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SHLD1_MOUSE
ID   SHLD1_MOUSE             Reviewed;         206 AA.
AC   Q9D112; A2AW53;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Shieldin complex subunit 1 {ECO:0000250|UniProtKB:Q8IYI0};
DE   AltName: Full=RINN1-REV7-interacting novel NHEJ regulator 3 {ECO:0000250|UniProtKB:Q8IYI0};
GN   Name=Shld1 {ECO:0000250|UniProtKB:Q8IYI0};
GN   Synonyms=RINN3 {ECO:0000250|UniProtKB:Q8IYI0};
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;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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:Q8IYI0}.
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. {ECO:0000250|UniProtKB:Q8IYI0}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q8IYI0}.
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DR   EMBL; AK004090; BAB23163.1; -; mRNA.
DR   EMBL; AL935270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC100475; AAI00476.1; -; mRNA.
DR   CCDS; CCDS50727.1; -.
DR   RefSeq; NP_082913.1; NM_028637.1.
DR   RefSeq; XP_011238102.1; XM_011239800.1.
DR   RefSeq; XP_011238103.1; XM_011239801.2.
DR   RefSeq; XP_011238104.1; XM_011239802.2.
DR   RefSeq; XP_011238105.1; XM_011239803.1.
DR   AlphaFoldDB; Q9D112; -.
DR   SMR; Q9D112; -.
DR   ComplexPortal; CPX-3483; Shieldin complex.
DR   STRING; 10090.ENSMUSP00000105759; -.
DR   PhosphoSitePlus; Q9D112; -.
DR   PaxDb; Q9D112; -.
DR   PRIDE; Q9D112; -.
DR   Antibodypedia; 49253; 69 antibodies from 11 providers.
DR   DNASU; 73747; -.
DR   Ensembl; ENSMUST00000061891; ENSMUSP00000057009; ENSMUSG00000044991.
DR   Ensembl; ENSMUST00000110132; ENSMUSP00000105759; ENSMUSG00000044991.
DR   GeneID; 73747; -.
DR   KEGG; mmu:73747; -.
DR   UCSC; uc008mne.2; mouse.
DR   CTD; 149840; -.
DR   MGI; MGI:1920997; Shld1.
DR   VEuPathDB; HostDB:ENSMUSG00000044991; -.
DR   eggNOG; ENOG502SUXK; Eukaryota.
DR   GeneTree; ENSGT00390000014969; -.
DR   HOGENOM; CLU_090358_0_0_1; -.
DR   InParanoid; Q9D112; -.
DR   OMA; VLRSFQM; -.
DR   OrthoDB; 1336753at2759; -.
DR   PhylomeDB; Q9D112; -.
DR   TreeFam; TF336046; -.
DR   BioGRID-ORCS; 73747; 0 hits in 71 CRISPR screens.
DR   PRO; PR:Q9D112; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9D112; protein.
DR   Bgee; ENSMUSG00000044991; Expressed in interventricular septum and 218 other tissues.
DR   ExpressionAtlas; Q9D112; baseline and differential.
DR   Genevisible; Q9D112; MM.
DR   GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR   GO; GO:0005694; C:chromosome; 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: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; IPR027821; SHLD1.
DR   PANTHER; PTHR36863; PTHR36863; 1.
DR   Pfam; PF15021; DUF4521; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA damage; DNA repair; Reference proteome.
FT   CHAIN           1..206
FT                   /note="Shieldin complex subunit 1"
FT                   /id="PRO_0000286613"
FT   REGION          27..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   206 AA;  22697 MW;  F855D4B8A0ABB66E CRC64;
     MESQAATPSS LSGESCTLDL PAVCDTSSYE ASQRVSQGSS NSLSSLESHP FLSSSTTDPD
     SNSLNTEQKG SWDSENFWLD PSSKGQLETN EEEDGLRKSL DRFYEAFAHP LPGSGDPLSA
     SVCQCLSQTI SELEGQESQR YALRSFQMAQ VIFSRDGCSI LQRHSRDTRF YPLEQEGSSV
     DDEEPTPGLS REVIRFLLEQ TVMKDS
 
 
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