STRAP_MOUSE - dbPTM
STRAP_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STRAP_MOUSE
UniProt AC Q9Z1Z2
Protein Name Serine-threonine kinase receptor-associated protein
Gene Name Strap
Organism Mus musculus (Mouse).
Sequence Length 350
Subcellular Localization Cytoplasm. Nucleus. Localized predominantly in the cytoplasm but also found in the nucleus..
Protein Description The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein (By similarity)..
Protein Sequence MAMRQTPLTCSGHTRPVVDLAFSGITPYGYFLISACKDGKPMLRQGDTGDWIGTFLGHKGAVWGATLNKDATKAATAAADFTAKVWDAVSGDELMTLAHKHIVKTVDFTQDSNYLLTGGQDKLLRIYDLNKPEAEPKEISGHTSGIKKALWCSDDKQILSADDKTVRLWDHATMTEVKSLNFNMSVSSMEYIPEGEILVITYGRSIAFHSAVSLEPIKSFEAPATINSASLHPEKEFLVAGGEDFKLYKYDYNSGEELESYKGHFGPIHCVRFSPDGELYASGSEDGTLRLWQTVVGKTYGLWKCVLPEEDSGELAKPKIGFPETAEEELEEIASENSDSIYSSTPEVKA
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
59UbiquitinationIGTFLGHKGAVWGAT
HHHHHCCCCCEEEEE		46.93-
73UbiquitinationTLNKDATKAATAAAD
ECCHHHHHHHHHHHH		37.43-
104AcetylationLAHKHIVKTVDFTQD
HHHHCEEEEEECCCC		42.0822826441
114PhosphorylationDFTQDSNYLLTGGQD
ECCCCCCCEEECCCC		13.67-
122AcetylationLLTGGQDKLLRIYDL
EEECCCCEEEEEEEC		41.3523236377
122UbiquitinationLLTGGQDKLLRIYDL
EEECCCCEEEEEEEC		41.35-
131UbiquitinationLRIYDLNKPEAEPKE
EEEEECCCCCCCCCC		52.08-
156AcetylationALWCSDDKQILSADD
EEEECCCCCEECCCC		44.2022826441
219PhosphorylationVSLEPIKSFEAPATI
CCCCCCCCCCCCEEE		29.10-
249AcetylationGEDFKLYKYDYNSGE
CCCEEEEEECCCCCC		41.9222826441
252PhosphorylationFKLYKYDYNSGEELE
EEEEEECCCCCCCHH		14.2426525534
254PhosphorylationLYKYDYNSGEELESY
EEEECCCCCCCHHHC		41.1626525534
262AcetylationGEELESYKGHFGPIH
CCCHHHCCCCCCCEE		56.0122826441
280PhosphorylationFSPDGELYASGSEDG
ECCCCCEEECCCCCC		8.4017203969
282PhosphorylationPDGELYASGSEDGTL
CCCCEEECCCCCCCE		29.3326525534
305GlutathionylationKTYGLWKCVLPEEDS
CCCEEEEEECCCCCC		2.2824333276
305S-nitrosylationKTYGLWKCVLPEEDS
CCCEEEEEECCCCCC		2.2820925432
305S-nitrosocysteineKTYGLWKCVLPEEDS
CCCEEEEEECCCCCC		2.28-
312PhosphorylationCVLPEEDSGELAKPK
EECCCCCCCCCCCCC		37.1325266776
317UbiquitinationEDSGELAKPKIGFPE
CCCCCCCCCCCCCCC		60.51-
319UbiquitinationSGELAKPKIGFPETA
CCCCCCCCCCCCCCH		55.55-
325PhosphorylationPKIGFPETAEEELEE
CCCCCCCCHHHHHHH		39.3425159016
335PhosphorylationEELEEIASENSDSIY
HHHHHHHHHCCCCCC		42.8626824392
338PhosphorylationEEIASENSDSIYSST
HHHHHHCCCCCCCCC		28.7827087446
340PhosphorylationIASENSDSIYSSTPE
HHHHCCCCCCCCCCC		24.2127087446
342PhosphorylationSENSDSIYSSTPEVK
HHCCCCCCCCCCCCC		10.6623984901
343PhosphorylationENSDSIYSSTPEVKA
HCCCCCCCCCCCCCC		26.5125159016
344PhosphorylationNSDSIYSSTPEVKA-
CCCCCCCCCCCCCC-		30.8925159016
345PhosphorylationSDSIYSSTPEVKA--
CCCCCCCCCCCCC--		19.9627087446
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
188SPhosphorylationKinaseMELKQ61846
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STRAP_MOUSE !!
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 STRAP_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of STRAP_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STRAP_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-342, AND MASSSPECTROMETRY.

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