ID NSE1_MOUSE Reviewed; 266 AA.
AC Q9D720; Q3TLN4; Q8K2B4; Q9CY20;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 08-NOV-2023, entry version 146.
DE RecName: Full=Non-structural maintenance of chromosomes element 1 homolog;
DE Short=Non-SMC element 1 homolog;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8WV22};
GN Name=Nsmce1;
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, Mammary gland, and Tongue;
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 MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor, and Testis;
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 [3]
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: RING-type zinc finger-containing E3 ubiquitin ligase that
CC assembles with melanoma antigen protein (MAGE) to catalyze the direct
CC transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a
CC specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE
CC stimulates and specifies ubiquitin ligase activity likely through
CC recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme
CC at the E3:substrate complex. Involved in maintenance of genome
CC integrity, DNA damage response and DNA repair. NSMCE3/MAGEG1 and NSMCE1
CC ubiquitin ligase are components of SMC5-SMC6 complex and may positively
CC regulate homologous recombination-mediated DNA repair.
CC {ECO:0000250|UniProtKB:Q8WV22}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q8WV22};
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 NSMCE3.
CC {ECO:0000250|UniProtKB:Q8WV22}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WV22}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:Q8WV22}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q8WV22}.
CC -!- SIMILARITY: Belongs to the NSE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31848.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH49558.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB27329.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE38758.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK009715; BAB26459.1; -; mRNA.
DR EMBL; AK011011; BAB27329.1; ALT_INIT; mRNA.
DR EMBL; AK160217; BAE35695.1; -; mRNA.
DR EMBL; AK166410; BAE38758.1; ALT_INIT; mRNA.
DR EMBL; BC031848; AAH31848.1; ALT_INIT; mRNA.
DR EMBL; BC049558; AAH49558.1; ALT_INIT; mRNA.
DR RefSeq; NP_080606.2; NM_026330.3.
DR RefSeq; XP_006508198.1; XM_006508135.3.
DR RefSeq; XP_006508199.1; XM_006508136.2.
DR RefSeq; XP_017167758.1; XM_017312269.1.
DR AlphaFoldDB; Q9D720; -.
DR SMR; Q9D720; -.
DR BioGRID; 212386; 6.
DR STRING; 10090.ENSMUSP00000033006; -.
DR PhosphoSitePlus; Q9D720; -.
DR EPD; Q9D720; -.
DR MaxQB; Q9D720; -.
DR PaxDb; 10090-ENSMUSP00000033006; -.
DR PeptideAtlas; Q9D720; -.
DR ProteomicsDB; 293905; -.
DR Pumba; Q9D720; -.
DR DNASU; 67711; -.
DR GeneID; 67711; -.
DR KEGG; mmu:67711; -.
DR UCSC; uc009jqa.2; mouse.
DR AGR; MGI:1914961; -.
DR CTD; 197370; -.
DR MGI; MGI:1914961; Nsmce1.
DR eggNOG; KOG4718; Eukaryota.
DR InParanoid; Q9D720; -.
DR OrthoDB; 4844at2759; -.
DR PhylomeDB; Q9D720; -.
DR TreeFam; TF314721; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR BioGRID-ORCS; 67711; 23 hits in 114 CRISPR screens.
DR ChiTaRS; Nsmce1; mouse.
DR PRO; PR:Q9D720; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D720; Protein.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR CDD; cd16493; RING-CH-C4HC3_NSE1; 1.
DR Gene3D; 3.90.1150.220; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011513; Nse1.
DR InterPro; IPR014857; Nse1_RING_C4HC3-type.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR20973; NON-SMC ELEMENT 1-RELATED; 1.
DR PANTHER; PTHR20973:SF0; NON-STRUCTURAL MAINTENANCE OF CHROMOSOMES ELEMENT 1 HOMOLOG; 1.
DR Pfam; PF07574; SMC_Nse1; 1.
DR Pfam; PF08746; zf-RING-like; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA recombination; DNA repair; Metal-binding;
KW Nucleus; Reference proteome; Telomere; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..266
FT /note="Non-structural maintenance of chromosomes element 1
FT homolog"
FT /id="PRO_0000270945"
FT ZN_FING 191..232
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..102
FT /note="Interaction with NSMCE3"
FT /evidence="ECO:0000250|UniProtKB:Q8WV22"
FT REGION 246..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 187
FT /note="S -> F (in Ref. 1; BAB27329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 266 AA; 30708 MW; F5728C530532E03A CRC64;
MQGSTRRAGA MTDVHRRFLQ LLMTHGVLEE WEVRRLQNHC YQVHDRNATV DKLEDFINNI
NSVLESLYIE IKKGVTEDDG RPIYALVNLA TTSVSKMATD FAENELDLFR KALELIVDSE
TGFASSTNIL NLVDQLKGKK MRKKEAEQVL QKFVQSKWLI EKEGEFTLHG RAILEMEQFI
RESYPDSVKM CNICHGLLIQ GQSCETCGIR MHLPCVAKYF QSIPEPHCPH CNDYWPHDIP
EVYNPEKERE AGISKSSRKS LRTRQH
//
