Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  MMS19 nucleotide excision repair protein homolog  

UniProtKB / Swiss-Prot ID :  MMS19_HUMAN

Gene Name (Synonyms) : 
MMS19, MMS19L  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Cytoplasm, cytoskeleton, spindle. 

Protein Function :  May play a role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription by interacting with ERCC2/XPD and ERCC3/XPB helicases, both subunits of NER- transcription factor TFIIH. May also function as a transcriptional coactivator of estrogen receptor (ER). May be involved in regulation of ER activity by bridging TFIIH with ER or may facilitate TFIIH-mediated phosphorylation of ER in specific promoters and cell types. As part of the mitotic spindle- associated MMXD complex it plays a role in chromosome segregation. 

Protein Sequence MAAAAAVEAAAPMGALWGLVHDFVVGQQEGPADQVAADVKSGNYTVLQVVEALGSSLENPEPRTRARAIQ...
Predicted Secondary Structure CCCHHHHHHHHHHHHHHHHHHHHHHCCCCCCHHHHHHHHHHCCCHHHHHHHHHHHHHCCCCHHHHHHHHH...
Protein Variant
LocationDescription
68A -> G (in dbSNP:rs2275586). VAR_023448
98R -> W (in dbSNP:rs29001280). VAR_023449
197V -> I (in dbSNP:rs29001285). VAR_023450
306R -> H (in dbSNP:rs29001306). VAR_023451
365M -> V (in dbSNP:rs29001309). VAR_023452
409Q -> P (in dbSNP:rs29001311). VAR_023453
434Q -> E (in dbSNP:rs29001314). VAR_023454
526V -> I (in dbSNP:rs17112809). VAR_023455
558A -> V (in dbSNP:rs12360068). VAR_023456
790G -> D (in dbSNP:rs3740526). VAR_023457
983R -> H (in dbSNP:rs29001332). VAR_023458
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAAAA
---CCCHHH
19.67UniProtKB
Link-
273PhosphoserineSEVLSAKLD
HHHHHHHHH
28.65Phosphositeplus
Link-
373Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)WPSAKLLQA
HHHHHHHHH
54.81Phosphositeplus
Link-
496N6-acetyllysineLSFLKEDSQ
HHHHHCCCC
58.42HPRD
Link-
496N6-acetyllysineLSFLKEDSQ
HHHHHCCCC
58.42Phosphositeplus
Link-
496N6-acetyllysine.LSFLKEDSQ
HHHHHCCCC
58.42UniProtKB
Link-
888Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PQDVKPNYL
CCCCCCHHH
35.52Phosphositeplus
Link-
1027PhosphoserineFLLGSPGS
EECCCCCC
26.51HPRD
Link-
1027PhosphoserineFLLGSPGS
EECCCCCC
26.51Phosphositeplus
Link-
1027Phosphoserine.FLLGSPGS
EECCCCCC
26.51UniProtKB
Link-
1030PhosphoserineGSPGS
CCCCC
40.19HPRD
Link-
1030PhosphoserineGSPGS
CCCCC
40.19Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ESR1_HUMANin vitro
yeast 2-hybrid
HPRD:17579HPRD11279242
TF2H1_HUMANin vitro
in vivo
HPRD:17579HPRD11071939
ESR2_HUMANin vitro
yeast 2-hybrid
HPRD:17579HPRD11279242
NCOA3_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:17579HPRD11279242
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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
ReferencePubMed
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures