Q96SD1 (DCR1C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DCLRE1C
Synonyms:	ARTEMIS, ASCID, SCIDA, SNM1C

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	692 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Adaptive immunity DNA damage DNA recombination DNA repair Immunity
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation SCID
Ligand	Magnesium
Molecular function	Endonuclease Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Inferred from electronic annotation. Source: Compara DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW double-strand break repair Inferred from electronic annotation. Source: Compara response to ionizing radiation Inferred from electronic annotation. Source: Compara telomere maintenance Inferred from electronic annotation. Source: Compara
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	5'-3' exonuclease activity Inferred from direct assay Ref.8. Source: MGI single-stranded DNA specific endodeoxyribonuclease activity Inferred from direct assay Ref.8. Source: MGI
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 692

692

Protein artemis

PRO_0000209122

Amino acid modifications

Modified residue

645

1

Phosphoserine; by ATM Ref.11 Ref.16

Natural variations

Alternative sequence

1 – 120

120

Missing in isoform 2.

VSP_014888

Alternative sequence

1 – 115

115

Missing in isoform 3.

VSP_014889

Alternative sequence

116 – 121

6

CPGSVM → MKHQER in isoform 3.

VSP_014890

Alternative sequence

386 – 434

49

EEEDD…RQTPG → GSHSVTQARMRWCHHDSLYP LTPGIKRSSCLSLLTSWITG AYRHAQLMI in isoform 4.

VSP_014891

Alternative sequence

435 – 692

258

Missing in isoform 4.

VSP_014892

Natural variant

35

1

H → D in Omenn syndrome. Ref.24

VAR_023077

Natural variant

118

1

G → V in RS-SCID. Ref.20

VAR_023078

Natural variant

135

1

G → E in RS-SCID. Ref.20

VAR_023079

Natural variant

140

1

A → V. Ref.4

VAR_060689

Natural variant

153

1

G → R. Ref.4

VAR_060690

Natural variant

171

1

P → R. Ref.3 Ref.4
Corresponds to variant rs35441642 [ dbSNP | Ensembl ].

VAR_048892

Natural variant

243

1

H → R. Ref.4 Ref.7
Corresponds to variant rs12768894 [ dbSNP | Ensembl ].

VAR_048893

Natural variant

320

1

S → C. Ref.4
Corresponds to variant rs41298896 [ dbSNP | Ensembl ].

VAR_048894

Natural variant

329

1

L → M. Ref.4

VAR_060691

Experimental info

Mutagenesis

17

1

D → N or A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12

Mutagenesis

33

1

H → A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12

Mutagenesis

35

1

H → A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12

Mutagenesis

37

1

D → N or A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12 Ref.14

Mutagenesis

38

1

H → A: Reduces PRKDC-dependent endonuclease activity, although V(D)J recombination is largely normal. Ref.10 Ref.12

Mutagenesis

115

1

H → A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12

Mutagenesis

136

1

D → N or A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12

Mutagenesis

165

1

D → N or A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.8 Ref.10 Ref.12

Mutagenesis

319

1

H → A: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination. Ref.10 Ref.12

Mutagenesis

516

1

S → A: Reduced IR induced phosphorylation; when associated with A-534; A-538; A-548; A-553; A-561 and A-562. Ref.11

Mutagenesis

534

1

S → A: Reduced IR induced phosphorylation; when associated with A-516; A-538; A-548; A-553; A-561 and A-562. Ref.11

Mutagenesis

538

1

S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-548; A-553; A-561 and A-562. Ref.11

Mutagenesis

548

1

S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-553; A-561 and A-562. Ref.11

Mutagenesis

553

1

S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-561 and A-562. Ref.11

Mutagenesis

561

1

S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-553 and A-562. Ref.11

Mutagenesis

562

1

S → A: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-553 and A-561. Ref.11

Sequence conflict

560

1

L → V in CAC37570. Ref.1

Sequence conflict

560

1

L → V in AAM53255. Ref.2

Sequence conflict

560

1

L → V in AAM53256. Ref.2

Sequence conflict

560

1

L → V in AAM53257. Ref.2

Sequence conflict

560

1

L → V in AAM53258. Ref.2

Sequence conflict

560

1

L → V in AAM53259. Ref.2

Sequence conflict

560

1

L → V in AAM53260. Ref.2

Secondary structure

1

.

.

.

692

Helix Strand Turn

Details...

Helix

489 – 491

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 19, 2005. Version 2. Checksum: 24B857F5B473637B	FASTA	692	78,436
	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
	Isoform 2 (SCIDA) [UniParc]. Checksum: 4FDCC319F5C79FBB	FASTA	572	64,652
	10 20 30 40 50 60 MFLFQGNNGT VLYTGDFRLA QGEAARMELL HSGGRVKDIQ SVYLDTTFCD PRFYQIPSRE 70 80 90 100 110 120 ECLSGVLELV RSWITRSPYH VVWLNCKAAY GYEYLFTNLS EELGVQVHVN KLDMFRNMPE 130 140 150 160 170 180 ILHHLTTDRN TQIHACRHPK AEEYFQWSKL PCGITSRNRI PLHIISIKPS TMWFGERSRK 190 200 210 220 230 240 TNVIVRTGES SYRACFSFHS SYSEIKDFLS YLCPVNAYPN VIPVGTTMDK VVEILKPLCR 250 260 270 280 290 300 SSQSTEPKYK PLGKLKRART VHRDSEEEDD YLFDDPLPIP LRHKVPYPET FHPEVFSMTA 310 320 330 340 350 360 VSEKQPEKLR QTPGCCRAEC MQSSRFTNFV DCEESNSESE EEVGIPASLQ GDLGSVLHLQ 370 380 390 400 410 420 KADGDVPQWE VFFKRNDEIT DESLENFPSS TVAGGSQSPK LFSDSDGEST HISSQNSSQS 430 440 450 460 470 480 THITEQGSQG WDSQSDTVLL SSQERNSGDI TSLDKADYRP TIKENIPASL MEQNVICPKD 490 500 510 520 530 540 TYSDLKSRDK DVTIVPSTGE PTTLSSETHI PEEKSLLNLS TNADSQSSSD FEVPSTPEAE 550 560 570 LPKREHLQYL YEKLATGESI AVKKRKCSLL DT
	Isoform 3 [UniParc]. Checksum: 9E1705D68AD06BDE	FASTA	577	65,331
	10 20 30 40 50 60 MKHQERFLFQ GNNGTVLYTG DFRLAQGEAA RMELLHSGGR VKDIQSVYLD TTFCDPRFYQ 70 80 90 100 110 120 IPSREECLSG VLELVRSWIT RSPYHVVWLN CKAAYGYEYL FTNLSEELGV QVHVNKLDMF 130 140 150 160 170 180 RNMPEILHHL TTDRNTQIHA CRHPKAEEYF QWSKLPCGIT SRNRIPLHII SIKPSTMWFG 190 200 210 220 230 240 ERSRKTNVIV RTGESSYRAC FSFHSSYSEI KDFLSYLCPV NAYPNVIPVG TTMDKVVEIL 250 260 270 280 290 300 KPLCRSSQST EPKYKPLGKL KRARTVHRDS EEEDDYLFDD PLPIPLRHKV PYPETFHPEV 310 320 330 340 350 360 FSMTAVSEKQ PEKLRQTPGC CRAECMQSSR FTNFVDCEES NSESEEEVGI PASLQGDLGS 370 380 390 400 410 420 VLHLQKADGD VPQWEVFFKR NDEITDESLE NFPSSTVAGG SQSPKLFSDS DGESTHISSQ 430 440 450 460 470 480 NSSQSTHITE QGSQGWDSQS DTVLLSSQER NSGDITSLDK ADYRPTIKEN IPASLMEQNV 490 500 510 520 530 540 ICPKDTYSDL KSRDKDVTIV PSTGEPTTLS SETHIPEEKS LLNLSTNADS QSSSDFEVPS 550 560 570 TPEAELPKRE HLQYLYEKLA TGESIAVKKR KCSLLDT
	Isoform 4 [UniParc]. Checksum: 3C651C16302A8AFA	FASTA	434	49,944
	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 VHRDSGSHSV TQARMRWCHH DSLYPLTPGI KRSSCLSLLT 430 SWITGAYRHA QLMI

References

	« Hide 'large scale' referencesShow '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. , 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]	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 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

DCLRE1Cbase

DCLRE1C mutation db

GeneReviews

NIEHS-SNPs

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.

IPI

IPI00290459.
IPI00290918.
IPI00396624.
IPI00607742.

RefSeq

NP_001029027.1. NM_001033855.1.
NP_001029029.1. NM_001033857.1.
NP_001029030.1. NM_001033858.1.
NP_071932.2. NM_022487.2.

UniGene

Hs.656065.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q96SD1.

ModBase

Search...

PTM databases

PhosphoSite

Q96SD1.

Polymorphism databases

DMDM

71153325.

Proteomic databases

PaxDb

Q96SD1.

PRIDE

Q96SD1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000357717; ENSP00000350349; ENSG00000152457.
ENST00000378241; ENSP00000367487; ENSG00000152457.
ENST00000378246; ENSP00000367492; ENSG00000152457.
ENST00000378249; ENSP00000367496; ENSG00000152457.
ENST00000378254; ENSP00000367502; ENSG00000152457.
ENST00000378255; ENSP00000367503; ENSG00000152457.
ENST00000378258; ENSP00000367506; ENSG00000152457.
ENST00000378278; ENSP00000367527; ENSG00000152457.
ENST00000378289; ENSP00000367538; ENSG00000152457.
ENST00000396817; ENSP00000380030; ENSG00000152457.
ENST00000418843; ENSP00000391428; ENSG00000152457.
ENST00000453695; ENSP00000400529; ENSG00000152457.
ENST00000456122; ENSP00000413180; ENSG00000152457.

GeneID

64421.

KEGG

hsa:64421.

UCSC

uc001inl.3. human.
uc001ino.3. human.
uc010qbx.2. human.

Organism-specific databases

CTD

64421.

GeneCards

GC10M014939.

HGNC

HGNC:17642. DCLRE1C.

MIM

602450. phenotype.
603554. phenotype.
605988. gene.

neXtProt

NX_Q96SD1.

Orphanet

39041. Omenn syndrome.
275. Severe combined immunodeficiency due to DCLRE1C deficiency.

PharmGKB

PA27176.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1236.

HOVERGEN

HBG081421.

InParanoid

Q96SD1.

KO

K10887.

OMA

RTRTIHR.

PhylomeDB

Q96SD1.

Gene expression databases

ArrayExpress

Q96SD1.

Bgee

Q96SD1.

Genevestigator

Q96SD1.

GermOnline

ENSG00000152457. Homo sapiens.

Family and domain databases

Gene3D

3.60.15.10. 1 hit.

InterPro

IPR001279. Beta-lactamas-like.
IPR011084. DRMBL.
[Graphical view]

Pfam

PF07522. DRMBL. 1 hit.
[Graphical view]

SMART

SM00849. Lactamase_B. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

64421.

NextBio

66403.

SOURCE

Search...

Entry information

Entry name

DCR1C_HUMAN

Accession

Primary (citable) accession number: Q96SD1
Secondary accession number(s): D3DRT6 , 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:	May 29, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.