ID O43410_HUMAN Unreviewed; 341 AA. AC O43410; DT 01-JUN-1998, integrated into UniProtKB/TrEMBL. DT 01-JUN-1998, sequence version 1. DT 03-AUG-2022, entry version 87. DE RecName: Full=MMS19 nucleotide excision repair protein {ECO:0000256|RuleBase:RU367072}; DE Flags: Fragment; 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 {ECO:0000313|EMBL:AAC19154.1}; RN [1] {ECO:0000313|EMBL:AAC19154.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:AAC19154.1}; RX PubMed=8619474; DOI=10.1006/abio.1996.0138; RA Andersson B., Wentland M.A., Ricafrente J.Y., Liu W., Gibbs R.A.; RT "A "double adaptor" method for improved shotgun library construction."; RL Anal. Biochem. 236:107-113(1996). RN [2] {ECO:0000313|EMBL:AAC19154.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:AAC19154.1}; RX PubMed=9110174; RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.; RT "Large-scale concatenation cDNA sequencing."; RL Genome Res. 7:353-358(1997). 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 iron-sulfur proteins. {ECO:0000256|RuleBase:RU367072}. CC -!- SUBUNIT: Component of the CIA complex. {ECO:0000256|RuleBase:RU367072}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle CC {ECO:0000256|RuleBase:RU367072}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367072}. CC -!- SIMILARITY: Belongs to the MET18/MMS19 family. CC {ECO:0000256|RuleBase:RU367072}. 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; AF007151; AAC19154.1; -; mRNA. DR PeptideAtlas; O43410; -. DR PRIDE; O43410; -. DR GO; GO:0097361; C:CIA complex; IEA:UniProtKB-UniRule. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule. DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IEA:UniProtKB-UniRule. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR039920; MET18/MMS19. DR InterPro; IPR024687; MMS19_C. DR PANTHER; PTHR12891; PTHR12891; 1. DR Pfam; PF12460; MMS19_C; 1. DR SUPFAM; SSF48371; SSF48371; 1. PE 2: Evidence at transcript level; KW Cytoplasm {ECO:0000256|RuleBase:RU367072}; KW Cytoskeleton {ECO:0000256|RuleBase:RU367072}; KW DNA damage {ECO:0000256|RuleBase:RU367072}; KW DNA repair {ECO:0000256|RuleBase:RU367072}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367072}. FT DOMAIN 102..314 FT /note="MMS19_C" FT /evidence="ECO:0000259|Pfam:PF12460" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAC19154.1" SQ SEQUENCE 341 AA; 37208 MW; 8C6206B901B810EA CRC64; GFKDQLCSLV FMALTDPSTQ LQLVGIRTLT VLGAQPDLLS YEDLELAVGH LYRLSFLKED SQSCRVAALE ASGTLAALYP VAFSSHLVPK LAEELRVGES NLTNGDEPTQ CSRHLCCLQA LSAVSTHPSI VKETLPLLLQ HLWQVNRGNM VAQSSDVIAV CQSLRQMAEK CQQDPESCWY FHQTAIPCLL ALAVQASMPE KEPSVLRKVL LEDEVLAAMV SVIGTATTHL SPELAAQSVT HIVPLFLDGN VSFLPENSFP SRFQPFQDGS SGQRRLIALL MAFVCSLPRN VEIPQLNQLM RELLELSCST AAPFLPPLLP SALQDSSTST LQGSSWMNSY S //