TGT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TGT_HUMAN
• UniProt AC: Q9BXR0
• Protein Name: Queuine tRNA-ribosyltransferase catalytic subunit 1 {ECO:0000255|HAMAP-Rule:MF_03218}
• Gene Name: QTRT1 {ECO:0000255|HAMAP-Rule:MF_03218}
• Organism: Homo sapiens (Human).
• Sequence Length: 403
• Subcellular Localization: Cytoplasm . Mitochondrion outer membrane ; Peripheral membrane protein ; Cytoplasmic side . Weakly associates with mitochondria, possibly via QTRT2.
• Protein Description: Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). [PubMed: 11255023]
• Protein Sequence: MAGAATQASLESAPRIMRLVAECSRSRARAGELWLPHGTVATPVFMPVGTQATMKGITTEQLDALGCRICLGNTYHLGLRPGPELIQKANGLHGFMNWPHNLLTDSGGFQMVSLVSLSEVTEEGVRFRSPYDGNETLLSPEKSVQIQNALGSDIIMQLDDVVSSTVTGPRVEEAMYRSIRWLDRCIAAHQRPDKQNLFAIIQGGLDADLRATCLEEMTKRDVPGFAIGGLSGGESKSQFWRMVALSTSRLPKDKPRYLMGVGYATDLVVCVALGCDMFDCVFPTRTARFGSALVPTGNLQLRKKVFEKDFGPIDPECTCPTCQKHSRAFLHALLHSDNTAALHHLTVHNIAYQLQLMSAVRTSIVEKRFPDFVRDFMGAMYGDPTLCPTWATDALASVGITLG

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	------MAGAATQAS ------CCCHHHHHH	19.14	22814378
6	Phosphorylation	--MAGAATQASLESA --CCCHHHHHHHHHH	24.92	25002506
9	Phosphorylation	AGAATQASLESAPRI CCHHHHHHHHHHHHH	23.89	28857561
12	Phosphorylation	ATQASLESAPRIMRL HHHHHHHHHHHHHHH	49.19	25002506
55	Ubiquitination	VGTQATMKGITTEQL CCCCCCCCCCCHHHH	42.69	-
55	Ubiquitination	VGTQATMKGITTEQL CCCCCCCCCCCHHHH	42.69	-
131	Phosphorylation	GVRFRSPYDGNETLL CCEECCCCCCCCCCC	37.42	27642862
136	Phosphorylation	SPYDGNETLLSPEKS CCCCCCCCCCCHHHH	36.68	21815630
139	Phosphorylation	DGNETLLSPEKSVQI CCCCCCCCHHHHHHH	33.84	25159151
219	Ubiquitination	TCLEEMTKRDVPGFA HHHHHHHHCCCCCEE	45.34	-
231	Phosphorylation	GFAIGGLSGGESKSQ CEEECCCCCCCCHHH	48.29	20068231
235	Phosphorylation	GGLSGGESKSQFWRM CCCCCCCCHHHHHHH	40.66	20068231
236	Ubiquitination	GLSGGESKSQFWRMV CCCCCCCHHHHHHHH	43.93	-
246	Phosphorylation	FWRMVALSTSRLPKD HHHHHHHHHCCCCCC	18.01	26437602
308	Ubiquitination	LRKKVFEKDFGPIDP EEHHHHHCCCCCCCC	47.06	-
324	Ubiquitination	CTCPTCQKHSRAFLH CCCCCHHHHHHHHHH	45.77	-
367	Ubiquitination	VRTSIVEKRFPDFVR HHHHHHHHHCHHHHH	48.74	-

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
139	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TGT_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 TGT_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSN6_HUMAN	COPS6	physical	16169070
SETB1_HUMAN	SETDB1	physical	16169070
SH3G3_HUMAN	SH3GL3	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
ZBT16_HUMAN	ZBTB16	physical	16169070
PLSI_HUMAN	PLS1	physical	26186194
PRAME_HUMAN	PRAME	physical	26186194
CH60_HUMAN	HSPD1	physical	26186194
APBB2_HUMAN	APBB2	physical	26186194
APBB1_HUMAN	APBB1	physical	26186194
DPOE4_HUMAN	POLE4	physical	26186194
APBB2_HUMAN	APBB2	physical	28514442
PRAME_HUMAN	PRAME	physical	28514442
APBB1_HUMAN	APBB1	physical	28514442
PLSI_HUMAN	PLS1	physical	28514442
CH60_HUMAN	HSPD1	physical	28514442
DPOE4_HUMAN	POLE4	physical	28514442
A4_HUMAN	APP	physical	28514442

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.