SRS12_HUMAN - dbPTM
SRS12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRS12_HUMAN
UniProt AC Q8WXF0
Protein Name Serine/arginine-rich splicing factor 12
Gene Name SRSF12
Organism Homo sapiens (Human).
Sequence Length 261
Subcellular Localization Nucleus .
Protein Description Splicing factor that seems to antagonize SR proteins in pre-mRNA splicing regulation..
Protein Sequence MSRYTRPPNTSLFIRNVADATRPEDLRREFGRYGPIVDVYIPLDFYTRRPRGFAYVQFEDVRDAEDALYNLNRKWVCGRQIEIQFAQGDRKTPGQMKSKERHPCSPSDHRRSRSPSQRRTRSRSSSWGRNRRRSDSLKESRHRRFSYSQSKSRSKSLPRRSTSARQSRTPRRNFGSRGRSRSKSLQKRSKSIGKSQSSSPQKQTSSGTKSRSHGRHSDSIARSPCKSPKGYTNSETKVQTAKHSHFRSHSRSRSYRHKNSW
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------MSRYTRPPN
------CCCCCCCCC		33.7129116813
5Phosphorylation---MSRYTRPPNTSL
---CCCCCCCCCCCE		35.2729116813
51PhosphorylationDFYTRRPRGFAYVQF
HHHCCCCCCEEEEEE		51.5632142685
55PhosphorylationRRPRGFAYVQFEDVR
CCCCCEEEEEEECCC		7.79-
104PhosphorylationKSKERHPCSPSDHRR
CCCCCCCCCHHHHCC		8.3633259812
105PhosphorylationSKERHPCSPSDHRRS
CCCCCCCCHHHHCCC		31.7129691806
107PhosphorylationERHPCSPSDHRRSRS
CCCCCCHHHHCCCCC		29.7429691806
112PhosphorylationSPSDHRRSRSPSQRR
CHHHHCCCCCHHHHH		36.7524719451
120PhosphorylationRSPSQRRTRSRSSSW
CCHHHHHHHHHHCHH		34.8724719451
122PhosphorylationPSQRRTRSRSSSWGR
HHHHHHHHHHCHHHC		35.5820363803
124PhosphorylationQRRTRSRSSSWGRNR
HHHHHHHHCHHHCCC		29.9420363803
125PhosphorylationRRTRSRSSSWGRNRR
HHHHHHHCHHHCCCC		29.0620363803
126PhosphorylationRTRSRSSSWGRNRRR
HHHHHHCHHHCCCCC		34.4924719451
132PhosphorylationSSWGRNRRRSDSLKE
CHHHCCCCCCCHHHH		46.1032645325
134PhosphorylationWGRNRRRSDSLKESR
HHCCCCCCCHHHHHH		29.7326471730
136PhosphorylationRNRRRSDSLKESRHR
CCCCCCCHHHHHHHH		42.4624719451
146PhosphorylationESRHRRFSYSQSKSR
HHHHHHHCHHHHHHC		23.2822617229
147PhosphorylationSRHRRFSYSQSKSRS
HHHHHHCHHHHHHCC		14.1721406692
148PhosphorylationRHRRFSYSQSKSRSK
HHHHHCHHHHHHCCC		27.1220363803
150PhosphorylationRRFSYSQSKSRSKSL
HHHCHHHHHHCCCCC		27.0220363803
152PhosphorylationFSYSQSKSRSKSLPR
HCHHHHHHCCCCCCC		47.2127732954
154PhosphorylationYSQSKSRSKSLPRRS
HHHHHHCCCCCCCCC		33.4224719451
156PhosphorylationQSKSRSKSLPRRSTS
HHHHCCCCCCCCCCC		44.8730177828
161PhosphorylationSKSLPRRSTSARQSR
CCCCCCCCCCHHHCC		28.1727732954
162PhosphorylationKSLPRRSTSARQSRT
CCCCCCCCCHHHCCC		25.2927732954
163PhosphorylationSLPRRSTSARQSRTP
CCCCCCCCHHHCCCC		23.7727732954
167PhosphorylationRSTSARQSRTPRRNF
CCCCHHHCCCCCCCC		32.3527732954
169PhosphorylationTSARQSRTPRRNFGS
CCHHHCCCCCCCCCC		26.7927732954
176PhosphorylationTPRRNFGSRGRSRSK
CCCCCCCCCCHHHHH		27.6820068231
180PhosphorylationNFGSRGRSRSKSLQK
CCCCCCHHHHHHHHH		43.6720068231
191PhosphorylationSLQKRSKSIGKSQSS
HHHHHHHHHCCCCCC		37.5130177828
195PhosphorylationRSKSIGKSQSSSPQK
HHHHHCCCCCCCCCC		30.0420363803
197PhosphorylationKSIGKSQSSSPQKQT
HHHCCCCCCCCCCCC		39.6120363803
198PhosphorylationSIGKSQSSSPQKQTS
HHCCCCCCCCCCCCC		38.1030631047
199PhosphorylationIGKSQSSSPQKQTSS
HCCCCCCCCCCCCCC		36.2820363803
204PhosphorylationSSSPQKQTSSGTKSR
CCCCCCCCCCCCCCC		31.7130576142
205PhosphorylationSSPQKQTSSGTKSRS
CCCCCCCCCCCCCCC		25.03-
206PhosphorylationSPQKQTSSGTKSRSH
CCCCCCCCCCCCCCC		54.6030631047
208PhosphorylationQKQTSSGTKSRSHGR
CCCCCCCCCCCCCCC		28.00-
210PhosphorylationQTSSGTKSRSHGRHS
CCCCCCCCCCCCCCC		38.5620726782
212PhosphorylationSSGTKSRSHGRHSDS
CCCCCCCCCCCCCCC		37.0730576142
217PhosphorylationSRSHGRHSDSIARSP
CCCCCCCCCCCCCCC		31.5222496350
219PhosphorylationSHGRHSDSIARSPCK
CCCCCCCCCCCCCCC		22.5917287340
223PhosphorylationHSDSIARSPCKSPKG
CCCCCCCCCCCCCCC		26.1517287340
227PhosphorylationIARSPCKSPKGYTNS
CCCCCCCCCCCCCCC		38.2617287340
236PhosphorylationKGYTNSETKVQTAKH
CCCCCCCCHHHHCCC		36.01-
236O-linked_GlycosylationKGYTNSETKVQTAKH
CCCCCCCCHHHHCCC		36.0123301498
240PhosphorylationNSETKVQTAKHSHFR
CCCCHHHHCCCHHHC		40.43-
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 SRS12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRS12_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 SRS12_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KI13B_HUMANKIF13Bphysical
27173435
GGYF1_HUMANGIGYF1physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
SYDE1_HUMANSYDE1physical
27173435
F110B_HUMANFAM110Bphysical
27173435
F110A_HUMANFAM110Aphysical
27173435
HDAC4_HUMANHDAC4physical
27173435
CING_HUMANCGNphysical
27173435
CBY1_HUMANCBY1physical
27173435
NGAP_HUMANRASAL2physical
27173435
KIF1C_HUMANKIF1Cphysical
27173435
SH3B4_HUMANSH3BP4physical
27173435
NAV1_HUMANNAV1physical
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 SRS12_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-219; SER-223 ANDSER-227, AND MASS SPECTROMETRY.

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