dbPTM

SART3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SART3_HUMAN
UniProt AC	Q15020
Protein Name	Squamous cell carcinoma antigen recognized by T-cells 3 {ECO:0000305}
Gene Name	SART3 {ECO:0000312\|HGNC:HGNC:16860}
Organism	Homo sapiens (Human).
Sequence Length	963
Subcellular Localization	Nucleus, nucleoplasm . Nucleus, Cajal body . Nucleus speckle . Cytoplasm .
Protein Description	U6 snRNP-binding protein that functions as a recycling factor of the splicing machinery. Promotes the initial reassembly of U4 and U6 snRNPs following their ejection from the spliceosome during its maturation. [PubMed: 12032085 Also binds U6atac snRNPs and may function as a recycling factor for U4atac/U6atac spliceosomal snRNP, an initial step in the assembly of U12-type spliceosomal complex. The U12-type spliceosomal complex plays a role in the splicing of introns with non-canonical splice sites]
Protein Sequence	MATAAETSASEPEAESKAGPKADGEEDEVKAARTRRKVLSRAVAAATYKTMGPAWDQQEEGVSESDGDEYAMASSAESSPGEYEWEYDEEEEKNQLEIERLEEQLSINVYDYNCHVDLIRLLRLEGELTKVRMARQKMSEIFPLTEELWLEWLHDEISMAQDGLDREHVYDLFEKAVKDYICPNIWLEYGQYSVGGIGQKGGLEKVRSVFERALSSVGLHMTKGLALWEAYREFESAIVEAARLEKVHSLFRRQLAIPLYDMEATFAEYEEWSEDPIPESVIQNYNKALQQLEKYKPYEEALLQAEAPRLAEYQAYIDFEMKIGDPARIQLIFERALVENCLVPDLWIRYSQYLDRQLKVKDLVLSVHNRAIRNCPWTVALWSRYLLAMERHGVDHQVISVTFEKALNAGFIQATDYVEIWQAYLDYLRRRVDFKQDSSKELEELRAAFTRALEYLKQEVEERFNESGDPSCVIMQNWARIEARLCNNMQKARELWDSIMTRGNAKYANMWLEYYNLERAHGDTQHCRKALHRAVQCTSDYPEHVCEVLLTMERTEGSLEDWDIAVQKTETRLARVNEQRMKAAEKEAALVQQEEEKAEQRKRARAEKKALKKKKKIRGPEKRGADEDDEKEWGDDEEEQPSKRRRVENSIPAAGETQNVEVAAGPAGKCAAVDVEPPSKQKEKAASLKRDMPKVLHDSSKDSITVFVSNLPYSMQEPDTKLRPLFEACGEVVQIRPIFSNRGDFRGYCYVEFKEEKSALQALEMDRKSVEGRPMFVSPCVDKSKNPDFKVFRYSTSLEKHKLFISGLPFSCTKEELEEICKAHGTVKDLRLVTNRAGKPKGLAYVEYENESQASQAVMKMDGMTIKENIIKVAISNPPQRKVPEKPETRKAPGGPMLLPQTYGARGKGRTQLSLLPRALQRPSAAAPQAENGPAAAPAVAAPAATEAPKMSNADFAKLFLRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATAAETSA ------CCCHHCCCC	13.12	20068231
3	Phosphorylation	-----MATAAETSAS -----CCCHHCCCCC	25.71	21955146
7	Phosphorylation	-MATAAETSASEPEA -CCCHHCCCCCCCHH	25.51	23401153
8	Phosphorylation	MATAAETSASEPEAE CCCHHCCCCCCCHHH	22.69	29255136
10	Phosphorylation	TAAETSASEPEAESK CHHCCCCCCCHHHHH	54.15	29255136
16	Phosphorylation	ASEPEAESKAGPKAD CCCCHHHHHCCCCCC	34.55	29255136
48	Phosphorylation	RAVAAATYKTMGPAW HHHHHHHHHCCCCCH	10.35	-
130	Ubiquitination	RLEGELTKVRMARQK HHCCHHHHHHHHHHH	40.23	-
130	Ubiquitination	RLEGELTKVRMARQK HHCCHHHHHHHHHHH	40.23	-
130	2-Hydroxyisobutyrylation	RLEGELTKVRMARQK HHCCHHHHHHHHHHH	40.23	-
208	Phosphorylation	GGLEKVRSVFERALS CCHHHHHHHHHHHHH	33.86	24719451
215	Phosphorylation	SVFERALSSVGLHMT HHHHHHHHHCCCHHH	23.22	23186163
216	Phosphorylation	VFERALSSVGLHMTK HHHHHHHHCCCHHHH	22.51	24719451
221	Sulfoxidation	LSSVGLHMTKGLALW HHHCCCHHHHHHHHH	5.08	21406390
246	2-Hydroxyisobutyrylation	VEAARLEKVHSLFRR HHHHHHHHHHHHHHH	50.25	-
294	Ubiquitination	KALQQLEKYKPYEEA HHHHHHHHCCCHHHH	68.14	21890473
294	Ubiquitination	KALQQLEKYKPYEEA HHHHHHHHCCCHHHH	68.14	21890473
294 (in isoform 1)	Ubiquitination	-	68.14	21890473
294 (in isoform 2)	Ubiquitination	-	68.14	21890473
295	Phosphorylation	ALQQLEKYKPYEEAL HHHHHHHCCCHHHHH	14.07	28152594
296	Ubiquitination	LQQLEKYKPYEEALL HHHHHHCCCHHHHHH	52.79	-
298	Phosphorylation	QLEKYKPYEEALLQA HHHHCCCHHHHHHHC	23.42	28152594
341	Glutathionylation	ERALVENCLVPDLWI HHHHHHCCCCCCHHH	2.28	22555962
350	Phosphorylation	VPDLWIRYSQYLDRQ CCCHHHHHHHHHCCC	7.32	19835603
351	Phosphorylation	PDLWIRYSQYLDRQL CCHHHHHHHHHCCCC	11.51	19835603
353	Phosphorylation	LWIRYSQYLDRQLKV HHHHHHHHHCCCCCH	12.48	19835603
356	Methylation	RYSQYLDRQLKVKDL HHHHHHCCCCCHHHH	40.93	115493369
361	2-Hydroxyisobutyrylation	LDRQLKVKDLVLSVH HCCCCCHHHHHHHHH	43.70	-
435	Ubiquitination	LRRRVDFKQDSSKEL HHHCCCCCCCCHHHH	49.05	-
435	2-Hydroxyisobutyrylation	LRRRVDFKQDSSKEL HHHCCCCCCCCHHHH	49.05	-
446	Methylation	SKELEELRAAFTRAL HHHHHHHHHHHHHHH	27.44	115493357
455	Ubiquitination	AFTRALEYLKQEVEE HHHHHHHHHHHHHHH	21.76	-
457	Acetylation	TRALEYLKQEVEERF HHHHHHHHHHHHHHH	43.44	26051181
491	Ubiquitination	RLCNNMQKARELWDS HHHCCHHHHHHHHHH	38.35	-
501	Phosphorylation	ELWDSIMTRGNAKYA HHHHHHHHHCCHHHH	33.48	29496963
502	Methylation	LWDSIMTRGNAKYAN HHHHHHHHCCHHHHH	20.98	115493363
506	Acetylation	IMTRGNAKYANMWLE HHHHCCHHHHHHHHH	49.23	7366827
532	Ubiquitination	QHCRKALHRAVQCTS HHHHHHHHHHHHCCC	22.10	21890473
532	Acetylation	QHCRKALHRAVQCTS HHHHHHHHHHHHCCC	22.10	-
541	Phosphorylation	AVQCTSDYPEHVCEV HHHCCCCCHHHHHHH	15.41	22817900
550	Ubiquitination	EHVCEVLLTMERTEG HHHHHHHHEEECCCC	5.31	-
555	Phosphorylation	VLLTMERTEGSLEDW HHHEEECCCCCHHHH	31.24	28122231
558	Phosphorylation	TMERTEGSLEDWDIA EEECCCCCHHHHHHH	23.50	28122231
568	Acetylation	DWDIAVQKTETRLAR HHHHHHHHHHHHHHH	41.55	23236377
568 (in isoform 1)	Ubiquitination	-	41.55	21890473
568	Malonylation	DWDIAVQKTETRLAR HHHHHHHHHHHHHHH	41.55	26320211
568	Ubiquitination	DWDIAVQKTETRLAR HHHHHHHHHHHHHHH	41.55	2190698
586	Malonylation	QRMKAAEKEAALVQQ HHHHHHHHHHHHHHH	48.18	26320211
586	Acetylation	QRMKAAEKEAALVQQ HHHHHHHHHHHHHHH	48.18	25953088
586	Ubiquitination	QRMKAAEKEAALVQQ HHHHHHHHHHHHHHH	48.18	-
643	Acetylation	DEEEQPSKRRRVENS CCCCCCCHHHHHHHC	57.52	26051181
650	Phosphorylation	KRRRVENSIPAAGET HHHHHHHCCCCCCCC	19.22	25849741
657	Phosphorylation	SIPAAGETQNVEVAA CCCCCCCCCCEEEEE	25.24	29978859
679	Phosphorylation	AVDVEPPSKQKEKAA EEECCCCCHHHHHHH	59.44	28555341
687	Phosphorylation	KQKEKAASLKRDMPK HHHHHHHHHCCCCCH	39.00	24719451
694	Ubiquitination	SLKRDMPKVLHDSSK HHCCCCCHHHCCCCC	51.28	-
703	Phosphorylation	LHDSSKDSITVFVSN HCCCCCCCEEEEECC	24.72	20068231
705	Phosphorylation	DSSKDSITVFVSNLP CCCCCCEEEEECCCC	16.31	20068231
709	Phosphorylation	DSITVFVSNLPYSMQ CCEEEEECCCCCCCC	22.61	20068231
713	Phosphorylation	VFVSNLPYSMQEPDT EEECCCCCCCCCCCC	21.68	20068231
714	Phosphorylation	FVSNLPYSMQEPDTK EECCCCCCCCCCCCC	16.43	20068231
720	Phosphorylation	YSMQEPDTKLRPLFE CCCCCCCCCCHHHHH	42.57	20068231
740	Phosphorylation	VQIRPIFSNRGDFRG EEEEECCCCCCCCCC	26.74	-
754	Acetylation	GYCYVEFKEEKSALQ CEEEEEECHHHHHHH	52.00	26822725
765	Sulfoxidation	SALQALEMDRKSVEG HHHHHHHHCCCCCCC	6.67	21406390
769	Phosphorylation	ALEMDRKSVEGRPMF HHHHCCCCCCCCCEE	26.71	23401153
778	Phosphorylation	EGRPMFVSPCVDKSK CCCCEEEECCCCCCC	11.00	29496963
794	Phosphorylation	PDFKVFRYSTSLEKH CCCCEEEEECCHHHC	12.58	26657352
795	Phosphorylation	DFKVFRYSTSLEKHK CCCEEEEECCHHHCC	13.78	25159151
796	Phosphorylation	FKVFRYSTSLEKHKL CCEEEEECCHHHCCE	28.53	25159151
797	Phosphorylation	KVFRYSTSLEKHKLF CEEEEECCHHHCCEE	28.70	23312004
822	Ubiquitination	EELEEICKAHGTVKD HHHHHHHHHHCCHHH	49.43	-
831	Ubiquitination	HGTVKDLRLVTNRAG HCCHHHHHHHHCCCC	36.93	-
831	Methylation	HGTVKDLRLVTNRAG HCCHHHHHHHHCCCC	36.93	115493351
834	Phosphorylation	VKDLRLVTNRAGKPK HHHHHHHHCCCCCCC	24.47	-
852	Phosphorylation	YVEYENESQASQAVM EEEECCHHHHHHHHH	42.50	17525332
867	Ubiquitination	KMDGMTIKENIIKVA HHCCCEEEHHHHHHH	35.23	-
889	Phosphorylation	KVPEKPETRKAPGGP CCCCCCCCCCCCCCC	46.10	-
906	Methylation	LPQTYGARGKGRTQL CCCCCCCCCCCHHHH	42.89	24129315
906	Dimethylation	LPQTYGARGKGRTQL CCCCCCCCCCCHHHH	42.89	-
908	Methylation	QTYGARGKGRTQLSL CCCCCCCCCHHHHHH	39.40	115368095
911	Phosphorylation	GARGKGRTQLSLLPR CCCCCCHHHHHHHHH	42.40	21964256
914	Phosphorylation	GKGRTQLSLLPRALQ CCCHHHHHHHHHHHC	20.31	21406692
918	Methylation	TQLSLLPRALQRPSA HHHHHHHHHHCCCCC	48.15	54559081
922	Ubiquitination	LLPRALQRPSAAAPQ HHHHHHCCCCCCCCC	28.17	-
924	Phosphorylation	PRALQRPSAAAPQAE HHHHCCCCCCCCCCC	32.50	21406692
946	O-linked_Glycosylation	AVAAPAATEAPKMSN CCCCCCCCCCCCCCC	34.48	28411811
946	Phosphorylation	AVAAPAATEAPKMSN CCCCCCCCCCCCCCC	34.48	21406692
958	Ubiquitination	MSNADFAKLFLRK-- CCCHHHHHHHCCC--	39.50	21890473
958 (in isoform 1)	Ubiquitination	-	39.50	21890473

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 SART3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SART3_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 SART3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LSM7_HUMAN	LSM7	physical	15452143
PRPF3_HUMAN	PRPF3	physical	15452143
PRP4_HUMAN	PRPF4	physical	15452143
FRG1_HUMAN	FRG1	physical	19615732
PRP4_HUMAN	PRPF4	physical	19615732
PRPF3_HUMAN	PRPF3	physical	19615732
PPIH_HUMAN	PPIH	physical	19615732
LSM6_HUMAN	LSM6	physical	19615732
LSM4_HUMAN	LSM4	physical	19615732
NEPRO_HUMAN	C3orf17	physical	19615732
PRP31_HUMAN	PRPF31	physical	19615732
RRP15_HUMAN	RRP15	physical	19615732
DDX47_HUMAN	DDX47	physical	19615732
LSM7_HUMAN	LSM7	physical	19615732
LSM8_HUMAN	LSM8	physical	19615732
SRBD1_HUMAN	SRBD1	physical	19615732
MEPCE_HUMAN	MEPCE	physical	19615732
LSM2_HUMAN	LSM2	physical	19615732
STPAP_HUMAN	TUT1	physical	19615732
CENPU_HUMAN	CENPU	physical	19615732
RPF2_HUMAN	RPF2	physical	19615732
CMS1_HUMAN	CMSS1	physical	19615732
UBP15_HUMAN	USP15	physical	19615732
SNUT2_HUMAN	USP39	physical	19615732
UBP4_HUMAN	USP4	physical	19615732
UBP4_HUMAN	USP4	physical	20595234
SRC8_HUMAN	CTTN	physical	22939629
SPEB_HUMAN	AGMAT	physical	22939629
TPR_HUMAN	TPR	physical	22939629
ICAL_HUMAN	CAST	physical	22863883
CSN5_HUMAN	COPS5	physical	22863883
NUP50_HUMAN	NUP50	physical	22863883
PSA3_HUMAN	PSMA3	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
PSB3_HUMAN	PSMB3	physical	22863883
PSME4_HUMAN	PSME4	physical	22863883
UBP15_HUMAN	USP15	physical	24526689
H2B2E_HUMAN	HIST2H2BE	physical	24526689
H2A2C_HUMAN	HIST2H2AC	physical	24526689
UBP15_MOUSE	Usp15	physical	24984263
NFM_HUMAN	NEFM	physical	24984263
SYVC_HUMAN	VARS	physical	24984263
SF3B1_HUMAN	SF3B1	physical	24984263
NU160_HUMAN	NUP160	physical	24984263
SYIC_HUMAN	IARS	physical	24984263
AMOT_HUMAN	AMOT	physical	24984263
TR150_HUMAN	THRAP3	physical	24984263
BCLF1_HUMAN	BCLAF1	physical	24984263
UBP15_HUMAN	USP15	physical	24984263
UBC_HUMAN	UBC	physical	24984263
DSG2_HUMAN	DSG2	physical	24984263
RAB1A_HUMAN	RAB1A	physical	24984263
HIF1A_HUMAN	HIF1A	physical	24984263
LPPRC_HUMAN	LRPPRC	physical	24984263
DHX9_HUMAN	DHX9	physical	24984263
DNJC9_HUMAN	DNAJC9	physical	26344197
T2EB_HUMAN	GTF2E2	physical	26344197
UBR4_HUMAN	UBR4	physical	26344197
SART3_HUMAN	SART3	physical	27060135
UBP4_HUMAN	USP4	physical	27060135
UBP15_HUMAN	USP15	physical	27060135
IMA1_HUMAN	KPNA2	physical	27060135
UBP15_HUMAN	USP15	physical	27255711
SART3_HUMAN	SART3	physical	27255711
UBP15_HUMAN	USP15	physical	28088760
PRP31_HUMAN	PRPF31	physical	28088760
UBP4_HUMAN	USP4	physical	28088760
UBP4_HUMAN	USP4	physical	27990632
RNPS1_HUMAN	RNPS1	physical	27990632
STPAP_HUMAN	TUT1	physical	28514442
MEPCE_HUMAN	MEPCE	physical	28514442
ZSC21_HUMAN	ZSCAN21	physical	28514442
ACD11_HUMAN	ACAD11	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
ELAV4_HUMAN	ELAVL4	physical	28514442
UBP15_HUMAN	USP15	physical	28514442
LSM8_HUMAN	LSM8	physical	28514442
ZN845_HUMAN	ZNF845	physical	28514442
RS15_HUMAN	RPS15	physical	28514442
NOG1_HUMAN	GTPBP4	physical	28514442
POP7_HUMAN	POP7	physical	28514442
LSM2_HUMAN	LSM2	physical	28514442
SPT2_HUMAN	SPTY2D1	physical	28514442
CARF_HUMAN	CDKN2AIP	physical	28514442
LSM4_HUMAN	LSM4	physical	28514442
LARP1_HUMAN	LARP1	physical	28514442
LSM3_HUMAN	LSM3	physical	28514442
TOE1_HUMAN	TOE1	physical	28514442
FCF1_HUMAN	FCF1	physical	28514442
RLA2_HUMAN	RPLP2	physical	28514442
RRP12_HUMAN	RRP12	physical	28514442
RL13_HUMAN	RPL13	physical	28514442
ZN589_HUMAN	ZNF589	physical	28514442
RS8_HUMAN	RPS8	physical	28514442
LARP7_HUMAN	LARP7	physical	28514442
RL17_HUMAN	RPL17	physical	28514442
RL7A_HUMAN	RPL7A	physical	28514442
NOP2_HUMAN	NOP2	physical	28514442
NSA2_HUMAN	NSA2	physical	28514442
RS3A_HUMAN	RPS3A	physical	28514442
ZNF48_HUMAN	ZNF48	physical	28514442
ZSC25_HUMAN	ZSCAN25	physical	28514442
RL7L_HUMAN	RPL7L1	physical	28514442
RBM28_HUMAN	RBM28	physical	28514442
RS3_HUMAN	RPS3	physical	28514442
YBOX1_HUMAN	YBX1	physical	28514442
RL3_HUMAN	RPL3	physical	28514442
HP1B3_HUMAN	HP1BP3	physical	28514442
NOC4L_HUMAN	NOC4L	physical	28514442
SPB1_HUMAN	FTSJ3	physical	28514442
POP1_HUMAN	POP1	physical	28514442
DDX24_HUMAN	DDX24	physical	28514442
RL6_HUMAN	RPL6	physical	28514442
DHX30_HUMAN	DHX30	physical	28514442
YBOX3_HUMAN	YBX3	physical	28514442
RL4_HUMAN	RPL4	physical	28514442
RL27_HUMAN	RPL27	physical	28514442
BRX1_HUMAN	BRIX1	physical	28514442
RL19_HUMAN	RPL19	physical	28514442
RL13A_HUMAN	RPL13A	physical	28514442
SMD2_HUMAN	SNRPD2	physical	28514442
MPP10_HUMAN	MPHOSPH10	physical	28514442
DHX57_HUMAN	DHX57	physical	28514442
RRP1B_HUMAN	RRP1B	physical	28514442
THOC4_HUMAN	ALYREF	physical	27173435
LSM8_HUMAN	LSM8	physical	27173435
LSM4_HUMAN	LSM4	physical	27173435
LSM6_HUMAN	LSM6	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
175900	Disseminated superficial actinic porokeratosis 1 (DSAP1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SART3_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-8 AND SER-10, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7; SER-8 AND SER-10, ANDMASS SPECTROMETRY.	19369195 [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-8 AND SER-10, AND MASS SPECTROMETRY.	19413330 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852, AND MASSSPECTROMETRY.	17525332 [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-10 AND SER-16, AND MASSSPECTROMETRY.	17081983 [Abstract]