SRSF7_HUMAN - dbPTM
SRSF7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRSF7_HUMAN
UniProt AC Q16629
Protein Name Serine/arginine-rich splicing factor 7
Gene Name SRSF7
Organism Homo sapiens (Human).
Sequence Length 238
Subcellular Localization Nucleus . Cytoplasm .
Protein Description Required for pre-mRNA splicing. Can also modulate alternative splicing in vitro. Represses the splicing of MAPT/Tau exon 10. May function as export adapter involved in mRNA nuclear export such as of histone H2A. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. RNA-binding is semi-sequence specific..
Protein Sequence MSRYGRYGGETKVYVGNLGTGAGKGELERAFSYYGPLRTVWIARNPPGFAFVEFEDPRDAEDAVRGLDGKVICGSRVRVELSTGMPRRSRFDRPPARRPFDPNDRCYECGEKGHYAYDCHRYSRRRRSRSRSRSHSRSRGRRYSRSRSRSRGRRSRSASPRRSRSISLRRSRSASLRRSRSGSIKGSRYFQSPSRSRSRSRSISRPRSSRSKSRSPSPKRSRSPSGSPRRSASPERMD
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 Orthologous
Protein Cluster
2Phosphorylation------MSRYGRYGG
------CCCCCCCCC		33.9226074081
4Phosphorylation----MSRYGRYGGET
----CCCCCCCCCEE		9.9226074081
7Phosphorylation-MSRYGRYGGETKVY
-CCCCCCCCCEEEEE		25.7220068231
11PhosphorylationYGRYGGETKVYVGNL
CCCCCCEEEEEEEEC		29.1420068231
12UbiquitinationGRYGGETKVYVGNLG
CCCCCEEEEEEEECC		27.5421890473
12SumoylationGRYGGETKVYVGNLG
CCCCCEEEEEEEECC		27.54-
12UbiquitinationGRYGGETKVYVGNLG
CCCCCEEEEEEEECC		27.5423000965
12AcetylationGRYGGETKVYVGNLG
CCCCCEEEEEEEECC		27.5426051181
12 (in isoform 1)Ubiquitination-27.5421890473
12 (in isoform 2)Ubiquitination-27.5421890473
12 (in isoform 3)Ubiquitination-27.5421890473
12UbiquitinationGRYGGETKVYVGNLG
CCCCCEEEEEEEECC		27.5421890473
12SumoylationGRYGGETKVYVGNLG
CCCCCEEEEEEEECC		27.54-
14PhosphorylationYGGETKVYVGNLGTG
CCCEEEEEEEECCCC		12.2828152594
14NitrationYGGETKVYVGNLGTG
CCCEEEEEEEECCCC		12.28-
20PhosphorylationVYVGNLGTGAGKGEL
EEEEECCCCCCHHHH		27.3320068231
24 (in isoform 1)Ubiquitination-48.9921890473
24 (in isoform 2)Ubiquitination-48.9921890473
24UbiquitinationNLGTGAGKGELERAF
ECCCCCCHHHHHHHH		48.9923000965
24 (in isoform 3)Ubiquitination-48.9921890473
24SumoylationNLGTGAGKGELERAF
ECCCCCCHHHHHHHH		48.9928112733
24UbiquitinationNLGTGAGKGELERAF
ECCCCCCHHHHHHHH		48.9921890473
24UbiquitinationNLGTGAGKGELERAF
ECCCCCCHHHHHHHH		48.9921890473
24SumoylationNLGTGAGKGELERAF
ECCCCCCHHHHHHHH		48.99-
242-HydroxyisobutyrylationNLGTGAGKGELERAF
ECCCCCCHHHHHHHH		48.99-
24AcetylationNLGTGAGKGELERAF
ECCCCCCHHHHHHHH		48.9919608861
24MalonylationNLGTGAGKGELERAF
ECCCCCCHHHHHHHH		48.9926320211
32PhosphorylationGELERAFSYYGPLRT
HHHHHHHHCCCCCEE		19.2328152594
33PhosphorylationELERAFSYYGPLRTV
HHHHHHHCCCCCEEE		13.1427273156
34PhosphorylationLERAFSYYGPLRTVW
HHHHHHCCCCCEEEE		15.8628152594
702-HydroxyisobutyrylationAVRGLDGKVICGSRV
HHCCCCCEEECCCEE		28.26-
70 (in isoform 1)Ubiquitination-28.2621890473
70AcetylationAVRGLDGKVICGSRV
HHCCCCCEEECCCEE		28.2623749302
70UbiquitinationAVRGLDGKVICGSRV
HHCCCCCEEECCCEE		28.2623000965
82PhosphorylationSRVRVELSTGMPRRS
CEEEEEECCCCCCCC		14.9221406692
83PhosphorylationRVRVELSTGMPRRSR
EEEEEECCCCCCCCC		50.5625137130
85SulfoxidationRVELSTGMPRRSRFD
EEEECCCCCCCCCCC		2.0621406390
89PhosphorylationSTGMPRRSRFDRPPA
CCCCCCCCCCCCCCC		38.2828555341
98MethylationFDRPPARRPFDPNDR
CCCCCCCCCCCCCCC		38.04115916789
105MethylationRPFDPNDRCYECGEK
CCCCCCCCCCCCCCC		31.40115916785
107PhosphorylationFDPNDRCYECGEKGH
CCCCCCCCCCCCCCC		18.3628152594
112UbiquitinationRCYECGEKGHYAYDC
CCCCCCCCCCHHHHH		35.9523000965
112AcetylationRCYECGEKGHYAYDC
CCCCCCCCCCHHHHH		35.9525825284
1122-HydroxyisobutyrylationRCYECGEKGHYAYDC
CCCCCCCCCCHHHHH		35.95-
115PhosphorylationECGEKGHYAYDCHRY
CCCCCCCHHHHHHHH		18.6128152594
117PhosphorylationGEKGHYAYDCHRYSR
CCCCCHHHHHHHHHH		16.3728152594
122PhosphorylationYAYDCHRYSRRRRSR
HHHHHHHHHHHHHHH		5.2726657352
123PhosphorylationAYDCHRYSRRRRSRS
HHHHHHHHHHHHHHH		21.1926657352
128PhosphorylationRYSRRRRSRSRSRSH
HHHHHHHHHHHHHHC		32.5626657352
143PhosphorylationSRSRGRRYSRSRSRS
HHHHHHHHHHHHHHH		13.6917081983
146PhosphorylationRGRRYSRSRSRSRGR
HHHHHHHHHHHHHCC		28.7717081983
155PhosphorylationSRSRGRRSRSASPRR
HHHHCCCCCCCCCCH		29.2629743597
157PhosphorylationSRGRRSRSASPRRSR
HHCCCCCCCCCCHHH		34.0529743597
159PhosphorylationGRRSRSASPRRSRSI
CCCCCCCCCCHHHHH		21.8629743597
163PhosphorylationRSASPRRSRSISLRR
CCCCCCHHHHHHHHH		31.4922167270
165PhosphorylationASPRRSRSISLRRSR
CCCCHHHHHHHHHHH		20.1322167270
167PhosphorylationPRRSRSISLRRSRSA
CCHHHHHHHHHHHCC		19.6420164059
171PhosphorylationRSISLRRSRSASLRR
HHHHHHHHHCCCCHH		24.9328355574
173PhosphorylationISLRRSRSASLRRSR
HHHHHHHCCCCHHHC		24.3728355574
175PhosphorylationLRRSRSASLRRSRSG
HHHHHCCCCHHHCCC		24.5322167270
179PhosphorylationRSASLRRSRSGSIKG
HCCCCHHHCCCCCCC		25.1028176443
181PhosphorylationASLRRSRSGSIKGSR
CCCHHHCCCCCCCCC		37.8328176443
183PhosphorylationLRRSRSGSIKGSRYF
CHHHCCCCCCCCCCC		23.5228176443
185AcetylationRSRSGSIKGSRYFQS
HHCCCCCCCCCCCCC		53.1619608861
187PhosphorylationRSGSIKGSRYFQSPS
CCCCCCCCCCCCCCC		20.8520068231
189PhosphorylationGSIKGSRYFQSPSRS
CCCCCCCCCCCCCCC		13.9922167270
192PhosphorylationKGSRYFQSPSRSRSR
CCCCCCCCCCCCCCC		18.2319664994
194PhosphorylationSRYFQSPSRSRSRSR
CCCCCCCCCCCCCCC		48.4029255136
196PhosphorylationYFQSPSRSRSRSRSI
CCCCCCCCCCCCCCC		38.6625159151
198PhosphorylationQSPSRSRSRSRSISR
CCCCCCCCCCCCCCC		35.5426055452
200PhosphorylationPSRSRSRSRSISRPR
CCCCCCCCCCCCCCC		31.4620363803
202PhosphorylationRSRSRSRSISRPRSS
CCCCCCCCCCCCCCC		26.6027794612
204PhosphorylationRSRSRSISRPRSSRS
CCCCCCCCCCCCCCC		37.1627794612
208PhosphorylationRSISRPRSSRSKSRS
CCCCCCCCCCCCCCC		32.5520873877
208 (in isoform 4)Phosphorylation-32.5527174698
209PhosphorylationSISRPRSSRSKSRSP
CCCCCCCCCCCCCCC		41.6820873877
209 (in isoform 4)Phosphorylation-41.6827174698
210PhosphorylationISRPRSSRSKSRSPS
CCCCCCCCCCCCCCC		49.7233259812
211PhosphorylationSRPRSSRSKSRSPSP
CCCCCCCCCCCCCCC		36.6127135362
211 (in isoform 4)Phosphorylation-36.6127174698
213PhosphorylationPRSSRSKSRSPSPKR
CCCCCCCCCCCCCCC		38.9620363803
213 (in isoform 4)Phosphorylation-38.9627174698
215PhosphorylationSSRSKSRSPSPKRSR
CCCCCCCCCCCCCCC		36.5020363803
215 (in isoform 4)Phosphorylation-36.5027174698
217PhosphorylationRSKSRSPSPKRSRSP
CCCCCCCCCCCCCCC		44.2828102081
219 (in isoform 4)Phosphorylation-68.3027107777
221PhosphorylationRSPSPKRSRSPSGSP
CCCCCCCCCCCCCCC		43.1421601212
221 (in isoform 4)Phosphorylation-43.1427107777
223PhosphorylationPSPKRSRSPSGSPRR
CCCCCCCCCCCCCCC		25.3526055452
225PhosphorylationPKRSRSPSGSPRRSA
CCCCCCCCCCCCCCC		53.8226329039
227PhosphorylationRSRSPSGSPRRSASP
CCCCCCCCCCCCCCC		21.4125159151
231PhosphorylationPSGSPRRSASPERMD
CCCCCCCCCCCCCCC		34.0822167270
233PhosphorylationGSPRRSASPERMD--
CCCCCCCCCCCCC--		28.6522167270
236MethylationRRSASPERMD-----
CCCCCCCCCC-----		37.6424412291
236DimethylationRRSASPERMD-----
CCCCCCCCCC-----		37.64-
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 SRSF7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRSF7_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 SRSF7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DUS11_HUMANDUSP11physical
9685386
CDK19_HUMANCDK19physical
12501247
RBBP6_HUMANRBBP6physical
18624398
U2AF1_HUMANU2AF1physical
22939629
U2AF2_HUMANU2AF2physical
22939629
TRA2B_HUMANTRA2Bphysical
22939629
SNUT1_HUMANSART1physical
22939629
SNUT2_HUMANUSP39physical
22939629
TF3C1_HUMANGTF3C1physical
22939629
TRI55_HUMANTRIM55physical
22939629
STT3B_HUMANSTT3Bphysical
22939629
TM9S2_HUMANTM9SF2physical
22939629
VASN_HUMANVASNphysical
22939629
SURF4_HUMANSURF4physical
22939629
TFPI1_HUMANTFPIphysical
22939629
ZRAB2_HUMANZRANB2physical
22939629
SON_HUMANSONphysical
22939629
LC7L2_HUMANLUC7L2physical
25416956
EIF3D_HUMANEIF3Dphysical
26344197
SRSF1_HUMANSRSF1physical
26344197
SRSF6_HUMANSRSF6physical
26344197
SRSF9_HUMANSRSF9physical
26344197
TRA2B_HUMANTRA2Bphysical
26344197
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 SRSF7_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-24 AND LYS-185, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-192; SER-194 ANDSER-196, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-194, ANDMASS SPECTROMETRY.
"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-163; SER-165; SER-167;SER-171; SER-173; SER-175; SER-192; SER-194; SER-231 AND SER-233, ANDMASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-217; SER-221;SER-225; SER-227 AND SER-233, AND MASS SPECTROMETRY.

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