PRAX_MOUSE - dbPTM
PRAX_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRAX_MOUSE
UniProt AC O55103
Protein Name Periaxin
Gene Name Prx
Organism Mus musculus (Mouse).
Sequence Length 1391
Subcellular Localization Cell membrane . Cell junction . Colocalizes with ACTB at tricellular junctions between eye lens fiber cells.
Isoform 1: Cell membrane
Peripheral membrane protein
Cytoplasmic side . Nucleus . Cytoplasm . Detected in the Schwann cell nucleus
Protein Description Scaffolding protein that functions as part of a dystroglycan complex in Schwann cells, and as part of EZR and AHNAK-containing complexes in eye lens fiber cells. [PubMed: 11430802]
Protein Sequence MEARSRSAEELRRAELVEIIVETEAQTGVSGFNVAGGGKEGIFVRELREDSPAAKSLSLQEGDQLLSARVFFENFKYEDALRLLQCAEPYKVSFCLKRTVPTGDLALRPGTVSGYEMKGPRAKVAKLNIQSLAPVKKKKMVTGALGTPADLAPVDVEFSFPKFSRLRRGLKAEAVKGPVPAAPARRRLQLPRLRVREVAEEAQVARMAAAAPPPRKAKAEAEAATGAGFTAPQIELVGPRLPSAEVGVPQVSVPKGTPSTEAASGFALHLPTLGLGAPAAPAVEPPATGIQVPQVELPTLPSLPTLPTLPCLDTQEGAAVVKVPTLDVAAPSMGVDLALPGAEVEAQGEVPEVALKMPRLSFPRFGIRGKEATEAKVVKGSPEAKAKGPRLRMPTFGLSLLEPRPSGPEAVAESKLKLPTLKMPSFGIGVAGPEVKAPTGPEVKLPKVPEVKLPKVPEAAIPDVQLPEVQLPKMSDMKLPKIPEMVVPDVRLPEVQLPKVPEMKVPEMKLPKWPEMAVPDVHLPDVQLPKVPEMKLPKVPEMAVPDVHLPDVQLPKVPEMKLPEMKLPKVPEMAVPDVRLPEVQLPKVSEVKLPKMPEMAVPDVHLPELQLPKMSEVKLPKMPEMAVPDVRLPEVQLPKVSEMKLPKMPEMTMPDIRLPEVQLPKVPDIKLPEMKLPEIKLPKVPDMAVPDVPLPELQLPKVSDIRLPEMQVSQVPEVQLPKMPEMKLSKVPEVQRKSAGAEQAKGTEFSFKLPKMTMPKLGKVGKPGEASIEVPDKLMTLPCLQPEVGTEASHVGVPSLSLPSVELDLPGALGLEGQVQEAVPGKVEKPEGPRVAVGVGEVGFRVPSVEIVTPQLPTVEVEKEQLEMVEMKVKPSSKFSLPKFGLSGPKAVKGEVEGPGRATKLKVSKFTISLPKARAGTEAEAKGAGEAGLLPALDLSIPQLSLDAQLPSGKVEVADSKPKSSRFALPKFGVKGRDSEADVLVAGEAELEGKGWGWDGKVKMPKLKMPSFGLSRGKEAETQDGRVSPGEKLEAIAGQLKIPAVELVTPGAQETEKVTSGVKPSGLQVSTTGQVVAEGQESVQRVSTLGISLPQVELASFGEAGPEIVAPSAEGTAGSRVQVPQVMLELPGTQVAGGDLLVGEGIFKMPTVTVPQLELDVGLGHEAQAGEAAKSEGGIKLKLPTLGTGSRGEGVEPQGPEAQRTFHLSLPDVELTSPVSSHAEYQVVEGDGDGGHKLKVRLPLFGLAKAKEGIEVGEKVKSPKLRLPRVGFSQSESVSGEGSPSPEEEEEGSGEGASSRRGRVRVRLPRVGLASPSKVSKGQEGDATSKSPVGEKSPKFRFPRVSLSPKARSGSRDREEGGFRVRLPSVGFSETAVPGSTRIEGTQAAAI
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
7Phosphorylation-MEARSRSAEELRRA
-CCHHHCCHHHHHHH		41.0822817900
102PhosphorylationCLKRTVPTGDLALRP
EEECCCCCCCEEECC		38.7028285833
111PhosphorylationDLALRPGTVSGYEMK
CEEECCCEECCEECC		17.7428285833
139 (in isoform 2)Phosphorylation-47.7028464351
142PhosphorylationVKKKKMVTGALGTPA
CCCHHCCCCCCCCCC		17.15-
243PhosphorylationLVGPRLPSAEVGVPQ
EECCCCCCCCCCCCE		41.47-
381PhosphorylationEAKVVKGSPEAKAKG
EEEEECCCHHHHHCC		17.5326824392
615PhosphorylationELQLPKMSEVKLPKM
CCCCCCCCCCCCCCC		45.4229514104
750PhosphorylationQAKGTEFSFKLPKMT
CCCCCCEEEECCCCC		18.4222817900
771PhosphorylationVGKPGEASIEVPDKL
CCCCCCCCEECCCCC		18.2523375375
848PhosphorylationEVGFRVPSVEIVTPQ
CCCEECCCEEEECCC		29.53-
913PhosphorylationKVSKFTISLPKARAG
EEEEEEEECCCCCCC		35.2521454597
921PhosphorylationLPKARAGTEAEAKGA
CCCCCCCCHHHHCCC		30.9121454597
979PhosphorylationFGVKGRDSEADVLVA
CCCCCCCCCCCEEEE		33.0722817900
1011PhosphorylationMPKLKMPSFGLSRGK
CCCCCCCCCCCCCCC		28.5722817900
1022PhosphorylationSRGKEAETQDGRVSP
CCCCCCCCCCCCCCC		38.7226824392
1028PhosphorylationETQDGRVSPGEKLEA
CCCCCCCCCHHHHHH		26.3126824392
1188PhosphorylationLKLPTLGTGSRGEGV
EECCCCCCCCCCCCC		34.7921082442
1190PhosphorylationLPTLGTGSRGEGVEP
CCCCCCCCCCCCCCC		36.6321183079
1216PhosphorylationSLPDVELTSPVSSHA
CCCCCEECCCCCCCE		19.9225338131
1279PhosphorylationFSQSESVSGEGSPSP
CCCCCCCCCCCCCCH		40.1722817900
1283PhosphorylationESVSGEGSPSPEEEE
CCCCCCCCCCHHHCC		20.2222817900
1285PhosphorylationVSGEGSPSPEEEEEG
CCCCCCCCHHHCCCC		46.7922817900
1293PhosphorylationPEEEEEGSGEGASSR
HHHCCCCCCCCCCCC		36.6322817900
1315PhosphorylationLPRVGLASPSKVSKG
CCCCCCCCHHHCCCC		34.4526824392
1317PhosphorylationRVGLASPSKVSKGQE
CCCCCCHHHCCCCCC		43.1028464351
1328PhosphorylationKGQEGDATSKSPVGE
CCCCCCCCCCCCCCC		41.2321082442
1331PhosphorylationEGDATSKSPVGEKSP
CCCCCCCCCCCCCCC		25.2826824392
1337PhosphorylationKSPVGEKSPKFRFPR
CCCCCCCCCCCCCCC		29.0822817900
1355PhosphorylationSPKARSGSRDREEGG
CCCCCCCCCCCHHCC		32.0528464351
1369PhosphorylationGFRVRLPSVGFSETA
CEEEECCCCCCCCCC		39.1926824392
1373PhosphorylationRLPSVGFSETAVPGS
ECCCCCCCCCCCCCC		28.2729899451
1375PhosphorylationPSVGFSETAVPGSTR
CCCCCCCCCCCCCCE		31.5820415495
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 PRAX_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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

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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-381 AND SER-1028, ANDMASS SPECTROMETRY.

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