dbPTM

TSNAX_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TSNAX_HUMAN
UniProt AC	Q99598
Protein Name	Translin-associated protein X
Gene Name	TSNAX
Organism	Homo sapiens (Human).
Sequence Length	290
Subcellular Localization	Cytoplasm, perinuclear region. Golgi apparatus. Nucleus. Accumulate in the Golgi complex of mid-late pachytene spermatocytes (By similarity). Expressed in the cytoplasm in the presence of TSN..
Protein Description	Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis..
Protein Sequence	MSNKEGSGGFRKRKHDNFPHNQRREGKDVNSSSPVMLAFKSFQQELDARHDKYERLVKLSRDITVESKRTIFLLHRITSAPDMEDILTESEIKLDGVRQKIFQVAQELSGEDMHQFHRAITTGLQEYVEAVSFQHFIKTRSLISMDEINKQLIFTTEDNGKENKTPSSDAQDKQFGTWRLRVTPVDYLLGVADLTGELMRMCINSVGNGDIDTPFEVSQFLRQVYDGFSFIGNTGPYEVSKKLYTLKQSLAKVENACYALKVRGSEIPKHMLADVFSVKTEMIDQEEGIS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSNKEGSGG ------CCCCCCCCC	57.52	23401153
4	Ubiquitination	----MSNKEGSGGFR ----CCCCCCCCCCC	57.03	-
4	Acetylation	----MSNKEGSGGFR ----CCCCCCCCCCC	57.03	-
7	Phosphorylation	-MSNKEGSGGFRKRK -CCCCCCCCCCCCCC	36.51	21815630
14	Ubiquitination	SGGFRKRKHDNFPHN CCCCCCCCCCCCCCC	59.34	-
27	Ubiquitination	HNQRREGKDVNSSSP CCCCCCCCCCCCCCH	54.47	-
27	Acetylation	HNQRREGKDVNSSSP CCCCCCCCCCCCCCH	54.47	26051181
31	Phosphorylation	REGKDVNSSSPVMLA CCCCCCCCCCHHHHH	31.85	23401153
32	Phosphorylation	EGKDVNSSSPVMLAF CCCCCCCCCHHHHHH	33.20	23401153
33	Phosphorylation	GKDVNSSSPVMLAFK CCCCCCCCHHHHHHH	22.72	19664994
36	Sulfoxidation	VNSSSPVMLAFKSFQ CCCCCHHHHHHHHHH	2.25	21406390
40	Ubiquitination	SPVMLAFKSFQQELD CHHHHHHHHHHHHHH	44.76	-
41	Phosphorylation	PVMLAFKSFQQELDA HHHHHHHHHHHHHHH	23.10	26074081
68	Acetylation	RDITVESKRTIFLLH CCCCCCCCCHHEEEE	39.80	19608861
68	Ubiquitination	RDITVESKRTIFLLH CCCCCCCCCHHEEEE	39.80	19608861
68	Malonylation	RDITVESKRTIFLLH CCCCCCCCCHHEEEE	39.80	26320211
68	2-Hydroxyisobutyrylation	RDITVESKRTIFLLH CCCCCCCCCHHEEEE	39.80	-
78	Phosphorylation	IFLLHRITSAPDMED HEEEEECCCCCCHHH	20.84	27732954
79	Phosphorylation	FLLHRITSAPDMEDI EEEEECCCCCCHHHH	35.12	27732954
83	Sulfoxidation	RITSAPDMEDILTES ECCCCCCHHHHHCHH	4.92	21406390
88	Phosphorylation	PDMEDILTESEIKLD CCHHHHHCHHHCCHH	37.49	-
93	Ubiquitination	ILTESEIKLDGVRQK HHCHHHCCHHHHHHH	36.15	21906983
127	Phosphorylation	ITTGLQEYVEAVSFQ HHHHHHHHHHHHCHH	7.22	-
139	Phosphorylation	SFQHFIKTRSLISMD CHHHHHHHCCCCCHH	22.22	29083192
141	Phosphorylation	QHFIKTRSLISMDEI HHHHHHCCCCCHHHH	34.97	29083192
144	Phosphorylation	IKTRSLISMDEINKQ HHHCCCCCHHHHHCE	26.02	29083192
145	Sulfoxidation	KTRSLISMDEINKQL HHCCCCCHHHHHCEE	4.20	21406390
150	Ubiquitination	ISMDEINKQLIFTTE CCHHHHHCEEEEEEC	52.74	21890473
150	Ubiquitination	ISMDEINKQLIFTTE CCHHHHHCEEEEEEC	52.74	21906983
155	Phosphorylation	INKQLIFTTEDNGKE HHCEEEEEECCCCCC	23.45	29083192
156	Phosphorylation	NKQLIFTTEDNGKEN HCEEEEEECCCCCCC	30.50	29083192
161	Ubiquitination	FTTEDNGKENKTPSS EEECCCCCCCCCCCC	65.45	-
165	Phosphorylation	DNGKENKTPSSDAQD CCCCCCCCCCCHHCC	39.73	21815630
167	Phosphorylation	GKENKTPSSDAQDKQ CCCCCCCCCHHCCCC	46.19	24719451
168	Phosphorylation	KENKTPSSDAQDKQF CCCCCCCCHHCCCCC	37.86	28857561
173	Ubiquitination	PSSDAQDKQFGTWRL CCCHHCCCCCCEEEE	35.13	21906983
173	Ubiquitination	PSSDAQDKQFGTWRL CCCHHCCCCCCEEEE	35.13	21890473
179	Methylation	DKQFGTWRLRVTPVD CCCCCEEEEEEECHH	16.68	115388277
181	Methylation	QFGTWRLRVTPVDYL CCCEEEEEEECHHHH	22.99	115388285
237	Phosphorylation	FIGNTGPYEVSKKLY CCCCCCCHHHHHHHH	30.24	19060867
241	Acetylation	TGPYEVSKKLYTLKQ CCCHHHHHHHHHHHH	52.56	23954790
241	Ubiquitination	TGPYEVSKKLYTLKQ CCCHHHHHHHHHHHH	52.56	21906983
241	Ubiquitination	TGPYEVSKKLYTLKQ CCCHHHHHHHHHHHH	52.56	21890473
242	Acetylation	GPYEVSKKLYTLKQS CCHHHHHHHHHHHHH	38.94	9854593
242	Ubiquitination	GPYEVSKKLYTLKQS CCHHHHHHHHHHHHH	38.94	-
244	Phosphorylation	YEVSKKLYTLKQSLA HHHHHHHHHHHHHHH	20.93	-
247	Ubiquitination	SKKLYTLKQSLAKVE HHHHHHHHHHHHHHH	30.00	-
247	Acetylation	SKKLYTLKQSLAKVE HHHHHHHHHHHHHHH	30.00	25953088
247	Malonylation	SKKLYTLKQSLAKVE HHHHHHHHHHHHHHH	30.00	26320211
247	Succinylation	SKKLYTLKQSLAKVE HHHHHHHHHHHHHHH	30.00	23954790
249	Phosphorylation	KLYTLKQSLAKVENA HHHHHHHHHHHHHHH	28.80	24247654
252	Acetylation	TLKQSLAKVENACYA HHHHHHHHHHHHHHH	56.21	23954790
252	Malonylation	TLKQSLAKVENACYA HHHHHHHHHHHHHHH	56.21	26320211
252	Ubiquitination	TLKQSLAKVENACYA HHHHHHHHHHHHHHH	56.21	19608861
258	Phosphorylation	AKVENACYALKVRGS HHHHHHHHHHEECCC	16.74	29496907
261	Acetylation	ENACYALKVRGSEIP HHHHHHHEECCCCCC	23.01	25953088
261	Ubiquitination	ENACYALKVRGSEIP HHHHHHHEECCCCCC	23.01	21890473
261	Ubiquitination	ENACYALKVRGSEIP HHHHHHHEECCCCCC	23.01	21906983
269	Ubiquitination	VRGSEIPKHMLADVF ECCCCCCHHHHHHHH	47.51	21890473
269	Ubiquitination	VRGSEIPKHMLADVF ECCCCCCHHHHHHHH	47.51	21906983
277	Phosphorylation	HMLADVFSVKTEMID HHHHHHHHCCHHHCC	23.66	29523821
279	Sumoylation	LADVFSVKTEMIDQE HHHHHHCCHHHCCCC	37.25	28112733
280	Phosphorylation	ADVFSVKTEMIDQEE HHHHHCCHHHCCCCC	28.73	28985074
290	Phosphorylation	IDQEEGIS------- CCCCCCCC-------	45.05	22617229

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 TSNAX_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GA45G_HUMAN	GADD45G	physical	16189514
PBIP1_HUMAN	PBXIP1	physical	16189514
MR1L1_HUMAN	MRFAP1L1	physical	16189514
TSN_MOUSE	Tsn	physical	11278549
TSN_HUMAN	TSN	physical	22939629
RALYL_HUMAN	RALYL	physical	19447967
ARFP1_HUMAN	ARFIP1	physical	22863883
BOP1_HUMAN	BOP1	physical	22863883
HIRP3_HUMAN	HIRIP3	physical	22863883
SC24A_HUMAN	SEC24A	physical	22863883
SNX6_HUMAN	SNX6	physical	22863883
STAT1_HUMAN	STAT1	physical	22863883
AIMP1_HUMAN	AIMP1	physical	25416956
BL1S5_HUMAN	BLOC1S5	physical	25416956
CARD9_HUMAN	CARD9	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
KLC3_HUMAN	KLC3	physical	25416956
SOGA1_HUMAN	SOGA1	physical	26186194
GOGA3_HUMAN	GOLGA3	physical	26186194
CE128_HUMAN	CEP128	physical	26186194
KIF2A_HUMAN	KIF2A	physical	26186194
RGPD8_HUMAN	RGPD8	physical	26186194
RGPD5_HUMAN	RGPD5	physical	26186194
PCNT_HUMAN	PCNT	physical	26186194
TSN_HUMAN	TSN	physical	26186194
SMG7_HUMAN	SMG7	physical	26186194
IF6_HUMAN	EIF6	physical	26344197
ACV1B_HUMAN	ACVR1B	physical	26496610
C4BPA_HUMAN	C4BPA	physical	26496610
CETN2_HUMAN	CETN2	physical	26496610
CREM_HUMAN	CREM	physical	26496610
EVPL_HUMAN	EVPL	physical	26496610
FYN_HUMAN	FYN	physical	26496610
GOGA3_HUMAN	GOLGA3	physical	26496610
HEXB_HUMAN	HEXB	physical	26496610
KIF2A_HUMAN	KIF2A	physical	26496610
LYN_HUMAN	LYN	physical	26496610
MTRR_HUMAN	MTRR	physical	26496610
ORC4_HUMAN	ORC4	physical	26496610
PRDX1_HUMAN	PRDX1	physical	26496610
PFKAL_HUMAN	PFKL	physical	26496610
TRI27_HUMAN	TRIM27	physical	26496610
RS3_HUMAN	RPS3	physical	26496610
TAF11_HUMAN	TAF11	physical	26496610
TAF12_HUMAN	TAF12	physical	26496610
TPD52_HUMAN	TPD52	physical	26496610
TSN_HUMAN	TSN	physical	26496610
U2AF1_HUMAN	U2AF1	physical	26496610
1433E_HUMAN	YWHAE	physical	26496610
FXR1_HUMAN	FXR1	physical	26496610
AK17A_HUMAN	AKAP17A	physical	26496610
BAP1_HUMAN	BAP1	physical	26496610
DYL1_HUMAN	DYNLL1	physical	26496610
TOP3B_HUMAN	TOP3B	physical	26496610
MOT4_HUMAN	SLC16A3	physical	26496610
U5S1_HUMAN	EFTUD2	physical	26496610
FXR2_HUMAN	FXR2	physical	26496610
MLEC_HUMAN	MLEC	physical	26496610
KIF14_HUMAN	KIF14	physical	26496610
PDCD6_HUMAN	PDCD6	physical	26496610
ATP5H_HUMAN	ATP5H	physical	26496610
HNRPQ_HUMAN	SYNCRIP	physical	26496610
TXN4A_HUMAN	TXNL4A	physical	26496610
RRAS2_HUMAN	RRAS2	physical	26496610
TCF25_HUMAN	TCF25	physical	26496610
EXOS7_HUMAN	EXOSC7	physical	26496610
RT27_HUMAN	MRPS27	physical	26496610
ECM29_HUMAN	KIAA0368	physical	26496610
VIR_HUMAN	KIAA1429	physical	26496610
CI114_HUMAN	C9orf114	physical	26496610
GAR1_HUMAN	GAR1	physical	26496610
RFOX1_HUMAN	RBFOX1	physical	26496610
SMU1_HUMAN	SMU1	physical	26496610
PR40A_HUMAN	PRPF40A	physical	26496610
BRE1A_HUMAN	RNF20	physical	26496610
AK1BA_HUMAN	AKR1B10	physical	26496610
DEFM_HUMAN	PDF	physical	26496610
NT5D2_HUMAN	NT5DC2	physical	26496610
RM38_HUMAN	MRPL38	physical	26496610
GGCT_HUMAN	GGCT	physical	26496610
NUF2_HUMAN	NUF2	physical	26496610
RAM_HUMAN	FAM103A1	physical	26496610
MAK16_HUMAN	MAK16	physical	26496610
SOGA1_HUMAN	SOGA1	physical	26496610
C2D1B_HUMAN	CC2D1B	physical	26496610
F133B_HUMAN	FAM133B	physical	26496610
KIF24_HUMAN	KIF24	physical	26496610
KIF2A_HUMAN	KIF2A	physical	28514442
CE128_HUMAN	CEP128	physical	28514442
SOGA1_HUMAN	SOGA1	physical	28514442
STRAP_HUMAN	STRAP	physical	28514442
TSN_HUMAN	TSN	physical	28514442
RGPD8_HUMAN	RGPD8	physical	28514442
GOGA3_HUMAN	GOLGA3	physical	28514442
RGPD5_HUMAN	RGPD5	physical	28514442
SMG7_HUMAN	SMG7	physical	28514442
PCNT_HUMAN	PCNT	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 TSNAX_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND MASS SPECTROMETRY.	19608861 [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-33, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-33, AND MASSSPECTROMETRY.	19413330 [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-33, AND MASSSPECTROMETRY.	18669648 [Abstract]