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MMS22_MOUSE
ID   MMS22_MOUSE             Reviewed;        1238 AA.
AC   B1AUR6; B7ZN61; D3YXA0; Q6R5F9; Q80UT0;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Protein MMS22-like;
DE   AltName: Full=Methyl methanesulfonate-sensitivity protein 22-like;
GN   Name=Mms22l;
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] (ISOFORM 2).
RC   STRAIN=CD-1;
RX   PubMed=14691545; DOI=10.1371/journal.pbio.0000074;
RA   Sharov A.A., Piao Y., Matoba R., Dudekula D.B., Qian Y., VanBuren V.,
RA   Falco G., Martin P.R., Stagg C.A., Bassey U.C., Wang Y., Carter M.G.,
RA   Hamatani T., Aiba K., Akutsu H., Sharova L., Tanaka T.S., Kimber W.L.,
RA   Yoshikawa T., Jaradat S.A., Pantano S., Nagaraja R., Boheler K.R., Taub D.,
RA   Hodes R.J., Longo D.L., Schlessinger D., Keller J., Klotz E., Kelsoe G.,
RA   Umezawa A., Vescovi A.L., Rossant J., Kunath T., Hogan B.L.M., Curci A.,
RA   D'Urso M., Kelso J., Hide W., Ko M.S.H.;
RT   "Transcriptome analysis of mouse stem cells and early embryos.";
RL   PLoS Biol. 1:410-419(2003).
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] OF 216-1238.
RC   STRAIN=129; TISSUE=Brain, and Mammary tumor;
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   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 MMS22L-TONSL complex, a complex that
CC       promotes homologous recombination-mediated repair of double-strand
CC       breaks (DSBs) at stalled or collapsed replication forks. The MMS22L-
CC       TONSL complex is required to maintain genome integrity during DNA
CC       replication. It mediates the assembly of RAD51 filaments on single-
CC       stranded DNA (ssDNA): the MMS22L-TONSL complex is recruited to DSBs
CC       following histone replacement by histone chaperones and eviction of the
CC       replication protein A complex (RPA/RP-A) from DSBs. Following
CC       recruitment to DSBs, the TONSL-MMS22L complex promotes recruitment of
CC       RAD51 filaments and subsequent homologous recombination. Within the
CC       complex, MMS22L acts by binding ssDNA. {ECO:0000250|UniProtKB:Q6ZRQ5}.
CC   -!- SUBUNIT: Component of the MMS22L-TONSL complex, a complex at least
CC       composed of MMS22L and TONSL/NFKBIL2. Interacts with RAD51; interaction
CC       is direct. {ECO:0000250|UniProtKB:Q6ZRQ5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6ZRQ5}.
CC       Chromosome {ECO:0000250|UniProtKB:Q6ZRQ5}. Note=Localizes to DNA damage
CC       sites, accumulates at stressed replication forks. Recruited to stalled
CC       or collapsed replication forks; directly binds replication protein A
CC       complex (RPA/RP-A)-coated single-stranded DNA (ssDNA).
CC       {ECO:0000250|UniProtKB:Q6ZRQ5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=B1AUR6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B1AUR6-2; Sequence=VSP_040445, VSP_040446;
CC   -!- PTM: Degraded by the ubiquitin-proteasome system upon replication
CC       stress. {ECO:0000250|UniProtKB:Q6ZRQ5}.
CC   -!- SIMILARITY: Belongs to the MMS22 family. MMS22L subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI37911.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI45029.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY512923; AAR87794.1; -; mRNA.
DR   EMBL; AL671913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX296536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC051674; AAH51674.1; -; mRNA.
DR   EMBL; BC137910; AAI37911.1; ALT_INIT; mRNA.
DR   EMBL; BC145028; AAI45029.1; ALT_INIT; mRNA.
DR   CCDS; CCDS18006.2; -. [B1AUR6-1]
DR   RefSeq; NP_955761.2; NM_199467.2. [B1AUR6-1]
DR   AlphaFoldDB; B1AUR6; -.
DR   BioGRID; 229314; 4.
DR   STRING; 10090.ENSMUSP00000103857; -.
DR   iPTMnet; B1AUR6; -.
DR   PhosphoSitePlus; B1AUR6; -.
DR   EPD; B1AUR6; -.
DR   MaxQB; B1AUR6; -.
DR   PaxDb; B1AUR6; -.
DR   PeptideAtlas; B1AUR6; -.
DR   PRIDE; B1AUR6; -.
DR   ProteomicsDB; 295570; -. [B1AUR6-1]
DR   ProteomicsDB; 295571; -. [B1AUR6-2]
DR   Antibodypedia; 55212; 12 antibodies from 7 providers.
DR   DNASU; 212377; -.
DR   Ensembl; ENSMUST00000108222; ENSMUSP00000103857; ENSMUSG00000045751. [B1AUR6-1]
DR   GeneID; 212377; -.
DR   KEGG; mmu:212377; -.
DR   UCSC; uc008sdv.2; mouse. [B1AUR6-1]
DR   UCSC; uc008sdy.1; mouse. [B1AUR6-2]
DR   CTD; 253714; -.
DR   MGI; MGI:2684980; Mms22l.
DR   VEuPathDB; HostDB:ENSMUSG00000045751; -.
DR   eggNOG; ENOG502QQCR; Eukaryota.
DR   GeneTree; ENSGT00390000011769; -.
DR   InParanoid; B1AUR6; -.
DR   OMA; GFLPSNC; -.
DR   OrthoDB; 523276at2759; -.
DR   PhylomeDB; B1AUR6; -.
DR   TreeFam; TF353832; -.
DR   BioGRID-ORCS; 212377; 35 hits in 114 CRISPR screens.
DR   ChiTaRS; Mms22l; mouse.
DR   PRO; PR:B1AUR6; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; B1AUR6; protein.
DR   Bgee; ENSMUSG00000045751; Expressed in ventricular zone and 143 other tissues.
DR   ExpressionAtlas; B1AUR6; baseline and differential.
DR   Genevisible; B1AUR6; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0035101; C:FACT complex; ISO:MGI.
DR   GO; GO:0042555; C:MCM complex; ISO:MGI.
DR   GO; GO:0043596; C:nuclear replication fork; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR   InterPro; IPR042320; MMS22-like.
DR   InterPro; IPR029424; MMS22L_C.
DR   InterPro; IPR029425; MMS22L_N.
DR   PANTHER; PTHR28547; PTHR28547; 1.
DR   Pfam; PF14911; MMS22L_C; 1.
DR   Pfam; PF14910; MMS22L_N; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Chromosome; DNA damage;
KW   DNA repair; DNA-binding; Nucleus; Reference proteome.
FT   CHAIN           1..1238
FT                   /note="Protein MMS22-like"
FT                   /id="PRO_0000403772"
FT   VAR_SEQ         1..276
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14691545"
FT                   /id="VSP_040445"
FT   VAR_SEQ         793
FT                   /note="N -> NS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14691545"
FT                   /id="VSP_040446"
SQ   SEQUENCE   1238 AA;  140582 MW;  9C2733D598CF2F2D CRC64;
     MDGCSAASTF LTDSLELELG TEWCKPPCFS CAFDNREGKF SGESYLASGA LKRLILNLDP
     LPTNFEEDTV ELFGFQWVTE TALVYSCREL FHLFRQQIFN LESLVQVSCD FGKIATLHAK
     ADSIRQQCVV FLHYIKVFIF RCLKVQEAES HSRPAHPYEA LEAQLPSMLV DELRGLLLYI
     GHLAALPSVT VGAFVNQNQM KLFPPSWHLL HLYLDTHWLV LEILHILGEK LKQVVYGRQF
     IGQAGDNLTN VSLFEEHCEH LFCDLICLSL NRFDKVMPSE ALLISHCPCS CVKELWVLLI
     HLLDHRRKWS VADSFWNWLN KLLRTLFEKS SDQRRSSVSL TQAKDPLGFS WWISVHVASL
     YQIDRHGVSD KMKQMESNWS FIEELLKRSV TVQDSILEEQ LRMHLHCCLT LCDFWEPNIS
     VVTILWEYYS KNLNSSFSIS WLPLKGLTNI IKSPLSMLTL VRNCCSDKQD PDLYKSSSSY
     IIFLCILAKV VKKAMRTSGP HPWKQVKGRI YSKFHQKRME ELTEVGLQNF FSLFLLLAAV
     AEIEDVASHV LDLLRFLRPA SMSSHGALVW KGQMAFLLMY AQKNLDIGVW AEKLSCEFQE
     KAKEFLVSKN DEMVQRHALW TLLCIYIDGV QEVFETSSCL YPSHEHLLND GFSMLLPACR
     ESELRTVLNF LQAVLARIRS VHQQLCQELQ RENVDLTVQS SLSAKERPLA AVAGALWRHF
     FSFLKSQRMT QVVPLSQLAD AAADFTLLAV DMPNTAPPDL QPQPVISIIQ LFGWDDIIWP
     QVVARYLSHL LQNSTVYEAL SQSSCVSSQS LTIRSWVRCV LQMHIKHLSD PDLLIDVNPE
     QAVEKEYMEQ LAEMTRLLFT LSEVKSVFSK AQIEQLPSPD DPKQALIQFL EAVGVTYRTL
     QTFSDKSAMV TKSLEYLGEV LKYIKPYLGK KVSSAGLQLT YGIMGILVKS WAHIFATSKA
     QKLLFRIIDC LLLPHTVLQQ DKELPGPMLT AIQKTLPLYL QGICIVCCQS QNPNAYLNQL
     LRNVIEQYIG RFLPTSPCVS DLGQHPVLLA LRNPASVPSM TPLRKHTVHA IRKSYLEFKG
     SSPPPRLASV LAFVLQLFKD TEMGACDLEL LLPGILKCLV LVNEPQVKKL ATENLQCMVQ
     TCQVGSEGGP ATQLTSLFRQ FIQDYGMQYS YQVYSILETV ATLNQHVVIQ LIPTLTQSLK
     DSELKWGLGR NIAQREAYSR LLSGLGQVGQ GEKQRLEK
 
 
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