PININ_MOUSE - dbPTM
PININ_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PININ_MOUSE
UniProt AC O35691
Protein Name Pinin
Gene Name Pnn
Organism Mus musculus (Mouse).
Sequence Length 725
Subcellular Localization Nucleus speckle. Cell junction, desmosome. Cell-cell contact area, predominantly desmosome of intercellular adherens junction. Not a nucleocytoplasmic shuttling protein (By similarity)..
Protein Description Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Component of the PSAP complex which binds RNA in a sequence-independent manner and is proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. Involved in the establishment and maintenance of epithelia cell-cell adhesion (By similarity)..
Protein Sequence MAVAVRALQEQLEKAKESLKNVDENIRKLTGRDPNDVRPIQARLLALSGPGGGRGRGSLLLRRGFSDSGGGPPAKQRDLEGAVSRLGGERRTRRESRQESDPEDDDVKKPALQSSVVATSKERTRDLIQDQNMDEKGKQRNRRIFGLLMGTLQKFKQESTVATERQKRRQEIEQKLEVQAEEERKQVENERRELFEERRAKQTELRLLEQKVELAQLQEEWNEHNAKIIKYIRTKTKPHLFYIPGRMCPATQKLIEESQRKMNALFEGRRIEFAEQINKMEARPRRQSMKEKEHQVVRNEEQKAEQEEGKVAQREEELEETGNQHNDVEVEEAGEEEEKEAGIVHSDAEKEQEEEEQKQEMEVKTEEEAEVREGEKQQDSQPEEVMDVLEMVESVKHVIAEQEVMETNQVESIEPSENETSKELEPEMEFDVEPDKECKSLSPGKENINSQEVEKESEEKEEKEEKEPEPQPEPVAQPQPPPQPLPQSQPHSQPHSQPQPVLQSQPLCQPETLPLAVLQPPPQVIQEQGNLLPERKDFPLESIKLPEVSVEPVLTVHSENKSKNKTRSRSRGRARNKTSKSRSRSSSSSSSSSSSTSSSSGSSSSSGSSSSRSSSSSSSSTSGSSSRDSSSSTSSSSESRSRSRGRGHNRDRKHRRSMDRKRRDTSGLERSHKSSKGGSSRDRKGSKDKSSRPDRKRSISESSRSGKRSSRSERDRKSDRKDKRR
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------MAVAVRALQ
------CHHHHHHHH		9.66-
20AcetylationEKAKESLKNVDENIR
HHHHHHHHCHHHHHH		65.2922826441
48PhosphorylationQARLLALSGPGGGRG
HHHHHHHCCCCCCCC		37.0222942356
54DimethylationLSGPGGGRGRGSLLL
HCCCCCCCCHHHEEE		34.60-
54MethylationLSGPGGGRGRGSLLL
HCCCCCCCCHHHEEE		34.6024129315
56DimethylationGPGGGRGRGSLLLRR
CCCCCCCHHHEEECC		30.11-
56MethylationGPGGGRGRGSLLLRR
CCCCCCCHHHEEECC		30.1112020251
58PhosphorylationGGGRGRGSLLLRRGF
CCCCCHHHEEECCCC		17.9329176673
66PhosphorylationLLLRRGFSDSGGGPP
EEECCCCCCCCCCCC		33.4227087446
68PhosphorylationLRRGFSDSGGGPPAK
ECCCCCCCCCCCCHH		37.8325521595
84PhosphorylationRDLEGAVSRLGGERR
HCHHHHHHHHCCCHH		22.6629514104
92PhosphorylationRLGGERRTRRESRQE
HHCCCHHHHHHHHCC		40.0622817900
96PhosphorylationERRTRRESRQESDPE
CHHHHHHHHCCCCCC		37.1425521595
100PhosphorylationRRESRQESDPEDDDV
HHHHHCCCCCCCCCC		50.5627087446
114PhosphorylationVKKPALQSSVVATSK
CCCHHHHHHEEECCH		26.4225619855
115PhosphorylationKKPALQSSVVATSKE
CCHHHHHHEEECCHH		13.9825619855
119PhosphorylationLQSSVVATSKERTRD
HHHHEEECCHHHHHH		28.8125619855
120PhosphorylationQSSVVATSKERTRDL
HHHEEECCHHHHHHH		23.8425619855
136UbiquitinationQDQNMDEKGKQRNRR
HHCCCCHHHHHHHHH		68.12-
138AcetylationQNMDEKGKQRNRRIF
CCCCHHHHHHHHHHH		58.098276361
154AcetylationLLMGTLQKFKQESTV
HHHHHHHHHHHHHHH		58.618276373
156AcetylationMGTLQKFKQESTVAT
HHHHHHHHHHHHHHH		61.2622826441
159PhosphorylationLQKFKQESTVATERQ
HHHHHHHHHHHHHHH		26.20-
237SuccinylationKYIRTKTKPHLFYIP
HHHHHCCCCCEEECC		31.8123806337
237SuccinylationKYIRTKTKPHLFYIP
HHHHHCCCCCEEECC		31.81-
237AcetylationKYIRTKTKPHLFYIP
HHHHHCCCCCEEECC		31.8123806337
253AcetylationRMCPATQKLIEESQR
CCCHHHHHHHHHHHH		47.2622826441
288PhosphorylationEARPRRQSMKEKEHQ
HCCHHHHHHHHHHHH		29.9723684622
346PhosphorylationKEAGIVHSDAEKEQE
HHHCCCCCHHHHHHH		27.8525521595
365PhosphorylationKQEMEVKTEEEAEVR
HHHHCCCHHHHHHHH		54.5327600695
380PhosphorylationEGEKQQDSQPEEVMD
CCCCCCCCCCHHHHH		43.2127087446
381PhosphorylationGEKQQDSQPEEVMDV
CCCCCCCCCHHHHHH		58.6824719451
412PhosphorylationMETNQVESIEPSENE
HHHCCCCCCCCCCCC		33.1425266776
416PhosphorylationQVESIEPSENETSKE
CCCCCCCCCCCCCCC		40.0223984901
420PhosphorylationIEPSENETSKELEPE
CCCCCCCCCCCCCCC		57.5923984901
421PhosphorylationEPSENETSKELEPEM
CCCCCCCCCCCCCCC		20.2523984901
440PhosphorylationEPDKECKSLSPGKEN
CCCCCCCCCCCCCCC		45.8227742792
442PhosphorylationDKECKSLSPGKENIN
CCCCCCCCCCCCCCC		38.4026824392
450PhosphorylationPGKENINSQEVEKES
CCCCCCCHHHHHHHH		24.7425521595
457PhosphorylationSQEVEKESEEKEEKE
HHHHHHHHHHHHHHH		63.2225619855
555PhosphorylationVSVEPVLTVHSENKS
CEEEEEEEECCCCCC		19.1928285833
558PhosphorylationEPVLTVHSENKSKNK
EEEEEECCCCCCCCC		38.2326745281
603PhosphorylationTSSSSGSSSSSGSSS
CCCCCCCCCCCCCCC		37.4517203969
604PhosphorylationSSSSGSSSSSGSSSS
CCCCCCCCCCCCCCC		30.1617203969
605PhosphorylationSSSGSSSSSGSSSSR
CCCCCCCCCCCCCCC		40.4417203969
606PhosphorylationSSGSSSSSGSSSSRS
CCCCCCCCCCCCCCC		44.6417203969
608PhosphorylationGSSSSSGSSSSRSSS
CCCCCCCCCCCCCCC		29.0617203969
609PhosphorylationSSSSSGSSSSRSSSS
CCCCCCCCCCCCCCC		35.5417203969
610PhosphorylationSSSSGSSSSRSSSSS
CCCCCCCCCCCCCCC		31.3117203969
611PhosphorylationSSSGSSSSRSSSSSS
CCCCCCCCCCCCCCC		37.8217203969
630PhosphorylationGSSSRDSSSSTSSSS
CCCCCCCCCCCCCCH		32.3722345495
635PhosphorylationDSSSSTSSSSESRSR
CCCCCCCCCHHHHHH		37.6622345495
636PhosphorylationSSSSTSSSSESRSRS
CCCCCCCCHHHHHHC		37.5822345495
637PhosphorylationSSSTSSSSESRSRSR
CCCCCCCHHHHHHCC		41.3522345495
643PhosphorylationSSESRSRSRGRGHNR
CHHHHHHCCCCCCCH		40.0922345495
665PhosphorylationMDRKRRDTSGLERSH
HHHHHHCCCCCCHHH		23.9225266776
666PhosphorylationDRKRRDTSGLERSHK
HHHHHCCCCCCHHHC		45.7426824392
679PhosphorylationHKSSKGGSSRDRKGS
HCCCCCCCCCCCCCC		30.7619144319
698PhosphorylationSRPDRKRSISESSRS
CCCCHHHHHCHHHHH		33.2426824392
700PhosphorylationPDRKRSISESSRSGK
CCHHHHHCHHHHHCC		32.4525521595
702PhosphorylationRKRSISESSRSGKRS
HHHHHCHHHHHCCCC		25.0225521595
703PhosphorylationKRSISESSRSGKRSS
HHHHCHHHHHCCCCC		26.8125521595
705PhosphorylationSISESSRSGKRSSRS
HHCHHHHHCCCCCHH		51.0925266776
709PhosphorylationSSRSGKRSSRSERDR
HHHHCCCCCHHHHHH		33.3222802335
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 PININ_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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

loading...

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-66; SER-100 AND SER-380,AND MASS SPECTROMETRY.
"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-66; SER-100; SER-380 ANDSER-679, 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-96; SER-100 AND SER-346,AND MASS 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-440 AND SER-442, ANDMASS SPECTROMETRY.

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