative/NK-cell-positive with sensitivity to ionizing radiation (RSSCID) [MIM:602450]: A form of severe combined immunodeficiency, a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy with recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. Individuals affected by RS-SCID show defects in the DNA repair machinery necessary for coding joint formation and the completion of V(D)J recombination. A subset of cells from such patients show increased radiosensitivity.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Severe combined immunodeficiency Athabaskan type (SCIDA) [MIM:602450]: A variety of SCID with sensitivity to ionizing radiation. A founder mutation has been detected in Athabascan-speaking native Americans, being inherited as an autosomal recessive trait. Affected individuals exhibit clinical symptoms and defects in DNA repair comparable to those seen in RS-SCID.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Omenn syndrome (OS) [MIM:603554]: Severe immunodeficiency characterized by the presence of activated, anergic, oligoclonal T-cells, hypereosinophilia, and high IgE levels.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171D → N or A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. 2 Publications
Mutagenesisi33 – 331H → A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. 2 Publications
Mutagenesisi35 – 351H → A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. 2 Publications
Mutagenesisi37 – 371D → N or A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. 3 Publications
Mutagenesisi38 – 381H → A: Reduces PRKDC-dependent endonuclease activity, although V(D)J recombination is largely normal. 2 Publications
Mutagenesisi115 – 1151H → A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. 2 Publications
Mutagenesisi136 – 1361D → N or A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. 2 Publications
Mutagenesisi165 – 1651D → N or A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. 3 Publications
Mutagenesisi319 – 3191H → A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. 2 Publications
Mutagenesisi516 – 5161S → A: Reduced IR induced phosphorylation; when associated with A-534; A-538; A-548; A-553; A-561 and A-562. 1 Publication
Mutagenesisi534 – 5341S → A: Reduced IR induced phosphorylation; when associated with A-516; A-538; A-548; A-553; A-561 and A-562. 1 Publication
Mutagenesisi538 – 5381S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-548; A-553; A-561 and A-562. 1 Publication
Mutagenesisi548 – 5481S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-553; A-561 and A-562. 1 Publication
Mutagenesisi553 – 5531S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-561 and A-562. 1 Publication
Mutagenesisi561 – 5611S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-553 and A-562. 1 Publication
Mutagenesisi562 – 5621S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-553 and A-561. 1 Publication

Keywords - Diseasei

Disease mutation, SCID

Organism-specific databases

MIMi602450. phenotype.
603554. phenotype.
Orphaneti39041. Omenn syndrome.
275. Severe combined immunodeficiency due to DCLRE1C deficiency.
PharmGKBiPA27176.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 692692Protein artemisPRO_0000209122Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei645 – 6451Phosphoserine; by ATM2 Publications

Post-translational modificationi

Phosphorylation on undefined residues by PRKDC may stimulate endonucleolytic activity on 5' and 3' hairpins and overhangs. PRKDC must remain present, even after phosphorylation, for efficient hairpin opening. Also phosphorylated by ATM in response to ionizing radiation (IR) and by ATR in response to ultraviolet (UV) radiation.7 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96SD1.
PaxDbiQ96SD1.
PRIDEiQ96SD1.

PTM databases

PhosphoSiteiQ96SD1.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in the kidney, lung, pancreas and placenta (at the mRNA level). Expression is not increased in thymus or bone marrow, sites of V(D)J recombination.1 Publication

Gene expression databases

BgeeiQ96SD1.
ExpressionAtlasiQ96SD1. baseline and differential.
GenevestigatoriQ96SD1.

Interactioni

Subunit structurei

Interacts with ATM, BRCA1, PRKDC and TP53BP1. Also exhibits ATM- and phosphorylation-dependent interaction with the MRN complex, composed of MRE11A/MRE11, RAD50, and NBN.7 Publications

Protein-protein interaction databases

BioGridi122170. 33 interactions.

Structurei

Secondary structure

1
692
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi489 – 4913

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3W1BX-ray2.40B485-495[»]
3W1GX-ray2.55B485-495[»]
4HTPX-ray2.25C/E485-495[»]
ProteinModelPortaliQ96SD1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1236.
GeneTreeiENSGT00530000063183.
HOVERGENiHBG081421.
InParanoidiQ96SD1.
KOiK10887.
OMAiMFRNMPD.
OrthoDBiEOG70CR8F.
PhylomeDBiQ96SD1.
TreeFamiTF329572.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Beta-lactamas-like.
IPR011084. DRMBL.
[Graphical view]
PfamiPF07522. DRMBL. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96SD1-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSSFEGQMAE YPTISIDRFD RENLRARAYF LSHCHKDHMK GLRAPTLKRR
60 70 80 90 100
LECSLKVYLY CSPVTKELLL TSPKYRFWKK RIISIEIETP TQISLVDEAS
110 120 130 140 150
GEKEEIVVTL LPAGHCPGSV MFLFQGNNGT VLYTGDFRLA QGEAARMELL
160 170 180 190 200
HSGGRVKDIQ SVYLDTTFCD PRFYQIPSRE ECLSGVLELV RSWITRSPYH
210 220 230 240 250
VVWLNCKAAY GYEYLFTNLS EELGVQVHVN KLDMFRNMPE ILHHLTTDRN
260 270 280 290 300
TQIHACRHPK AEEYFQWSKL PCGITSRNRI PLHIISIKPS TMWFGERSRK
310 320 330 340 350
TNVIVRTGES SYRACFSFHS SYSEIKDFLS YLCPVNAYPN VIPVGTTMDK
360 370 380 390 400
VVEILKPLCR SSQSTEPKYK PLGKLKRART VHRDSEEEDD YLFDDPLPIP
410 420 430 440 450
LRHKVPYPET FHPEVFSMTA VSEKQPEKLR QTPGCCRAEC MQSSRFTNFV
460 470 480 490 500
DCEESNSESE EEVGIPASLQ GDLGSVLHLQ KADGDVPQWE VFFKRNDEIT
510 520 530 540 550
DESLENFPSS TVAGGSQSPK LFSDSDGEST HISSQNSSQS THITEQGSQG
560 570 580 590 600
WDSQSDTVLL SSQERNSGDI TSLDKADYRP TIKENIPASL MEQNVICPKD
610 620 630 640 650
TYSDLKSRDK DVTIVPSTGE PTTLSSETHI PEEKSLLNLS TNADSQSSSD
660 670 680 690
FEVPSTPEAE LPKREHLQYL YEKLATGESI AVKKRKCSLL DT
Length:692
Mass (Da):78,436
Last modified:July 19, 2005 - v2
Checksum:i24B857F5B473637B
GO
Isoform 2 (identifier: Q96SD1-2) [UniParc]FASTAAdd to Basket

Also known as: SCIDA

The sequence of this isoform differs from the canonical sequence as follows:
     1-120: Missing.

Show »
Length:572
Mass (Da):64,652
Checksum:i4FDCC319F5C79FBB
GO
Isoform 3 (identifier: Q96SD1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-115: Missing.
     116-121: CPGSVM → MKHQER

Show »
Length:577
Mass (Da):65,331
Checksum:i9E1705D68AD06BDE
GO
Isoform 4 (identifier: Q96SD1-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     386-434: EEEDDYLFDD...QPEKLRQTPG → GSHSVTQARM...GAYRHAQLMI
     435-692: Missing.

Show »
Length:434
Mass (Da):49,944
Checksum:i3C651C16302A8AFA
GO

Sequence cautioni

The sequence CAI40018.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI40019.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI40021.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI40023.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti560 – 5601L → V in CAC37570. (PubMed:11336668)Curated
Sequence conflicti560 – 5601L → V in AAM53255. (PubMed:12055248)Curated
Sequence conflicti560 – 5601L → V in AAM53256. (PubMed:12055248)Curated
Sequence conflicti560 – 5601L → V in AAM53257. (PubMed:12055248)Curated
Sequence conflicti560 – 5601L → V in AAM53258. (PubMed:12055248)Curated
Sequence conflicti560 – 5601L → V in AAM53259. (PubMed:12055248)Curated
Sequence conflicti560 – 5601L → V in AAM53260. (PubMed:12055248)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351H → D in Omenn syndrome. 1 Publication
VAR_023077
Natural varianti118 – 1181G → V in RS-SCID. 1 Publication
VAR_023078
Natural varianti135 – 1351G → E in RS-SCID. 1 Publication
VAR_023079
Natural varianti140 – 1401A → V.1 Publication
Corresponds to variant rs41297016 [ dbSNP | Ensembl ].
VAR_060689
Natural varianti153 – 1531G → R.1 Publication
Corresponds to variant rs41297018 [ dbSNP | Ensembl ].
VAR_060690
Natural varianti171 – 1711P → R.2 Publications
Corresponds to variant rs35441642 [ dbSNP | Ensembl ].
VAR_048892
Natural varianti243 – 2431H → R.2 Publications
Corresponds to variant rs12768894 [ dbSNP | Ensembl ].
VAR_048893
Natural varianti320 – 3201S → C.1 Publication
Corresponds to variant rs41298896 [ dbSNP | Ensembl ].
VAR_048894
Natural varianti329 – 3291L → M.1 Publication
Corresponds to variant rs41299658 [ dbSNP | Ensembl ].
VAR_060691

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 120120Missing in isoform 2. 1 PublicationVSP_014888Add
BLAST
Alternative sequencei1 – 115115Missing in isoform 3. 3 PublicationsVSP_014889Add
BLAST
Alternative sequencei116 – 1216CPGSVM → MKHQER in isoform 3. 3 PublicationsVSP_014890
Alternative sequencei386 – 43449EEEDD…RQTPG → GSHSVTQARMRWCHHDSLYP LTPGIKRSSCLSLLTSWITG AYRHAQLMI in isoform 4. 1 PublicationVSP_014891Add
BLAST
Alternative sequencei435 – 692258Missing in isoform 4. 1 PublicationVSP_014892Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ296101 mRNA. Translation: CAC37570.1.
AF395747 mRNA. Translation: AAM53255.1.
AF395748 mRNA. Translation: AAM53256.1.
AF395749 mRNA. Translation: AAM53257.1.
AF395750 mRNA. Translation: AAM53258.1.
AF395751 mRNA. Translation: AAM53259.1.
AF395752 mRNA. Translation: AAM53260.1.
AK021422 mRNA. Translation: BAB13820.1.
DQ504427 Genomic DNA. Translation: ABF47101.1.
AL360083 Genomic DNA. Translation: CAI40018.1. Sequence problems.
AL360083 Genomic DNA. Translation: CAI40019.1. Sequence problems.
AL360083 Genomic DNA. Translation: CAI40020.1.
AL360083 Genomic DNA. Translation: CAI40021.1. Sequence problems.
AL360083 Genomic DNA. Translation: CAI40022.1.
AL360083 Genomic DNA. Translation: CAI40023.1. Sequence problems.
AL360083 Genomic DNA. Translation: CAI40024.1.
AL360083, AC069544 Genomic DNA. Translation: CAI40025.1.
CH471072 Genomic DNA. Translation: EAW86248.1.
CH471072 Genomic DNA. Translation: EAW86250.1.
CH471072 Genomic DNA. Translation: EAW86251.1.
BC000863 mRNA. Translation: AAH00863.1.
BC009185 mRNA. Translation: AAH09185.1.
BC022254 mRNA. Translation: AAH22254.1.
CCDSiCCDS31149.1. [Q96SD1-1]
CCDS31150.1. [Q96SD1-2]
CCDS7105.1. [Q96SD1-3]
RefSeqiNP_001029027.1. NM_001033855.2. [Q96SD1-1]
NP_001029029.1. NM_001033857.2. [Q96SD1-2]
NP_001029030.1. NM_001033858.2. [Q96SD1-2]
NP_001276005.1. NM_001289076.1. [Q96SD1-3]
NP_001276006.1. NM_001289077.1. [Q96SD1-2]
NP_001276007.1. NM_001289078.1. [Q96SD1-3]
NP_001276008.1. NM_001289079.1. [Q96SD1-2]
NP_071932.2. NM_022487.3. [Q96SD1-3]
XP_005252615.1. XM_005252558.1. [Q96SD1-2]
XP_006717554.1. XM_006717491.1. [Q96SD1-3]
UniGeneiHs.655932.
Hs.656065.

Genome annotation databases

EnsembliENST00000357717; ENSP00000350349; ENSG00000152457. [Q96SD1-3]
ENST00000378246; ENSP00000367492; ENSG00000152457. [Q96SD1-3]
ENST00000378249; ENSP00000367496; ENSG00000152457. [Q96SD1-3]
ENST00000378254; ENSP00000367502; ENSG00000152457. [Q96SD1-2]
ENST00000378255; ENSP00000367503; ENSG00000152457. [Q96SD1-2]
ENST00000378258; ENSP00000367506; ENSG00000152457. [Q96SD1-2]
ENST00000378278; ENSP00000367527; ENSG00000152457. [Q96SD1-1]
ENST00000378289; ENSP00000367538; ENSG00000152457. [Q96SD1-4]
ENST00000396817; ENSP00000380030; ENSG00000152457. [Q96SD1-2]
GeneIDi64421.
KEGGihsa:64421.
UCSCiuc001inl.3. human. [Q96SD1-1]
uc001ino.3. human. [Q96SD1-3]
uc010qbx.2. human. [Q96SD1-4]

Polymorphism databases

DMDMi71153325.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

DCLRE1Cbase

DCLRE1C mutation db

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ296101 mRNA. Translation: CAC37570.1 .
AF395747 mRNA. Translation: AAM53255.1 .
AF395748 mRNA. Translation: AAM53256.1 .
AF395749 mRNA. Translation: AAM53257.1 .
AF395750 mRNA. Translation: AAM53258.1 .
AF395751 mRNA. Translation: AAM53259.1 .
AF395752 mRNA. Translation: AAM53260.1 .
AK021422 mRNA. Translation: BAB13820.1 .
DQ504427 Genomic DNA. Translation: ABF47101.1 .
AL360083 Genomic DNA. Translation: CAI40018.1 . Sequence problems.
AL360083 Genomic DNA. Translation: CAI40019.1 . Sequence problems.
AL360083 Genomic DNA. Translation: CAI40020.1 .
AL360083 Genomic DNA. Translation: CAI40021.1 . Sequence problems.
AL360083 Genomic DNA. Translation: CAI40022.1 .
AL360083 Genomic DNA. Translation: CAI40023.1 . Sequence problems.
AL360083 Genomic DNA. Translation: CAI40024.1 .
AL360083 , AC069544 Genomic DNA. Translation: CAI40025.1 .
CH471072 Genomic DNA. Translation: EAW86248.1 .
CH471072 Genomic DNA. Translation: EAW86250.1 .
CH471072 Genomic DNA. Translation: EAW86251.1 .
BC000863 mRNA. Translation: AAH00863.1 .
BC009185 mRNA. Translation: AAH09185.1 .
BC022254 mRNA. Translation: AAH22254.1 .
CCDSi CCDS31149.1. [Q96SD1-1 ]
CCDS31150.1. [Q96SD1-2 ]
CCDS7105.1. [Q96SD1-3 ]
RefSeqi NP_001029027.1. NM_001033855.2. [Q96SD1-1 ]
NP_001029029.1. NM_001033857.2. [Q96SD1-2 ]
NP_001029030.1. NM_001033858.2. [Q96SD1-2 ]
NP_001276005.1. NM_001289076.1. [Q96SD1-3 ]
NP_001276006.1. NM_001289077.1. [Q96SD1-2 ]
NP_001276007.1. NM_001289078.1. [Q96SD1-3 ]
NP_001276008.1. NM_001289079.1. [Q96SD1-2 ]
NP_071932.2. NM_022487.3. [Q96SD1-3 ]
XP_005252615.1. XM_005252558.1. [Q96SD1-2 ]
XP_006717554.1. XM_006717491.1. [Q96SD1-3 ]
UniGenei Hs.655932.
Hs.656065.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3W1B X-ray 2.40 B 485-495 [» ]
3W1G X-ray 2.55 B 485-495 [» ]
4HTP X-ray 2.25 C/E 485-495 [» ]
ProteinModelPortali Q96SD1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122170. 33 interactions.

PTM databases

PhosphoSitei Q96SD1.

Polymorphism databases

DMDMi 71153325.

Proteomic databases

MaxQBi Q96SD1.
PaxDbi Q96SD1.
PRIDEi Q96SD1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357717 ; ENSP00000350349 ; ENSG00000152457 . [Q96SD1-3 ]
ENST00000378246 ; ENSP00000367492 ; ENSG00000152457 . [Q96SD1-3 ]
ENST00000378249 ; ENSP00000367496 ; ENSG00000152457 . [Q96SD1-3 ]
ENST00000378254 ; ENSP00000367502 ; ENSG00000152457 . [Q96SD1-2 ]
ENST00000378255 ; ENSP00000367503 ; ENSG00000152457 . [Q96SD1-2 ]
ENST00000378258 ; ENSP00000367506 ; ENSG00000152457 . [Q96SD1-2 ]
ENST00000378278 ; ENSP00000367527 ; ENSG00000152457 . [Q96SD1-1 ]
ENST00000378289 ; ENSP00000367538 ; ENSG00000152457 . [Q96SD1-4 ]
ENST00000396817 ; ENSP00000380030 ; ENSG00000152457 . [Q96SD1-2 ]
GeneIDi 64421.
KEGGi hsa:64421.
UCSCi uc001inl.3. human. [Q96SD1-1 ]
uc001ino.3. human. [Q96SD1-3 ]
uc010qbx.2. human. [Q96SD1-4 ]

Organism-specific databases

CTDi 64421.
GeneCardsi GC10M014939.
HGNCi HGNC:17642. DCLRE1C.
MIMi 602450. phenotype.
603554. phenotype.
605988. gene.
neXtProti NX_Q96SD1.
Orphaneti 39041. Omenn syndrome.
275. Severe combined immunodeficiency due to DCLRE1C deficiency.
PharmGKBi PA27176.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1236.
GeneTreei ENSGT00530000063183.
HOVERGENi HBG081421.
InParanoidi Q96SD1.
KOi K10887.
OMAi MFRNMPD.
OrthoDBi EOG70CR8F.
PhylomeDBi Q96SD1.
TreeFami TF329572.

Miscellaneous databases

GenomeRNAii 64421.
NextBioi 66403.
PROi Q96SD1.
SOURCEi Search...

Gene expression databases

Bgeei Q96SD1.
ExpressionAtlasi Q96SD1. baseline and differential.
Genevestigatori Q96SD1.

Family and domain databases

Gene3Di 3.60.15.10. 1 hit.
InterProi IPR001279. Beta-lactamas-like.
IPR011084. DRMBL.
[Graphical view ]
Pfami PF07522. DRMBL. 1 hit.
[Graphical view ]
SMARTi SM00849. Lactamase_B. 1 hit.
[Graphical view ]
SUPFAMi SSF56281. SSF56281. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Artemis, a novel DNA double-strand break repair/V(D)J recombination protein, is mutated in human severe combined immune deficiency."
    Moshous D., Callebaut I., de Chasseval R., Corneo B., Cavazzana-Calvo M., le Deist F., Tezcan I., Sanal O., Bertrand Y., Philippe N., Fischer A., de Villartay J.-P.
    Cell 105:177-186(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN RSSCID.
  2. "A founder mutation in Artemis, an SNM1-like protein, causes SCID in Athabascan-speaking native Americans."
    Li L., Moshous D., Zhou Y., Wang J., Xie G., Salido E., Hu D., de Villartay J.-P., Cowan M.J.
    J. Immunol. 168:6323-6329(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN SCIDA.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ARG-171.
    Tissue: Embryo.
  4. NIEHS SNPs program
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-140; ARG-153; ARG-171; ARG-243; CYS-320 AND MET-329.
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 401-692 (ISOFORMS 1/2/3), VARIANT ARG-243.
    Tissue: Cervix carcinoma, Lung carcinoma and Skeletal muscle.
  8. "Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination."
    Ma Y., Pannicke U., Schwarz K., Lieber M.R.
    Cell 108:781-794(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRKDC, PHOSPHORYLATION BY PRKDC, MUTAGENESIS OF ASP-165.
  9. "Metallo-beta-lactamase fold within nucleic acids processing enzymes: the beta-CASP family."
    Callebaut I., Moshous D., Mornon J.-P., de Villartay J.-P.
    Nucleic Acids Res. 30:3592-3601(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA REPAIR METALLO-BETA-LACTAMASE FAMILY.
  10. "Functional and biochemical dissection of the structure-specific nuclease ARTEMIS."
    Pannicke U., Ma Y., Hopfner K.-P., Niewolik D., Lieber M.R., Schwarz K.
    EMBO J. 23:1987-1997(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-17; HIS-33; HIS-35; ASP-37; HIS-38; HIS-115; ASP-136; ASP-165 AND HIS-319, PHOSPHORYLATION BY PRKDC.
  11. Cited for: FUNCTION, MUTAGENESIS OF SER-516; SER-534; SER-538; SER-548; SER-553; SER-561 AND SER-562, PHOSPHORYLATION BY ATM, PHOSPHORYLATION AT SER-645.
  12. "The metallo-beta-lactamase/beta-CASP domain of Artemis constitutes the catalytic core for V(D)J recombination."
    Poinsignon C., Moshous D., Callebaut I., de Chasseval R., Villey I., de Villartay J.-P.
    J. Exp. Med. 199:315-321(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRKDC, MUTAGENESIS OF ASP-17; HIS-33; HIS-35; ASP-37; HIS-38; HIS-115; ASP-136; ASP-165 AND HIS-319.
  13. "A biochemically defined system for mammalian nonhomologous DNA end joining."
    Ma Y., Lu H., Tippin B., Goodman M.F., Shimazaki N., Koiwai O., Hsieh C.-L., Schwarz K., Lieber M.R.
    Mol. Cell 16:701-713(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRKDC.
  14. "A pathway of double-strand break rejoining dependent upon ATM, Artemis, and proteins locating to gamma-H2AX foci."
    Riballo E., Kuehne M., Rief N., Doherty A., Smith G.C.M., Recio M.-J., Reis C., Dahm K., Fricke A., Krempler A., Parker A.R., Jackson S.P., Gennery A., Jeggo P.A., Loebrich M.
    Mol. Cell 16:715-724(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53BP1, MUTAGENESIS OF ASP-37, PHOSPHORYLATION BY ATM.
  15. "Artemis is a phosphorylation target of ATM and ATR and is involved in the G2/M DNA damage checkpoint response."
    Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D., Legerski R.J.
    Mol. Cell. Biol. 24:9207-9220(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATM; BRCA1; THE MRN COMPLEX AND PRKDC, PHOSPHORYLATION BY ATM; ATR AND PRKDC.
  16. "Ataxia-telangiectasia-mutated dependent phosphorylation of Artemis in response to DNA damage."
    Chen L., Morio T., Minegishi Y., Nakada S., Nagasawa M., Komatsu K., Chessa L., Villa A., Lecis D., Delia D., Mizutani S.
    Cancer Sci. 96:134-141(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE MRN COMPLEX, PHOSPHORYLATION BY ATM, PHOSPHORYLATION AT SER-645.
  17. "Artemis deficiency confers a DNA double-strand break repair defect and Artemis phosphorylation status is altered by DNA damage and cell cycle progression."
    Wang J., Pluth J.M., Cooper P.K., Cowan M.J., Chen D.J., Yannone S.M.
    DNA Repair 4:556-570(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION BY PRKDC, PHOSPHORYLATION IN RESPONSE TO DNA DAMAGE.
  18. "The Artemis:DNA-PKcs endonuclease cleaves DNA loops, flaps, and gaps."
    Ma Y., Schwarz K., Lieber M.R.
    DNA Repair 4:845-851(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRKDC.
  19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "Radiosensitive SCID patients with Artemis gene mutations show a complete B-cell differentiation arrest at the pre-B-cell receptor checkpoint in bone marrow."
    Noordzij J.G., Verkaik N.S., van der Burg M., van Veelen L.R., de Bruin-Versteeg S., Wiegant W., Vossen J.M.J.J., Weemaes C.M.R., de Groot R., Zdzienicka M.Z., van Gent D.C., van Dongen J.J.M.
    Blood 101:1446-1452(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS RSSCID VAL-118 AND GLU-135.
  21. "Expansion of clonotype-restricted HLA-identical maternal CD4+ T cells in a patient with severe combined immunodeficiency and a homozygous mutation in the Artemis gene."
    Kobayashi N., Agematsu K., Nagumo H., Yasui K., Katsuyama Y., Yoshizawa K., Ota M., Yachie A., Komiyama A.
    Clin. Immunol. 108:159-166(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN RSSCID.
  22. "Novel Artemis gene mutations of radiosensitive severe combined immunodeficiency in Japanese families."
    Kobayashi N., Agematsu K., Sugita K., Sako M., Nonoyama S., Yachie A., Kumaki S., Tsuchiya S., Ochs H.D., Sugita K., Fukushima Y., Komiyama A.
    Hum. Genet. 112:348-352(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN RSSCID.
  23. "Partial T and B lymphocyte immunodeficiency and predisposition to lymphoma in patients with hypomorphic mutations in Artemis."
    Moshous D., Pannetier C., de Chasseval R., le Deist F., Cavazzana-Calvo M., Romana S., Macintyre E., Canioni D., Brousse N., Fischer A., Casanova J.-L., de Villartay J.-P.
    J. Clin. Invest. 111:381-387(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN RSSCID.
  24. Cited for: VARIANT OMENN SYNDROME ASP-35.

Entry informationi

Entry nameiDCR1C_HUMAN
AccessioniPrimary (citable) accession number: Q96SD1
Secondary accession number(s): D3DRT6
, Q1HCL2, Q5JSR4, Q5JSR5, Q5JSR7, Q5JSR8, Q5JSR9, Q5JSS0, Q5JSS7, Q6PK14, Q8N101, Q8N132, Q8TBW9, Q9BVW9, Q9HAM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: October 29, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3