SPF30_HUMAN - dbPTM
SPF30_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPF30_HUMAN
UniProt AC O75940
Protein Name Survival of motor neuron-related-splicing factor 30
Gene Name SMNDC1
Organism Homo sapiens (Human).
Sequence Length 238
Subcellular Localization Nucleus speckle. Nucleus, Cajal body. Detected in nuclear speckles containing snRNP and in Cajal (coiled) bodies.
Protein Description Necessary for spliceosome assembly. Overexpression causes apoptosis..
Protein Sequence MSEDLAKQLASYKAQLQQVEAALSGNGENEDLLKLKKDLQEVIELTKDLLSTQPSETLASSDSFASTQPTHSWKVGDKCMAVWSEDGQCYEAEIEEIDEENGTAAITFAGYGNAEVTPLLNLKPVEEGRKAKEDSGNKPMSKKEMIAQQREYKKKKALKKAQRIKELEQEREDQKVKWQQFNNRAYSKNKKGQVKRSIFASPESVTGKVGVGTCGIADKPMTQYQDTSKYNVRHLMPQ
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
7Acetylation-MSEDLAKQLASYKA
-CCHHHHHHHHHHHH		53.8125953088
13UbiquitinationAKQLASYKAQLQQVE
HHHHHHHHHHHHHHH		27.4529967540
37UbiquitinationEDLLKLKKDLQEVIE
HHHHHHHHHHHHHHH		74.2833845483
46PhosphorylationLQEVIELTKDLLSTQ
HHHHHHHHHHHHCCC		15.1025690035
51PhosphorylationELTKDLLSTQPSETL
HHHHHHHCCCCCCCC		32.0928450419
52PhosphorylationLTKDLLSTQPSETLA
HHHHHHCCCCCCCCC		44.4628450419
55PhosphorylationDLLSTQPSETLASSD
HHHCCCCCCCCCCCC		33.1428450419
57PhosphorylationLSTQPSETLASSDSF
HCCCCCCCCCCCCCC		31.7730576142
60PhosphorylationQPSETLASSDSFAST
CCCCCCCCCCCCCCC		37.4830576142
61PhosphorylationPSETLASSDSFASTQ
CCCCCCCCCCCCCCC		31.5028450419
63PhosphorylationETLASSDSFASTQPT
CCCCCCCCCCCCCCC		25.3528450419
66PhosphorylationASSDSFASTQPTHSW
CCCCCCCCCCCCCCC		26.0928450419
67PhosphorylationSSDSFASTQPTHSWK
CCCCCCCCCCCCCCE		34.8328450419
70PhosphorylationSFASTQPTHSWKVGD
CCCCCCCCCCCEECC		20.8028450419
72PhosphorylationASTQPTHSWKVGDKC
CCCCCCCCCEECCEE		30.9430576142
99UbiquitinationAEIEEIDEENGTAAI
EEEEEECCCCCEEEE		60.0524816145
121UbiquitinationAEVTPLLNLKPVEEG
CEEEECCCCEECHHH		54.4224816145
135PhosphorylationGRKAKEDSGNKPMSK
HHCCCCCCCCCCCCH		45.4126074081
138UbiquitinationAKEDSGNKPMSKKEM
CCCCCCCCCCCHHHH		45.6924816145
141PhosphorylationDSGNKPMSKKEMIAQ
CCCCCCCCHHHHHHH		49.4526074081
1422-HydroxyisobutyrylationSGNKPMSKKEMIAQQ
CCCCCCCHHHHHHHH		46.64-
152PhosphorylationMIAQQREYKKKKALK
HHHHHHHHHHHHHHH		30.2326074081
156UbiquitinationQREYKKKKALKKAQR
HHHHHHHHHHHHHHH		68.7624816145
160UbiquitinationKKKKALKKAQRIKEL
HHHHHHHHHHHHHHH		51.0724816145
165UbiquitinationLKKAQRIKELEQERE
HHHHHHHHHHHHHHH		59.44-
177UbiquitinationEREDQKVKWQQFNNR
HHHHHHHCHHHHHHH		46.4527667366
184MethylationKWQQFNNRAYSKNKK
CHHHHHHHHHCCCCC		35.69115367587
186PhosphorylationQQFNNRAYSKNKKGQ
HHHHHHHHCCCCCCC		19.5526074081
187PhosphorylationQFNNRAYSKNKKGQV
HHHHHHHCCCCCCCE		28.8626074081
195UbiquitinationKNKKGQVKRSIFASP
CCCCCCEEEEEECCC		32.3224816145
197PhosphorylationKKGQVKRSIFASPES
CCCCEEEEEECCCCC		19.1523403867
201PhosphorylationVKRSIFASPESVTGK
EEEEEECCCCCCCCC		20.6019664994
204PhosphorylationSIFASPESVTGKVGV
EEECCCCCCCCCEEC		28.5030266825
206PhosphorylationFASPESVTGKVGVGT
ECCCCCCCCCEECCC		40.3330266825
208AcetylationSPESVTGKVGVGTCG
CCCCCCCCEECCCCC		26.8425953088
213PhosphorylationTGKVGVGTCGIADKP
CCCEECCCCCCCCCC		12.73-
219AcetylationGTCGIADKPMTQYQD
CCCCCCCCCCCCCCC		27.8919608861
219UbiquitinationGTCGIADKPMTQYQD
CCCCCCCCCCCCCCC		27.8919608861
222PhosphorylationGIADKPMTQYQDTSK
CCCCCCCCCCCCCCC		32.4328796482
224PhosphorylationADKPMTQYQDTSKYN
CCCCCCCCCCCCCCC		10.1328796482
227PhosphorylationPMTQYQDTSKYNVRH
CCCCCCCCCCCCHHH		16.1628796482
228PhosphorylationMTQYQDTSKYNVRHL
CCCCCCCCCCCHHHC		41.2428796482
229UbiquitinationTQYQDTSKYNVRHLM
CCCCCCCCCCHHHCC		42.8332015554
229AcetylationTQYQDTSKYNVRHLM
CCCCCCCCCCHHHCC		42.8326051181
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 SPF30_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPF30_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 SPF30_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SF3B3_HUMANSF3B3physical
17353931
SF3B2_HUMANSF3B2physical
17353931
RL3_HUMANRPL3physical
17353931
TSR1_HUMANTSR1physical
17353931
EWS_HUMANEWSR1physical
17353931
CK5P3_HUMANCDK5RAP3physical
17353931
FDFT_HUMANFDFT1physical
17353931
SF3A3_HUMANSF3A3physical
17353931
SSF1_HUMANPPANphysical
17353931
MRM3_HUMANRNMTL1physical
17353931
SF3B4_HUMANSF3B4physical
17353931
RUVB1_HUMANRUVBL1physical
17353931
SF3B1_HUMANSF3B1physical
17353931
DDX21_HUMANDDX21physical
17353931
U520_HUMANSNRNP200physical
11331595
PRPF3_HUMANPRPF3physical
22365833
NF2IP_HUMANNFATC2IPphysical
26344197
RGAP1_HUMANRACGAP1physical
26344197
RBM42_HUMANRBM42physical
26344197
RRBP1_HUMANRRBP1physical
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 SPF30_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-219, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND MASSSPECTROMETRY.
"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-201, 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-201, AND MASSSPECTROMETRY.

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