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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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. DR Genevisible; Q96T76; HS. 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, FT 1007-R-R-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, FT 1007-R-R-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 //