ID MMS19_HUMAN Reviewed; 1030 AA.
AC Q96T76; B0QZ75; B3KPE5; B4DQX2; B4E2I3; D3DR55; F8W9Y2; Q17RZ8; Q5T455;
AC Q66K82; Q7L4W8; Q969Z1; Q96DF1; Q96MR1; Q96RK5; Q96SK1; Q9BUE2; Q9BYS9;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 27-MAR-2024, entry version 189.
DE RecName: Full=MMS19 nucleotide excision repair protein homolog {ECO:0000305};
DE Short=hMMS19;
DE AltName: Full=MET18 homolog;
DE AltName: Full=MMS19-like protein;
GN Name=MMS19 {ECO:0000312|HGNC:HGNC:13824}; Synonyms=MMS19L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-68, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ERCC2 AND ERCC3.
RC TISSUE=Cervix carcinoma;
RX PubMed=11071939; DOI=10.1093/nar/28.22.4506;
RA Seroz T., Winkler G.S., Auriol J., Verhage R.A., Vermeulen W., Smit B.,
RA Brouwer J., Eker A.P.M., Weeda G., Egly J.-M., Hoeijmakers J.H.J.;
RT "Cloning of a human homolog of the yeast nucleotide excision repair gene
RT MMS19 and interaction with transcription repair factor TFIIH via the XPB
RT and XPD helicases.";
RL Nucleic Acids Res. 28:4506-4513(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-68, INTERACTION WITH
RP NCOA3, AND SUBCELLULAR LOCATION.
RX PubMed=11279242; DOI=10.1074/jbc.m101041200;
RA Wu X., Li H., Chen J.D.;
RT "The human homologue of the yeast DNA repair and TFIIH regulator MMS19 is
RT an AF-1-specific coactivator of estrogen receptor.";
RL J. Biol. Chem. 276:23962-23968(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND VARIANT GLY-68.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 48-1030 (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 127-1030 (ISOFORM 2), AND VARIANTS GLY-68 AND
RP ASP-790.
RC TISSUE=Teratocarcinoma, Tongue, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-68; TRP-98; ILE-197;
RP HIS-306; VAL-365; PRO-409; GLU-434; ILE-526; VAL-558; ASP-790 AND HIS-983.
RG NIEHS SNPs program;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-68.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP GLY-68 AND ASP-790.
RC TISSUE=Brain, Lymph, and Uterus;
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-496, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP FUNCTION, IDENTIFICATION IN MMXD COMPLEX, INTERACTION WITH CIAO2B, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20797633; DOI=10.1016/j.molcel.2010.07.029;
RA Ito S., Tan L.J., Andoh D., Narita T., Seki M., Hirano Y., Narita K.,
RA Kuraoka I., Hiraoka Y., Tanaka K.;
RT "MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in chromosome
RT segregation.";
RL Mol. Cell 39:632-640(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP FUNCTION, AND IDENTIFICATION IN THE CIA COMPLEX.
RX PubMed=22678362; DOI=10.1126/science.1219723;
RA Stehling O., Vashisht A.A., Mascarenhas J., Jonsson Z.O., Sharma T.,
RA Netz D.J., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "MMS19 assembles iron-sulfur proteins required for DNA metabolism and
RT genomic integrity.";
RL Science 337:195-199(2012).
RN [15]
RP FUNCTION, IDENTIFICATION IN THE CIA COMPLEX, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH RTEL1.
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).
RN [16]
RP FUNCTION, IDENTIFICATION IN THE CIA COMPLEX, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH BRIP1; CIAO2B; CIAO3; ERCC2 AND RTEL1.
RX PubMed=23585563; DOI=10.1074/jbc.m112.416602;
RA Seki M., Takeda Y., Iwai K., Tanaka K.;
RT "IOP1 protein is an external component of the human cytosolic iron-sulfur
RT cluster assembly (CIA) machinery and functions in the MMS19 protein-
RT dependent CIA pathway.";
RL J. Biol. Chem. 288:16680-16689(2013).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP FUNCTION, INTERACTION WITH KIF4A, AND SUBCELLULAR LOCATION.
RX PubMed=29848660; DOI=10.1242/jcs.211433;
RA Ben-Shimon L., Paul V.D., David-Kadoch G., Volpe M., Stuempfig M., Bill E.,
RA Muehlenhoff U., Lill R., Ben-Aroya S.;
RT "Fe-S cluster coordination of the chromokinesin KIF4A alters its
RT subcellular localization during mitosis.";
RL J. Cell Sci. 131:0-0(2018).
RN [19]
RP FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF LYS-993; LYS-1002;
RP 1007-LYS-LYS-1008 AND LYS-1013.
RX PubMed=29225034; DOI=10.1016/j.molcel.2017.11.010;
RA Weon J.L., Yang S.W., Potts P.R.;
RT "Cytosolic Iron-Sulfur Assembly Is Evolutionarily Tuned by a Cancer-
RT Amplified Ubiquitin Ligase.";
RL Mol. Cell 69:113-125(2018).
RN [20]
RP INTERACTION WITH CCDC117.
RX PubMed=30742009; DOI=10.1038/s41598-019-39078-5;
RA Horton A.J., Brooker J., Streitfeld W.S., Flessa M.E., Pillai B.,
RA Simpson R., Clark C.D., Gooz M.B., Sutton K.K., Foley A.C., Lee K.H.;
RT "Nkx2-5 Second Heart Field Target Gene Ccdc117 Regulates DNA Metabolism and
RT Proliferation.";
RL Sci. Rep. 9:1738-1738(2019).
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 (PubMed:29848660). In the CIA complex,
CC MMS19 acts as an adapter between early-acting CIA components and a
CC subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ
CC and RTEL1, thereby playing a key role in nucleotide excision repair
CC (NER), homologous recombination-mediated double-strand break DNA
CC repair, DNA replication and RNA polymerase II (POL II) transcription
CC (PubMed:22678362, PubMed:22678361, PubMed:29225034, PubMed:23585563).
CC As part of the mitotic spindle-associated MMXD complex, plays a role in
CC chromosome segregation, probably by facilitating iron-sulfur (Fe-S)
CC cluster assembly into ERCC2/XPD (PubMed:20797633). Together with CIAO2,
CC facilitates the transfer of Fe-S clusters to the motor protein KIF4A,
CC which ensures proper localization of KIF4A to mitotic machinery
CC components to promote the progression of mitosis (PubMed:29848660).
CC Indirectly acts as a transcriptional coactivator of estrogen receptor
CC (ER), via its role in iron-sulfur insertion into some component of the
CC TFIIH-machinery (PubMed:11279242). {ECO:0000269|PubMed:11279242,
CC ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:22678361,
CC ECO:0000269|PubMed:22678362, ECO:0000269|PubMed:23585563,
CC ECO:0000269|PubMed:29225034, ECO:0000269|PubMed:29848660}.
CC -!- SUBUNIT: Component of the CIA complex (PubMed:22678362,
CC PubMed:22678361, PubMed:23585563). In the CIA complex, interacts
CC directly with CIAO2B and CIAO3 (PubMed:23585563). Component of the MMXD
CC complex, composed of CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5
CC (PubMed:20797633). Interacts with CIAO2B; the interaction is direct
CC (PubMed:20797633). Interacts with ERCC2/XPD; the interaction is direct
CC (PubMed:11071939, PubMed:23585563). Interacts with ERCC3/XPB and
CC NCOA3/RAC3 (PubMed:11071939, PubMed:11279242). Interacts with RTEL1;
CC the interaction mediates the association of RTEL1 with the CIA complex
CC (PubMed:22678361, PubMed:23585563). Interacts with BRIP1
CC (PubMed:23585563). 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 (PubMed:29848660). Interacts
CC with CCDC117; the interaction is indirect (PubMed:30742009).
CC {ECO:0000269|PubMed:11071939, ECO:0000269|PubMed:11279242,
CC ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:22678361,
CC ECO:0000269|PubMed:22678362, ECO:0000269|PubMed:23585563,
CC ECO:0000269|PubMed:29848660, ECO:0000269|PubMed:30742009}.
CC -!- INTERACTION:
CC Q96T76; Q9BX63: BRIP1; NbExp=4; IntAct=EBI-1044169, EBI-3509650;
CC Q96T76; O76071: CIAO1; NbExp=13; IntAct=EBI-1044169, EBI-725145;
CC Q96T76; Q9Y3D0: CIAO2B; NbExp=15; IntAct=EBI-1044169, EBI-744045;
CC Q96T76; Q9H6Q4: CIAO3; NbExp=3; IntAct=EBI-1044169, EBI-10977788;
CC Q96T76; P18074: ERCC2; NbExp=9; IntAct=EBI-1044169, EBI-6380590;
CC Q96T76; Q9NZ71: RTEL1; NbExp=4; IntAct=EBI-1044169, EBI-2859587;
CC Q96T76-8; O76071: CIAO1; NbExp=5; IntAct=EBI-10190644, EBI-725145;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20797633}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:20797633,
CC ECO:0000269|PubMed:29848660}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:29848660}. Note=In
CC mitosis, enriched on centrosomes during prophase, localizes to the
CC spindle during metaphase and surrounds compacted spindle midzone
CC microtubules during telophase. {ECO:0000269|PubMed:29848660}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q96T76-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96T76-7; Sequence=VSP_040312, VSP_040313;
CC Name=3;
CC IsoId=Q96T76-6; Sequence=VSP_040310, VSP_040311;
CC Name=4;
CC IsoId=Q96T76-5; Sequence=VSP_015565;
CC Name=5;
CC IsoId=Q96T76-8; Sequence=VSP_044182;
CC Name=6;
CC IsoId=Q96T76-9; Sequence=VSP_044183;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in
CC testis. {ECO:0000269|PubMed:11071939, ECO:0000269|PubMed:11328871}.
CC -!- PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination by
CC MAGEF1-NSMCE1 ubiquitin ligase complex leading to proteasomal
CC degradation. {ECO:0000269|PubMed:29225034}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MET18/MMS19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH80532.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAB55315.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71223.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAG51657.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC29239.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mms19l/";
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DR EMBL; AJ306408; CAC29239.1; ALT_FRAME; mRNA.
DR EMBL; AF357881; AAK70402.1; -; mRNA.
DR EMBL; AF319947; AAK52668.1; -; mRNA.
DR EMBL; AK027710; BAB55315.1; ALT_INIT; mRNA.
DR EMBL; AK056244; BAG51657.1; ALT_INIT; mRNA.
DR EMBL; AK056581; BAB71223.1; ALT_SEQ; mRNA.
DR EMBL; AK298995; BAG61084.1; -; mRNA.
DR EMBL; AK304287; BAG65145.1; -; mRNA.
DR EMBL; AY974244; AAX59033.1; -; Genomic_DNA.
DR EMBL; AL355490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49924.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49927.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49928.1; -; Genomic_DNA.
DR EMBL; BC002692; AAH02692.1; -; mRNA.
DR EMBL; BC006575; AAH06575.2; -; mRNA.
DR EMBL; BC009396; AAH09396.2; -; mRNA.
DR EMBL; BC080532; AAH80532.1; ALT_SEQ; mRNA.
DR EMBL; BC117129; AAI17130.1; -; mRNA.
DR CCDS; CCDS73177.1; -. [Q96T76-9]
DR CCDS; CCDS7464.1; -. [Q96T76-1]
DR CCDS; CCDS81493.1; -. [Q96T76-5]
DR RefSeq; NP_001276332.1; NM_001289403.1. [Q96T76-9]
DR RefSeq; NP_001276333.1; NM_001289404.1.
DR RefSeq; NP_001276334.1; NM_001289405.1. [Q96T76-1]
DR RefSeq; NP_001317057.1; NM_001330128.1. [Q96T76-5]
DR RefSeq; NP_071757.4; NM_022362.4. [Q96T76-1]
DR RefSeq; XP_016872013.1; XM_017016524.1.
DR AlphaFoldDB; Q96T76; -.
DR SMR; Q96T76; -.
DR BioGRID; 122103; 315.
DR ComplexPortal; CPX-2837; CIAO1-CIAO2B-CIAO3-MMS19 cytosolic iron-sulfur protein assembly complex.
DR CORUM; Q96T76; -.
DR IntAct; Q96T76; 71.
DR MINT; Q96T76; -.
DR STRING; 9606.ENSP00000359818; -.
DR GlyGen; Q96T76; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96T76; -.
DR MetOSite; Q96T76; -.
DR PhosphoSitePlus; Q96T76; -.
DR SwissPalm; Q96T76; -.
DR BioMuta; MMS19; -.
DR DMDM; 150421597; -.
DR EPD; Q96T76; -.
DR jPOST; Q96T76; -.
DR MassIVE; Q96T76; -.
DR MaxQB; Q96T76; -.
DR PaxDb; 9606-ENSP00000412698; -.
DR PeptideAtlas; Q96T76; -.
DR ProteomicsDB; 30403; -.
DR ProteomicsDB; 78210; -. [Q96T76-1]
DR ProteomicsDB; 78211; -. [Q96T76-5]
DR ProteomicsDB; 78212; -. [Q96T76-6]
DR ProteomicsDB; 78213; -. [Q96T76-7]
DR Pumba; Q96T76; -.
DR TopDownProteomics; Q96T76-6; -. [Q96T76-6]
DR Antibodypedia; 30936; 186 antibodies from 27 providers.
DR DNASU; 64210; -.
DR Ensembl; ENST00000327238.14; ENSP00000320059.10; ENSG00000155229.21. [Q96T76-5]
DR Ensembl; ENST00000355839.10; ENSP00000348097.6; ENSG00000155229.21. [Q96T76-9]
DR Ensembl; ENST00000370782.6; ENSP00000359818.1; ENSG00000155229.21. [Q96T76-1]
DR Ensembl; ENST00000415383.5; ENSP00000395045.1; ENSG00000155229.21. [Q96T76-6]
DR Ensembl; ENST00000438925.7; ENSP00000412698.2; ENSG00000155229.21. [Q96T76-1]
DR Ensembl; ENST00000441194.5; ENSP00000413801.1; ENSG00000155229.21. [Q96T76-6]
DR GeneID; 64210; -.
DR KEGG; hsa:64210; -.
DR MANE-Select; ENST00000438925.7; ENSP00000412698.2; NM_022362.5; NP_071757.4.
DR UCSC; uc001kns.5; human. [Q96T76-1]
DR AGR; HGNC:13824; -.
DR CTD; 64210; -.
DR DisGeNET; 64210; -.
DR GeneCards; MMS19; -.
DR HGNC; HGNC:13824; MMS19.
DR HPA; ENSG00000155229; Low tissue specificity.
DR MIM; 614777; gene.
DR neXtProt; NX_Q96T76; -.
DR OpenTargets; ENSG00000155229; -.
DR PharmGKB; PA162395974; -.
DR VEuPathDB; HostDB:ENSG00000155229; -.
DR eggNOG; KOG1967; Eukaryota.
DR GeneTree; ENSGT00390000015583; -.
DR HOGENOM; CLU_3299103_0_0_1; -.
DR InParanoid; Q96T76; -.
DR OMA; FSFMPEF; -.
DR OrthoDB; 38995at2759; -.
DR PhylomeDB; Q96T76; -.
DR TreeFam; TF314469; -.
DR PathwayCommons; Q96T76; -.
DR Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly.
DR SignaLink; Q96T76; -.
DR BioGRID-ORCS; 64210; 600 hits in 1171 CRISPR screens.
DR ChiTaRS; MMS19; human.
DR GeneWiki; MMS19; -.
DR GenomeRNAi; 64210; -.
DR Pharos; Q96T76; Tbio.
DR PRO; PR:Q96T76; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q96T76; Protein.
DR Bgee; ENSG00000155229; Expressed in right hemisphere of cerebellum and 205 other cell types or tissues.
DR ExpressionAtlas; Q96T76; baseline and differential.
DR Genevisible; Q96T76; HS.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0097361; C:CIA complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0071817; C:MMXD complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; NAS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; NAS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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; DNA REPAIR/TRANSCRIPTION PROTEIN MET18/MMS19; 1.
DR PANTHER; PTHR12891:SF0; MMS19 NUCLEOTIDE EXCISION REPAIR PROTEIN HOMOLOG; 1.
DR Pfam; PF12460; MMS19_C; 1.
DR Pfam; PF14500; MMS19_N; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Chromosome partition;
KW Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..1030
FT /note="MMS19 nucleotide excision repair protein homolog"
FT /id="PRO_0000096514"
FT REPEAT 866..904
FT /note="HEAT 1"
FT REPEAT 908..946
FT /note="HEAT 2"
FT REPEAT 949..987
FT /note="HEAT 3"
FT REPEAT 990..1028
FT /note="HEAT 4"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 496
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1027
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1
FT /note="M -> MRGEPVSSHRPYPLPRSLVRVM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044182"
FT VAR_SEQ 38..40
FT /note="DVK -> GPL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040310"
FT VAR_SEQ 41..1030
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040311"
FT VAR_SEQ 165..207
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044183"
FT VAR_SEQ 309..406
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015565"
FT VAR_SEQ 309..318
FT /note="VFQTASERVE -> TAGTTCVNRT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040312"
FT VAR_SEQ 319..1030
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040313"
FT VARIANT 68
FT /note="A -> G (in dbSNP:rs2275586)"
FT /evidence="ECO:0000269|PubMed:11071939,
FT ECO:0000269|PubMed:11279242, ECO:0000269|PubMed:11328871,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.7"
FT /id="VAR_023448"
FT VARIANT 98
FT /note="R -> W (in dbSNP:rs29001280)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_023449"
FT VARIANT 197
FT /note="V -> I (in dbSNP:rs29001285)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_023450"
FT VARIANT 306
FT /note="R -> H (in dbSNP:rs29001306)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_023451"
FT VARIANT 365
FT /note="M -> V (in dbSNP:rs29001309)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_023452"
FT VARIANT 409
FT /note="Q -> P (in dbSNP:rs29001311)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_023453"
FT VARIANT 434
FT /note="Q -> E (in dbSNP:rs29001314)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_023454"
FT VARIANT 526
FT /note="V -> I (in dbSNP:rs17112809)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_023455"
FT VARIANT 558
FT /note="A -> V (in dbSNP:rs12360068)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_023456"
FT VARIANT 790
FT /note="G -> D (in dbSNP:rs3740526)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5"
FT /id="VAR_023457"
FT VARIANT 983
FT /note="R -> H (in dbSNP:rs29001332)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_023458"
FT MUTAGEN 993
FT /note="K->R: Impairs MAGEF1-NSMCE1-mediated
FT polyubiquitination when associated with R-1002, 1007-R-R-
FT 1008 and R-1013."
FT /evidence="ECO:0000269|PubMed:29225034"
FT MUTAGEN 1002
FT /note="K->R: Impairs MAGEF1-NSMCE1-mediated
FT polyubiquitination when associated with R-993, 1007-R-R-
FT 1008 and R-1013."
FT /evidence="ECO:0000269|PubMed:29225034"
FT MUTAGEN 1007..1008
FT /note="KK->RR: Impairs MAGEF1-NSMCE1-mediated
FT polyubiquitination when associated with R-993, R-1002 and
FT R-1013."
FT /evidence="ECO:0000269|PubMed:29225034"
FT MUTAGEN 1013
FT /note="K->R: Impairs MAGEF1-NSMCE1-mediated
FT polyubiquitination when associated with R-993, R-1002 and
FT 1007-R-R-1008."
FT /evidence="ECO:0000269|PubMed:29225034"
FT CONFLICT 179
FT /note="Q -> H (in Ref. 2; AAK70402)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="V -> D (in Ref. 2; AAK70402)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="L -> P (in Ref. 2; AAK70402)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="Q -> R (in Ref. 4; BAG51657)"
FT /evidence="ECO:0000305"
FT CONFLICT 502..503
FT /note="CR -> W (in Ref. 4; BAG51657)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="E -> K (in Ref. 4; BAG65145)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="E -> G (in Ref. 4; BAB55315)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="I -> V (in Ref. 4; BAG65145)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="L -> F (in Ref. 2; AAK70402)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1030 AA; 113290 MW; 7EC22CF0E38EFE1D CRC64;
MAAAAAVEAA APMGALWGLV HDFVVGQQEG PADQVAADVK SGNYTVLQVV EALGSSLENP
EPRTRARAIQ LLSQVLLHCH TLLLEKEVVH LILFYENRLK DHHLVIPSVL QGLKALSLCV
ALPPGLAVSV LKAIFQEVHV QSLPQVDRHT VYNIITNFMR TREEELKSLG ADFTFGFIQV
MDGEKDPRNL LVAFRIVHDL ISRDYSLGPF VEELFEVTSC YFPIDFTPPP NDPHGIQRED
LILSLRAVLA STPRFAEFLL PLLIEKVDSE VLSAKLDSLQ TLNACCAVYG QKELKDFLPS
LWASIRREVF QTASERVEAE GLAALHSLTA CLSRSVLRAD AEDLLDSFLS NILQDCRHHL
CEPDMKLVWP SAKLLQAAAG ASARACDSVT SNVLPLLLEQ FHKHSQSSQR RTILEMLLGF
LKLQQKWSYE DKDQRPLNGF KDQLCSLVFM ALTDPSTQLQ LVGIRTLTVL GAQPDLLSYE
DLELAVGHLY RLSFLKEDSQ SCRVAALEAS GTLAALYPVA FSSHLVPKLA EELRVGESNL
TNGDEPTQCS RHLCCLQALS AVSTHPSIVK ETLPLLLQHL WQVNRGNMVA QSSDVIAVCQ
SLRQMAEKCQ QDPESCWYFH QTAIPCLLAL AVQASMPEKE PSVLRKVLLE DEVLAAMVSV
IGTATTHLSP ELAAQSVTHI VPLFLDGNVS FLPENSFPSR FQPFQDGSSG QRRLIALLMA
FVCSLPRNVE IPQLNQLMRE LLELSCCHSC PFSSTAAAKC FAGLLNKHPA GQQLDEFLQL
AVDKVEAGLG SGPCRSQAFT LLLWVTKALV LRYHPLSSCL TARLMGLLSD PELGPAAADG
FSLLMSDCTD VLTRAGHAEV RIMFRQRFFT DNVPALVQGF HAAPQDVKPN YLKGLSHVLN
RLPKPVLLPE LPTLLSLLLE ALSCPDCVVQ LSTLSCLQPL LLEAPQVMSL HVDTLVTKFL
NLSSSPSMAV RIAALQCMHA LTRLPTPVLL PYKPQVIRAL AKPLDDKKRL VRKEAVSARG
EWFLLGSPGS
//
