NSE3_MOUSE
ID NSE3_MOUSE Reviewed; 279 AA.
AC Q9CPR8; Q569V7; Q9D378;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Non-structural maintenance of chromosomes element 3 homolog;
DE Short=Non-SMC element 3 homolog;
DE AltName: Full=MAGE-G1 antigen;
DE AltName: Full=Necdin-like protein 2;
GN Name=Nsmce3; Synonyms=Mageg1, Ndnl2;
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 [MRNA].
RA Auquier P.H., Chomez P.M., De Backer O.R., Bertrand M.J.M.;
RT "Ten new murine members of the MAGE gene family.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Embryo, Embryonic stem cell, Head, Medulla oblongata, and
RC Spinal cord;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
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).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11782285; DOI=10.1186/1471-2156-2-22;
RA Chibuk T.K., Bischof J.M., Wevrick R.;
RT "A necdin/MAGE-like gene in the chromosome 15 autism susceptibility region:
RT expression, imprinting, and mapping of the human and mouse orthologues.";
RL BMC Genet. 2:22-22(2001).
RN [5]
RP POSSIBLE FUNCTION, INTERACTION WITH E2F1 AND NGFR, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=14593116; DOI=10.1074/jbc.m308454200;
RA Kuwako K., Taniura H., Yoshikawa K.;
RT "Necdin-related MAGE proteins differentially interact with the E2F1
RT transcription factor and the p75 neurotrophin receptor.";
RL J. Biol. Chem. 279:1703-1712(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the SMC5-SMC6 complex, a complex involved in
CC repair of DNA double-strand breaks by homologous recombination. The
CC complex may promote sister chromatid homologous recombination by
CC recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The
CC complex is required for telomere maintenance via recombination in ALT
CC (alternative lengthening of telomeres) cell lines and mediates
CC sumoylation of shelterin complex (telosome) components which is
CC proposed to lead to shelterin complex disassembly in ALT-associated PML
CC bodies (APBs). In vitro enhances ubiquitin ligase activity of NSMCE1.
CC Proposed to act through recruitment and/or stabilization of the Ubl-
CC conjugating enzyme (E2) at the E3:substrate complex (By similarity).
CC May be a growth suppressor that facilitates the entry of the cell into
CC cell cycle arrest (PubMed:14593116). {ECO:0000250|UniProtKB:Q96MG7,
CC ECO:0000269|PubMed:14593116}.
CC -!- SUBUNIT: Component of the SMC5-SMC6 complex which consists at least of
CC SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3. NSMCE1, NSMCE4A
CC or EID3 and NSMCE3 probably form a subcomplex that bridges the head
CC domains of the SMC5:SMC6 heterodimer. Interacts with PJA1 (By
CC similarity). Interacts with E2F1 (via C-terminus) (PubMed:14593116).
CC Interacts with NGFR (via C-terminus) (PubMed:14593116). Interacts with
CC NSMCE1. Interacts with NSMCE4. Interacts with SMC6. Interacts with EID3
CC (By similarity). {ECO:0000250|UniProtKB:Q96MG7,
CC ECO:0000269|PubMed:14593116}.
CC -!- INTERACTION:
CC Q9CPR8; Q61501: E2f1; NbExp=5; IntAct=EBI-5529102, EBI-1025536;
CC Q9CPR8; P08138: NGFR; Xeno; NbExp=3; IntAct=EBI-5529102, EBI-1387782;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14593116}. Nucleus
CC {ECO:0000269|PubMed:14593116}. Chromosome, telomere {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11782285,
CC ECO:0000269|PubMed:14593116}.
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DR EMBL; AF319979; AAK01207.1; -; mRNA.
DR EMBL; AK010294; BAB26830.1; -; mRNA.
DR EMBL; AK017727; BAB30899.1; -; mRNA.
DR EMBL; AK018250; BAB31133.1; -; mRNA.
DR EMBL; AK049759; BAC33907.1; -; mRNA.
DR EMBL; AK076471; BAC36358.1; -; mRNA.
DR EMBL; BC034892; AAH34892.1; -; mRNA.
DR EMBL; BC092289; AAH92289.2; -; mRNA.
DR CCDS; CCDS21337.1; -.
DR RefSeq; NP_075728.1; NM_023239.4.
DR AlphaFoldDB; Q9CPR8; -.
DR SMR; Q9CPR8; -.
DR BioGRID; 211620; 2.
DR IntAct; Q9CPR8; 3.
DR STRING; 10090.ENSMUSP00000091889; -.
DR PhosphoSitePlus; Q9CPR8; -.
DR EPD; Q9CPR8; -.
DR MaxQB; Q9CPR8; -.
DR PaxDb; Q9CPR8; -.
DR PRIDE; Q9CPR8; -.
DR ProteomicsDB; 295529; -.
DR DNASU; 66647; -.
DR Ensembl; ENSMUST00000094331; ENSMUSP00000091889; ENSMUSG00000070520.
DR GeneID; 66647; -.
DR KEGG; mmu:66647; -.
DR UCSC; uc009hgm.1; mouse.
DR CTD; 56160; -.
DR MGI; MGI:1913897; Nsmce3.
DR VEuPathDB; HostDB:ENSMUSG00000070520; -.
DR eggNOG; KOG4562; Eukaryota.
DR GeneTree; ENSGT00940000163627; -.
DR HOGENOM; CLU_039582_2_0_1; -.
DR InParanoid; Q9CPR8; -.
DR OMA; YPTKKHL; -.
DR OrthoDB; 1195799at2759; -.
DR PhylomeDB; Q9CPR8; -.
DR TreeFam; TF328505; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR BioGRID-ORCS; 66647; 26 hits in 105 CRISPR screens.
DR PRO; PR:Q9CPR8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CPR8; protein.
DR Bgee; ENSMUSG00000070520; Expressed in lobe of prostate and 249 other tissues.
DR Genevisible; Q9CPR8; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030915; C:Smc5-Smc6 complex; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
DR GO; GO:0071478; P:cellular response to radiation; ISS:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR Gene3D; 1.10.10.1200; -; 1.
DR Gene3D; 1.10.10.1210; -; 1.
DR InterPro; IPR037445; MAGE.
DR InterPro; IPR041898; MAGE_WH1.
DR InterPro; IPR041899; MAGE_WH2.
DR InterPro; IPR002190; MHD_dom.
DR PANTHER; PTHR11736; PTHR11736; 1.
DR Pfam; PF01454; MAGE; 1.
DR SMART; SM01373; MAGE; 1.
DR PROSITE; PS50838; MAGE; 1.
PE 1: Evidence at protein level;
KW Chromosome; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW Growth regulation; Nucleus; Phosphoprotein; Reference proteome; Telomere;
KW Tumor antigen; Ubl conjugation pathway.
FT CHAIN 1..279
FT /note="Non-structural maintenance of chromosomes element 3
FT homolog"
FT /id="PRO_0000156734"
FT DOMAIN 59..259
FT /note="MAGE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00127"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..279
FT /note="Interaction with NSMCE1"
FT /evidence="ECO:0000250"
FT COMPBIAS 32..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MG7"
FT CONFLICT 36
FT /note="G -> A (in Ref. 2; BAB31133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 31460 MW; FE2435919BD63160 CRC64;
MLQKPRGRGR PSTQADPERD WGGAGEEGPS TSRAAGGSSQ GSRASLSAPT VGPRTQKQLE
LKVAELVQFL LIKDQKKIPI KRTDILKHVV GDYRDVYPNL LKLAAERLQY VFGYKLVELE
PKSHSYILIN MLEPVEADAE MRGDQGTPIS GLLMIVLGLI FMKGNTITET EVWDFLRRLG
VYPTKKHLIF GDPKKLITED FVRQRYLEYR RIPHTDPVDY ELQWGPRTNL ETSKMKVLKF
VAKVHNQDPK DWPTQYCEAL ADEESRARPA TASAPATSS
