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MMS19 nucleotide excision repair protein homolog (hMMS19) (MET18 homolog) (MMS19-like protein)

 MMS19_HUMAN             Reviewed;        1030 AA.
Q96T76; B0QZ75; B3KPE5; B4DQX2; B4E2I3; D3DR55; F8W9Y2; Q17RZ8;
Q5T455; Q66K82; Q7L4W8; Q969Z1; Q96DF1; Q96MR1; Q96RK5; Q96SK1;
Q9BUE2; Q9BYS9;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 2.
07-NOV-2018, entry version 158.
RecName: Full=MMS19 nucleotide excision repair protein homolog;
Short=hMMS19;
AltName: Full=MET18 homolog;
AltName: Full=MMS19-like protein;
Name=MMS19 {ECO:0000312|HGNC:HGNC:13824}; Synonyms=MMS19L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-68, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH ERCC2 AND
ERCC3.
TISSUE=Cervix carcinoma;
PubMed=11071939; DOI=10.1093/nar/28.22.4506;
Seroz T., Winkler G.S., Auriol J., Verhage R.A., Vermeulen W.,
Smit B., Brouwer J., Eker A.P.M., Weeda G., Egly J.-M.,
Hoeijmakers J.H.J.;
"Cloning of a human homolog of the yeast nucleotide excision repair
gene MMS19 and interaction with transcription repair factor TFIIH via
the XPB and XPD helicases.";
Nucleic Acids Res. 28:4506-4513(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-68, INTERACTION
WITH NCOA3, AND SUBCELLULAR LOCATION.
PubMed=11279242; DOI=10.1074/jbc.M101041200;
Wu X., Li H., Chen J.D.;
"The human homologue of the yeast DNA repair and TFIIH regulator MMS19
is an AF-1-specific coactivator of estrogen receptor.";
J. Biol. Chem. 276:23962-23968(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND VARIANT GLY-68.
PubMed=11328871; DOI=10.1093/nar/29.9.1884;
Queimado L., Rao M., Schultz R.A., Koonin E.V., Aravind L., Nardo T.,
Stefanini M., Friedberg E.C.;
"Cloning the human and mouse MMS19 genes and functional
complementation of a yeast mms19 deletion mutant.";
Nucleic Acids Res. 29:1884-1891(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 48-1030 (ISOFORM 4), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 127-1030 (ISOFORM 2), AND VARIANTS
GLY-68 AND ASP-790.
TISSUE=Teratocarcinoma, Tongue, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-68; TRP-98;
ILE-197; HIS-306; VAL-365; PRO-409; GLU-434; ILE-526; VAL-558; ASP-790
AND HIS-983.
NIEHS SNPs program;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-68.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND
VARIANTS GLY-68 AND ASP-790.
TISSUE=Brain, Lymph, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-496, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
FUNCTION, IDENTIFICATION IN MMXD COMPLEX, INTERACTION WITH CIAO2B, AND
SUBCELLULAR LOCATION.
PubMed=20797633; DOI=10.1016/j.molcel.2010.07.029;
Ito S., Tan L.J., Andoh D., Narita T., Seki M., Hirano Y., Narita K.,
Kuraoka I., Hiraoka Y., Tanaka K.;
"MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in
chromosome segregation.";
Mol. Cell 39:632-640(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
FUNCTION, AND IDENTIFICATION IN THE CIA COMPLEX.
PubMed=22678362; DOI=10.1126/science.1219723;
Stehling O., Vashisht A.A., Mascarenhas J., Jonsson Z.O., Sharma T.,
Netz D.J., Pierik A.J., Wohlschlegel J.A., Lill R.;
"MMS19 assembles iron-sulfur proteins required for DNA metabolism and
genomic integrity.";
Science 337:195-199(2012).
[15]
FUNCTION, IDENTIFICATION IN THE CIA COMPLEX, SUBCELLULAR LOCATION, AND
INTERACTION WITH RTEL1.
PubMed=22678361; DOI=10.1126/science.1219664;
Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M.,
Boulton S.J.;
"MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA
metabolism.";
Science 337:243-245(2012).
[16]
FUNCTION, IDENTIFICATION IN THE CIA COMPLEX, SUBCELLULAR LOCATION, AND
INTERACTION WITH BRIP1; CIAO2B; CIAO3; ERCC2 AND RTEL1.
PubMed=23585563; DOI=10.1074/jbc.M112.416602;
Seki M., Takeda Y., Iwai K., Tanaka K.;
"IOP1 protein is an external component of the human cytosolic iron-
sulfur cluster assembly (CIA) machinery and functions in the MMS19
protein-dependent CIA pathway.";
J. Biol. Chem. 288:16680-16689(2013).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF LYS-993; LYS-1002;
1007-LYS-LYS-1008 AND LYS-1013.
PubMed=29225034; DOI=10.1016/j.molcel.2017.11.010;
Weon J.L., Yang S.W., Potts P.R.;
"Cytosolic Iron-Sulfur Assembly Is Evolutionarily Tuned by a Cancer-
Amplified Ubiquitin Ligase.";
Mol. Cell 69:113-125(2018).
-!- FUNCTION: Key component of the cytosolic iron-sulfur protein
assembly (CIA) complex, a multiprotein complex that mediates the
incorporation of iron-sulfur cluster into apoproteins specifically
involved in DNA metabolism and genomic integrity. In the CIA
complex, MMS19 acts as an adapter between early-acting CIA
components and a subset of cellular target iron-sulfur proteins
such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in
nucleotide excision repair (NER), homologous recombination-
mediated double-strand break DNA repair, DNA replication and RNA
polymerase II (POL II) transcription (PubMed:22678362,
PubMed:22678361, PubMed:29225034, PubMed:23585563). As part of the
mitotic spindle-associated MMXD complex, plays a role in
chromosome segregation, probably by facilitating iron-sulfur
cluster assembly into ERCC2/XPD (PubMed:20797633). Indirectly acts
as a transcriptional coactivator of estrogen receptor (ER), via
its role in iron-sulfur insertion into some component of the
TFIIH-machinery (PubMed:11279242). {ECO:0000269|PubMed:11279242,
ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:22678361,
ECO:0000269|PubMed:22678362, ECO:0000269|PubMed:23585563,
ECO:0000269|PubMed:29225034}.
-!- SUBUNIT: Component of the CIA complex (PubMed:22678362,
PubMed:22678361, PubMed:23585563). In the CIA complex, interacts
directly with CIAO2B and CIAO3 (PubMed:23585563). Component of the
MMXD complex, composed of CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5
(PubMed:20797633). Interacts with CIAO2B; the interaction is
direct (PubMed:20797633). Interacts with ERCC2/XPD; the
interaction is direct (PubMed:11071939, PubMed:23585563).
Interacts with ERCC3/XPB and NCOA3/RAC3 (PubMed:11071939,
PubMed:11279242). Interacts with RTEL1; the interaction mediates
the association of RTEL1 with the CIA complex (PubMed:22678361,
PubMed:23585563). Interacts with BRIP1 (PubMed:23585563).
{ECO:0000269|PubMed:11071939, ECO:0000269|PubMed:11279242,
ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:22678361,
ECO:0000269|PubMed:22678362, ECO:0000269|PubMed:23585563}.
-!- INTERACTION:
O76071:CIAO1; NbExp=9; IntAct=EBI-1044169, EBI-725145;
P18074:ERCC2; NbExp=7; IntAct=EBI-1044169, EBI-6380590;
Q9Y3D0:FAM96B; NbExp=11; IntAct=EBI-1044169, EBI-744045;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20797633}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:20797633}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q96T76-1; Sequence=Displayed;
Name=2;
IsoId=Q96T76-7; Sequence=VSP_040312, VSP_040313;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=3;
IsoId=Q96T76-6; Sequence=VSP_040310, VSP_040311;
Note=No experimental confirmation available. May be produced at
very low levels due to a premature stop codon in the mRNA,
leading to nonsense-mediated mRNA decay.;
Name=4;
IsoId=Q96T76-5; Sequence=VSP_015565;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q96T76-8; Sequence=VSP_044182;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q96T76-9; Sequence=VSP_044183;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression
in testis. {ECO:0000269|PubMed:11071939,
ECO:0000269|PubMed:11328871}.
-!- PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination
by MAGEF1-NSMCE1 ubiquitin ligase complex leading to proteasomal
degradation. {ECO:0000269|PubMed:29225034}.
-!- SIMILARITY: Belongs to the MET18/MMS19 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH80532.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
Sequence=BAB55315.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB71223.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
Sequence=BAG51657.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAC29239.1; Type=Frameshift; Positions=373, 412; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mms19l/";
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EMBL; AJ306408; CAC29239.1; ALT_FRAME; mRNA.
EMBL; AF357881; AAK70402.1; -; mRNA.
EMBL; AF319947; AAK52668.1; -; mRNA.
EMBL; AK027710; BAB55315.1; ALT_INIT; mRNA.
EMBL; AK056244; BAG51657.1; ALT_INIT; mRNA.
EMBL; AK056581; BAB71223.1; ALT_SEQ; mRNA.
EMBL; AK298995; BAG61084.1; -; mRNA.
EMBL; AK304287; BAG65145.1; -; mRNA.
EMBL; AY974244; AAX59033.1; -; Genomic_DNA.
EMBL; AL355490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49924.1; -; Genomic_DNA.
EMBL; CH471066; EAW49927.1; -; Genomic_DNA.
EMBL; CH471066; EAW49928.1; -; Genomic_DNA.
EMBL; BC002692; AAH02692.1; -; mRNA.
EMBL; BC006575; AAH06575.2; -; mRNA.
EMBL; BC009396; AAH09396.2; -; mRNA.
EMBL; BC080532; AAH80532.1; ALT_SEQ; mRNA.
EMBL; BC117129; AAI17130.1; -; mRNA.
CCDS; CCDS73177.1; -. [Q96T76-9]
CCDS; CCDS7464.1; -. [Q96T76-1]
CCDS; CCDS81493.1; -. [Q96T76-5]
RefSeq; NP_001276332.1; NM_001289403.1. [Q96T76-9]
RefSeq; NP_001276333.1; NM_001289404.1.
RefSeq; NP_001276334.1; NM_001289405.1. [Q96T76-1]
RefSeq; NP_001317057.1; NM_001330128.1. [Q96T76-5]
RefSeq; NP_071757.4; NM_022362.4. [Q96T76-1]
RefSeq; XP_016872013.1; XM_017016524.1.
UniGene; Hs.500721; -.
ProteinModelPortal; Q96T76; -.
BioGrid; 122103; 193.
IntAct; Q96T76; 28.
MINT; Q96T76; -.
STRING; 9606.ENSP00000359818; -.
iPTMnet; Q96T76; -.
PhosphoSitePlus; Q96T76; -.
BioMuta; MMS19; -.
DMDM; 150421597; -.
EPD; Q96T76; -.
MaxQB; Q96T76; -.
PaxDb; Q96T76; -.
PeptideAtlas; Q96T76; -.
PRIDE; Q96T76; -.
ProteomicsDB; 78210; -.
ProteomicsDB; 78211; -. [Q96T76-5]
ProteomicsDB; 78212; -. [Q96T76-6]
ProteomicsDB; 78213; -. [Q96T76-7]
TopDownProteomics; Q96T76-6; -. [Q96T76-6]
Ensembl; ENST00000327238; ENSP00000320059; ENSG00000155229. [Q96T76-5]
Ensembl; ENST00000355839; ENSP00000348097; ENSG00000155229. [Q96T76-9]
Ensembl; ENST00000370782; ENSP00000359818; ENSG00000155229. [Q96T76-1]
Ensembl; ENST00000415383; ENSP00000395045; ENSG00000155229. [Q96T76-6]
Ensembl; ENST00000438925; ENSP00000412698; ENSG00000155229. [Q96T76-1]
Ensembl; ENST00000441194; ENSP00000413801; ENSG00000155229. [Q96T76-6]
GeneID; 64210; -.
KEGG; hsa:64210; -.
UCSC; uc001kns.5; human. [Q96T76-1]
CTD; 64210; -.
DisGeNET; 64210; -.
EuPathDB; HostDB:ENSG00000155229.20; -.
GeneCards; MMS19; -.
H-InvDB; HIX0009091; -.
HGNC; HGNC:13824; MMS19.
HPA; HPA051936; -.
HPA; HPA056299; -.
MIM; 614777; gene.
neXtProt; NX_Q96T76; -.
OpenTargets; ENSG00000155229; -.
PharmGKB; PA162395974; -.
eggNOG; KOG1967; Eukaryota.
eggNOG; ENOG410XNMZ; LUCA.
GeneTree; ENSGT00390000015583; -.
HOGENOM; HOG000038024; -.
HOVERGEN; HBG057358; -.
InParanoid; Q96T76; -.
KO; K15075; -.
OMA; FEIFACY; -.
OrthoDB; EOG091G00K8; -.
PhylomeDB; Q96T76; -.
TreeFam; TF314469; -.
Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly.
ChiTaRS; MMS19; human.
GeneWiki; MMS19; -.
GenomeRNAi; 64210; -.
PRO; PR:Q96T76; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000155229; Expressed in 230 organ(s), highest expression level in right hemisphere of cerebellum.
CleanEx; HS_MMS19; -.
ExpressionAtlas; Q96T76; baseline and differential.
Genevisible; Q96T76; HS.
GO; GO:0097361; C:CIA complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0071817; C:MMXD complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0005675; C:transcription factor TFIIH holo complex; NAS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0030331; F:estrogen receptor binding; IPI:UniProtKB.
GO; GO:0030674; F:protein binding, bridging; NAS:UniProtKB.
GO; GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0006259; P:DNA metabolic process; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
GO; GO:0006289; P:nucleotide-excision repair; TAS:UniProtKB.
GO; GO:0000160; P:phosphorelay signal transduction system; NAS:UniProtKB.
GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IDA:UniProtKB.
GO; GO:0009725; P:response to hormone; NAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; NAS:UniProtKB.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR039920; MET18/MMS19.
InterPro; IPR024687; MMS19_C.
InterPro; IPR029240; MMS19_N.
PANTHER; PTHR12891; PTHR12891; 1.
Pfam; PF12460; MMS19_C; 1.
Pfam; PF14500; MMS19_N; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Chromosome partition;
Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:25944712}.
CHAIN 2 1030 MMS19 nucleotide excision repair protein
homolog.
/FTId=PRO_0000096514.
REPEAT 866 904 HEAT 1.
REPEAT 908 946 HEAT 2.
REPEAT 949 987 HEAT 3.
REPEAT 990 1028 HEAT 4.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:25944712}.
MOD_RES 496 496 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1027 1027 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 1 M -> MRGEPVSSHRPYPLPRSLVRVM (in isoform
5). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_044182.
VAR_SEQ 38 40 DVK -> GPL (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040310.
VAR_SEQ 41 1030 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040311.
VAR_SEQ 165 207 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044183.
VAR_SEQ 309 406 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_015565.
VAR_SEQ 309 318 VFQTASERVE -> TAGTTCVNRT (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040312.
VAR_SEQ 319 1030 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040313.
VARIANT 68 68 A -> G (in dbSNP:rs2275586).
{ECO:0000269|PubMed:11071939,
ECO:0000269|PubMed:11279242,
ECO:0000269|PubMed:11328871,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.5, ECO:0000269|Ref.7}.
/FTId=VAR_023448.
VARIANT 98 98 R -> W (in dbSNP:rs29001280).
{ECO:0000269|Ref.5}.
/FTId=VAR_023449.
VARIANT 197 197 V -> I (in dbSNP:rs29001285).
{ECO:0000269|Ref.5}.
/FTId=VAR_023450.
VARIANT 306 306 R -> H (in dbSNP:rs29001306).
{ECO:0000269|Ref.5}.
/FTId=VAR_023451.
VARIANT 365 365 M -> V (in dbSNP:rs29001309).
{ECO:0000269|Ref.5}.
/FTId=VAR_023452.
VARIANT 409 409 Q -> P (in dbSNP:rs29001311).
{ECO:0000269|Ref.5}.
/FTId=VAR_023453.
VARIANT 434 434 Q -> E (in dbSNP:rs29001314).
{ECO:0000269|Ref.5}.
/FTId=VAR_023454.
VARIANT 526 526 V -> I (in dbSNP:rs17112809).
{ECO:0000269|Ref.5}.
/FTId=VAR_023455.
VARIANT 558 558 A -> V (in dbSNP:rs12360068).
{ECO:0000269|Ref.5}.
/FTId=VAR_023456.
VARIANT 790 790 G -> D (in dbSNP:rs3740526).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.5}.
/FTId=VAR_023457.
VARIANT 983 983 R -> H (in dbSNP:rs29001332).
{ECO:0000269|Ref.5}.
/FTId=VAR_023458.
MUTAGEN 993 993 K->R: Impairs MAGEF1-NSMCE1-mediated
polyubiquitination when associated with
R-1002, 1007-R-R-1008 and R-1013.
{ECO:0000269|PubMed:29225034}.
MUTAGEN 1002 1002 K->R: Impairs MAGEF1-NSMCE1-mediated
polyubiquitination when associated with
R-993, 1007-R-R-1008 and R-1013.
{ECO:0000269|PubMed:29225034}.
MUTAGEN 1007 1008 KK->RR: Impairs MAGEF1-NSMCE1-mediated
polyubiquitination when associated with
R-993, R-1002 and R-1013.
{ECO:0000269|PubMed:29225034}.
MUTAGEN 1013 1013 K->R: Impairs MAGEF1-NSMCE1-mediated
polyubiquitination when associated with
R-993, R-1002 and 1007-R-R-1008.
{ECO:0000269|PubMed:29225034}.
CONFLICT 179 179 Q -> H (in Ref. 2; AAK70402).
{ECO:0000305}.
CONFLICT 389 389 V -> D (in Ref. 2; AAK70402).
{ECO:0000305}.
CONFLICT 394 394 L -> P (in Ref. 2; AAK70402).
{ECO:0000305}.
CONFLICT 473 473 Q -> R (in Ref. 4; BAG51657).
{ECO:0000305}.
CONFLICT 502 503 CR -> W (in Ref. 4; BAG51657).
{ECO:0000305}.
CONFLICT 607 607 E -> K (in Ref. 4; BAG65145).
{ECO:0000305}.
CONFLICT 640 640 E -> G (in Ref. 4; BAB55315).
{ECO:0000305}.
CONFLICT 661 661 I -> V (in Ref. 4; BAG65145).
{ECO:0000305}.
CONFLICT 741 741 L -> F (in Ref. 2; AAK70402).
{ECO:0000305}.
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


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