SHLD2_MOUSE
ID SHLD2_MOUSE Reviewed; 891 AA.
AC Q3UEN2; E9Q8K3;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Shieldin complex subunit 2 {ECO:0000305};
DE AltName: Full=Protein FAM35A {ECO:0000305};
DE AltName: Full=RINN1-REV7-interacting novel NHEJ regulator 2;
GN Name=Shld2 {ECO:0000312|MGI:MGI:1922948};
GN Synonyms=Fam35a {ECO:0000312|MGI:MGI:1922948},
GN Rinn2 {ECO:0000250|UniProtKB:Q86V20};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Component of the shieldin complex, which plays an important
CC role in repair of DNA double-stranded breaks (DSBs). During G1 and S
CC phase of the cell cycle, the complex functions downstream of TP53BP1 to
CC promote non-homologous end joining (NHEJ) and suppress DNA end
CC resection. Mediates various NHEJ-dependent processes including
CC immunoglobulin class-switch recombination, and fusion of unprotected
CC telomeres. {ECO:0000250|UniProtKB:Q86V20}.
CC -!- SUBUNIT: Component of the shieldin complex, consisting of SHLD1, SHLD2,
CC SHLD3 and MAD2L2/REV7. Within the complex, SHLD2 forms a scaffold which
CC interacts with a SHLD3-MAD2L2 subcomplex via its N-terminus, and with
CC SHLD1 via its C-terminus. Interacts with TP53BP1. Interacts with RIF1.
CC {ECO:0000250|UniProtKB:Q86V20}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q86V20}.
CC -!- SIMILARITY: Belongs to the SHLD2 family. {ECO:0000305}.
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DR EMBL; AK149442; BAE28879.1; -; mRNA.
DR EMBL; AC154738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC160930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS36874.1; -.
DR RefSeq; NP_083665.2; NM_029389.2.
DR RefSeq; XP_006519708.1; XM_006519645.3.
DR RefSeq; XP_006519709.1; XM_006519646.3.
DR RefSeq; XP_006519710.1; XM_006519647.3.
DR RefSeq; XP_006519711.1; XM_006519648.3.
DR RefSeq; XP_011243518.1; XM_011245216.2.
DR AlphaFoldDB; Q3UEN2; -.
DR ComplexPortal; CPX-3483; Shieldin complex.
DR STRING; 10090.ENSMUSP00000107548; -.
DR iPTMnet; Q3UEN2; -.
DR PhosphoSitePlus; Q3UEN2; -.
DR PaxDb; Q3UEN2; -.
DR PRIDE; Q3UEN2; -.
DR ProteomicsDB; 271541; -.
DR Antibodypedia; 45608; 77 antibodies from 18 providers.
DR DNASU; 75698; -.
DR Ensembl; ENSMUST00000111917; ENSMUSP00000107548; ENSMUSG00000041471.
DR GeneID; 75698; -.
DR KEGG; mmu:75698; -.
DR UCSC; uc007tap.1; mouse.
DR CTD; 54537; -.
DR MGI; MGI:1922948; Shld2.
DR VEuPathDB; HostDB:ENSMUSG00000041471; -.
DR eggNOG; ENOG502QW94; Eukaryota.
DR GeneTree; ENSGT00390000003133; -.
DR HOGENOM; CLU_016120_0_0_1; -.
DR InParanoid; Q3UEN2; -.
DR OMA; KKDHIWD; -.
DR OrthoDB; 412702at2759; -.
DR PhylomeDB; Q3UEN2; -.
DR TreeFam; TF332107; -.
DR BioGRID-ORCS; 75698; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Shld2; mouse.
DR PRO; PR:Q3UEN2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q3UEN2; protein.
DR Bgee; ENSMUSG00000041471; Expressed in animal zygote and 151 other tissues.
DR ExpressionAtlas; Q3UEN2; baseline and differential.
DR Genevisible; Q3UEN2; MM.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; ISO:MGI.
DR GO; GO:0045830; P:positive regulation of isotype switching; ISO:MGI.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0002208; P:somatic diversification of immunoglobulins involved in immune response; IC:ComplexPortal.
DR GO; GO:0043247; P:telomere maintenance in response to DNA damage; IC:ComplexPortal.
DR InterPro; IPR029715; FAM35A.
DR InterPro; IPR031589; FAM35A_C.
DR PANTHER; PTHR14495; PTHR14495; 1.
DR Pfam; PF15793; FAM35_C; 1.
PE 2: Evidence at transcript level;
KW Chromosome; DNA damage; DNA repair; Reference proteome.
FT CHAIN 1..891
FT /note="Shieldin complex subunit 2"
FT /id="PRO_0000087162"
FT REGION 1..61
FT /note="Sufficient for interaction with SHLD3 and MAD2L2"
FT /evidence="ECO:0000250|UniProtKB:Q86V20"
FT REGION 184..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..866
FT /note="Mediates interaction with SHLD1"
FT /evidence="ECO:0000250|UniProtKB:Q86V20"
FT COMPBIAS 333..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 891
FT /note="E -> GVMKQSVF (in Ref. 1; BAE28879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 891 AA; 99090 MW; 6C0E4DE9FE788087 CRC64;
MSQGSQVHIF LGAPVAPLKT TVSQGTASLM STANAWEKVR LFYKQHSLYL KAGDQEFKNL
EDCQVPKGLG PPGLLSGDVL TTSVRRSAQV DEDFKHSASE AQSVKSQVNL SDMTSGQMCG
LGDGVQHLPE EEKDQKLQCK NKKITDEQSK NQSDPCVRNF QRDLFALDLK CAAKLDLGCC
TEQMSTGTKP EPTGHRERQS QESFSDTRCE PQSEGAVRKA SDQRLSAEAE FLSVLTSSQR
AFLAQGNDKG QDCINKSTVN MEAEPTGSQG VRRTEGDFSK PGGDFEEESE NEQSQVYSLE
LFSPVCPESE SSHSHINPGK NLENTSSQEL FSNEENLPPN ELCSSHPSTA NRSWSCKDDS
HHSKALSEVH QVSKKPRMDS NIREAAKAVP QRVMSELKDS KKISLIKNCD SKNQKYNCLV
MVLTPCHVKE ITIKSGPNSG SKVPLATIVV IDQSEIKKRV VLWRTAAFGA LTVFLGDIIL
LTDVVLYEDQ WIGETVLQST FTSQLLNLGS YSYVQPEKYS NVIANVILQD LLTYVSTKHS
YLKDLPQRQP QKMNTVEFVE LEQLQPDILV HAVLRVVDVT VLTEALYSYR GQKQRKVVLT
VEQAQGQHYV LVLWGPGAAW YTQLQRKKDS IWEFKYLFVQ RNSILENLEL HTTLWSSCEC
LFDDDTRAIS FKTKFQKNTS SFVKISDLAT HLEDKYSGVV LIKAKVSELV FSAAAAQKIA
LNARSTLQSI FSSLPSIVYA GCAHCGSELE TDENRIYRQC LSCLPFVGKK IFYRPALMTI
VDGRYNTCVH VGSKMMEQIL LNISPDCLNR VIVPSSEVTY GMVASDLLHS LLAVSAEPCV
LKIQSLFELD ENSYPLQQDF SLLDFCPDSR KLWSPGLSLR AEGTGGIPGK E
