| UniProt ID | MMS19_HUMAN | |
|---|---|---|
| UniProt AC | Q96T76 | |
| Protein Name | MMS19 nucleotide excision repair protein homolog | |
| Gene Name | MMS19 {ECO:0000312|HGNC:HGNC:13824} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 1030 | |
| Subcellular Localization | Nucleus . Cytoplasm, cytoskeleton, spindle . | |
| Protein Description | 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] | |
| Protein Sequence | MAAAAAVEAAAPMGALWGLVHDFVVGQQEGPADQVAADVKSGNYTVLQVVEALGSSLENPEPRTRARAIQLLSQVLLHCHTLLLEKEVVHLILFYENRLKDHHLVIPSVLQGLKALSLCVALPPGLAVSVLKAIFQEVHVQSLPQVDRHTVYNIITNFMRTREEELKSLGADFTFGFIQVMDGEKDPRNLLVAFRIVHDLISRDYSLGPFVEELFEVTSCYFPIDFTPPPNDPHGIQREDLILSLRAVLASTPRFAEFLLPLLIEKVDSEVLSAKLDSLQTLNACCAVYGQKELKDFLPSLWASIRREVFQTASERVEAEGLAALHSLTACLSRSVLRADAEDLLDSFLSNILQDCRHHLCEPDMKLVWPSAKLLQAAAGASARACDSVTSNVLPLLLEQFHKHSQSSQRRTILEMLLGFLKLQQKWSYEDKDQRPLNGFKDQLCSLVFMALTDPSTQLQLVGIRTLTVLGAQPDLLSYEDLELAVGHLYRLSFLKEDSQSCRVAALEASGTLAALYPVAFSSHLVPKLAEELRVGESNLTNGDEPTQCSRHLCCLQALSAVSTHPSIVKETLPLLLQHLWQVNRGNMVAQSSDVIAVCQSLRQMAEKCQQDPESCWYFHQTAIPCLLALAVQASMPEKEPSVLRKVLLEDEVLAAMVSVIGTATTHLSPELAAQSVTHIVPLFLDGNVSFLPENSFPSRFQPFQDGSSGQRRLIALLMAFVCSLPRNVEIPQLNQLMRELLELSCCHSCPFSSTAAAKCFAGLLNKHPAGQQLDEFLQLAVDKVEAGLGSGPCRSQAFTLLLWVTKALVLRYHPLSSCLTARLMGLLSDPELGPAAADGFSLLMSDCTDVLTRAGHAEVRIMFRQRFFTDNVPALVQGFHAAPQDVKPNYLKGLSHVLNRLPKPVLLPELPTLLSLLLEALSCPDCVVQLSTLSCLQPLLLEAPQVMSLHVDTLVTKFLNLSSSPSMAVRIAALQCMHALTRLPTPVLLPYKPQVIRALAKPLDDKKRLVRKEAVSARGEWFLLGSPGS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAAAAAVEA ------CHHHHHHHH | 19.67 | 25944712 | |
| 9 | Ubiquitination | AAAAAVEAAAPMGAL HHHHHHHHHHHHHHH | 11.43 | 21890473 | |
| 74 | Ubiquitination | RAIQLLSQVLLHCHT HHHHHHHHHHHHHHH | 29.82 | 21963094 | |
| 81 | Ubiquitination | QVLLHCHTLLLEKEV HHHHHHHHHHHCHHH | 25.21 | 21963094 | |
| 95 | Ubiquitination | VVHLILFYENRLKDH HHHHHHHCCCCCCCC | 14.62 | 22505724 | |
| 117 | Ubiquitination | LQGLKALSLCVALPP HHHHHHHHHHHHCCC | 25.28 | 21963094 | |
| 132 | Ubiquitination | GLAVSVLKAIFQEVH CHHHHHHHHHHHHHH | 36.96 | 21963094 | |
| 134 | Ubiquitination | AVSVLKAIFQEVHVQ HHHHHHHHHHHHHHH | 3.33 | 29967540 | |
| 164 | Ubiquitination | NFMRTREEELKSLGA HHHHHCHHHHHHCCC | 66.40 | 30230243 | |
| 172 | Ubiquitination | ELKSLGADFTFGFIQ HHHHCCCCEEEEEEE | 41.12 | 21890473 | |
| 215 | Ubiquitination | GPFVEELFEVTSCYF HHHHHHHHHHEEEEC | 8.86 | 23000965 | |
| 232 | Ubiquitination | DFTPPPNDPHGIQRE CCCCCCCCCCCCCHH | 42.20 | 21963094 | |
| 249 | Ubiquitination | ILSLRAVLASTPRFA HHHHHHHHHCCHHHH | 2.80 | 29967540 | |
| 252 | Phosphorylation | LRAVLASTPRFAEFL HHHHHHCCHHHHHHH | 16.93 | 24825855 | |
| 268 | Ubiquitination | PLLIEKVDSEVLSAK HHHHHHCCHHHHHHH | 50.58 | 29967540 | |
| 269 | Phosphorylation | LLIEKVDSEVLSAKL HHHHHCCHHHHHHHH | 32.37 | 21406692 | |
| 271 | Ubiquitination | IEKVDSEVLSAKLDS HHHCCHHHHHHHHHH | 6.23 | 21963094 | |
| 273 | Phosphorylation | KVDSEVLSAKLDSLQ HCCHHHHHHHHHHHH | 28.65 | 21406692 | |
| 275 | Ubiquitination | DSEVLSAKLDSLQTL CHHHHHHHHHHHHHH | 49.83 | 21963094 | |
| 292 | Ubiquitination | CCAVYGQKELKDFLP HHHHHCHHHHHHHHH | 61.73 | 29967540 | |
| 295 | Ubiquitination | VYGQKELKDFLPSLW HHCHHHHHHHHHHHH | 47.74 | 21963094 | |
| 314 | Ubiquitination | REVFQTASERVEAEG HHHHHHHHHHHHHHH | 29.35 | 21963094 | |
| 327 | Phosphorylation | EGLAALHSLTACLSR HHHHHHHHHHHHHCC | 28.41 | 21406692 | |
| 328 | Ubiquitination | GLAALHSLTACLSRS HHHHHHHHHHHHCCH | 2.15 | 29967540 | |
| 329 | Phosphorylation | LAALHSLTACLSRSV HHHHHHHHHHHCCHH | 20.52 | 21406692 | |
| 330 | Ubiquitination | AALHSLTACLSRSVL HHHHHHHHHHCCHHH | 9.50 | 23000965 | |
| 333 | Phosphorylation | HSLTACLSRSVLRAD HHHHHHHCCHHHHCC | 23.53 | 21406692 | |
| 338 | Ubiquitination | CLSRSVLRADAEDLL HHCCHHHHCCHHHHH | 28.41 | 21963094 | |
| 366 | Acetylation | HLCEPDMKLVWPSAK HHCCCCHHHHHCCHH | 47.47 | 25953088 | |
| 366 | Ubiquitination | HLCEPDMKLVWPSAK HHCCCCHHHHHCCHH | 47.47 | - | |
| 369 | Ubiquitination | EPDMKLVWPSAKLLQ CCCHHHHHCCHHHHH | 7.49 | 21890473 | |
| 370 | Ubiquitination | PDMKLVWPSAKLLQA CCHHHHHCCHHHHHH | 19.55 | 30230243 | |
| 371 | Phosphorylation | DMKLVWPSAKLLQAA CHHHHHCCHHHHHHH | 23.48 | 20860994 | |
| 373 | Ubiquitination | KLVWPSAKLLQAAAG HHHHCCHHHHHHHHH | 54.81 | 21890473 | |
| 373 | Ubiquitination | KLVWPSAKLLQAAAG HHHHCCHHHHHHHHH | 54.81 | 21890473 | |
| 373 | Ubiquitination | KLVWPSAKLLQAAAG HHHHCCHHHHHHHHH | 54.81 | 23000965 | |
| 373 (in isoform 1) | Ubiquitination | - | 54.81 | 21890473 | |
| 382 | Phosphorylation | LQAAAGASARACDSV HHHHHHHCHHHHHHH | 19.85 | 20860994 | |
| 383 | Ubiquitination | QAAAGASARACDSVT HHHHHHCHHHHHHHH | 11.53 | 29967540 | |
| 394 | Ubiquitination | DSVTSNVLPLLLEQF HHHHHCHHHHHHHHH | 2.64 | 21890473 | |
| 398 | Ubiquitination | SNVLPLLLEQFHKHS HCHHHHHHHHHHHCC | 6.82 | 21963094 | |
| 412 | Ubiquitination | SQSSQRRTILEMLLG CHHHHHHHHHHHHHH | 31.91 | 21890473 | |
| 426 | Ubiquitination | GFLKLQQKWSYEDKD HHHHHHHHCCCCCCC | 25.75 | 29967540 | |
| 428 | Phosphorylation | LKLQQKWSYEDKDQR HHHHHHCCCCCCCCC | 26.19 | 22673903 | |
| 429 | Phosphorylation | KLQQKWSYEDKDQRP HHHHHCCCCCCCCCC | 27.34 | 22673903 | |
| 430 | Ubiquitination | LQQKWSYEDKDQRPL HHHHCCCCCCCCCCC | 53.74 | 30230243 | |
| 437 | Ubiquitination | EDKDQRPLNGFKDQL CCCCCCCCCCHHHHH | 12.18 | 21963094 | |
| 453 | Acetylation | SLVFMALTDPSTQLQ HHHHHHHCCCCHHHH | 36.00 | 19608861 | |
| 453 | Ubiquitination | SLVFMALTDPSTQLQ HHHHHHHCCCCHHHH | 36.00 | 21963094 | |
| 472 | Ubiquitination | RTLTVLGAQPDLLSY EEEEECCCCCCCCCH | 17.36 | 21963094 | |
| 473 | Ubiquitination | TLTVLGAQPDLLSYE EEEECCCCCCCCCHH | 30.18 | 21963094 | |
| 485 | Ubiquitination | SYEDLELAVGHLYRL CHHHHHHHHHHHHHH | 8.89 | 30230243 | |
| 492 | Ubiquitination | AVGHLYRLSFLKEDS HHHHHHHHHCCCCCC | 2.41 | 21963094 | |
| 493 | Phosphorylation | VGHLYRLSFLKEDSQ HHHHHHHHCCCCCCC | 21.38 | 24719451 | |
| 496 | Acetylation | LYRLSFLKEDSQSCR HHHHHCCCCCCCCHH | 58.42 | 19608861 | |
| 496 | Malonylation | LYRLSFLKEDSQSCR HHHHHCCCCCCCCHH | 58.42 | 26320211 | |
| 496 | Ubiquitination | LYRLSFLKEDSQSCR HHHHHCCCCCCCCHH | 58.42 | 21963094 | |
| 499 | Phosphorylation | LSFLKEDSQSCRVAA HHCCCCCCCCHHHEE | 25.69 | 23312004 | |
| 501 | Phosphorylation | FLKEDSQSCRVAALE CCCCCCCCHHHEEHH | 14.08 | 23312004 | |
| 510 | Phosphorylation | RVAALEASGTLAALY HHEEHHHHCCHHHHH | 23.96 | 23312004 | |
| 512 | Phosphorylation | AALEASGTLAALYPV EEHHHHCCHHHHHHH | 15.66 | 23312004 | |
| 517 | Phosphorylation | SGTLAALYPVAFSSH HCCHHHHHHHHHCCC | 7.31 | 23312004 | |
| 522 | Phosphorylation | ALYPVAFSSHLVPKL HHHHHHHCCCHHHHH | 13.70 | 23312004 | |
| 523 | Phosphorylation | LYPVAFSSHLVPKLA HHHHHHCCCHHHHHH | 17.87 | 23312004 | |
| 523 | Ubiquitination | LYPVAFSSHLVPKLA HHHHHHCCCHHHHHH | 17.87 | 21963094 | |
| 524 | Ubiquitination | YPVAFSSHLVPKLAE HHHHHCCCHHHHHHH | 29.64 | 21963094 | |
| 528 | Ubiquitination | FSSHLVPKLAEELRV HCCCHHHHHHHHHCC | 53.50 | 30230243 | |
| 535 | Ubiquitination | KLAEELRVGESNLTN HHHHHHCCCCCCCCC | 18.23 | 21963094 | |
| 567 | Ubiquitination | SAVSTHPSIVKETLP HHHHCCHHHHHHHHH | 32.20 | 30230243 | |
| 588 | Sulfoxidation | WQVNRGNMVAQSSDV HHHCCCCCCCCHHHH | 2.69 | 21406390 | |
| 591 | Ubiquitination | NRGNMVAQSSDVIAV CCCCCCCCHHHHHHH | 31.87 | 24816145 | |
| 592 | Ubiquitination | RGNMVAQSSDVIAVC CCCCCCCHHHHHHHH | 20.83 | 24816145 | |
| 629 | Ubiquitination | TAIPCLLALAVQASM HHHHHHHHHHHHHCC | 4.78 | 30230243 | |
| 642 | Ubiquitination | SMPEKEPSVLRKVLL CCCCCCCCHHHHHHC | 34.57 | 24816145 | |
| 643 | Ubiquitination | MPEKEPSVLRKVLLE CCCCCCCHHHHHHCC | 9.79 | 24816145 | |
| 687 | Ubiquitination | IVPLFLDGNVSFLPE EEEEECCCCCCCCCC | 38.29 | 21963094 | |
| 729 | Ubiquitination | VCSLPRNVEIPQLNQ HHCCCCCCCCHHHHH | 8.13 | 21963094 | |
| 730 | Ubiquitination | CSLPRNVEIPQLNQL HCCCCCCCCHHHHHH | 53.12 | 21963094 | |
| 789 | Ubiquitination | VDKVEAGLGSGPCRS HHHHHHCCCCCCHHH | 6.77 | 21963094 | |
| 790 | Ubiquitination | DKVEAGLGSGPCRSQ HHHHHCCCCCCHHHH | 29.64 | 21963094 | |
| 790 (in isoform 5) | Ubiquitination | - | 29.64 | 21906983 | |
| 806 | Ubiquitination | FTLLLWVTKALVLRY HHHHHHHHHHHHHHH | 10.06 | 24816145 | |
| 829 | Ubiquitination | ARLMGLLSDPELGPA HHHHHHHCCCCCCHH | 57.04 | 21963094 | |
| 834 | Ubiquitination | LLSDPELGPAAADGF HHCCCCCCHHHHHHH | 14.24 | 30230243 | |
| 835 | Ubiquitination | LSDPELGPAAADGFS HCCCCCCHHHHHHHH | 31.20 | 30230243 | |
| 844 | Ubiquitination | AADGFSLLMSDCTDV HHHHHHHHHHCCHHH | 2.75 | 21963094 | |
| 845 | Ubiquitination | ADGFSLLMSDCTDVL HHHHHHHHHCCHHHH | 3.73 | 21963094 | |
| 848 | Ubiquitination | FSLLMSDCTDVLTRA HHHHHHCCHHHHHHC | 2.47 | 24816145 | |
| 849 | Ubiquitination | SLLMSDCTDVLTRAG HHHHHCCHHHHHHCC | 33.85 | 24816145 | |
| 884 | Ubiquitination | VQGFHAAPQDVKPNY HCCCCCCCCCCCCCH | 31.52 | 21963094 | |
| 887 | Ubiquitination | FHAAPQDVKPNYLKG CCCCCCCCCCCHHHH | 10.53 | 21963094 | |
| 888 | Ubiquitination | HAAPQDVKPNYLKGL CCCCCCCCCCHHHHH | 35.52 | 21963094 | |
| 895 | Ubiquitination | KPNYLKGLSHVLNRL CCCHHHHHHHHHHHC | 2.82 | 30230243 | |
| 896 | Phosphorylation | PNYLKGLSHVLNRLP CCHHHHHHHHHHHCC | 21.88 | 20068231 | |
| 908 | Ubiquitination | RLPKPVLLPELPTLL HCCCCCCCCCHHHHH | 2.93 | 24816145 | |
| 909 | Ubiquitination | LPKPVLLPELPTLLS CCCCCCCCCHHHHHH | 36.60 | 24816145 | |
| 926 | Ubiquitination | LEALSCPDCVVQLST HHHCCCCCHHHHHHH | 42.02 | 21963094 | |
| 927 | Ubiquitination | EALSCPDCVVQLSTL HHCCCCCHHHHHHHH | 1.63 | 21963094 | |
| 948 | Ubiquitination | LLEAPQVMSLHVDTL HHHCCCHHEEEHHHH | 2.73 | 24816145 | |
| 950 | Ubiquitination | EAPQVMSLHVDTLVT HCCCHHEEEHHHHHH | 2.17 | 30230243 | |
| 963 | Phosphorylation | VTKFLNLSSSPSMAV HHHHHCCCCCHHHHH | 27.91 | 20071362 | |
| 963 | Ubiquitination | VTKFLNLSSSPSMAV HHHHHCCCCCHHHHH | 27.91 | 24816145 | |
| 964 | Phosphorylation | TKFLNLSSSPSMAVR HHHHCCCCCHHHHHH | 49.81 | 20071362 | |
| 964 | Ubiquitination | TKFLNLSSSPSMAVR HHHHCCCCCHHHHHH | 49.81 | 24816145 | |
| 965 | Phosphorylation | KFLNLSSSPSMAVRI HHHCCCCCHHHHHHH | 20.02 | 21712546 | |
| 967 | Phosphorylation | LNLSSSPSMAVRIAA HCCCCCHHHHHHHHH | 22.71 | 21712546 | |
| 992 | Phosphorylation | PTPVLLPYKPQVIRA CCCCCCCCCHHHHHH | 34.96 | 28152594 | |
| 993 | Ubiquitination | TPVLLPYKPQVIRAL CCCCCCCCHHHHHHH | 27.34 | PubMed | |
| 1002 | Ubiquitination | QVIRALAKPLDDKKR HHHHHHHCCCCCHHH | 47.14 | PubMed | |
| 1003 | Ubiquitination | VIRALAKPLDDKKRL HHHHHHCCCCCHHHH | 35.10 | 24816145 | |
| 1006 | Ubiquitination | ALAKPLDDKKRLVRK HHHCCCCCHHHHHHH | 67.09 | 24816145 | |
| 1007 | Ubiquitination | LAKPLDDKKRLVRKE HHCCCCCHHHHHHHH | 39.19 | PubMed | |
| 1013 | Ubiquitination | DKKRLVRKEAVSARG CHHHHHHHHHHHHCC | 42.41 | PubMed | |
| 1017 | Phosphorylation | LVRKEAVSARGEWFL HHHHHHHHHCCCEEE | 21.21 | - | |
| 1027 | Phosphorylation | GEWFLLGSPGS---- CCEEECCCCCC---- | 26.51 | 25159151 | |
| 1030 | Phosphorylation | FLLGSPGS------- EECCCCCC------- | 40.19 | 25159151 | |
| 1032 | Ubiquitination | LGSPGS--------- CCCCCC--------- | 30230243 | ||
| 1045 | Ubiquitination | ---------------------- ---------------------- | 24816145 | ||
| 1046 | Ubiquitination | ----------------------- ----------------------- | 24816145 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of MMS19_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MMS19_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of MMS19_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-496, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, AND MASSSPECTROMETRY. | |
