CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019666
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 MMS19 nucleotide excision repair protein homolog 
Protein Synonyms/Alias
 hMMS19; MET18 homolog; MMS19-like protein 
Gene Name
 MMS19 
Gene Synonyms/Alias
 MMS19L 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
275DSEVLSAKLDSLQTLubiquitination[1]
295VYGQKELKDFLPSLWubiquitination[1]
366HLCEPDMKLVWPSAKubiquitination[1]
373KLVWPSAKLLQAAAGubiquitination[1, 2, 3, 4, 5]
496LYRLSFLKEDSQSCRacetylation[6]
496LYRLSFLKEDSQSCRubiquitination[1]
888HAAPQDVKPNYLKGLubiquitination[1, 3]
993TPVLLPYKPQVIRALubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional 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) and RNA polymerase II (POL II) transcription. 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. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery. 
Sequence Annotation
 REPEAT 43 81 HEAT 1.
 REPEAT 253 291 HEAT 2.
 REPEAT 387 426 HEAT 3.
 REPEAT 866 904 HEAT 4.
 REPEAT 908 946 HEAT 5.
 REPEAT 949 987 HEAT 6.
 REPEAT 990 1028 HEAT 7.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 371 371 Phosphoserine (By similarity).
 MOD_RES 496 496 N6-acetyllysine.
 MOD_RES 1027 1027 Phosphoserine.  
Keyword
 Acetylation; Activator; Alternative splicing; Chromosome partition; Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1030 AA 
Protein Sequence
MAAAAAVEAA APMGALWGLV HDFVVGQQEG PADQVAADVK SGNYTVLQVV EALGSSLENP 60
EPRTRARAIQ LLSQVLLHCH TLLLEKEVVH LILFYENRLK DHHLVIPSVL QGLKALSLCV 120
ALPPGLAVSV LKAIFQEVHV QSLPQVDRHT VYNIITNFMR TREEELKSLG ADFTFGFIQV 180
MDGEKDPRNL LVAFRIVHDL ISRDYSLGPF VEELFEVTSC YFPIDFTPPP NDPHGIQRED 240
LILSLRAVLA STPRFAEFLL PLLIEKVDSE VLSAKLDSLQ TLNACCAVYG QKELKDFLPS 300
LWASIRREVF QTASERVEAE GLAALHSLTA CLSRSVLRAD AEDLLDSFLS NILQDCRHHL 360
CEPDMKLVWP SAKLLQAAAG ASARACDSVT SNVLPLLLEQ FHKHSQSSQR RTILEMLLGF 420
LKLQQKWSYE DKDQRPLNGF KDQLCSLVFM ALTDPSTQLQ LVGIRTLTVL GAQPDLLSYE 480
DLELAVGHLY RLSFLKEDSQ SCRVAALEAS GTLAALYPVA FSSHLVPKLA EELRVGESNL 540
TNGDEPTQCS RHLCCLQALS AVSTHPSIVK ETLPLLLQHL WQVNRGNMVA QSSDVIAVCQ 600
SLRQMAEKCQ QDPESCWYFH QTAIPCLLAL AVQASMPEKE PSVLRKVLLE DEVLAAMVSV 660
IGTATTHLSP ELAAQSVTHI VPLFLDGNVS FLPENSFPSR FQPFQDGSSG QRRLIALLMA 720
FVCSLPRNVE IPQLNQLMRE LLELSCCHSC PFSSTAAAKC FAGLLNKHPA GQQLDEFLQL 780
AVDKVEAGLG SGPCRSQAFT LLLWVTKALV LRYHPLSSCL TARLMGLLSD PELGPAAADG 840
FSLLMSDCTD VLTRAGHAEV RIMFRQRFFT DNVPALVQGF HAAPQDVKPN YLKGLSHVLN 900
RLPKPVLLPE LPTLLSLLLE ALSCPDCVVQ LSTLSCLQPL LLEAPQVMSL HVDTLVTKFL 960
NLSSSPSMAV RIAALQCMHA LTRLPTPVLL PYKPQVIRAL AKPLDDKKRL VRKEAVSARG 1020
EWFLLGSPGS 1030 
Gene Ontology
 GO:0097361; C:CIA complex; IDA:UniProtKB.
 GO:0005675; C:holo TFIIH complex; NAS:UniProtKB.
 GO:0071817; C:MMXD complex; IDA:UniProtKB.
 GO:0030674; F:protein binding, bridging; NAS:UniProtKB.
 GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
 GO:0007059; P:chromosome segregation; IMP:UniProtKB.
 GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
 GO:0006289; P:nucleotide-excision repair; NAS:UniProtKB.
 GO:0000160; P:phosphorelay signal transduction system; NAS:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IMP:UniProtKB.
 GO:0009725; P:response to hormone stimulus; NAS:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0006351; P:transcription, DNA-dependent; NAS:UniProtKB. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR024687; Tscrpt_MMS19_N. 
Pfam
 PF12460; MMS19_N 
SMART
  
PROSITE
 PS50077; HEAT_REPEAT 
PRINTS