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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	Defects in DCLRE1C are a cause of severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-negative/NK-cell-positive with sensitivity to ionizing radiation (RSSCID) [MIM:602450]. SCID refers to 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 with SCID 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. Ref.1 Ref.19 Ref.20 Ref.21 Ref.22 Defects in DCLRE1C are the cause of severe combined immunodeficiency Athabaskan type (SCIDA) [MIM:602450]. SCIDA is a variety of RS-SCID caused by a founder mutation in Athabascan-speaking native Americans, being inherited as an autosomal recessive trait with an estimated gene frequency of 2.1% in the Navajo population. Affected individuals exhibit clinical symptoms and defects in DNA repair comparable to those seen in RS-SCID. Ref.2 Defects in DCLRE1C are a cause of Omenn syndrome (OS) [MIM:603554]. OS is characterized by severe combined immunodeficiency associated with erythrodermia, hepatosplenomegaly, lymphadenopathy and alopecia. Affected individuals have elevated T-lymphocyte counts with a restricted T-cell receptor (TCR) repertoire. They also generally lack B-lymphocytes, but have normal natural killer (NK) cell function (T+ B- NK+).
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	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW
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.23		VAR_023077
	Natural variant	118	1	G → V in RS-SCID. Ref.19		VAR_023078
	Natural variant	135	1	G → E in RS-SCID. Ref.19		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

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: 11336668] [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: 12055248] [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: 14702039] [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: 15164054] [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: 15489334] [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: 11955432] [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: 12177301] [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: 15071507] [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: 15468306] [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: 14744996] [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: 15574326] [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: 15574327] [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: 15456891] [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: 15723659] [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: 15811628] [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: 15936993] [Abstract] Cited for: FUNCTION, INTERACTION WITH PRKDC.
[19]	"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: 12406895] [Abstract] Cited for: VARIANTS RSSCID VAL-118 AND GLU-135.
[20]	"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: 12921762] [Abstract] Cited for: INVOLVEMENT IN RSSCID.
[21]	"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: 12592555] [Abstract] Cited for: INVOLVEMENT IN RSSCID.
[22]	"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: 12569164] [Abstract] Cited for: INVOLVEMENT IN RSSCID.
[23]	"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: 15731174] [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
ProteinModelPortal	Q96SD1.
SMR	Q96SD1. Positions 24-138.
ModBase	Search...
Protein-protein interaction databases
STRING	Q96SD1.
PTM databases
PhosphoSite	Q96SD1.
Polymorphism databases
DMDM	71153325.
Proteomic databases
PRIDE	Q96SD1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000378278; ENSP00000367527; ENSG00000152457.
GeneID	64421.
KEGG	hsa:64421.
UCSC	uc001inl.1. human. uc001inn.1. human. uc001ino.1. 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, alymphocytotic type.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00530000063183.
HOVERGEN	HBG081421.
InParanoid	Q96SD1.
PhylomeDB	Q96SD1.
Gene expression databases
ArrayExpress	Q96SD1.
Bgee	Q96SD1.
Genevestigator	Q96SD1.
GermOnline	ENSG00000152457. Homo sapiens.
Family and domain databases
InterPro	IPR001279. Beta-lactamas-like. IPR011084. DRMBL. [Graphical view]
KO	K10887.
Pfam	PF07522. DRMBL. 1 hit. [Graphical view]
SMART	SM00849. Lactamase_B. 1 hit. [Graphical view]
ProtoNet	Search...
Other
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:	January 25, 2012
This is version 79 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.