TRI45_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRI45_HUMAN
• UniProt AC: Q9H8W5
• Protein Name: Tripartite motif-containing protein 45
• Gene Name: TRIM45
• Organism: Homo sapiens (Human).
• Sequence Length: 580
• Subcellular Localization: Cytoplasm . Nucleus .
• Protein Description: May act as a transcriptional repressor in mitogen-activated protein kinase signaling pathway..
• Protein Sequence: MSENRKPLLGFVSKLTSGTALGNSGKTHCPLCLGLFKAPRLLPCLHTVCTTCLEQLEPFSVVDIRGGDSDTSSEGSIFQELKPRSLQSQIGILCPVCDAQVDLPMGGVKALTIDHLAVNDVMLESLRGEGQGLVCDLCNDREVEKRCQTCKANLCHFCCQAHRRQKKTTYHTMVDLKDLKGYSRIGKPILCPVHPAEELRLFCEFCDRPVCQDCVVGEHREHPCDFTSNVIHKHGDSVWELLKGTQPHVEALEEALAQIHIINSALQKRVEAVAADVRTFSEGYIKAIEEHRDKLLKQLEDIRAQKENSLQLQKAQLEQLLADMRTGVEFTEHLLTSGSDLEILITKRVVVERLRKLNKVQYSTRPGVNDKIRFCPQEKAGQCRGYEIYGTINTKEVDPAKCVLQGEDLHRAREKQTASFTLLCKDAAGEIMGRGGDNVQVAVVPKDKKDSPVRTMVQDNKDGTYYISYTPKEPGVYTVWVCIKEQHVQGSPFTVMVRRKHRPHSGVFHCCTFCSSGGQKTARCACGGTMPGGYLGCGHGHKGHPGHPHWSCCGKFNEKSECTWTGGQSAPRSLLRTVAL

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	Phosphorylation	------MSENRKPLL ------CCCCCCCCH	43.51	26074081
13	Phosphorylation	KPLLGFVSKLTSGTA CCCHHHHHHHCCCCC	21.49	26074081
50	Phosphorylation	PCLHTVCTTCLEQLE HHHHHHHHHHHHHCC	19.06	18452278
168	Phosphorylation	AHRRQKKTTYHTMVD HHHHCCCCEEEEEEE	39.35	29083192
169	Phosphorylation	HRRQKKTTYHTMVDL HHHCCCCEEEEEEEH	23.37	29083192
170	Phosphorylation	RRQKKTTYHTMVDLK HHCCCCEEEEEEEHH	10.67	29083192
172	Phosphorylation	QKKTTYHTMVDLKDL CCCCEEEEEEEHHHC	14.42	29083192
267	Ubiquitination	HIINSALQKRVEAVA HHHHHHHHHHHHHHH	31.09	22817900
279	Phosphorylation	AVAADVRTFSEGYIK HHHCCHHHHCHHHHH	31.21	24275569
306	Ubiquitination	LEDIRAQKENSLQLQ HHHHHHHHHHCHHHH	58.85	29967540
371	Ubiquitination	TRPGVNDKIRFCPQE CCCCCCCCEEECCHH	30.49	22817900
465	Phosphorylation	QDNKDGTYYISYTPK EECCCCEEEEEECCC	12.34	28331001
466	Phosphorylation	DNKDGTYYISYTPKE ECCCCEEEEEECCCC	5.34	28331001
470	Phosphorylation	GTYYISYTPKEPGVY CEEEEEECCCCCCEE	22.54	28331001
491	Phosphorylation	KEQHVQGSPFTVMVR EECCCCCCCEEEEEE	10.35	-
521	Phosphorylation	CSSGGQKTARCACGG ECCCCCEEEEEECCC	16.08	-
551	Phosphorylation	HPGHPHWSCCGKFNE CCCCCCCCCCCCCCC	9.11	-

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

Oops, there are no upstream regulatory protein records of TRI45_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRI45_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 TRI45_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UB2D1_HUMAN	UBE2D1	physical	21143188
UB2D2_HUMAN	UBE2D2	physical	21143188
UB2D3_HUMAN	UBE2D3	physical	21143188
UB2D4_HUMAN	UBE2D4	physical	21143188
UB2E1_HUMAN	UBE2E1	physical	21143188
UB2E2_HUMAN	UBE2E2	physical	21143188
UB2E3_HUMAN	UBE2E3	physical	21143188
RACK1_HUMAN	GNB2L1	physical	24681954
TRI45_HUMAN	TRIM45	physical	24681954
UBE2B_HUMAN	UBE2B	physical	24681954
P53_HUMAN	TP53	physical	28542145

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

Ubiquitylation

"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-371, AND MASSSPECTROMETRY.
PubMed: 17370265