MMS19_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MMS19_MOUSE
• UniProt AC: Q9D071
• Protein Name: MMS19 nucleotide excision repair protein homolog
• Gene Name: Mms19
• Organism: Mus musculus (Mouse).
• Sequence Length: 1031
• 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. 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..
• Protein Sequence: MAAATGLEEAVAPMGALCGLVQDFVMGQQEGPADQVAADVKSGGYTVLQVVEALGSSLENAEPRTRARGAQLLSQVLLQCHSLLSEKEVVHLILFYENRLKDHHLVVPSVLQGLRALSMSVALPPGLAVSVLKAIFQEVHVQSLLQVDRHTVFSIITNFMRSREEELKGLGADFTFGFIQVMDGEKDPRNLLLAFRIVHDLISKDYSLGPFVEELFEVTSCYFPIDFTPPPNDPYGIQREDLILSLRAVLASTPRFAEFLLPLLIEKVDSEILSAKLDSLQTLNACCAVYGQKELKDFLPSLWASIRREVFQTASERVEAEGLAALHSLTACLSCSVLRADAEDLLGSFLSNILQDCRHHLCEPDMKLVWPSAKLLQAAAGASARACEHLTSNVLPLLLEQFHKHSQSNQRRTILEMILGFLKLQQKWSYEDRDERPLSSFKDQLCSLVFMALTDPSTQLQLVGIRTLTVLGAQPGLLSAEDLELAVGHLYRLTFLEEDSQSCRVAALEASGTLATLYPGAFSRHLLPKLAEELHKGESDVARADGPTKCSRHFRCLQALSAVSTHPSIVKETLPLLLQHLCQANKGNMVTESSEVVAVCQSLQQVAEKCQQDPESYWYFHKTAVPCLFALAVQASMPEKESSVLRKVLLEDEVLAALASVIGTATTHLSPELAAQSVTCIVPLFLDGNTSFLPENSFPDQFQPFQDGSSGQRRLVALLTAFVCSLPRNVEIPQLNRLMRELLKQSCGHSCPFSSTAATKCFAGLLNKQPPGQQLEEFLQLAVGTVEAGLASESSRDQAFTLLLWVTKALVLRYHPLSACLTTRLMGLLSDPELGCAAADGFSLLMSDCTDVLTRAGHADVRIMFRQRFFTDNVPALVQGFHAAPQDVKPNYLKGLSHVLNRLPKPVLLPELPTLLSLLLEALSCPDSVVQLSTLSCLQPLLLEAPQIMSLHVDTLVTKFLNLSSSYSMAVRIAALQCMHALTRLPTSVLLPYKSQVIRALAKPLDDKKRLVRKEAVSARGEWFLLGSPGS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAATGLEE ------CCCCCCHHH	19.67	-
372	Phosphorylation	DMKLVWPSAKLLQAA CHHHHHCCHHHHHHH	23.48	17203969
746	Phosphorylation	MRELLKQSCGHSCPF HHHHHHHHCCCCCCC	22.07	-
820	Glutathionylation	RYHPLSACLTTRLMG HHCHHHHHHHHHHHH	2.89	24333276
987	Phosphorylation	HALTRLPTSVLLPYK HHHHHCCCCHHHCCH	35.74	24719451
993	Phosphorylation	PTSVLLPYKSQVIRA CCCHHHCCHHHHHHH	24.20	24719451
1028	Phosphorylation	GEWFLLGSPGS---- CCEEECCCCCC----	26.51	29899451
1031	Phosphorylation	FLLGSPGS------- EECCCCCC-------	40.19	26643407

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of MMS19_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MMS19_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of MMS19_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CIAO1_HUMAN	CIAO1	physical	26496610
MIP18_HUMAN	FAM96B	physical	26496610
CDKAL_HUMAN	CDKAL1	physical	26496610
TDIF1_HUMAN	DNTTIP1	physical	26496610

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND MASSSPECTROMETRY.
PubMed: 17203969