MMS19_MOUSE
ID MMS19_MOUSE Reviewed; 1031 AA.
AC Q9D071; F8WHX3; Q925N8; Q9CWX3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=MMS19 nucleotide excision repair protein homolog {ECO:0000305};
DE AltName: Full=MET18 homolog;
DE AltName: Full=MMS19-like protein;
GN Name=Mms19 {ECO:0000312|MGI:MGI:1919449}; Synonyms=Mms19l;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster;
RX PubMed=11328871; DOI=10.1093/nar/29.9.1884;
RA Queimado L., Rao M., Schultz R.A., Koonin E.V., Aravind L., Nardo T.,
RA Stefanini M., Friedberg E.C.;
RT "Cloning the human and mouse MMS19 genes and functional complementation of
RT a yeast mms19 deletion mutant.";
RL Nucleic Acids Res. 29:1884-1891(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, Embryo, Pituitary, and Vagina;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=22678361; DOI=10.1126/science.1219664;
RA Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M., Boulton S.J.;
RT "MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism.";
RL Science 337:243-245(2012).
CC -!- FUNCTION: Key component of the cytosolic iron-sulfur protein assembly
CC (CIA) complex, a multiprotein complex that mediates the incorporation
CC of iron-sulfur cluster into apoproteins specifically involved in DNA
CC metabolism and genomic integrity. In the CIA complex, MMS19 acts as an
CC adapter between early-acting CIA components and a subset of cellular
CC target Fe/S proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby
CC playing a key role in nucleotide excision repair (NER), homologous
CC recombination-mediated double-strand break DNA repair, DNA replication
CC and RNA polymerase II (POL II) transcription. As a CIA complex
CC component and in collaboration with CIAO1 and CIAO2, binds to and
CC facilitates the assembly of most cytosolic-nuclear Fe/S proteins. As
CC part of the mitotic spindle-associated MMXD complex, plays a role in
CC chromosome segregation, probably by facilitating iron-sulfur cluster
CC assembly into ERCC2/XPD. Together with CIAO2, facilitates the transfer
CC of Fe-S clusters to the motor protein KIF4A, which ensures proper
CC localization of KIF4A to mitotic machinery components to promote the
CC progression of mitosis. Indirectly acts as a transcriptional
CC coactivator of estrogen receptor (ER), via its role in iron-sulfur
CC insertion into some component of the TFIIH-machinery.
CC {ECO:0000250|UniProtKB:Q96T76}.
CC -!- SUBUNIT: Component of the CIA complex. In the CIA complex, interacts
CC directly with CIAO2B and CIAO3. Component of the MMXD complex, composed
CC of CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5. Interacts with CIAO2B; the
CC interaction is direct. Interacts with ERCC2/XPD; the interaction is
CC direct. Interacts with ERCC3/XPB and NCOA3/RAC3. Interacts with RTEL1;
CC the interaction mediates the association of RTEL1 with the CIA complex.
CC Interacts with BRIP1. Interacts with KIF4A; the interaction facilitates
CC the transfer of Fe-S clusters to KIF4A to ensure proper localization of
CC KIF4A to the mitotic machinery components. Interacts with CCDC117; the
CC interaction is indirect (By similarity).
CC {ECO:0000250|UniProtKB:Q96T76}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96T76}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96T76}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9D071-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D071-2; Sequence=VSP_015569, VSP_015570;
CC Name=3;
CC IsoId=Q9D071-3; Sequence=VSP_044184;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in
CC testis. {ECO:0000269|PubMed:11328871}.
CC -!- PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination.
CC {ECO:0000250|UniProtKB:Q96T76}.
CC -!- DISRUPTION PHENOTYPE: Embryonically lethality before the implantation
CC stage. {ECO:0000269|PubMed:22678361}.
CC -!- SIMILARITY: Belongs to the MET18/MMS19 family. {ECO:0000305}.
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DR EMBL; AF319949; AAK52670.1; -; mRNA.
DR EMBL; AK010326; BAB26853.1; -; mRNA.
DR EMBL; AK011754; BAB27822.1; -; mRNA.
DR EMBL; AK028317; BAC25875.1; -; mRNA.
DR EMBL; AK030619; BAC27050.1; -; mRNA.
DR EMBL; AK036983; BAC29658.1; -; mRNA.
DR EMBL; AC140193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050817; AAH50817.1; -; mRNA.
DR CCDS; CCDS29818.1; -. [Q9D071-1]
DR RefSeq; NP_082428.1; NM_028152.3. [Q9D071-1]
DR PDB; 6TBL; X-ray; 2.65 A; A/B=911-1031.
DR PDB; 6TC0; X-ray; 3.60 A; C/F=1-1031.
DR PDBsum; 6TBL; -.
DR PDBsum; 6TC0; -.
DR AlphaFoldDB; Q9D071; -.
DR SMR; Q9D071; -.
DR BioGRID; 215214; 12.
DR IntAct; Q9D071; 9.
DR STRING; 10090.ENSMUSP00000130900; -.
DR iPTMnet; Q9D071; -.
DR PhosphoSitePlus; Q9D071; -.
DR SwissPalm; Q9D071; -.
DR EPD; Q9D071; -.
DR MaxQB; Q9D071; -.
DR PaxDb; Q9D071; -.
DR PeptideAtlas; Q9D071; -.
DR PRIDE; Q9D071; -.
DR ProteomicsDB; 252579; -. [Q9D071-1]
DR ProteomicsDB; 252580; -. [Q9D071-2]
DR ProteomicsDB; 252581; -. [Q9D071-3]
DR Antibodypedia; 30936; 176 antibodies from 27 providers.
DR DNASU; 72199; -.
DR Ensembl; ENSMUST00000026168; ENSMUSP00000026168; ENSMUSG00000025159. [Q9D071-3]
DR Ensembl; ENSMUST00000171561; ENSMUSP00000130900; ENSMUSG00000025159. [Q9D071-1]
DR GeneID; 72199; -.
DR KEGG; mmu:72199; -.
DR UCSC; uc008hmv.1; mouse. [Q9D071-1]
DR CTD; 64210; -.
DR MGI; MGI:1919449; Mms19.
DR VEuPathDB; HostDB:ENSMUSG00000025159; -.
DR eggNOG; KOG1967; Eukaryota.
DR GeneTree; ENSGT00390000015583; -.
DR InParanoid; Q9D071; -.
DR OMA; FSFMPEF; -.
DR OrthoDB; 944339at2759; -.
DR PhylomeDB; Q9D071; -.
DR TreeFam; TF314469; -.
DR BioGRID-ORCS; 72199; 27 hits in 112 CRISPR screens.
DR ChiTaRS; Mms19; mouse.
DR PRO; PR:Q9D071; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9D071; protein.
DR Bgee; ENSMUSG00000025159; Expressed in embryonic post-anal tail and 253 other tissues.
DR ExpressionAtlas; Q9D071; baseline and differential.
DR Genevisible; Q9D071; MM.
DR GO; GO:0097361; C:CIA complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0071817; C:MMXD complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0006259; P:DNA metabolic process; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039920; MET18/MMS19.
DR InterPro; IPR024687; MMS19_C.
DR InterPro; IPR029240; MMS19_N.
DR PANTHER; PTHR12891; PTHR12891; 1.
DR Pfam; PF12460; MMS19_C; 1.
DR Pfam; PF14500; MMS19_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Chromosome partition; Cytoplasm; Cytoskeleton; DNA damage; DNA repair;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96T76"
FT CHAIN 2..1031
FT /note="MMS19 nucleotide excision repair protein homolog"
FT /id="PRO_0000096515"
FT REPEAT 867..905
FT /note="HEAT 1"
FT REPEAT 909..947
FT /note="HEAT 2"
FT REPEAT 950..988
FT /note="HEAT 3"
FT REPEAT 991..1029
FT /note="HEAT 4"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96T76"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T76"
FT VAR_SEQ 166..208
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_044184"
FT VAR_SEQ 887..889
FT /note="DVK -> GES (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015569"
FT VAR_SEQ 890..1031
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015570"
FT CONFLICT 16
FT /note="A -> P (in Ref. 2; BAB26853)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="I -> V (in Ref. 1; AAK52670)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="I -> V (in Ref. 1; AAK52670)"
FT /evidence="ECO:0000305"
FT HELIX 915..922
FT /evidence="ECO:0007829|PDB:6TBL"
FT HELIX 928..944
FT /evidence="ECO:0007829|PDB:6TBL"
FT HELIX 946..949
FT /evidence="ECO:0007829|PDB:6TBL"
FT HELIX 950..952
FT /evidence="ECO:0007829|PDB:6TBL"
FT HELIX 953..963
FT /evidence="ECO:0007829|PDB:6TBL"
FT HELIX 969..982
FT /evidence="ECO:0007829|PDB:6TBL"
FT HELIX 987..1000
FT /evidence="ECO:0007829|PDB:6TBL"
FT TURN 1001..1003
FT /evidence="ECO:0007829|PDB:6TBL"
FT HELIX 1004..1006
FT /evidence="ECO:0007829|PDB:6TBL"
FT HELIX 1010..1024
FT /evidence="ECO:0007829|PDB:6TBL"
FT TURN 1025..1027
FT /evidence="ECO:0007829|PDB:6TBL"
SQ SEQUENCE 1031 AA; 113089 MW; 4A3FBD0A1E52FA2D CRC64;
MAAATGLEEA VAPMGALCGL VQDFVMGQQE GPADQVAADV KSGGYTVLQV VEALGSSLEN
AEPRTRARGA QLLSQVLLQC HSLLSEKEVV HLILFYENRL KDHHLVVPSV LQGLRALSMS
VALPPGLAVS VLKAIFQEVH VQSLLQVDRH TVFSIITNFM RSREEELKGL GADFTFGFIQ
VMDGEKDPRN LLLAFRIVHD LISKDYSLGP FVEELFEVTS CYFPIDFTPP PNDPYGIQRE
DLILSLRAVL ASTPRFAEFL LPLLIEKVDS EILSAKLDSL QTLNACCAVY GQKELKDFLP
SLWASIRREV FQTASERVEA EGLAALHSLT ACLSCSVLRA DAEDLLGSFL SNILQDCRHH
LCEPDMKLVW PSAKLLQAAA GASARACEHL TSNVLPLLLE QFHKHSQSNQ RRTILEMILG
FLKLQQKWSY EDRDERPLSS FKDQLCSLVF MALTDPSTQL QLVGIRTLTV LGAQPGLLSA
EDLELAVGHL YRLTFLEEDS QSCRVAALEA SGTLATLYPG AFSRHLLPKL AEELHKGESD
VARADGPTKC SRHFRCLQAL SAVSTHPSIV KETLPLLLQH LCQANKGNMV TESSEVVAVC
QSLQQVAEKC QQDPESYWYF HKTAVPCLFA LAVQASMPEK ESSVLRKVLL EDEVLAALAS
VIGTATTHLS PELAAQSVTC IVPLFLDGNT SFLPENSFPD QFQPFQDGSS GQRRLVALLT
AFVCSLPRNV EIPQLNRLMR ELLKQSCGHS CPFSSTAATK CFAGLLNKQP PGQQLEEFLQ
LAVGTVEAGL ASESSRDQAF TLLLWVTKAL VLRYHPLSAC LTTRLMGLLS DPELGCAAAD
GFSLLMSDCT DVLTRAGHAD VRIMFRQRFF TDNVPALVQG FHAAPQDVKP NYLKGLSHVL
NRLPKPVLLP ELPTLLSLLL EALSCPDSVV QLSTLSCLQP LLLEAPQIMS LHVDTLVTKF
LNLSSSYSMA VRIAALQCMH ALTRLPTSVL LPYKSQVIRA LAKPLDDKKR LVRKEAVSAR
GEWFLLGSPG S
