TR112_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TR112_HUMAN
• UniProt AC: Q9UI30
• Protein Name: Multifunctional methyltransferase subunit TRM112-like protein
• Gene Name: TRMT112
• Organism: Homo sapiens (Human).
• Sequence Length: 125
• Subcellular Localization: Nucleus, nucleoplasm . Cytoplasm, perinuclear region . Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes (PubMed:25851604).
• Protein Description: Acts as an activator of both rRNA/tRNA and protein methyltransferases. [PubMed: 25851604 Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA]
• Protein Sequence: MKLLTHNLLSSHVRGVGSRGFPLRLQATEVRICPVEFNPNFVARMIPKVEWSAFLEAADNLRLIQVPKGPVEGYEENEEFLRTMHHLLLEVEVIEGTLQCPESGRMFPISRGIPNMLLSEEETES

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	Ubiquitination	------MKLLTHNLL ------CCCHHHHHH	52.80	21890473
2	Sumoylation	------MKLLTHNLL ------CCCHHHHHH	52.80	-
2	Sumoylation	------MKLLTHNLL ------CCCHHHHHH	52.80	-
5	Phosphorylation	---MKLLTHNLLSSH ---CCCHHHHHHHHH	21.10	26074081
10	Phosphorylation	LLTHNLLSSHVRGVG CHHHHHHHHHCCCCC	22.89	26074081
11	Phosphorylation	LTHNLLSSHVRGVGS HHHHHHHHHCCCCCC	26.43	26074081
14	Methylation	NLLSSHVRGVGSRGF HHHHHHCCCCCCCCC	28.76	54556837
24	Methylation	GSRGFPLRLQATEVR CCCCCCCEEEECEEE	25.62	115480001
33	S-nitrosylation	QATEVRICPVEFNPN EECEEEEECCCCCCC	1.85	19483679
33	Glutathionylation	QATEVRICPVEFNPN EECEEEEECCCCCCC	1.85	22555962
33	S-nitrosocysteine	QATEVRICPVEFNPN EECEEEEECCCCCCC	1.85	-
48	Ubiquitination	FVARMIPKVEWSAFL HHHCCCCEECHHHHH	41.69	21906983
68	Ubiquitination	LRLIQVPKGPVEGYE EEEEECCCCCCCCCH	76.59	21906983
74	Phosphorylation	PKGPVEGYEENEEFL CCCCCCCCHHCHHHH	13.43	22817900
103	Phosphorylation	GTLQCPESGRMFPIS EEEECCCCCCEEEEC	19.49	26074081
110	Phosphorylation	SGRMFPISRGIPNML CCCEEEECCCCCCCC	25.37	26074081
119	Phosphorylation	GIPNMLLSEEETES- CCCCCCCCHHHHCC-	38.71	30266825
123	Phosphorylation	MLLSEEETES----- CCCCHHHHCC-----	44.82	30266825
125	Phosphorylation	LSEEETES------- CCHHHHCC-------	53.60	30266825

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

Oops, there are no upstream regulatory protein records of TR112_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TR112_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TR112_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAND1_HUMAN	CAND1	physical	22863883
IPO7_HUMAN	IPO7	physical	22863883
SCOC_HUMAN	SCOC	physical	26344197

Drug and Disease Associations

• 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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASSSPECTROMETRY.
PubMed: 19690332

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASSSPECTROMETRY.
PubMed: 18669648