SRSF5_HUMAN - dbPTM
SRSF5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRSF5_HUMAN
UniProt AC Q13243
Protein Name Serine/arginine-rich splicing factor 5
Gene Name SRSF5
Organism Homo sapiens (Human).
Sequence Length 272
Subcellular Localization Nucleus.
Protein Description Plays a role in constitutive splicing and can modulate the selection of alternative splice sites..
Protein Sequence MSGCRVFIGRLNPAAREKDVERFFKGYGRIRDIDLKRGFGFVEFEDPRDADDAVYELDGKELCSERVTIEHARARSRGGRGRGRYSDRFSSRRPRNDRRNAPPVRTENRLIVENLSSRVSWQDLKDFMRQAGEVTFADAHRPKLNEGVVEFASYGDLKNAIEKLSGKEINGRKIKLIEGSKRHSRSRSRSRSRTRSSSRSRSRSRSRSRKSYSRSRSRSRSRSRSKSRSVSRSPVPEKSQKRGSSSRSKSPASVDRQRSRSRSRSRSVDSGN
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------MSGCRVFIG
------CCCCEEEEE		46.7526074081
2Acetylation------MSGCRVFIG
------CCCCEEEEE		46.75-
5Methylation---MSGCRVFIGRLN
---CCCCEEEEECCC		29.8816187991
10MethylationGCRVFIGRLNPAARE
CCEEEEECCCHHHHH		26.8616188001
25 (in isoform 2)Ubiquitination-48.8121890473
25MethylationKDVERFFKGYGRIRD
HHHHHHHHHCCCEEE		48.8172666109
25 (in isoform 3)Ubiquitination-48.8121890473
25UbiquitinationKDVERFFKGYGRIRD
HHHHHHHHHCCCEEE		48.8121890473
25AcetylationKDVERFFKGYGRIRD
HHHHHHHHHCCCEEE		48.8126051181
36SuccinylationRIRDIDLKRGFGFVE
CEEEEECCCCCCEEE		46.8823954790
48MethylationFVEFEDPRDADDAVY
EEEECCCCCCCCCEE		65.16115916769
55PhosphorylationRDADDAVYELDGKEL
CCCCCCEEEECCHHH		16.7028796482
60AcetylationAVYELDGKELCSERV
CEEEECCHHHCCCCE		47.3726051181
60UbiquitinationAVYELDGKELCSERV
CEEEECCHHHCCCCE		47.3722053931
60 (in isoform 1)Ubiquitination-47.3721890473
73MethylationRVTIEHARARSRGGR
CEEHHHHHHHCCCCC		32.2354559249
75MethylationTIEHARARSRGGRGR
EHHHHHHHCCCCCCC		22.72115916773
85PhosphorylationGGRGRGRYSDRFSSR
CCCCCCCCCCCCCCC		20.1129214152
86PhosphorylationGRGRGRYSDRFSSRR
CCCCCCCCCCCCCCC		22.4329496963
88MethylationGRGRYSDRFSSRRPR
CCCCCCCCCCCCCCC		27.6624381503
90PhosphorylationGRYSDRFSSRRPRND
CCCCCCCCCCCCCCC		24.6723917254
91PhosphorylationRYSDRFSSRRPRNDR
CCCCCCCCCCCCCCC		29.6023312004
92MethylationYSDRFSSRRPRNDRR
CCCCCCCCCCCCCCC		51.96115916777
116PhosphorylationRLIVENLSSRVSWQD
CEEEECCHHCCCHHH		27.9029255136
117PhosphorylationLIVENLSSRVSWQDL
EEEECCHHCCCHHHH		39.6119664994
120PhosphorylationENLSSRVSWQDLKDF
ECCHHCCCHHHHHHH		20.2229978859
122 (in isoform 3)Ubiquitination-38.3621890473
125 (in isoform 1)Ubiquitination-58.1521890473
125UbiquitinationRVSWQDLKDFMRQAG
CCCHHHHHHHHHHHC		58.1521890473
125AcetylationRVSWQDLKDFMRQAG
CCCHHHHHHHHHHHC		58.1526051181
135PhosphorylationMRQAGEVTFADAHRP
HHHHCCCEEHHCCCC		14.59-
143AcetylationFADAHRPKLNEGVVE
EHHCCCCCCCCCCEE		64.9926051181
153PhosphorylationEGVVEFASYGDLKNA
CCCEEEHHHHHHHHH		34.6627499020
154PhosphorylationGVVEFASYGDLKNAI
CCEEEHHHHHHHHHH		15.9528152594
158UbiquitinationFASYGDLKNAIEKLS
EHHHHHHHHHHHHHH		49.42-
163AcetylationDLKNAIEKLSGKEIN
HHHHHHHHHHCCCCC		41.6723749302
163UbiquitinationDLKNAIEKLSGKEIN
HHHHHHHHHHCCCCC		41.67-
165PhosphorylationKNAIEKLSGKEINGR
HHHHHHHHCCCCCCE		59.9129391485
167UbiquitinationAIEKLSGKEINGRKI
HHHHHHCCCCCCEEE		52.63-
167AcetylationAIEKLSGKEINGRKI
HHHHHHCCCCCCEEE		52.6319608861
175AcetylationEINGRKIKLIEGSKR
CCCCEEEEEEECCCH		46.5825953088
175UbiquitinationEINGRKIKLIEGSKR
CCCCEEEEEEECCCH		46.58-
181AcetylationIKLIEGSKRHSRSRS
EEEEECCCHHCCCCH		66.0625953088
184PhosphorylationIEGSKRHSRSRSRSR
EECCCHHCCCCHHCH		35.6617081983
186PhosphorylationGSKRHSRSRSRSRSR
CCCHHCCCCHHCHHC		37.3117081983
196PhosphorylationRSRSRTRSSSRSRSR
HCHHCCCCHHHHHHH		31.8626074081
197PhosphorylationSRSRTRSSSRSRSRS
CHHCCCCHHHHHHHH		26.8726074081
198PhosphorylationRSRTRSSSRSRSRSR
HHCCCCHHHHHHHHH		35.2126074081
200PhosphorylationRTRSSSRSRSRSRSR
CCCCHHHHHHHHHHH		36.2326074081
202PhosphorylationRSSSRSRSRSRSRSR
CCHHHHHHHHHHHHH		35.5426074081
204PhosphorylationSSRSRSRSRSRSRKS
HHHHHHHHHHHHHHH		35.5426074081
206PhosphorylationRSRSRSRSRSRKSYS
HHHHHHHHHHHHHHH		35.5426074081
208PhosphorylationRSRSRSRSRKSYSRS
HHHHHHHHHHHHHHH		45.3524144214
211PhosphorylationSRSRSRKSYSRSRSR
HHHHHHHHHHHHHHH		27.5120068231
212PhosphorylationRSRSRKSYSRSRSRS
HHHHHHHHHHHHHHH		15.9020068231
213PhosphorylationSRSRKSYSRSRSRSR
HHHHHHHHHHHHHHH		30.7620068231
215PhosphorylationSRKSYSRSRSRSRSR
HHHHHHHHHHHHHHH		28.7720068231
225PhosphorylationRSRSRSRSKSRSVSR
HHHHHHHHCCCCCCC		35.9124144214
227PhosphorylationRSRSRSKSRSVSRSP
HHHHHHCCCCCCCCC		30.9120164059
229PhosphorylationRSRSKSRSVSRSPVP
HHHHCCCCCCCCCCC		31.3829255136
231PhosphorylationRSKSRSVSRSPVPEK
HHCCCCCCCCCCCHH		28.4329255136
233PhosphorylationKSRSVSRSPVPEKSQ
CCCCCCCCCCCHHHH		23.8129255136
244PhosphorylationEKSQKRGSSSRSKSP
HHHHCCCCCCCCCCC		29.2223663014
245PhosphorylationKSQKRGSSSRSKSPA
HHHCCCCCCCCCCCH		32.3723663014
246PhosphorylationSQKRGSSSRSKSPAS
HHCCCCCCCCCCCHH		42.1223663014
248PhosphorylationKRGSSSRSKSPASVD
CCCCCCCCCCCHHHH		39.1626055452
250PhosphorylationGSSSRSKSPASVDRQ
CCCCCCCCCHHHHHH		27.2628355574
253PhosphorylationSRSKSPASVDRQRSR
CCCCCCHHHHHHHHH		28.1228355574
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 SRSF5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRSF5_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 SRSF5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
U2AF1_HUMANU2AF1physical
22939629
U2AF2_HUMANU2AF2physical
22939629
SRSF7_HUMANSRSF7physical
22939629
TRA2B_HUMANTRA2Bphysical
22939629
TPR_HUMANTPRphysical
22939629
SMU1_HUMANSMU1physical
22939629
SRRM2_HUMANSRRM2physical
22939629
SNUT2_HUMANUSP39physical
22939629
SNUT1_HUMANSART1physical
22939629
TRA2A_HUMANTRA2Aphysical
22939629
UT14A_HUMANUTP14Aphysical
22939629
TIM50_HUMANTIMM50physical
22939629
SURF4_HUMANSURF4physical
22939629
TF3C1_HUMANGTF3C1physical
22939629
SFXN3_HUMANSFXN3physical
22939629
TR112_HUMANTRMT112physical
22939629
VASN_HUMANVASNphysical
22939629
VATC1_HUMANATP6V1C1physical
22939629
TI17B_HUMANTIMM17Bphysical
22939629
TMCO1_HUMANTMCO1physical
22939629
SON_HUMANSONphysical
22939629
TMX2_HUMANTMX2physical
22939629
TM14B_HUMANTMEM14Bphysical
22939629
SURF1_HUMANSURF1physical
22939629
SMN_HUMANSMN1physical
22939629
RUXF_HUMANSNRPFphysical
22365833
PP2BB_HUMANPPP3CBphysical
22863883
NUCL_HUMANNCLphysical
26344197
SRRM2_HUMANSRRM2physical
26344197
TRA2B_HUMANTRA2Bphysical
26344197
SRSF3_HUMANSRSF3physical
27173435
SRSF6_HUMANSRSF6physical
27173435
PR38A_HUMANPRPF38Aphysical
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 SRSF5_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-167, AND MASS SPECTROMETRY.
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-229; SER-231 ANDSER-233, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND MASSSPECTROMETRY.
"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-227; SER-229; SER-231;SER-233; SER-250 AND SER-253, AND MASS SPECTROMETRY.
"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-231; SER-233 ANDSER-253, AND MASS SPECTROMETRY.

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