SREK1_HUMAN - dbPTM
SREK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SREK1_HUMAN
UniProt AC Q8WXA9
Protein Name Splicing regulatory glutamine/lysine-rich protein 1
Gene Name SREK1
Organism Homo sapiens (Human).
Sequence Length 508
Subcellular Localization Nucleus.
Protein Description Participates in the regulation of alternative splicing by modulating the activity of other splice facors. Inhibits the splicing activity of SFRS1, SFRS2 and SFRS6. Augments the splicing activity of SFRS3 (By similarity)..
Protein Sequence MTSLMPGAGLLPIPTPNPLTTLGVSLSSLGAIPAAALDPNIATLGEIPQPPLMGNVDPSKIDEIRRTVYVGNLNSQTTTADQLLEFFKQVGEVKFVRMAGDETQPTRFAFVEFADQNSVPRALAFNGVMFGDRPLKINHSNNAIVKPPEMTPQAAAKELEEVMKRVREAQSFISAAIEPESGKSNERKGGRSRSHTRSKSRSSSKSHSRRKRSQSKHRSRSHNRSRSRQKDRRRSKSPHKKRSKSRERRKSRSRSHSRDKRKDTREKIKEKERVKEKDREKEREREKEREKEKERGKNKDRDKEREKDREKDKEKDREREREKEHEKDRDKEKEKEQDKEKEREKDRSKEIDEKRKKDKKSRTPPRSYNASRRSRSSSRERRRRRSRSSSRSPRTSKTIKRKSSRSPSPRSRNKKDKKREKERDHISERRERERSTSMRKSSNDRDGKEKLEKNSTSLKEKEHNKEPDSSVSKEVDDKDAPRTEENKIQHNGNCQLNEENLSTKTEAV
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
3 (in isoform 2)Phosphorylation-22.7522210691
16 (in isoform 2)Phosphorylation-34.7822210691
31 (in isoform 2)Phosphorylation-15.1922210691
32 (in isoform 2)Phosphorylation-1.9522210691
51 (in isoform 2)Phosphorylation-29.7221406692
61 (in isoform 2)Phosphorylation-7.2521406692
62 (in isoform 2)Phosphorylation-49.3520068231
66 (in isoform 2)Phosphorylation-33.9221406692
100UbiquitinationVKFVRMAGDETQPTR
EEEEEECCCCCCCCE		24.7633845483
146UbiquitinationHSNNAIVKPPEMTPQ
CCCCCCCCCCCCCHH		49.0629967540
151PhosphorylationIVKPPEMTPQAAAKE
CCCCCCCCHHHHHHH		15.5828985074
171PhosphorylationKRVREAQSFISAAIE
HHHHHHHHHHHHHHC		31.4330266825
174PhosphorylationREAQSFISAAIEPES
HHHHHHHHHHHCCCC		15.0530266825
181PhosphorylationSAAIEPESGKSNERK
HHHHCCCCCCCCCCC		63.3430266825
183AcetylationAIEPESGKSNERKGG
HHCCCCCCCCCCCCC		60.4326051181
184PhosphorylationIEPESGKSNERKGGR
HCCCCCCCCCCCCCC		47.6630266825
200PhosphorylationRSHTRSKSRSSSKSH
CCCCCCCCCCCCCHH		38.3526074081
202PhosphorylationHTRSKSRSSSKSHSR
CCCCCCCCCCCHHHH		46.1626074081
203PhosphorylationTRSKSRSSSKSHSRR
CCCCCCCCCCHHHHH		40.4526074081
204PhosphorylationRSKSRSSSKSHSRRK
CCCCCCCCCHHHHHH		39.1526074081
206PhosphorylationKSRSSSKSHSRRKRS
CCCCCCCHHHHHHHH		28.7426074081
208PhosphorylationRSSSKSHSRRKRSQS
CCCCCHHHHHHHHHH		40.6526074081
251PhosphorylationKSRERRKSRSRSHSR
HHHHHHHHHHHHHHH		33.4127174698
253PhosphorylationRERRKSRSRSHSRDK
HHHHHHHHHHHHHHH		45.2727174698
262UbiquitinationSHSRDKRKDTREKIK
HHHHHHHHHHHHHHH		70.0129967540
267 (in isoform 2)Phosphorylation-56.6527251275
287 (in isoform 2)Phosphorylation-69.1927251275
297 (in isoform 2)Phosphorylation-68.0227251275
300 (in isoform 2)Phosphorylation-73.7024719451
361PhosphorylationKRKKDKKSRTPPRSY
HHHHCCCCCCCCCCC		47.3123403867
363PhosphorylationKKDKKSRTPPRSYNA
HHCCCCCCCCCCCCH		44.7423898821
367PhosphorylationKSRTPPRSYNASRRS
CCCCCCCCCCHHHHC		28.6323403867
387DimethylationERRRRRSRSSSRSPR
HHHHHHHHHHCCCCC		38.45-
387MethylationERRRRRSRSSSRSPR
HHHHHHHHHHCCCCC		38.4524390275
389PhosphorylationRRRRSRSSSRSPRTS
HHHHHHHHCCCCCCH		28.7622210691
390PhosphorylationRRRSRSSSRSPRTSK
HHHHHHHCCCCCCHH		37.7222210691
392PhosphorylationRSRSSSRSPRTSKTI
HHHHHCCCCCCHHHH		22.2323532336
394MethylationRSSSRSPRTSKTIKR
HHHCCCCCCHHHHHH		53.5324390283
394DimethylationRSSSRSPRTSKTIKR
HHHCCCCCCHHHHHH		53.53-
403PhosphorylationSKTIKRKSSRSPSPR
HHHHHHHHCCCCCCC		34.7120363803
404PhosphorylationKTIKRKSSRSPSPRS
HHHHHHHCCCCCCCC		39.5528102081
406PhosphorylationIKRKSSRSPSPRSRN
HHHHHCCCCCCCCCC		31.5128102081
408PhosphorylationRKSSRSPSPRSRNKK
HHHCCCCCCCCCCHH		33.9028102081
411PhosphorylationSRSPSPRSRNKKDKK
CCCCCCCCCCHHHHH		43.5223403867
427PhosphorylationEKERDHISERRERER
HHHHHHHHHHHHHHH		22.9424719451
435PhosphorylationERRERERSTSMRKSS
HHHHHHHHHHHHHHC		21.7827273156
436PhosphorylationRRERERSTSMRKSSN
HHHHHHHHHHHHHCC		32.5320736484
437PhosphorylationRERERSTSMRKSSND
HHHHHHHHHHHHCCC		20.1727273156
441PhosphorylationRSTSMRKSSNDRDGK
HHHHHHHHCCCCCHH		24.8220736484
442PhosphorylationSTSMRKSSNDRDGKE
HHHHHHHCCCCCHHH		45.8727273156
456PhosphorylationEKLEKNSTSLKEKEH
HHHHHCCCCHHHHHH		47.6923403867
465AcetylationLKEKEHNKEPDSSVS
HHHHHHCCCCCCCCC		72.9626051181
479 (in isoform 2)Phosphorylation-69.6524719451
487AcetylationAPRTEENKIQHNGNC
CCCCHHCCCCCCCCC		47.2026051181
502PhosphorylationQLNEENLSTKTEAV-
CCCCCCCCCCCCCC-		39.1730266825
503PhosphorylationLNEENLSTKTEAV--
CCCCCCCCCCCCC--		45.1930266825
504SumoylationNEENLSTKTEAV---
CCCCCCCCCCCC---		40.7828112733
505PhosphorylationEENLSTKTEAV----
CCCCCCCCCCC----		29.3028348404
520 (in isoform 2)Phosphorylation--
522 (in isoform 2)Phosphorylation--
524Phosphorylation-----------------------
-----------------------		33259812
524 (in isoform 2)Phosphorylation--
527 (in isoform 2)Phosphorylation--
543 (in isoform 2)Phosphorylation-24719451
621 (in isoform 2)Phosphorylation-27251275
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 SREK1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SREK1_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 SREK1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRSF3_HUMANSRSF3physical
11991645
SRSF2_HUMANSRSF2physical
11991645
SRSF2_HUMANSRSF2physical
14559993
SRSF8_HUMANSRSF8physical
14559993
SRSF7_HUMANSRSF7physical
14559993
DGKD_HUMANDGKDphysical
14559993
TARB1_HUMANTARBP1physical
14559993
SHLB2_HUMANSH3GLB2physical
14559993
SRSF3_HUMANSRSF3physical
14559993
SMD1_HUMANSNRPD1physical
14559993
SMD3_HUMANSNRPD3physical
14559993
SF3A3_HUMANSF3A3physical
14559993
SF3B3_HUMANSF3B3physical
14559993
U5S1_HUMANEFTUD2physical
14559993
ROA1_HUMANHNRNPA1physical
14559993
ROA2_HUMANHNRNPA2B1physical
14559993
ROA3_HUMANHNRNPA3physical
14559993
HNRPC_HUMANHNRNPCphysical
14559993
HNRPD_HUMANHNRNPDphysical
14559993
RBMX_HUMANRBMXphysical
14559993
HNRPK_HUMANHNRNPKphysical
14559993
HNRPU_HUMANHNRNPUphysical
14559993
HNRH1_HUMANHNRNPH1physical
14559993
SRSF1_HUMANSRSF1physical
14559993
SRSF4_HUMANSRSF4physical
14559993
SRSF5_HUMANSRSF5physical
14559993
SRSF6_HUMANSRSF6physical
14559993
SRSF9_HUMANSRSF9physical
14559993
TRA2B_HUMANTRA2Bphysical
14559993
DX39B_HUMANDDX39Bphysical
14559993
DDX17_HUMANDDX17physical
14559993
DDX3X_HUMANDDX3Xphysical
14559993
SRS10_HUMANSRSF10physical
14559993
C1QBP_HUMANC1QBPphysical
14559993
PABP1_HUMANPABPC1physical
14559993
PABP4_HUMANPABPC4physical
14559993
PARP1_HUMANPARP1physical
14559993
SAFB1_HUMANSAFBphysical
14559993
SFPQ_HUMANSFPQphysical
14559993
ELAV1_HUMANELAVL1physical
14559993
ZRAB2_HUMANZRANB2physical
14559993
RBM10_HUMANRBM10physical
14559993
NPM_HUMANNPM1physical
14559993
NUCL_HUMANNCLphysical
14559993
SP16H_HUMANSUPT16Hphysical
14559993
SSRP1_HUMANSSRP1physical
14559993
YBOX1_HUMANYBX1physical
14559993
TR150_HUMANTHRAP3physical
14559993
SRPK1_HUMANSRPK1physical
14559993
RACK1_HUMANGNB2L1physical
14559993
SRPK3_HUMANSRPK3physical
14559993
HNRC1_HUMANHNRNPCL1physical
14559993
VP33A_HUMANVPS33Aphysical
22939629
SREK1_HUMANSREK1physical
25416956
PININ_HUMANPNNphysical
26186194
RNPS1_HUMANRNPS1physical
26186194
JMJD6_HUMANJMJD6physical
26186194
SRSF8_HUMANSRSF8physical
26186194
SRS10_HUMANSRSF10physical
26186194
PUF60_HUMANPUF60physical
26344197
PININ_HUMANPNNphysical
14559993
ILF2_HUMANILF2physical
14559993
CSK21_HUMANCSNK2A1physical
14559993
SRSF8_HUMANSRSF8physical
28514442
PININ_HUMANPNNphysical
28514442
SRS10_HUMANSRSF10physical
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 SREK1_HUMAN

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Related Literatures of Post-Translational Modification
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-184, AND MASSSPECTROMETRY.

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