dbPTM

SND1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SND1_HUMAN
UniProt AC	Q7KZF4
Protein Name	Staphylococcal nuclease domain-containing protein 1
Gene Name	SND1
Organism	Homo sapiens (Human).
Sequence Length	910
Subcellular Localization	Cytoplasm . Nucleus . Melanosome . In IL-4 stimulated cells colocalizes with STAT6 in the nucleus. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description	Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2)..
Protein Sequence	MASSAQSGGSSGGPAVPTVQRGIIKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGNLARRAAATQPDAKDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLGKDTNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSEGNGSHTIRDLKYTIENPRHFVDSHHQKPVNAIIEHVRDGSVVRALLLPDYYLVTVMLSGIKCPTFRREADGSETPEPFAAEAKFFTESRLLQRDVQIILESCHNQNILGTILHPNGNITELLLKEGFARCVDWSIAVYTRGAEKLRAAERFAKERRLRIWRDYVAPTANLDQKDKQFVAKVMQVLNADAIVVKLNSGDYKTIHLSSIRPPRLEGENTQDKNKKLRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYIRPASPATETVPAFSERTCATVTIGGINIAEALVSKGLATVIRYRQDDDQRSSHYDELLAAEARAIKNGKGLHSKKEVPIHRVADISGDTQKAKQFLPFLQRAGRSEAVVEYVFSGSRLKLYLPKETCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLHIDGANLSVLLVEHALSKVHFTAERSSYYKSLLSAEEAAKQKKEKVWAHYEEQPVEEVMPVLEEKERSASYKPVFVTEITDDLHFYVQDVETGTQLEKLMENMRNDIASHPPVEGSYAPRRGEFCIAKFVDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAFSTRVLPAQATEYAFAFIQVPQDDDARTDAVDSVVRDIQNTQCLLNVEHLSAGCPHVTLQFADSKGDVGLGLVKEGLVMVEVRKEKQFQKVITEYLNAQESAKSARLNLWRYGDFRADDADEFGYSR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASSAQSGG ------CCCCCCCCC	16.52	19413330
3	Phosphorylation	-----MASSAQSGGS -----CCCCCCCCCC	25.55	30108239
4	Phosphorylation	----MASSAQSGGSS ----CCCCCCCCCCC	22.31	30108239
7	Phosphorylation	-MASSAQSGGSSGGP -CCCCCCCCCCCCCC	44.85	30108239
10	Phosphorylation	SSAQSGGSSGGPAVP CCCCCCCCCCCCCCC	29.36	30108239
11	Phosphorylation	SAQSGGSSGGPAVPT CCCCCCCCCCCCCCH	51.55	30108239
18	Phosphorylation	SGGPAVPTVQRGIIK CCCCCCCHHHHHHHH	23.75	30108239
29	Phosphorylation	GIIKMVLSGCAIIVR HHHHHHHCCCEEEEC	22.03	19664995
31	Glutathionylation	IKMVLSGCAIIVRGQ HHHHHCCCEEEECCC	1.90	22555962
40	Methylation	IIVRGQPRGGPPPER EEECCCCCCCCCCHH	55.61	115917345
52	Phosphorylation	PERQINLSNIRAGNL CHHHCCCCHHHHHHH	26.23	23403867
71	Acetylation	AATQPDAKDTPDEPW HHCCCCCCCCCCCCC	70.30	26051181
71	Malonylation	AATQPDAKDTPDEPW HHCCCCCCCCCCCCC	70.30	26320211
71	Sumoylation	AATQPDAKDTPDEPW HHCCCCCCCCCCCCC	70.30	-
71	Ubiquitination	AATQPDAKDTPDEPW HHCCCCCCCCCCCCC	70.30	-
88	Ubiquitination	PAREFLRKKLIGKEV CHHHHHHHHCCCCEE	54.82	-
93	Acetylation	LRKKLIGKEVCFTIE HHHHCCCCEEEEEEE	39.72	26051181
93	Ubiquitination	LRKKLIGKEVCFTIE HHHHCCCCEEEEEEE	39.72	-
96	Glutathionylation	KLIGKEVCFTIENKT HCCCCEEEEEEECCC	2.33	22555962
96	S-palmitoylation	KLIGKEVCFTIENKT HCCCCEEEEEEECCC	2.33	29575903
98	Phosphorylation	IGKEVCFTIENKTPQ CCCEEEEEEECCCCC	23.43	30266825
102	Acetylation	VCFTIENKTPQGREY EEEEEECCCCCCCEE	49.11	25953088
102	Malonylation	VCFTIENKTPQGREY EEEEEECCCCCCCEE	49.11	26320211
102	Ubiquitination	VCFTIENKTPQGREY EEEEEECCCCCCCEE	49.11	-
103	Phosphorylation	CFTIENKTPQGREYG EEEEECCCCCCCEEE	32.21	30266825
107	Methylation	ENKTPQGREYGMIYL ECCCCCCCEEEEEEE	28.81	115917341
109	Phosphorylation	KTPQGREYGMIYLGK CCCCCCEEEEEEECC	15.61	27155012
111	Sulfoxidation	PQGREYGMIYLGKDT CCCCEEEEEEECCCC	1.46	30846556
113	Phosphorylation	GREYGMIYLGKDTNG CCEEEEEEECCCCCC	10.66	28152594
116	Ubiquitination	YGMIYLGKDTNGENI EEEEEECCCCCCCCH	59.80	-
126	Phosphorylation	NGENIAESLVAEGLA CCCCHHHHHHHHHHH	21.08	24532841
150	Phosphorylation	NPEQNRLSECEEQAK CHHHCCHHHHHHHHH	36.64	29255136
152	Glutathionylation	EQNRLSECEEQAKAA HHCCHHHHHHHHHHH	6.65	22555962
157	Acetylation	SECEEQAKAAKKGMW HHHHHHHHHHHCCCC	48.88	25953088
157	Ubiquitination	SECEEQAKAAKKGMW HHHHHHHHHHHCCCC	48.88	-
161	Ubiquitination	EQAKAAKKGMWSEGN HHHHHHHCCCCCCCC	49.63	-
165	Phosphorylation	AAKKGMWSEGNGSHT HHHCCCCCCCCCCCC	27.08	20860994
170	Phosphorylation	MWSEGNGSHTIRDLK CCCCCCCCCCCEEEE	22.81	20860994
172	Phosphorylation	SEGNGSHTIRDLKYT CCCCCCCCCEEEEEE	21.29	20860994
177	Acetylation	SHTIRDLKYTIENPR CCCCEEEEEEECCCC	44.64	26822725
177	Methylation	SHTIRDLKYTIENPR CCCCEEEEEEECCCC	44.64	133771
177	Ubiquitination	SHTIRDLKYTIENPR CCCCEEEEEEECCCC	44.64	21906983
179	Phosphorylation	TIRDLKYTIENPRHF CCEEEEEEECCCCHH	21.89	28348404
189	Phosphorylation	NPRHFVDSHHQKPVN CCCHHCCCCCCCCHH	19.98	22617229
193	Acetylation	FVDSHHQKPVNAIIE HCCCCCCCCHHHHHH	46.72	19608861
193	Malonylation	FVDSHHQKPVNAIIE HCCCCCCCCHHHHHH	46.72	26320211
193	Ubiquitination	FVDSHHQKPVNAIIE HCCCCCCCCHHHHHH	46.72	21890473
238	Phosphorylation	FRREADGSETPEPFA CEECCCCCCCCCCHH	38.55	29255136
240	Phosphorylation	READGSETPEPFAAE ECCCCCCCCCCHHHH	34.35	29255136
249	Acetylation	EPFAAEAKFFTESRL CCHHHHHHHHCHHHH	32.30	26051181
249	Ubiquitination	EPFAAEAKFFTESRL CCHHHHHHHHCHHHH	32.30	21906983
329	Nitration	RLRIWRDYVAPTANL HHHHHHHHCCCCCCC	7.02	-
329	Phosphorylation	RLRIWRDYVAPTANL HHHHHHHHCCCCCCC	7.02	21945579
333	Phosphorylation	WRDYVAPTANLDQKD HHHHCCCCCCCCHHH	20.59	-
339	2-Hydroxyisobutyrylation	PTANLDQKDKQFVAK CCCCCCHHHHHHHHH	67.56	-
339	Acetylation	PTANLDQKDKQFVAK CCCCCCHHHHHHHHH	67.56	23236377
339	Malonylation	PTANLDQKDKQFVAK CCCCCCHHHHHHHHH	67.56	26320211
339	Ubiquitination	PTANLDQKDKQFVAK CCCCCCHHHHHHHHH	67.56	-
341	2-Hydroxyisobutyrylation	ANLDQKDKQFVAKVM CCCCHHHHHHHHHHH	53.31	-
341	Acetylation	ANLDQKDKQFVAKVM CCCCHHHHHHHHHHH	53.31	25953088
341	Ubiquitination	ANLDQKDKQFVAKVM CCCCHHHHHHHHHHH	53.31	-
346	Ubiquitination	KDKQFVAKVMQVLNA HHHHHHHHHHHHHCC	32.70	-
348	Sulfoxidation	KQFVAKVMQVLNADA HHHHHHHHHHHCCCE	1.94	21406390
359	Ubiquitination	NADAIVVKLNSGDYK CCCEEEEEECCCCCE	30.93	-
365	Phosphorylation	VKLNSGDYKTIHLSS EEECCCCCEEEEECC	17.35	28102081
366	Ubiquitination	KLNSGDYKTIHLSSI EECCCCCEEEEECCC	45.82	21906983
371	Phosphorylation	DYKTIHLSSIRPPRL CCEEEEECCCCCCCC	15.01	30301811
372	Phosphorylation	YKTIHLSSIRPPRLE CEEEEECCCCCCCCC	29.04	25954137
383	Phosphorylation	PRLEGENTQDKNKKL CCCCCCCCCCCCCCC	33.57	21601212
389	Malonylation	NTQDKNKKLRPLYDI CCCCCCCCCCCCCCC	60.15	26320211
389	Ubiquitination	NTQDKNKKLRPLYDI CCCCCCCCCCCCCCC	60.15	-
398	Phosphorylation	RPLYDIPYMFEAREF CCCCCCCHHHHHHHH	18.12	-
399	Sulfoxidation	PLYDIPYMFEAREFL CCCCCCHHHHHHHHH	1.73	30846556
414	2-Hydroxyisobutyrylation	RKKLIGKKVNVTVDY HHHHCCCEEEEEEEE	33.55	-
414	Malonylation	RKKLIGKKVNVTVDY HHHHCCCEEEEEEEE	33.55	26320211
414	Ubiquitination	RKKLIGKKVNVTVDY HHHHCCCEEEEEEEE	33.55	-
418	Phosphorylation	IGKKVNVTVDYIRPA CCCEEEEEEEEECCC	11.49	28176443
421	Phosphorylation	KVNVTVDYIRPASPA EEEEEEEEECCCCCC	8.42	28176443
426	Phosphorylation	VDYIRPASPATETVP EEEECCCCCCCCCCC	20.11	19664994
429	Phosphorylation	IRPASPATETVPAFS ECCCCCCCCCCCCCC	35.26	28176443
431	Phosphorylation	PASPATETVPAFSER CCCCCCCCCCCCCCC	27.69	28176443
436	Phosphorylation	TETVPAFSERTCATV CCCCCCCCCCCEEEE	28.42	28176443
440	S-nitrosocysteine	PAFSERTCATVTIGG CCCCCCCEEEEEECC	3.61	-
440	S-nitrosylation	PAFSERTCATVTIGG CCCCCCCEEEEEECC	3.61	19483679
440	S-palmitoylation	PAFSERTCATVTIGG CCCCCCCEEEEEECC	3.61	29575903
473	Phosphorylation	RQDDDQRSSHYDELL ECCCCCCCCCHHHHH	18.81	20873877
474	Phosphorylation	QDDDQRSSHYDELLA CCCCCCCCCHHHHHH	28.40	20873877
476	Phosphorylation	DDQRSSHYDELLAAE CCCCCCCHHHHHHHH	17.04	-
497	Ubiquitination	GKGLHSKKEVPIHRV CCCCCCCCCCCCEEE	67.94	-
508	Phosphorylation	IHRVADISGDTQKAK CEEEECCCCCHHHHH	31.03	21815630
513	Sumoylation	DISGDTQKAKQFLPF CCCCCHHHHHHHHHH	60.69	-
513	2-Hydroxyisobutyrylation	DISGDTQKAKQFLPF CCCCCHHHHHHHHHH	60.69	-
513	Acetylation	DISGDTQKAKQFLPF CCCCCHHHHHHHHHH	60.69	25953088
513	Sumoylation	DISGDTQKAKQFLPF CCCCCHHHHHHHHHH	60.69	28112733
513	Ubiquitination	DISGDTQKAKQFLPF CCCCCHHHHHHHHHH	60.69	21906983
515	Acetylation	SGDTQKAKQFLPFLQ CCCHHHHHHHHHHHH	48.93	26051181
515	Ubiquitination	SGDTQKAKQFLPFLQ CCCHHHHHHHHHHHH	48.93	21906983
523	Methylation	QFLPFLQRAGRSEAV HHHHHHHHCCCCHHH	40.95	115917349
527	Phosphorylation	FLQRAGRSEAVVEYV HHHHCCCCHHHEEEE	29.05	21712546
533	Phosphorylation	RSEAVVEYVFSGSRL CCHHHEEEEECCCCE	8.66	28152594
536	Phosphorylation	AVVEYVFSGSRLKLY HHEEEEECCCCEEEE	26.30	28152594
538	Phosphorylation	VEYVFSGSRLKLYLP EEEEECCCCEEEECC	32.99	28152594
541	2-Hydroxyisobutyrylation	VFSGSRLKLYLPKET EECCCCEEEECCHHH	33.69	-
541	Acetylation	VFSGSRLKLYLPKET EECCCCEEEECCHHH	33.69	23749302
541	Malonylation	VFSGSRLKLYLPKET EECCCCEEEECCHHH	33.69	26320211
578	Phosphorylation	VQEGEPFSEEATLFT CCCCCCCCHHHHEEE	45.29	21712546
586	Ubiquitination	EEATLFTKELVLQRE HHHHEEEHHHHHEEE	41.54	-
600	Phosphorylation	EVEVEVESMDKAGNF EEEEEEEECCCCCCE	37.14	21712546
601	Sulfoxidation	VEVEVESMDKAGNFI EEEEEEECCCCCCEE	3.76	21406390
633	Phosphorylation	ALSKVHFTAERSSYY HHHHCCEEHHCHHHH	16.84	28555341
637	Phosphorylation	VHFTAERSSYYKSLL CCEEHHCHHHHHHHH	17.75	28857561
638	Phosphorylation	HFTAERSSYYKSLLS CEEHHCHHHHHHHHC	38.41	-
641	Sumoylation	AERSSYYKSLLSAEE HHCHHHHHHHHCHHH	26.79	-
641	Acetylation	AERSSYYKSLLSAEE HHCHHHHHHHHCHHH	26.79	19608861
641	Malonylation	AERSSYYKSLLSAEE HHCHHHHHHHHCHHH	26.79	26320211
641	Sumoylation	AERSSYYKSLLSAEE HHCHHHHHHHHCHHH	26.79	-
641	Ubiquitination	AERSSYYKSLLSAEE HHCHHHHHHHHCHHH	26.79	21890473
642	Phosphorylation	ERSSYYKSLLSAEEA HCHHHHHHHHCHHHH	20.58	23403867
645	Phosphorylation	SYYKSLLSAEEAAKQ HHHHHHHCHHHHHHH	38.64	25159151
651	2-Hydroxyisobutyrylation	LSAEEAAKQKKEKVW HCHHHHHHHHHHHHH	70.47	-
651	Ubiquitination	LSAEEAAKQKKEKVW HCHHHHHHHHHHHHH	70.47	-
656	Ubiquitination	AAKQKKEKVWAHYEE HHHHHHHHHHHHHHC	52.54	-
661	Phosphorylation	KEKVWAHYEEQPVEE HHHHHHHHHCCCHHH	17.26	21945579
676	Acetylation	VMPVLEEKERSASYK HHHHHHHHHHHCCCC	49.40	26051181
676	Ubiquitination	VMPVLEEKERSASYK HHHHHHHHHHHCCCC	49.40	-
679	Phosphorylation	VLEEKERSASYKPVF HHHHHHHHCCCCCEE	23.74	27251275
681	Phosphorylation	EEKERSASYKPVFVT HHHHHHCCCCCEEEE	34.63	27251275
682	Phosphorylation	EKERSASYKPVFVTE HHHHHCCCCCEEEEE	21.01	24275569
683	Ubiquitination	KERSASYKPVFVTEI HHHHCCCCCEEEEEE	32.01	-
705	Phosphorylation	VQDVETGTQLEKLME EEECCCHHHHHHHHH	37.08	21601212
720	Phosphorylation	NMRNDIASHPPVEGS HHHHHHHHCCCCCCC	36.54	21945579
727	Phosphorylation	SHPPVEGSYAPRRGE HCCCCCCCCCCCCCC	12.48	21945579
728	Phosphorylation	HPPVEGSYAPRRGEF CCCCCCCCCCCCCCE	31.33	21945579
736	S-palmitoylation	APRRGEFCIAKFVDG CCCCCCEEEEEECCC	2.29	21044946
739	Acetylation	RGEFCIAKFVDGEWY CCCEEEEEECCCCEE	26.47	26051181
739	Ubiquitination	RGEFCIAKFVDGEWY CCCEEEEEECCCCEE	26.47	21906983
746	Phosphorylation	KFVDGEWYRARVEKV EECCCCEEEEEEEEC	7.06	27642862
752	Acetylation	WYRARVEKVESPAKI EEEEEEEECCCCCEE	48.74	19608861
752	Ubiquitination	WYRARVEKVESPAKI EEEEEEEECCCCCEE	48.74	-
755	Phosphorylation	ARVEKVESPAKIHVF EEEEECCCCCEEEEE	32.90	29214152
758	Acetylation	EKVESPAKIHVFYID EECCCCCEEEEEEEE	36.41	25953088
758	Malonylation	EKVESPAKIHVFYID EECCCCCEEEEEEEE	36.41	26320211
758	Ubiquitination	EKVESPAKIHVFYID EECCCCCEEEEEEEE	36.41	-
763	Phosphorylation	PAKIHVFYIDYGNRE CCEEEEEEEECCCCE	7.56	29214152
766	Phosphorylation	IHVFYIDYGNREVLP EEEEEEECCCCEECC	13.52	28152594
774	Phosphorylation	GNREVLPSTRLGTLS CCCEECCCCCCCCCC	23.23	26074081
775	Phosphorylation	NREVLPSTRLGTLSP CCEECCCCCCCCCCC	28.15	26074081
779	Phosphorylation	LPSTRLGTLSPAFST CCCCCCCCCCCCCCC	28.75	27794612
781	Phosphorylation	STRLGTLSPAFSTRV CCCCCCCCCCCCCCC	17.64	29255136
785	Phosphorylation	GTLSPAFSTRVLPAQ CCCCCCCCCCCCCCC	19.87	27794612
786	Phosphorylation	TLSPAFSTRVLPAQA CCCCCCCCCCCCCCC	20.53	23403867
787	Methylation	LSPAFSTRVLPAQAT CCCCCCCCCCCCCCC	27.12	115917353
794	Phosphorylation	RVLPAQATEYAFAFI CCCCCCCCEEEEEEE	19.90	26074081
796	Phosphorylation	LPAQATEYAFAFIQV CCCCCCEEEEEEEEC	11.58	27642862
824	Phosphorylation	VVRDIQNTQCLLNVE HHHHHHHCEEEEEHH	12.32	-
834	O-linked_Glycosylation	LLNVEHLSAGCPHVT EEEHHHHHCCCCEEE	25.23	23301498
834	Phosphorylation	LLNVEHLSAGCPHVT EEEHHHHHCCCCEEE	25.23	-
848	Sumoylation	TLQFADSKGDVGLGL EEEECCCCCCEECEE	60.73	-
848	Ubiquitination	TLQFADSKGDVGLGL EEEECCCCCCEECEE	60.73	21906983
857	Ubiquitination	DVGLGLVKEGLVMVE CEECEEEECCEEEEE	51.62	21906983
862	Sulfoxidation	LVKEGLVMVEVRKEK EEECCEEEEEECCHH	2.27	21406390
869	2-Hydroxyisobutyrylation	MVEVRKEKQFQKVIT EEEECCHHHHHHHHH	60.49	-
869	Ubiquitination	MVEVRKEKQFQKVIT EEEECCHHHHHHHHH	60.49	-
873	Acetylation	RKEKQFQKVITEYLN CCHHHHHHHHHHHHC	36.57	26822725
873	Ubiquitination	RKEKQFQKVITEYLN CCHHHHHHHHHHHHC	36.57	21906983
876	Phosphorylation	KQFQKVITEYLNAQE HHHHHHHHHHHCHHH	22.89	-
878	Phosphorylation	FQKVITEYLNAQESA HHHHHHHHHCHHHHH	9.15	28152594
884	Phosphorylation	EYLNAQESAKSARLN HHHCHHHHHHHHCCC	28.99	25159151
886	2-Hydroxyisobutyrylation	LNAQESAKSARLNLW HCHHHHHHHHCCCHH	54.66	-
886	Ubiquitination	LNAQESAKSARLNLW HCHHHHHHHHCCCHH	54.66	21906983
895	Phosphorylation	ARLNLWRYGDFRADD HCCCHHHHCCCCCCC	14.95	-
899	Methylation	LWRYGDFRADDADEF HHHHCCCCCCCCHHC	41.67	115917357
908	Phosphorylation	DDADEFGYSR----- CCCHHCCCCC-----	13.44	27273156
909	Phosphorylation	DADEFGYSR------ CCHHCCCCC------	31.71	29255136
910	Methylation	ADEFGYSR------- CHHCCCCC-------	41.92	115917361

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
103	T	Phosphorylation	Kinase	MAPK8	P45983	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SND1_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 SND1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STAT6_HUMAN	STAT6	physical	12234934
RPB1_HUMAN	POLR2A	physical	12234934
STAT6_HUMAN	STAT6	physical	20225206
A4_HUMAN	APP	physical	21832049
TOM22_HUMAN	TOMM22	physical	22939629
SPF30_HUMAN	SMNDC1	physical	22939629
VDAC2_HUMAN	VDAC2	physical	22939629
SSRG_HUMAN	SSR3	physical	22939629
G3BP1_HUMAN	G3BP1	physical	20643132
PRP8_HUMAN	PRPF8	physical	17632523
EIFCL_HUMAN	EIF3CL	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
RS11_HUMAN	RPS11	physical	22863883
RS2_HUMAN	RPS2	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS9_HUMAN	RPS9	physical	22863883
TDRD3_HUMAN	TDRD3	physical	26344197
TXND5_HUMAN	TXNDC5	physical	26344197
TRAP1_HUMAN	TRAP1	physical	27173435
IF2P_HUMAN	EIF5B	physical	27173435
G6PI_HUMAN	GPI	physical	27173435
PDIA3_HUMAN	PDIA3	physical	27173435
CRNN_HUMAN	CRNN	physical	27173435
PLST_HUMAN	PLS3	physical	27173435
SRP68_HUMAN	SRP68	physical	27173435

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 SND1_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-4 AND SER-10, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-193; LYS-641 AND LYS-752,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-909, 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-4 AND SER-10, AND MASS SPECTROMETRY.	19413330 [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 THR-429 AND SER-781, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-109, AND MASSSPECTROMETRY.	19534553 [Abstract]
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