dbPTM

THUM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	THUM1_HUMAN
UniProt AC	Q9NXG2
Protein Name	THUMP domain-containing protein 1
Gene Name	THUMPD1
Organism	Homo sapiens (Human).
Sequence Length	353
Subcellular Localization
Protein Description	Functions as a tRNA-binding adapter to mediate NAT10-dependent tRNA acetylation. [PubMed: 25653167]
Protein Sequence	MAAPAQQTTQPGGGKRKGKAQYVLAKRARRCDAGGPRQLEPGLQGILITCNMNERKCVEEAYSLLNEYGDDMYGPEKFTDKDQQPSGSEGEDDDAEAALKKEVGDIKASTEMRLRRFQSVESGANNVVFIRTLGIEPEKLVHHILQDMYKTKKKKTRVILRMLPISGTCKAFLEDMKKYAETFLEPWFKAPNKGTFQIVYKSRNNSHVNREEVIRELAGIVCTLNSENKVDLTNPQYTVVVEIIKAVCCLSVVKDYMLFRKYNLQEVVKSPKDPSQLNSKQGNGKEAKLESADKSDQNNTAEGKNNQQVPENTEELGQTKPTSNPQVVNEGGAKPELASQATEGSKSNENDFS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAPAQQTT ------CCCCCCCCC	23.35	22814378
8	O-linked_Glycosylation	MAAPAQQTTQPGGGK CCCCCCCCCCCCCCC	18.47	23301498
9	O-linked_Glycosylation	AAPAQQTTQPGGGKR CCCCCCCCCCCCCCC	28.55	23301498
15	Acetylation	TTQPGGGKRKGKAQY CCCCCCCCCCCCHHH	54.96	23749302
15	Ubiquitination	TTQPGGGKRKGKAQY CCCCCCCCCCCCHHH	54.96	-
22	Phosphorylation	KRKGKAQYVLAKRAR CCCCCHHHEEHHHHH	11.42	28796482
26	Acetylation	KAQYVLAKRARRCDA CHHHEEHHHHHHCCC	42.29	25953088
26	Methylation	KAQYVLAKRARRCDA CHHHEEHHHHHHCCC	42.29	91061
26	2-Hydroxyisobutyrylation	KAQYVLAKRARRCDA CHHHEEHHHHHHCCC	42.29	-
49	Phosphorylation	GLQGILITCNMNERK CCEEEEEECCCCHHH	8.38	-
79	Phosphorylation	MYGPEKFTDKDQQPS CCCCCCCCCCCCCCC	53.89	26503892
86	Phosphorylation	TDKDQQPSGSEGEDD CCCCCCCCCCCCCCC	51.09	19664994
88	Phosphorylation	KDQQPSGSEGEDDDA CCCCCCCCCCCCCHH	46.92	19664994
109	Phosphorylation	EVGDIKASTEMRLRR HHCCCCCCHHHHHHH	21.65	28857561
110	Phosphorylation	VGDIKASTEMRLRRF HCCCCCCHHHHHHHH	38.36	27251275
119	Phosphorylation	MRLRRFQSVESGANN HHHHHHHHHHCCCCC	25.74	23898821
122	Phosphorylation	RRFQSVESGANNVVF HHHHHHHCCCCCEEE	40.84	23312004
177	2-Hydroxyisobutyrylation	KAFLEDMKKYAETFL HHHHHHHHHHHHHHH	55.76	-
178	Ubiquitination	AFLEDMKKYAETFLE HHHHHHHHHHHHHHH	42.95	21890473
179	Phosphorylation	FLEDMKKYAETFLEP HHHHHHHHHHHHHHH	12.26	-
182	Phosphorylation	DMKKYAETFLEPWFK HHHHHHHHHHHHHHC	25.91	-
189	Ubiquitination	TFLEPWFKAPNKGTF HHHHHHHCCCCCCEE	60.09	21890473
254	Ubiquitination	VCCLSVVKDYMLFRK HHHHHHHHHHHHHHH	40.77	21890473
261	Malonylation	KDYMLFRKYNLQEVV HHHHHHHHCCHHHHH	31.02	26320211
261	2-Hydroxyisobutyrylation	KDYMLFRKYNLQEVV HHHHHHHHCCHHHHH	31.02	-
262	Phosphorylation	DYMLFRKYNLQEVVK HHHHHHHCCHHHHHC	19.49	23312004
269	Malonylation	YNLQEVVKSPKDPSQ CCHHHHHCCCCCHHH	67.24	26320211
270	Phosphorylation	NLQEVVKSPKDPSQL CHHHHHCCCCCHHHH	26.10	23401153
272	Ubiquitination	QEVVKSPKDPSQLNS HHHHCCCCCHHHHCC	84.83	-
275	Phosphorylation	VKSPKDPSQLNSKQG HCCCCCHHHHCCCCC	58.39	30266825
279	Phosphorylation	KDPSQLNSKQGNGKE CCHHHHCCCCCCCCC	34.64	30266825
285	Acetylation	NSKQGNGKEAKLESA CCCCCCCCCHHHHCC	59.50	8276627
288	Acetylation	QGNGKEAKLESADKS CCCCCCHHHHCCCCC	54.61	25953088
294	Acetylation	AKLESADKSDQNNTA HHHHCCCCCCCCCCC	56.50	25953088
295	Phosphorylation	KLESADKSDQNNTAE HHHCCCCCCCCCCCC	45.00	25159151
300	Phosphorylation	DKSDQNNTAEGKNNQ CCCCCCCCCCCCCCC	33.37	28985074
313	Phosphorylation	NQQVPENTEELGQTK CCCCCCCHHHHCCCC	29.22	23186163
319	Phosphorylation	NTEELGQTKPTSNPQ CHHHHCCCCCCCCCC	36.87	23186163
320	Acetylation	TEELGQTKPTSNPQV HHHHCCCCCCCCCCC	38.11	26051181
322	Phosphorylation	ELGQTKPTSNPQVVN HHCCCCCCCCCCCCC	42.57	23186163
322	O-linked_Glycosylation	ELGQTKPTSNPQVVN HHCCCCCCCCCCCCC	42.57	OGP
323	Phosphorylation	LGQTKPTSNPQVVNE HCCCCCCCCCCCCCC	55.85	23186163
334	Acetylation	VVNEGGAKPELASQA CCCCCCCCHHHHHHH	42.15	26051181
339	Phosphorylation	GAKPELASQATEGSK CCCHHHHHHHCCCCC	32.73	25849741
342	Phosphorylation	PELASQATEGSKSNE HHHHHHHCCCCCCCC	32.99	25159151
345	Phosphorylation	ASQATEGSKSNENDF HHHHCCCCCCCCCCC	27.03	25849741

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 THUM1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of THUM1_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 THUM1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
THUM3_HUMAN	THUMPD3	physical	22939629
YAP1_HUMAN	YAP1	physical	22939629
NP1L1_HUMAN	NAP1L1	physical	22863883
2ABA_HUMAN	PPP2R2A	physical	22863883
DDX21_HUMAN	DDX21	physical	26186194
NAT10_HUMAN	NAT10	physical	26186194
FDXA1_HUMAN	FDXACB1	physical	26186194
TRUA_HUMAN	PUS1	physical	26186194
PUS7_HUMAN	PUS7	physical	26186194
MTO1_HUMAN	MTO1	physical	26186194
TGT_HUMAN	QTRT1	physical	26186194
SYHC_HUMAN	HARS	physical	26344197
NDRG1_HUMAN	NDRG1	physical	26344197
HNRPQ_HUMAN	SYNCRIP	physical	26344197
THUM3_HUMAN	THUMPD3	physical	26344197
PUS7_HUMAN	PUS7	physical	28514442
TGT_HUMAN	QTRT1	physical	28514442
FDXA1_HUMAN	FDXACB1	physical	28514442
NAT10_HUMAN	NAT10	physical	28514442
TRUA_HUMAN	PUS1	physical	28514442
YBOX1_HUMAN	YBX1	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.

Regulatory Network of THUM1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-86 AND SER-88, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"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-86 AND SER-88, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-86 AND SER-88, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, AND MASSSPECTROMETRY.	18318008 [Abstract]
"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-86 AND SER-88, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, AND MASSSPECTROMETRY.	17081983 [Abstract]