SRRT_MOUSE - dbPTM
SRRT_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRRT_MOUSE
UniProt AC Q99MR6
Protein Name Serrate RNA effector molecule homolog
Gene Name Srrt
Organism Mus musculus (Mouse).
Sequence Length 875
Subcellular Localization Nucleus, nucleoplasm. Cytoplasm. Predominantly nuclear. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent way.
Protein Description Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped RNA); however interaction is probably mediated via its interaction with NCBP1/CBP80 component of the CBC complex. Involved in cell cycle progression at S phase. Does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription..
Protein Sequence MGDSDDEYDRRRRDKFRRERSDYDRSRERDERRRGDDWNDREWDRGRERRSRGEYRDYDRNRRERFSPPRHELSPPQKRMRRDWDEHSSDPYHSGYDMPYAGGGGGPTYGPPQPWGHPDVHIMQHHVLPIQARLGSIAEIDLGVPPPIMKSFKEFLLSLDDSVDETEAVKRYNDYKLDFRRQQMQDFFLAHKDEEWFRSKYHPDEVGKRRQEARGALQNRLKVFLSLMESGWFDNLLLDIDKADAIVKMLDAAVIKMEGGTENDLRILEQEEEEEQAGKTGEASKKEEARAGPALGEGERKANDKDEKKEDGKQAENDSSNDDKTKKSEGDGDKEEKKEEAEKEAKKSKKRNRKQSGDDSFDEGSVSESESESEGGQAEEEKEEAEEALKEKEKPKEEEKEKPKDAAGLECKPRPLHKTCSLFMRNIAPNISRAEIISLCKRYPGFMRVALSEPQPERRFFRRGWVTFDRSVNIKEICWNLQNIRLRECELSPGVNRDLTRRVRNINGITQHKQIVRNDIKLAAKLIHTLDDRTQLWASEPGTPPVPTSLPSQNPILKNITDYLIEEVSAEEEELLGSSGGPPPEEPPKEGNPAEINVERDEKLIKVLDKLLLYLRIVHSLDYYNTCEYPNEDEMPNRCGIIHVRGPMPPNRISHGEVLEWQKTFEEKLTPLLSVRESLSEEEAQKMGRKDPEQEVEKFVTSNTQELGKDKWLCPLSGKKFKGPEFVRKHIFNKHAEKIEEVKKEVAFFNNFLTDAKRPALPEIKPAQPPGPAQILPPGLTPGLPYPHQTPQGLMPYGQPRPPILGYGAGAVRPAVPTGGPPYPHAPYGAGRGNYDAFRGQGGYPGKPRNRMVRGDPRAIVEYRDLDAPDDVDFF
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
2Acetylation------MGDSDDEYD
------CCCCHHHHH		43.03-
4Phosphorylation----MGDSDDEYDRR
----CCCCHHHHHHH		41.0326824392
8PhosphorylationMGDSDDEYDRRRRDK
CCCCHHHHHHHHHHH		23.0318846507
21PhosphorylationDKFRRERSDYDRSRE
HHHHHHHHHHHHHHH		35.4525266776
23PhosphorylationFRRERSDYDRSRERD
HHHHHHHHHHHHHHH		17.9528066266
26PhosphorylationERSDYDRSRERDERR
HHHHHHHHHHHHHHH		35.2825266776
51PhosphorylationDRGRERRSRGEYRDY
HHHCHHHHCCCCCCC		51.3524719451
67PhosphorylationRNRRERFSPPRHELS
CCCCHHCCCCHHHCC		39.9727087446
74PhosphorylationSPPRHELSPPQKRMR
CCCHHHCCCCHHHHC		31.3927087446
88PhosphorylationRRDWDEHSSDPYHSG
CCCCCCCCCCCCCCC		34.10-
89PhosphorylationRDWDEHSSDPYHSGY
CCCCCCCCCCCCCCC		44.5023649490
94PhosphorylationHSSDPYHSGYDMPYA
CCCCCCCCCCCCCCC		32.9523649490
136PhosphorylationPIQARLGSIAEIDLG
HHHHCCCCCEEECCC		24.1828833060
153UbiquitinationPPIMKSFKEFLLSLD
CHHHHHHHHHHHCCC		55.4322790023
170UbiquitinationVDETEAVKRYNDYKL
CCHHHHHHHHHCCCC		57.1022790023
214MethylationGKRRQEARGALQNRL
HHHHHHHHHHHHHHH		30.1118965583
214DimethylationGKRRQEARGALQNRL
HHHHHHHHHHHHHHH		30.11-
279UbiquitinationEEEEQAGKTGEASKK
HHHHHCCCCCCHHHH		57.2722790023
319PhosphorylationGKQAENDSSNDDKTK
CCCCCCCCCCCHHHC		42.4927087446
320PhosphorylationKQAENDSSNDDKTKK
CCCCCCCCCCHHHCC		47.3327087446
356PhosphorylationKKRNRKQSGDDSFDE
HHHHHHCCCCCCCCC		47.4226525534
365PhosphorylationDDSFDEGSVSESESE
CCCCCCCCCCCCHHH		22.0325293948
367PhosphorylationSFDEGSVSESESESE
CCCCCCCCCCHHHCC		36.7825293948
369PhosphorylationDEGSVSESESESEGG
CCCCCCCCHHHCCCC		38.6325293948
371PhosphorylationGSVSESESESEGGQA
CCCCCCHHHCCCCCC		56.5625293948
373PhosphorylationVSESESESEGGQAEE
CCCCHHHCCCCCCHH		51.3125293948
419PhosphorylationKPRPLHKTCSLFMRN
CCCCHHHHHHHHHHH		9.1429176673
421PhosphorylationRPLHKTCSLFMRNIA
CCHHHHHHHHHHHCC		29.8529176673
475AcetylationFDRSVNIKEICWNLQ
ECCCCCHHHHHHCCC		35.5022826441
489S-palmitoylationQNIRLRECELSPGVN
CCCCCEECCCCCCCC		5.2926165157
492PhosphorylationRLRECELSPGVNRDL
CCEECCCCCCCCHHH		9.4126824392
529PhosphorylationLAAKLIHTLDDRTQL
HHHHHHHHCCCCCCH		25.5325367039
534PhosphorylationIHTLDDRTQLWASEP
HHHCCCCCCHHCCCC		34.7025619855
539PhosphorylationDRTQLWASEPGTPPV
CCCCHHCCCCCCCCC		32.5124925903
543PhosphorylationLWASEPGTPPVPTSL
HHCCCCCCCCCCCCC		34.8224925903
548PhosphorylationPGTPPVPTSLPSQNP
CCCCCCCCCCCCCCH		43.0324925903
549PhosphorylationGTPPVPTSLPSQNPI
CCCCCCCCCCCCCHH		32.0124925903
552PhosphorylationPVPTSLPSQNPILKN
CCCCCCCCCCHHHHH		48.1325619855
561PhosphorylationNPILKNITDYLIEEV
CHHHHHHHHHHHHHC		28.1626643407
563PhosphorylationILKNITDYLIEEVSA
HHHHHHHHHHHHCCH		10.8326643407
569PhosphorylationDYLIEEVSAEEEELL
HHHHHHCCHHHHHHH		32.9921659605
578PhosphorylationEEEELLGSSGGPPPE
HHHHHHCCCCCCCCC		26.2726643407
579PhosphorylationEEELLGSSGGPPPEE
HHHHHCCCCCCCCCC		46.0726643407
639S-nitrosocysteineEDEMPNRCGIIHVRG
CCCCCCCCEEEEECC		6.12-
639S-nitrosylationEDEMPNRCGIIHVRG
CCCCCCCCEEEEECC		6.1220925432
670PhosphorylationKTFEEKLTPLLSVRE
HHHHHHHHHHHHHHH		23.98-
678PhosphorylationPLLSVRESLSEEEAQ
HHHHHHHHCCHHHHH		26.99-
686UbiquitinationLSEEEAQKMGRKDPE
CCHHHHHHCCCCCHH		50.8222790023
709AcetylationSNTQELGKDKWLCPL
CCHHHHCCCCEEECC		69.6223806337
711AcetylationTQELGKDKWLCPLSG
HHHHCCCCEEECCCC		45.6223806337
717PhosphorylationDKWLCPLSGKKFKGP
CCEEECCCCCCCCCH		33.4424719451
719AcetylationWLCPLSGKKFKGPEF
EEECCCCCCCCCHHH		52.22132753
832MethylationHAPYGAGRGNYDAFR
CCCCCCCCCCCHHCC		29.65-
839MethylationRGNYDAFRGQGGYPG
CCCCHHCCCCCCCCC		37.9430986123
844PhosphorylationAFRGQGGYPGKPRNR
HCCCCCCCCCCCCCC		18.68-
849MethylationGGYPGKPRNRMVRGD
CCCCCCCCCCCCCCC		47.04-
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 SRRT_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-543, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory