dbPTM

CTU1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CTU1_HUMAN
UniProt AC	Q7Z7A3
Protein Name	Cytoplasmic tRNA 2-thiolation protein 1 {ECO:0000255\|HAMAP-Rule:MF_03053}
Gene Name	CTU1 {ECO:0000255\|HAMAP-Rule:MF_03053}
Organism	Homo sapiens (Human).
Sequence Length	348
Subcellular Localization	Cytoplasm.
Protein Description	Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position..
Protein Sequence	MPAPPCASCHAARAALRRPLSGQALCGACFCAAFEAEVLHTVLAGRLLPPGAVVAVGASGGKDSTVLAHVLRALAPRLGISLQLVAVDEGIGGYRDAALAAVRRQAARWELPLTVVAYEDLFGGWTMDAVARSTAGSGRSRSCCTFCGVLRRRALEEGARRVGATHIVTGHNADDMAETVLMNFLRGDAGRLARGGGLGSPGEGGALPRCRPLQFASQKEVVLYAHFRRLDYFSEECVYAPEAFRGHARDLLKRLEAARPSAVLDLVHSAERLALAPAARPPRPGACSRCGALASRALCQACALLDGLNRGRPRLAIGKGRRGLDEEATPGTPGDPARPPASKAVPTF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
81	Phosphorylation	LAPRLGISLQLVAVD HHHHHCCEEEEEEEE	14.31	-
94	Phosphorylation	VDEGIGGYRDAALAA EECCCCCHHHHHHHH	10.50	-
126	Phosphorylation	EDLFGGWTMDAVARS EHHHCCCCHHHHHHC	14.40	26074081
133	Phosphorylation	TMDAVARSTAGSGRS CHHHHHHCCCCCCCC	16.93	26074081
134	Phosphorylation	MDAVARSTAGSGRSR HHHHHHCCCCCCCCH	29.50	26074081
137	Phosphorylation	VARSTAGSGRSRSCC HHHCCCCCCCCHHHH	28.68	26074081
140	Phosphorylation	STAGSGRSRSCCTFC CCCCCCCCHHHHHHH	31.88	26074081
142	Phosphorylation	AGSGRSRSCCTFCGV CCCCCCHHHHHHHHH	18.13	26074081
145	Phosphorylation	GRSRSCCTFCGVLRR CCCHHHHHHHHHHHH	26.70	26074081
194	Methylation	GDAGRLARGGGLGSP CCHHHHHCCCCCCCC	49.21	-
200	Phosphorylation	ARGGGLGSPGEGGAL HCCCCCCCCCCCCCC	34.47	29255136
234	Phosphorylation	FRRLDYFSEECVYAP HHHCCCCCHHHCCCC	26.68	28348404
319	Ubiquitination	RPRLAIGKGRRGLDE CCCEEECCCCCCCCC	43.03	27667366
329	Phosphorylation	RGLDEEATPGTPGDP CCCCCCCCCCCCCCC	26.07	29255136
332	Phosphorylation	DEEATPGTPGDPARP CCCCCCCCCCCCCCC	25.87	29255136
342	Phosphorylation	DPARPPASKAVPTF- CCCCCCHHHCCCCC-	27.24	22199227
343	Ubiquitination	PARPPASKAVPTF-- CCCCCHHHCCCCC--	56.35	29967540

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of CTU1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CTU1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of CTU1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
URM1_HUMAN	URM1	physical	19017811
HSP74_HUMAN	HSPA4	physical	19017811
CTU2_HUMAN	CTU2	physical	19017811

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.

Regulatory Network of CTU1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-200, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-200, AND MASSSPECTROMETRY.	18691976 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.	16964243 [Abstract]