PSIP1_MOUSE - dbPTM
PSIP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSIP1_MOUSE
UniProt AC Q99JF8
Protein Name PC4 and SFRS1-interacting protein
Gene Name Psip1
Organism Mus musculus (Mouse).
Sequence Length 528
Subcellular Localization Nucleus.
Protein Description Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis (By similarity)..
Protein Sequence MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKFSSQQASTKQSNASSDVEVEEKETNVSKEDTDQEEKASNEDVTKAVDITTPKAARRGRKRKAEKQVDTEEAGMVTAATASNVKASPKRGRPAATEVKIPKPRGRPKVVKQPCPSDGDMVIDEDKSKKKGPEEKQPKKQLKKEEEGQKEEEKPRKEPDKKEGKKEVESKRKNLAKPGVTSTSDSEDEDDQEGEKKRKGGRNFQAAHRRNMLKGQHEKEAGDRKRKQEEQMETEQQNKDEGKKPEVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNKSLAEQRQHEEANKTKDQGKKGPNKKLEKEPTGTKSLNGGSDAQESNHPQHNGDSNEDGKDSREASSKTKPPGEEREAEISLKESTLDN
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
6Acetylation--MTRDFKPGDLIFA
--CCCCCCCCCEEEE		52.9922826441
56AcetylationETAFLGPKDIFPYSE
CCCCCCHHHCCCCCC		62.756568765
61PhosphorylationGPKDIFPYSENKEKY
CHHHCCCCCCCHHHH		20.1920469934
62PhosphorylationPKDIFPYSENKEKYG
HHHCCCCCCCHHHHC		34.6220469934
65AcetylationIFPYSENKEKYGKPN
CCCCCCCHHHHCCCC		52.086568915
65UbiquitinationIFPYSENKEKYGKPN
CCCCCCCHHHHCCCC		52.0822790023
91AcetylationIDNNPKVKFSSQQAS
CCCCCCCCCCCCCCC		45.7323806337
94PhosphorylationNPKVKFSSQQASTKQ
CCCCCCCCCCCCCCC		29.4622817900
98PhosphorylationKFSSQQASTKQSNAS
CCCCCCCCCCCCCCC		31.6225619855
99PhosphorylationFSSQQASTKQSNASS
CCCCCCCCCCCCCCC		35.8028285833
102PhosphorylationQQASTKQSNASSDVE
CCCCCCCCCCCCCCC		35.6025521595
105PhosphorylationSTKQSNASSDVEVEE
CCCCCCCCCCCCCCH		31.1825521595
106PhosphorylationTKQSNASSDVEVEEK
CCCCCCCCCCCCCHH		43.1727087446
115PhosphorylationVEVEEKETNVSKEDT
CCCCHHHHCCCHHHC		52.5724925903
118PhosphorylationEEKETNVSKEDTDQE
CHHHHCCCHHHCCHH		32.1924925903
122PhosphorylationTNVSKEDTDQEEKAS
HCCCHHHCCHHHHHC		40.4527087446
129PhosphorylationTDQEEKASNEDVTKA
CCHHHHHCCCCHHHH		52.3924925903
134PhosphorylationKASNEDVTKAVDITT
HHCCCCHHHHHHCCC		26.1324925903
135AcetylationASNEDVTKAVDITTP
HCCCCHHHHHHCCCH		46.3823806337
140PhosphorylationVTKAVDITTPKAARR
HHHHHHCCCHHHHHH		32.3624068923
141PhosphorylationTKAVDITTPKAARRG
HHHHHCCCHHHHHHH		24.1126824392
143AcetylationAVDITTPKAARRGRK
HHHCCCHHHHHHHCH		53.2223806337
152AcetylationARRGRKRKAEKQVDT
HHHHCHHHHHHCCCH		65.0223806337
155AcetylationGRKRKAEKQVDTEEA
HCHHHHHHCCCHHHH		61.5523806337
159PhosphorylationKAEKQVDTEEAGMVT
HHHHCCCHHHHHHCH		36.5525619855
164OxidationVDTEEAGMVTAATAS
CCHHHHHHCHHHHHH		2.8917242355
166PhosphorylationTEEAGMVTAATASNV
HHHHHHCHHHHHHCC		11.1524925903
169PhosphorylationAGMVTAATASNVKAS
HHHCHHHHHHCCCCC		28.3124925903
171PhosphorylationMVTAATASNVKASPK
HCHHHHHHCCCCCCC		37.4924925903
176PhosphorylationTASNVKASPKRGRPA
HHHCCCCCCCCCCCC		25.8224925903
200AcetylationRGRPKVVKQPCPSDG
CCCCCCCCCCCCCCC		52.0622826441
205PhosphorylationVVKQPCPSDGDMVID
CCCCCCCCCCCCCCC		62.0325521595
269PhosphorylationNLAKPGVTSTSDSED
HHCCCCCCCCCCCCC		32.0018388127
270PhosphorylationLAKPGVTSTSDSEDE
HCCCCCCCCCCCCCC		24.4124925903
271PhosphorylationAKPGVTSTSDSEDED
CCCCCCCCCCCCCCC		27.4718388127
272PhosphorylationKPGVTSTSDSEDEDD
CCCCCCCCCCCCCCC		38.6218388127
274PhosphorylationGVTSTSDSEDEDDQE
CCCCCCCCCCCCCCH		46.8718388127
302UbiquitinationAHRRNMLKGQHEKEA
HHHHHHHHHHHHHHH		45.84-
344PhosphorylationKVEKKRETSMDSRLQ
HHHHHHHHCHHHHHH		33.1322817900
345PhosphorylationVEKKRETSMDSRLQR
HHHHHHHCHHHHHHH		18.8126824392
362UbiquitinationAEIKNSLKIDNLDVN
HHHHHCCCCCCCCHH		48.08-
413AcetylationVSQVIMEKSTMLYNK
HHHHHHHHHHHHHHH		33.5722826441
420AcetylationKSTMLYNKFKNMFLV
HHHHHHHHHCCEEEE		44.1323806337
422UbiquitinationTMLYNKFKNMFLVGE
HHHHHHHCCEEEECC		49.46-
432PhosphorylationFLVGEGDSVITQVLN
EEECCCCHHHHHHHC		26.6924759943
435PhosphorylationGEGDSVITQVLNKSL
CCCCHHHHHHHCHHH		15.5229895711
440UbiquitinationVITQVLNKSLAEQRQ
HHHHHHCHHHHHHHH		42.56-
441PhosphorylationITQVLNKSLAEQRQH
HHHHHCHHHHHHHHH		31.5729550500
465AcetylationGKKGPNKKLEKEPTG
CCCCCCCCCCCCCCC		69.4023806337
475PhosphorylationKEPTGTKSLNGGSDA
CCCCCCCCCCCCCCC		27.2328973931
494PhosphorylationHPQHNGDSNEDGKDS
CCCCCCCCCCCCCCH		43.4428973931
505PhosphorylationGKDSREASSKTKPPG
CCCHHHHHHCCCCCC		27.8418779572
515CitrullinationTKPPGEEREAEISLK
CCCCCHHHHHHEECC		44.0924463520
515CitrullinationTKPPGEEREAEISLK
CCCCCHHHHHHEECC		44.09-
520PhosphorylationEEREAEISLKESTLD
HHHHHHEECCHHHCC		25.5422817900
522UbiquitinationREAEISLKESTLDN-
HHHHEECCHHHCCC-		42.71-
525PhosphorylationEISLKESTLDN----
HEECCHHHCCC----		38.94-
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 PSIP1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSIP1_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 PSIP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PSIP1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSIP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-176, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-272 ANDSER-274, AND MASS SPECTROMETRY.
"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-274, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-274, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-129; SER-272AND SER-274, AND MASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-274, ANDMASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-134 AND THR-141, ANDMASS SPECTROMETRY.

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