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Q96SD1 (DCR1C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DCLRE1C
Synonyms:ARTEMIS, ASCID, SCIDA, SNM1C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length692 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.2 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18

Subunit structure

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. Ref.8 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18

Subcellular location

Nucleus Ref.2 Ref.10.

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. Ref.1

Post-translational modification

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. Ref.8 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.20 Ref.21 Ref.22 Ref.23

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2

Omenn syndrome (OS) [MIM:603554]: Severe immunodeficiency characterized by the presence of activated, anergic, oligoclonal T-cells, hypereosinophilia, and high IgE levels.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the DNA repair metallo-beta-lactamase (DRMBL) family.

Sequence caution

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.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96SD1-1)

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.
Isoform 2 (identifier: Q96SD1-2)

Also known as: SCIDA;

The sequence of this isoform differs from the canonical sequence as follows:
     1-120: Missing.
Isoform 3 (identifier: Q96SD1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-115: Missing.
     116-121: CPGSVM → MKHQER
Isoform 4 (identifier: Q96SD1-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 692692Protein artemis
PRO_0000209122

Amino acid modifications

Modified residue6451Phosphoserine; by ATM Ref.11 Ref.16

Natural variations

Alternative sequence1 – 120120Missing in isoform 2.
VSP_014888
Alternative sequence1 – 115115Missing in isoform 3.
VSP_014889
Alternative sequence116 – 1216CPGSVM → MKHQER in isoform 3.
VSP_014890
Alternative sequence386 – 43449EEEDD…RQTPG → GSHSVTQARMRWCHHDSLYP LTPGIKRSSCLSLLTSWITG AYRHAQLMI in isoform 4.
VSP_014891
Alternative sequence435 – 692258Missing in isoform 4.
VSP_014892
Natural variant351H → D in Omenn syndrome. Ref.24
VAR_023077
Natural variant1181G → V in RS-SCID. Ref.20
VAR_023078
Natural variant1351G → E in RS-SCID. Ref.20
VAR_023079
Natural variant1401A → V. Ref.4
Corresponds to variant rs41297016 [ dbSNP | Ensembl ].
VAR_060689
Natural variant1531G → R. Ref.4
Corresponds to variant rs41297018 [ dbSNP | Ensembl ].
VAR_060690
Natural variant1711P → R. Ref.3 Ref.4
Corresponds to variant rs35441642 [ dbSNP | Ensembl ].
VAR_048892
Natural variant2431H → R. Ref.4 Ref.7
Corresponds to variant rs12768894 [ dbSNP | Ensembl ].
VAR_048893
Natural variant3201S → C. Ref.4
Corresponds to variant rs41298896 [ dbSNP | Ensembl ].
VAR_048894
Natural variant3291L → M. Ref.4
Corresponds to variant rs41299658 [ dbSNP | Ensembl ].
VAR_060691

Experimental info

Mutagenesis171D → N or A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12
Mutagenesis331H → A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12
Mutagenesis351H → A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12
Mutagenesis371D → N or A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12 Ref.14
Mutagenesis381H → A: Reduces PRKDC-dependent endonuclease activity, although V(D)J recombination is largely normal. Ref.10 Ref.12
Mutagenesis1151H → A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12
Mutagenesis1361D → N or A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12
Mutagenesis1651D → N or A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.8 Ref.10 Ref.12
Mutagenesis3191H → A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12
Mutagenesis5161S → A: Reduced IR induced phosphorylation; when associated with A-534; A-538; A-548; A-553; A-561 and A-562. Ref.11
Mutagenesis5341S → A: Reduced IR induced phosphorylation; when associated with A-516; A-538; A-548; A-553; A-561 and A-562. Ref.11
Mutagenesis5381S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-548; A-553; A-561 and A-562. Ref.11
Mutagenesis5481S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-553; A-561 and A-562. Ref.11
Mutagenesis5531S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-561 and A-562. Ref.11
Mutagenesis5611S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-553 and A-562. Ref.11
Mutagenesis5621S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-553 and A-561. Ref.11
Sequence conflict5601L → V in CAC37570. Ref.1
Sequence conflict5601L → V in AAM53255. Ref.2
Sequence conflict5601L → V in AAM53256. Ref.2
Sequence conflict5601L → V in AAM53257. Ref.2
Sequence conflict5601L → V in AAM53258. Ref.2
Sequence conflict5601L → V in AAM53259. Ref.2
Sequence conflict5601L → V in AAM53260. Ref.2

Secondary structure

... 692
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 19, 2005. Version 2.
Checksum: 24B857F5B473637B

FASTA69278,436
        10         20         30         40         50         60 
MSSFEGQMAE YPTISIDRFD RENLRARAYF LSHCHKDHMK GLRAPTLKRR LECSLKVYLY 

        70         80         90        100        110        120 
CSPVTKELLL TSPKYRFWKK RIISIEIETP TQISLVDEAS GEKEEIVVTL LPAGHCPGSV 

       130        140        150        160        170        180 
MFLFQGNNGT VLYTGDFRLA QGEAARMELL HSGGRVKDIQ SVYLDTTFCD PRFYQIPSRE 

       190        200        210        220        230        240 
ECLSGVLELV RSWITRSPYH VVWLNCKAAY GYEYLFTNLS EELGVQVHVN KLDMFRNMPE 

       250        260        270        280        290        300 
ILHHLTTDRN TQIHACRHPK AEEYFQWSKL PCGITSRNRI PLHIISIKPS TMWFGERSRK 

       310        320        330        340        350        360 
TNVIVRTGES SYRACFSFHS SYSEIKDFLS YLCPVNAYPN VIPVGTTMDK VVEILKPLCR 

       370        380        390        400        410        420 
SSQSTEPKYK PLGKLKRART VHRDSEEEDD YLFDDPLPIP LRHKVPYPET FHPEVFSMTA 

       430        440        450        460        470        480 
VSEKQPEKLR QTPGCCRAEC MQSSRFTNFV DCEESNSESE EEVGIPASLQ GDLGSVLHLQ 

       490        500        510        520        530        540 
KADGDVPQWE VFFKRNDEIT DESLENFPSS TVAGGSQSPK LFSDSDGEST HISSQNSSQS 

       550        560        570        580        590        600 
THITEQGSQG WDSQSDTVLL SSQERNSGDI TSLDKADYRP TIKENIPASL MEQNVICPKD 

       610        620        630        640        650        660 
TYSDLKSRDK DVTIVPSTGE PTTLSSETHI PEEKSLLNLS TNADSQSSSD FEVPSTPEAE 

       670        680        690 
LPKREHLQYL YEKLATGESI AVKKRKCSLL DT 

« Hide

Isoform 2 (SCIDA) [UniParc].

Checksum: 4FDCC319F5C79FBB
Show »

FASTA57264,652
Isoform 3 [UniParc].

Checksum: 9E1705D68AD06BDE
Show »

FASTA57765,331
Isoform 4 [UniParc].

Checksum: 3C651C16302A8AFA
Show »

FASTA43449,944

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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. expand/collapse author list , 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
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]"Phosphorylation of Artemis following irradiation-induced DNA damage."
Poinsignon C., de Chasseval R., Soubeyrand S., Moshous D., Fischer A., Hache R.J.G., de Villartay J.-P.
Eur. J. Immunol. 34:3146-3155(2004) [PubMed] [Europe PMC] [Abstract]
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]"Omenn syndrome due to ARTEMIS mutations."
Ege M., Ma Y., Manfras B., Kalwak K., Lu H., Lieber M.R., Schwarz K., Pannicke U.
Blood 105:4179-4186(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OMENN SYNDROME ASP-35.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001029027.1. NM_001033855.2.
NP_001029029.1. NM_001033857.2.
NP_001029030.1. NM_001033858.2.
NP_071932.2. NM_022487.3.
XP_005252615.1. XM_005252558.1.
UniGeneHs.655932.
Hs.656065.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3W1BX-ray2.40B485-495[»]
3W1GX-ray2.55B485-495[»]
4HTPX-ray2.25C/E485-495[»]
ProteinModelPortalQ96SD1.
SMRQ96SD1. Positions 3-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122170. 12 interactions.

PTM databases

PhosphoSiteQ96SD1.

Polymorphism databases

DMDM71153325.

Proteomic databases

PaxDbQ96SD1.
PRIDEQ96SD1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357717; 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]
ENST00000453695; ENSP00000400529; ENSG00000152457. [Q96SD1-2]
GeneID64421.
KEGGhsa:64421.
UCSCuc001inl.3. human. [Q96SD1-1]
uc001ino.3. human. [Q96SD1-3]
uc010qbx.2. human. [Q96SD1-4]

Organism-specific databases

CTD64421.
GeneCardsGC10M014939.
HGNCHGNC:17642. DCLRE1C.
MIM602450. phenotype.
603554. phenotype.
605988. gene.
neXtProtNX_Q96SD1.
Orphanet39041. Omenn syndrome.
275. Severe combined immunodeficiency due to DCLRE1C deficiency.
PharmGKBPA27176.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1236.
HOVERGENHBG081421.
InParanoidQ96SD1.
KOK10887.
OMAMFRNMPD.
OrthoDBEOG70CR8F.
PhylomeDBQ96SD1.
TreeFamTF329572.

Gene expression databases

ArrayExpressQ96SD1.
BgeeQ96SD1.
GenevestigatorQ96SD1.

Family and domain databases

Gene3D3.60.15.10. 1 hit.
InterProIPR001279. Beta-lactamas-like.
IPR011084. DRMBL.
[Graphical view]
PfamPF07522. DRMBL. 1 hit.
[Graphical view]
SMARTSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMSSF56281. SSF56281. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi64421.
NextBio66403.
PROQ96SD1.
SOURCESearch...

Entry information

Entry nameDCR1C_HUMAN
AccessionPrimary (citable) accession number: Q96SD1
Secondary accession number(s): D3DRT6 expand/collapse secondary AC list , Q1HCL2, Q5JSR4, Q5JSR5, Q5JSR7, Q5JSR8, Q5JSR9, Q5JSS0, Q5JSS7, Q6PK14, Q8N101, Q8N132, Q8TBW9, Q9BVW9, Q9HAM4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM