MMS19
entrez
64210
canonical
uniprot
Q96T76
canonical
ensembl
ENSG00000155229
resolver
ensp
ENSP00000320059
resolver
ensp
ENSP00000348097
resolver
ensp
ENSP00000359818
resolver
ensp
ENSP00000410008
resolver
ensp
ENSP00000412698
resolver
ensp
ENSP00000566648
resolver
ensp
ENSP00000566654
resolver
ensp
ENSP00000566659
resolver
ensp
ENSP00000566665
resolver
ensp
ENSP00000603350
resolver
ensp
ENSP00000656055
resolver
genesymbol
MMS19
resolver
genesymbol_syn
MMS19L
resolver
hgnc
HGNC:13824
resolver
uniprot
B0QZ75
resolver
uniprot
B3KPE5
resolver
uniprot
B4DQX2
resolver
uniprot
B4E2I3
resolver
uniprot
D3DR55
resolver
uniprot
F8W9Y2
resolver
uniprot
Q17RZ8
resolver
uniprot
Q5T455
resolver
uniprot
Q66K82
resolver
uniprot
Q7L4W8
resolver
uniprot
Q969Z1
resolver
uniprot
Q96DF1
resolver
uniprot
Q96MR1
resolver
uniprot
Q96RK5
resolver
uniprot
Q96SK1
resolver
uniprot
Q9BUE2
resolver
uniprot
Q9BYS9
resolver
uniprot_entry
MMS19_HUMAN
resolver
uniprot_sec
B0QZ75
resolver
uniprot_sec
B3KPE5
resolver
uniprot_sec
B4DQX2
resolver
uniprot_sec
B4E2I3
resolver
uniprot_sec
D3DR55
resolver
uniprot_sec
F8W9Y2
resolver
uniprot_sec
Q17RZ8
resolver
uniprot_sec
Q5T455
resolver
uniprot_sec
Q66K82
resolver
uniprot_sec
Q7L4W8
resolver
uniprot_sec
Q969Z1
resolver
uniprot_sec
Q96DF1
resolver
uniprot_sec
Q96MR1
resolver
uniprot_sec
Q96RK5
resolver
uniprot_sec
Q96SK1
resolver
uniprot_sec
Q9BUE2
resolver
uniprot_sec
Q9BYS9
resolver
amino_acid_sequence
MAAAAAVEAAAPMGALWGLVHDFVVGQQEGPADQVAADVKSGNYTVLQVVEALGSSLENPEPRTRARAIQLLSQVLLHCHTLLLEKEVVHLILFYENRLKDHHLVIPSVLQGLKALSLCVALPPGLAVSVLKAIFQEVHVQSLPQVDRHTVYNIITNFMRTREEELKSLGADFTFGFIQVMDGEKDPRNLLVAFRIVHDLISRDYSLGPFVEELFEVTSCYFPIDFTPPPNDPHGIQREDLILSLRAVLASTPRFAEFLLPLLIEKVDSEVLSAKLDSLQTLNACCAVYGQKELKDFLPSLWASIRREVFQTASERVEAEGLAALHSLTACLSRSVLRADAEDLLDSFLSNILQDCRHHLCEPDMKLVWPSAKLLQAAAGASARACDSVTSNVLPLLLEQFHKHSQSSQRRTILEMLLGFLKLQQKWSYEDKDQRPLNGFKDQLCSLVFMALTDPSTQLQLVGIRTLTVLGAQPDLLSYEDLELAVGHLYRLSFLKEDSQSCRVAALEASGTLAALYPVAFSSHLVPKLAEELRVGESNLTNGDEPTQCSRHLCCLQALSAVSTHPSIVKETLPLLLQHLWQVNRGNMVAQSSDVIAVCQSLRQMAEKCQQDPESCWYFHQTAIPCLLALAVQASMPEKEPSVLRKVLLEDEVLAAMVSVIGTATTHLSPELAAQSVTHIVPLFLDGNVSFLPENSFPSRFQPFQDGSSGQRRLIALLMAFVCSLPRNVEIPQLNQLMRELLELSCCHSCPFSSTAAAKCFAGLLNKHPAGQQLDEFLQLAVDKVEAGLGSGPCRSQAFTLLLWVTKALVLRYHPLSSCLTARLMGLLSDPELGPAAADGFSLLMSDCTDVLTRAGHAEVRIMFRQRFFTDNVPALVQGFHAAPQDVKPNYLKGLSHVLNRLPKPVLLPELPTLLSLLLEALSCPDCVVQLSTLSCLQPLLLEAPQVMSLHVDTLVTKFLNLSSSPSMAVRIAALQCMHALTRLPTPVLLPYKPQVIRALAKPLDDKKRLVRKEAVSARGEWFLLGSPGS
uniprot
proteins
function
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 (PubMed:29848660). 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:22678361, PubMed:22678362, PubMed:23585563, PubMed:29225034). As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur (Fe-S) cluster assembly into ERCC2/XPD (PubMed:20797633). Together with CIAO2, facilitates the transfer of Fe-S clusters to the motor protein KIF4A, which ensures proper localization of KIF4A to mitotic machinery components to promote the progression of mitosis (PubMed:29848660). 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, ECO:0000269|PubMed:29848660}.
uniprot
proteins
mass_dalton
113290
uniprot
proteins
mutagenesis
MUTAGEN 993; /note="K->R: Impairs MAGEF1-NSMCE1-mediated polyubiquitination when associated with R-1002, 1007-R-R-1008 and R-1013."; /evidence="ECO:0000269|PubMed:29225034"; MUTAGEN 1002; /note="K->R: Impairs MAGEF1-NSMCE1-mediated polyubiquitination when associated with R-993, 1007-R-R-1008 and R-1013."; /evidence="ECO:0000269|PubMed:29225034"; MUTAGEN 1007..1008; /note="KK->RR: Impairs MAGEF1-NSMCE1-mediated polyubiquitination when associated with R-993, R-1002 and R-1013."; /evidence="ECO:0000269|PubMed:29225034"; MUTAGEN 1013; /note="K->R: Impairs MAGEF1-NSMCE1-mediated polyubiquitination when associated with R-993, R-1002 and 1007-R-R-1008."; /evidence="ECO:0000269|PubMed:29225034
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination by MAGEF1-NSMCE1 ubiquitin ligase complex leading to proteasomal degradation. {ECO:0000269|PubMed:29225034}.
uniprot
proteins
protein_family
MET18/MMS19 family
uniprot
proteins
pubmed
11071939
uniprot
proteins
pubmed
11279242
uniprot
proteins
pubmed
11328871
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20797633
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22678361
uniprot
proteins
pubmed
22678362
uniprot
proteins
pubmed
23585563
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
29225034
uniprot
proteins
pubmed
29848660
uniprot
proteins
pubmed
30742009
uniprot
proteins
sequence_length
1030
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20797633}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:29848660}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:29848660}. Note=In mitosis, enriched on centrosomes during prophase, localizes to the spindle during metaphase and surrounds compacted spindle midzone microtubules during telophase. {ECO:0000269|PubMed:29848660}.
uniprot
proteins