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Protein artemis (EC 3.1.-.-) (DNA cross-link repair 1C protein) (Protein A-SCID) (SNM1 homolog C) (hSNM1C) (SNM1-like protein)

 DCR1C_HUMAN             Reviewed;         692 AA.
Q96SD1; D3DRT6; Q1HCL2; Q5JSR4; Q5JSR5; Q5JSR7; Q5JSR8; Q5JSR9;
Q5JSS0; Q5JSS7; Q6PK14; Q8N101; Q8N132; Q8TBW9; Q9BVW9; Q9HAM4;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 2.
25-OCT-2017, entry version 130.
RecName: Full=Protein artemis;
EC=3.1.-.-;
AltName: Full=DNA cross-link repair 1C protein;
AltName: Full=Protein A-SCID;
AltName: Full=SNM1 homolog C;
Short=hSNM1C;
AltName: Full=SNM1-like protein;
Name=DCLRE1C; Synonyms=ARTEMIS, ASCID, SCIDA, SNM1C;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND INVOLVEMENT IN RSSCID.
PubMed=11336668; DOI=10.1016/S0092-8674(01)00309-9;
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.;
"Artemis, a novel DNA double-strand break repair/V(D)J recombination
protein, is mutated in human severe combined immune deficiency.";
Cell 105:177-186(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULAR
LOCATION, AND INVOLVEMENT IN SCIDA.
PubMed=12055248; DOI=10.4049/jimmunol.168.12.6323;
Li L., Moshous D., Zhou Y., Wang J., Xie G., Salido E., Hu D.,
de Villartay J.-P., Cowan M.J.;
"A founder mutation in Artemis, an SNM1-like protein, causes SCID in
Athabascan-speaking native Americans.";
J. Immunol. 168:6323-6329(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
ARG-171.
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-140; ARG-153;
ARG-171; ARG-243; CYS-320 AND MET-329.
NIEHS SNPs program;
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
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.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 401-692 (ISOFORMS 1/2/3), AND VARIANT
ARG-243.
TISSUE=Cervix carcinoma, Lung carcinoma, and Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, INTERACTION WITH PRKDC, PHOSPHORYLATION BY PRKDC, AND
MUTAGENESIS OF ASP-165.
PubMed=11955432; DOI=10.1016/S0092-8674(02)00671-2;
Ma Y., Pannicke U., Schwarz K., Lieber M.R.;
"Hairpin opening and overhang processing by an Artemis/DNA-dependent
protein kinase complex in nonhomologous end joining and V(D)J
recombination.";
Cell 108:781-794(2002).
[9]
DNA REPAIR METALLO-BETA-LACTAMASE FAMILY.
PubMed=12177301; DOI=10.1093/nar/gkf470;
Callebaut I., Moshous D., Mornon J.-P., de Villartay J.-P.;
"Metallo-beta-lactamase fold within nucleic acids processing enzymes:
the beta-CASP family.";
Nucleic Acids Res. 30:3592-3601(2002).
[10]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-17; HIS-33; HIS-35;
ASP-37; HIS-38; HIS-115; ASP-136; ASP-165 AND HIS-319, AND
PHOSPHORYLATION BY PRKDC.
PubMed=15071507; DOI=10.1038/sj.emboj.7600206;
Pannicke U., Ma Y., Hopfner K.-P., Niewolik D., Lieber M.R.,
Schwarz K.;
"Functional and biochemical dissection of the structure-specific
nuclease ARTEMIS.";
EMBO J. 23:1987-1997(2004).
[11]
FUNCTION, MUTAGENESIS OF SER-516; SER-534; SER-538; SER-548; SER-553;
SER-561 AND SER-562, PHOSPHORYLATION BY ATM, AND PHOSPHORYLATION AT
SER-645.
PubMed=15468306; DOI=10.1002/eji.200425455;
Poinsignon C., de Chasseval R., Soubeyrand S., Moshous D., Fischer A.,
Hache R.J.G., de Villartay J.-P.;
"Phosphorylation of Artemis following irradiation-induced DNA
damage.";
Eur. J. Immunol. 34:3146-3155(2004).
[12]
FUNCTION, INTERACTION WITH PRKDC, AND MUTAGENESIS OF ASP-17; HIS-33;
HIS-35; ASP-37; HIS-38; HIS-115; ASP-136; ASP-165 AND HIS-319.
PubMed=14744996; DOI=10.1084/jem.20031142;
Poinsignon C., Moshous D., Callebaut I., de Chasseval R., Villey I.,
de Villartay J.-P.;
"The metallo-beta-lactamase/beta-CASP domain of Artemis constitutes
the catalytic core for V(D)J recombination.";
J. Exp. Med. 199:315-321(2004).
[13]
FUNCTION, AND INTERACTION WITH PRKDC.
PubMed=15574326; DOI=10.1016/j.molcel.2004.11.017;
Ma Y., Lu H., Tippin B., Goodman M.F., Shimazaki N., Koiwai O.,
Hsieh C.-L., Schwarz K., Lieber M.R.;
"A biochemically defined system for mammalian nonhomologous DNA end
joining.";
Mol. Cell 16:701-713(2004).
[14]
FUNCTION, INTERACTION WITH TP53BP1, MUTAGENESIS OF ASP-37, AND
PHOSPHORYLATION BY ATM.
PubMed=15574327; DOI=10.1016/j.molcel.2004.10.029;
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.;
"A pathway of double-strand break rejoining dependent upon ATM,
Artemis, and proteins locating to gamma-H2AX foci.";
Mol. Cell 16:715-724(2004).
[15]
FUNCTION, INTERACTION WITH ATM; BRCA1; THE MRN COMPLEX AND PRKDC, AND
PHOSPHORYLATION BY ATM; ATR AND PRKDC.
PubMed=15456891; DOI=10.1128/MCB.24.20.9207-9220.2004;
Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D.,
Legerski R.J.;
"Artemis is a phosphorylation target of ATM and ATR and is involved in
the G2/M DNA damage checkpoint response.";
Mol. Cell. Biol. 24:9207-9220(2004).
[16]
INTERACTION WITH THE MRN COMPLEX, PHOSPHORYLATION BY ATM, AND
PHOSPHORYLATION AT SER-645.
PubMed=15723659; DOI=10.1111/j.1349-7006.2005.00019.x;
Chen L., Morio T., Minegishi Y., Nakada S., Nagasawa M., Komatsu K.,
Chessa L., Villa A., Lecis D., Delia D., Mizutani S.;
"Ataxia-telangiectasia-mutated dependent phosphorylation of Artemis in
response to DNA damage.";
Cancer Sci. 96:134-141(2005).
[17]
FUNCTION, PHOSPHORYLATION BY PRKDC, AND PHOSPHORYLATION IN RESPONSE TO
DNA DAMAGE.
PubMed=15811628; DOI=10.1016/j.dnarep.2005.02.001;
Wang J., Pluth J.M., Cooper P.K., Cowan M.J., Chen D.J., Yannone S.M.;
"Artemis deficiency confers a DNA double-strand break repair defect
and Artemis phosphorylation status is altered by DNA damage and cell
cycle progression.";
DNA Repair 4:556-570(2005).
[18]
FUNCTION, AND INTERACTION WITH PRKDC.
PubMed=15936993; DOI=10.1016/j.dnarep.2005.04.013;
Ma Y., Schwarz K., Lieber M.R.;
"The Artemis:DNA-PKcs endonuclease cleaves DNA loops, flaps, and
gaps.";
DNA Repair 4:845-851(2005).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
VARIANTS RSSCID VAL-118 AND GLU-135.
PubMed=12406895; DOI=10.1182/blood-2002-01-0187;
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.;
"Radiosensitive SCID patients with Artemis gene mutations show a
complete B-cell differentiation arrest at the pre-B-cell receptor
checkpoint in bone marrow.";
Blood 101:1446-1452(2003).
[22]
INVOLVEMENT IN RSSCID.
PubMed=12921762; DOI=10.1016/S1521-6616(03)00095-0;
Kobayashi N., Agematsu K., Nagumo H., Yasui K., Katsuyama Y.,
Yoshizawa K., Ota M., Yachie A., Komiyama A.;
"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.";
Clin. Immunol. 108:159-166(2003).
[23]
INVOLVEMENT IN RSSCID.
PubMed=12592555; DOI=10.1007/s00439-002-0897-x;
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.;
"Novel Artemis gene mutations of radiosensitive severe combined
immunodeficiency in Japanese families.";
Hum. Genet. 112:348-352(2003).
[24]
INVOLVEMENT IN RSSCID.
PubMed=12569164; DOI=10.1172/JCI16774;
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.;
"Partial T and B lymphocyte immunodeficiency and predisposition to
lymphoma in patients with hypomorphic mutations in Artemis.";
J. Clin. Invest. 111:381-387(2003).
[25]
VARIANT OMENN SYNDROME ASP-35.
PubMed=15731174; DOI=10.1182/blood-2004-12-4861;
Ege M., Ma Y., Manfras B., Kalwak K., Lu H., Lieber M.R., Schwarz K.,
Pannicke U.;
"Omenn syndrome due to ARTEMIS mutations.";
Blood 105:4179-4186(2005).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:11336668, ECO:0000269|PubMed:11955432,
ECO:0000269|PubMed:12055248, ECO:0000269|PubMed:14744996,
ECO:0000269|PubMed:15071507, ECO:0000269|PubMed:15456891,
ECO:0000269|PubMed:15468306, ECO:0000269|PubMed:15574326,
ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:15811628,
ECO:0000269|PubMed:15936993}.
-!- SUBUNIT: Interacts with ATM, BRCA1, PRKDC and TP53BP1. Also
exhibits ATM- and phosphorylation-dependent interaction with the
MRN complex, composed of MRE11, RAD50, and NBN.
{ECO:0000269|PubMed:11955432, ECO:0000269|PubMed:14744996,
ECO:0000269|PubMed:15456891, ECO:0000269|PubMed:15574326,
ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:15723659,
ECO:0000269|PubMed:15936993}.
-!- INTERACTION:
P49917:LIG4; NbExp=16; IntAct=EBI-11694104, EBI-847896;
P78527:PRKDC; NbExp=4; IntAct=EBI-11694104, EBI-352053;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12055248,
ECO:0000269|PubMed:15071507}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q96SD1-1; Sequence=Displayed;
Name=2; Synonyms=SCIDA;
IsoId=Q96SD1-2; Sequence=VSP_014888;
Name=3;
IsoId=Q96SD1-3; Sequence=VSP_014889, VSP_014890;
Name=4;
IsoId=Q96SD1-4; Sequence=VSP_014891, VSP_014892;
-!- TISSUE SPECIFICITY: 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. {ECO:0000269|PubMed:11336668}.
-!- PTM: 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. {ECO:0000269|PubMed:11955432,
ECO:0000269|PubMed:15071507, ECO:0000269|PubMed:15456891,
ECO:0000269|PubMed:15468306, ECO:0000269|PubMed:15574327,
ECO:0000269|PubMed:15723659, ECO:0000269|PubMed:15811628}.
-!- DISEASE: 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.
{ECO:0000269|PubMed:11336668, ECO:0000269|PubMed:12406895,
ECO:0000269|PubMed:12569164, ECO:0000269|PubMed:12592555,
ECO:0000269|PubMed:12921762}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:12055248}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Omenn syndrome (OS) [MIM:603554]: Severe immunodeficiency
characterized by the presence of activated, anergic, oligoclonal
T-cells, hypereosinophilia, and high IgE levels.
{ECO:0000269|PubMed:15731174}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase
(DRMBL) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAI40018.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI40019.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI40021.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI40023.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=DCLRE1Cbase; Note=DCLRE1C mutation db;
URL="http://structure.bmc.lu.se/idbase/DCLRE1Cbase/";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/dclre1c/";
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EMBL; AJ296101; CAC37570.1; -; mRNA.
EMBL; AF395747; AAM53255.1; -; mRNA.
EMBL; AF395748; AAM53256.1; -; mRNA.
EMBL; AF395749; AAM53257.1; -; mRNA.
EMBL; AF395750; AAM53258.1; -; mRNA.
EMBL; AF395751; AAM53259.1; -; mRNA.
EMBL; AF395752; AAM53260.1; -; mRNA.
EMBL; AK021422; BAB13820.1; -; mRNA.
EMBL; DQ504427; ABF47101.1; -; Genomic_DNA.
EMBL; AL360083; CAI40018.1; ALT_SEQ; Genomic_DNA.
EMBL; AL360083; CAI40019.1; ALT_SEQ; Genomic_DNA.
EMBL; AL360083; CAI40020.1; -; Genomic_DNA.
EMBL; AL360083; CAI40021.1; ALT_SEQ; Genomic_DNA.
EMBL; AL360083; CAI40022.1; -; Genomic_DNA.
EMBL; AL360083; CAI40023.1; ALT_SEQ; Genomic_DNA.
EMBL; AL360083; CAI40024.1; -; Genomic_DNA.
EMBL; AL360083; CAI40025.1; -; Genomic_DNA.
EMBL; AC069544; CAI40025.1; JOINED; Genomic_DNA.
EMBL; CH471072; EAW86248.1; -; Genomic_DNA.
EMBL; CH471072; EAW86250.1; -; Genomic_DNA.
EMBL; CH471072; EAW86251.1; -; Genomic_DNA.
EMBL; BC000863; AAH00863.1; -; mRNA.
EMBL; BC009185; AAH09185.1; -; mRNA.
EMBL; BC022254; AAH22254.1; -; mRNA.
CCDS; CCDS31149.1; -. [Q96SD1-1]
CCDS; CCDS31150.1; -. [Q96SD1-2]
CCDS; CCDS7105.1; -. [Q96SD1-3]
RefSeq; NP_001029027.1; NM_001033855.2. [Q96SD1-1]
RefSeq; NP_001029029.1; NM_001033857.2. [Q96SD1-2]
RefSeq; NP_001029030.1; NM_001033858.2. [Q96SD1-2]
RefSeq; NP_001276005.1; NM_001289076.1. [Q96SD1-3]
RefSeq; NP_001276006.1; NM_001289077.1. [Q96SD1-2]
RefSeq; NP_001276007.1; NM_001289078.1. [Q96SD1-3]
RefSeq; NP_001276008.1; NM_001289079.1. [Q96SD1-2]
RefSeq; NP_071932.2; NM_022487.3. [Q96SD1-3]
RefSeq; XP_006717554.1; XM_006717491.3. [Q96SD1-3]
RefSeq; XP_011517918.1; XM_011519616.1. [Q96SD1-3]
RefSeq; XP_011517919.1; XM_011519617.1. [Q96SD1-3]
RefSeq; XP_011517921.1; XM_011519619.1. [Q96SD1-2]
RefSeq; XP_016872046.1; XM_017016557.1. [Q96SD1-3]
RefSeq; XP_016872047.1; XM_017016558.1. [Q96SD1-2]
UniGene; Hs.655932; -.
UniGene; Hs.656065; -.
UniGene; Hs.737284; -.
PDB; 3W1B; X-ray; 2.40 A; B=485-495.
PDB; 3W1G; X-ray; 2.55 A; B=485-495.
PDB; 4HTP; X-ray; 2.25 A; C/E=485-495.
PDBsum; 3W1B; -.
PDBsum; 3W1G; -.
PDBsum; 4HTP; -.
ProteinModelPortal; Q96SD1; -.
SMR; Q96SD1; -.
BioGrid; 122170; 36.
CORUM; Q96SD1; -.
IntAct; Q96SD1; 3.
STRING; 9606.ENSP00000367527; -.
BindingDB; Q96SD1; -.
iPTMnet; Q96SD1; -.
PhosphoSitePlus; Q96SD1; -.
BioMuta; DCLRE1C; -.
DMDM; 71153325; -.
EPD; Q96SD1; -.
MaxQB; Q96SD1; -.
PaxDb; Q96SD1; -.
PeptideAtlas; Q96SD1; -.
PRIDE; Q96SD1; -.
Ensembl; ENST00000357717; ENSP00000350349; ENSG00000152457. [Q96SD1-3]
Ensembl; ENST00000378246; ENSP00000367492; ENSG00000152457. [Q96SD1-3]
Ensembl; ENST00000378249; ENSP00000367496; ENSG00000152457. [Q96SD1-3]
Ensembl; ENST00000378254; ENSP00000367502; ENSG00000152457. [Q96SD1-2]
Ensembl; ENST00000378255; ENSP00000367503; ENSG00000152457. [Q96SD1-2]
Ensembl; ENST00000378258; ENSP00000367506; ENSG00000152457. [Q96SD1-2]
Ensembl; ENST00000378278; ENSP00000367527; ENSG00000152457. [Q96SD1-1]
Ensembl; ENST00000378289; ENSP00000367538; ENSG00000152457. [Q96SD1-4]
Ensembl; ENST00000396817; ENSP00000380030; ENSG00000152457. [Q96SD1-2]
GeneID; 64421; -.
KEGG; hsa:64421; -.
UCSC; uc001inl.5; human. [Q96SD1-1]
CTD; 64421; -.
DisGeNET; 64421; -.
EuPathDB; HostDB:ENSG00000152457.17; -.
GeneCards; DCLRE1C; -.
HGNC; HGNC:17642; DCLRE1C.
HPA; HPA069295; -.
MalaCards; DCLRE1C; -.
MIM; 602450; phenotype.
MIM; 603554; phenotype.
MIM; 605988; gene.
neXtProt; NX_Q96SD1; -.
OpenTargets; ENSG00000152457; -.
Orphanet; 39041; Omenn syndrome.
Orphanet; 275; Severe combined immunodeficiency due to DCLRE1C deficiency.
PharmGKB; PA27176; -.
eggNOG; KOG1361; Eukaryota.
eggNOG; COG1236; LUCA.
GeneTree; ENSGT00530000063183; -.
HOVERGEN; HBG081421; -.
InParanoid; Q96SD1; -.
KO; K10887; -.
OMA; CYSTHAS; -.
OrthoDB; EOG091G0TAU; -.
PhylomeDB; Q96SD1; -.
TreeFam; TF329572; -.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
SIGNOR; Q96SD1; -.
ChiTaRS; DCLRE1C; human.
GenomeRNAi; 64421; -.
PRO; PR:Q96SD1; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000152457; -.
ExpressionAtlas; Q96SD1; baseline and differential.
Genevisible; Q96SD1; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0070419; C:nonhomologous end joining complex; IDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
GO; GO:0008409; F:5'-3' exonuclease activity; IDA:MGI.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0004519; F:endonuclease activity; TAS:Reactome.
GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:MGI.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
GO; GO:0031848; P:protection from non-homologous end joining at telomere; IBA:GO_Central.
GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
GO; GO:0033151; P:V(D)J recombination; IEA:Ensembl.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR011084; DRMBL.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR036866; Metallo-hydrolase/OxRdtase.
Pfam; PF07522; DRMBL; 1.
Pfam; PF12706; Lactamase_B_2; 1.
SUPFAM; SSF56281; SSF56281; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing;
Complete proteome; Disease mutation; DNA damage; DNA recombination;
DNA repair; Endonuclease; Exonuclease; Hydrolase; Immunity; Magnesium;
Nuclease; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
SCID.
CHAIN 1 692 Protein artemis.
/FTId=PRO_0000209122.
MOD_RES 380 380 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8K4J0}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K4J0}.
MOD_RES 645 645 Phosphoserine; by ATM.
{ECO:0000269|PubMed:15468306,
ECO:0000269|PubMed:15723659}.
VAR_SEQ 1 120 Missing (in isoform 2).
{ECO:0000303|PubMed:12055248}.
/FTId=VSP_014888.
VAR_SEQ 1 115 Missing (in isoform 3).
{ECO:0000303|PubMed:12055248,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_014889.
VAR_SEQ 116 121 CPGSVM -> MKHQER (in isoform 3).
{ECO:0000303|PubMed:12055248,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_014890.
VAR_SEQ 386 434 EEEDDYLFDDPLPIPLRHKVPYPETFHPEVFSMTAVSEKQP
EKLRQTPG -> GSHSVTQARMRWCHHDSLYPLTPGIKRSS
CLSLLTSWITGAYRHAQLMI (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014891.
VAR_SEQ 435 692 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014892.
VARIANT 35 35 H -> D (in Omenn syndrome;
dbSNP:rs121908159).
{ECO:0000269|PubMed:15731174}.
/FTId=VAR_023077.
VARIANT 118 118 G -> V (in RSSCID).
{ECO:0000269|PubMed:12406895}.
/FTId=VAR_023078.
VARIANT 135 135 G -> E (in RSSCID).
{ECO:0000269|PubMed:12406895}.
/FTId=VAR_023079.
VARIANT 140 140 A -> V (in dbSNP:rs41297016).
{ECO:0000269|Ref.4}.
/FTId=VAR_060689.
VARIANT 153 153 G -> R (in dbSNP:rs41297018).
{ECO:0000269|Ref.4}.
/FTId=VAR_060690.
VARIANT 171 171 P -> R (in dbSNP:rs35441642).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.4}.
/FTId=VAR_048892.
VARIANT 243 243 H -> R (in dbSNP:rs12768894).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.4}.
/FTId=VAR_048893.
VARIANT 320 320 S -> C (in dbSNP:rs41298896).
{ECO:0000269|Ref.4}.
/FTId=VAR_048894.
VARIANT 329 329 L -> M (in dbSNP:rs41299658).
{ECO:0000269|Ref.4}.
/FTId=VAR_060691.
MUTAGEN 17 17 D->N,A: Abolishes PRKDC-dependent
endonuclease activity and V(D)J
recombination.
{ECO:0000269|PubMed:14744996,
ECO:0000269|PubMed:15071507}.
MUTAGEN 33 33 H->A: Abolishes PRKDC-dependent
endonuclease activity and V(D)J
recombination.
{ECO:0000269|PubMed:14744996,
ECO:0000269|PubMed:15071507}.
MUTAGEN 35 35 H->A: Abolishes PRKDC-dependent
endonuclease activity and V(D)J
recombination.
{ECO:0000269|PubMed:14744996,
ECO:0000269|PubMed:15071507}.
MUTAGEN 37 37 D->N,A: Abolishes PRKDC-dependent
endonuclease activity and V(D)J
recombination.
{ECO:0000269|PubMed:14744996,
ECO:0000269|PubMed:15071507,
ECO:0000269|PubMed:15574327}.
MUTAGEN 38 38 H->A: Reduces PRKDC-dependent
endonuclease activity, although V(D)J
recombination is largely normal.
{ECO:0000269|PubMed:14744996,
ECO:0000269|PubMed:15071507}.
MUTAGEN 115 115 H->A: Abolishes PRKDC-dependent
endonuclease activity and V(D)J
recombination.
{ECO:0000269|PubMed:14744996,
ECO:0000269|PubMed:15071507}.
MUTAGEN 136 136 D->N,A: Abolishes PRKDC-dependent
endonuclease activity and V(D)J
recombination.
{ECO:0000269|PubMed:14744996,
ECO:0000269|PubMed:15071507}.
MUTAGEN 165 165 D->N,A: Abolishes PRKDC-dependent
endonuclease activity and V(D)J
recombination.
{ECO:0000269|PubMed:11955432,
ECO:0000269|PubMed:14744996,
ECO:0000269|PubMed:15071507}.
MUTAGEN 319 319 H->A: Abolishes PRKDC-dependent
endonuclease activity and V(D)J
recombination.
{ECO:0000269|PubMed:14744996,
ECO:0000269|PubMed:15071507}.
MUTAGEN 516 516 S->A: Reduced IR induced phosphorylation;
when associated with A-534; A-538; A-548;
A-553; A-561 and A-562.
{ECO:0000269|PubMed:15468306}.
MUTAGEN 534 534 S->A: Reduced IR induced phosphorylation;
when associated with A-516; A-538; A-548;
A-553; A-561 and A-562.
{ECO:0000269|PubMed:15468306}.
MUTAGEN 538 538 S->A: Reduced IR induced phosphorylation;
when associated with A-516; A-534; A-548;
A-553; A-561 and A-562.
{ECO:0000269|PubMed:15468306}.
MUTAGEN 548 548 S->A: Reduced IR induced phosphorylation;
when associated with A-516; A-534; A-538;
A-553; A-561 and A-562.
{ECO:0000269|PubMed:15468306}.
MUTAGEN 553 553 S->A: Reduced IR induced phosphorylation;
when associated with A-516; A-534; A-538;
A-548; A-561 and A-562.
{ECO:0000269|PubMed:15468306}.
MUTAGEN 561 561 S->A: Reduced IR induced phosphorylation;
when associated with A-516; A-534; A-538;
A-548; A-553 and A-562.
{ECO:0000269|PubMed:15468306}.
MUTAGEN 562 562 S->A: Reduced IR induced phosphorylation;
when associated with A-516; A-534; A-538;
A-548; A-553 and A-561.
{ECO:0000269|PubMed:15468306}.
CONFLICT 560 560 L -> V (in Ref. 1; CAC37570 and 2;
AAM53255/AAM53256/AAM53257/AAM53258/
AAM53259/AAM53260). {ECO:0000305}.
HELIX 489 491 {ECO:0000244|PDB:4HTP}.
SEQUENCE 692 AA; 78436 MW; 24B857F5B473637B CRC64;
MSSFEGQMAE YPTISIDRFD RENLRARAYF LSHCHKDHMK GLRAPTLKRR LECSLKVYLY
CSPVTKELLL TSPKYRFWKK RIISIEIETP TQISLVDEAS GEKEEIVVTL LPAGHCPGSV
MFLFQGNNGT VLYTGDFRLA QGEAARMELL HSGGRVKDIQ SVYLDTTFCD PRFYQIPSRE
ECLSGVLELV RSWITRSPYH VVWLNCKAAY GYEYLFTNLS EELGVQVHVN KLDMFRNMPE
ILHHLTTDRN TQIHACRHPK AEEYFQWSKL PCGITSRNRI PLHIISIKPS TMWFGERSRK
TNVIVRTGES SYRACFSFHS SYSEIKDFLS YLCPVNAYPN VIPVGTTMDK VVEILKPLCR
SSQSTEPKYK PLGKLKRART VHRDSEEEDD YLFDDPLPIP LRHKVPYPET FHPEVFSMTA
VSEKQPEKLR QTPGCCRAEC MQSSRFTNFV DCEESNSESE EEVGIPASLQ GDLGSVLHLQ
KADGDVPQWE VFFKRNDEIT DESLENFPSS TVAGGSQSPK LFSDSDGEST HISSQNSSQS
THITEQGSQG WDSQSDTVLL SSQERNSGDI TSLDKADYRP TIKENIPASL MEQNVICPKD
TYSDLKSRDK DVTIVPSTGE PTTLSSETHI PEEKSLLNLS TNADSQSSSD FEVPSTPEAE
LPKREHLQYL YEKLATGESI AVKKRKCSLL DT


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