PRAX_HUMAN - dbPTM
PRAX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRAX_HUMAN
UniProt AC Q9BXM0
Protein Name Periaxin
Gene Name PRX
Organism Homo sapiens (Human).
Sequence Length 1461
Subcellular Localization Isoform 1: Cell membrane
Peripheral membrane protein
Cytoplasmic side . Nucleus . Cytoplasm . Detected in the Schwann cell nucleus prior to the onset of myelination. Detected in Schwann cells at periaxonal myelin membranes. Associated with the ce
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. Required for the maintenance of the peripheral myelin sheath that is essential for normal transmission of nerve impulses and normal perception of sensory stimuli. Required for normal transport of MBP mRNA from the perinuclear to the paranodal regions. Required for normal remyelination after nerve injury. Required for normal elongation of Schwann cells and normal length of the internodes between the nodes of Ranvier. The demyelinated nodes of Ranvier permit saltatory transmission of nerve impulses; shorter internodes cause slower transmission of nerve impulses. Required for the formation of appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane; the Schwann cell cytoplasm is restricted to regions between these appositions. Required for the formation of Cajal bands and of Schmidt-Lanterman incisures that correspond to short, cytoplasm-filled regions on myelinated nerves. Recruits DRP2 to the Schwann cell plasma membrane. Required for normal protein composition of the eye lens fiber cell plasma membrane and normal eye lens fiber cell morphology..
Protein Sequence MEARSRSAEELRRAELVEIIVETEAQTGVSGINVAGGGKEGIFVRELREDSPAARSLSLQEGDQLLSARVFFENFKYEDALRLLQCAEPYKVSFCLKRTVPTGDLALRPGTVSGYEIKGPRAKVAKLNIQSLSPVKKKKMVPGALGVPADLAPVDVEFSFPKFSRLRRGLKAEAVKGPVPAAPARRRLQLPRLRVREVAEEAQAARLAAAAPPPRKAKVEAEVAAGARFTAPQVELVGPRLPGAEVGVPQVSAPKAAPSAEAAGGFALHLPTLGLGAPAPPAVEAPAVGIQVPQVELPALPSLPTLPTLPCLETREGAVSVVVPTLDVAAPTVGVDLALPGAEVEARGEAPEVALKMPRLSFPRFGARAKEVAEAKVAKVSPEARVKGPRLRMPTFGLSLLEPRPAAPEVVESKLKLPTIKMPSLGIGVSGPEVKVPKGPEVKLPKAPEVKLPKVPEAALPEVRLPEVELPKVSEMKLPKVPEMAVPEVRLPEVELPKVSEMKLPKVPEMAVPEVRLPEVQLLKVSEMKLPKVPEMAVPEVRLPEVQLPKVSEMKLPEVSEVAVPEVRLPEVQLPKVPEMKVPEMKLPKVPEMKLPEMKLPEVQLPKVPEMAVPDVHLPEVQLPKVPEMKLPEMKLPEVKLPKVPEMAVPDVHLPEVQLPKVPEMKLPKMPEMAVPEVRLPEVQLPKVSEMKLPKVPEMAVPDVHLPEVQLPKVCEMKVPDMKLPEIKLPKVPEMAVPDVHLPEVQLPKVSEIRLPEMQVPKVPDVHLPKAPEVKLPRAPEVQLKATKAEQAEGMEFGFKMPKMTMPKLGRAESPSRGKPGEAGAEVSGKLVTLPCLQPEVDGEAHVGVPSLTLPSVELDLPGALGLQGQVPAAKMGKGERVEGPEVAAGVREVGFRVPSVEIVTPQLPAVEIEEGRLEMIETKVKPSSKFSLPKFGLSGPKVAKAEAEGAGRATKLKVSKFAISLPKARVGAEAEAKGAGEAGLLPALDLSIPQLSLDAHLPSGKVEVAGADLKFKGPRFALPKFGVRGRDTEAAELVPGVAELEGKGWGWDGRVKMPKLKMPSFGLARGKEAEVQGDRASPGEKAESTAVQLKIPEVELVTLGAQEEGRAEGAVAVSGMQLSGLKVSTAGQVVTEGHDAGLRMPPLGISLPQVELTGFGEAGTPGQQAQSTVPSAEGTAGYRVQVPQVTLSLPGAQVAGGELLVGEGVFKMPTVTVPQLELDVGLSREAQAGEAATGEGGLRLKLPTLGARARVGGEGAEEQPPGAERTFCLSLPDVELSPSGGNHAEYQVAEGEGEAGHKLKVRLPRFGLVRAKEGAEEGEKAKSPKLRLPRVGFSQSEMVTGEGSPSPEEEEEEEEEGSGEGASGRRGRVRVRLPRVGLAAPSKASRGQEGDAAPKSPVREKSPKFRFPRVSLSPKARSGSGDQEEGGLRVRLPSVGFSETGAPGPARMEGAQAAAV
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
5Phosphorylation---MEARSRSAEELR
---CCHHHCCHHHHH		37.3223403867
7Phosphorylation-MEARSRSAEELRRA
-CCHHHCCHHHHHHH		41.0823403867
58PhosphorylationSPAARSLSLQEGDQL
CCCHHHCCHHHHHHH		29.2928857561
67PhosphorylationQEGDQLLSARVFFEN
HHHHHHHHHHHHHHC		23.7124719451
99PhosphorylationVSFCLKRTVPTGDLA
EEEEEECCCCCCCEE		29.2924719451
102PhosphorylationCLKRTVPTGDLALRP
EEECCCCCCCEEECC		38.70-
111PhosphorylationDLALRPGTVSGYEIK
CEEECCCEECCEEEC		17.74-
113PhosphorylationALRPGTVSGYEIKGP
EECCCEECCEEECCC		35.18-
115PhosphorylationRPGTVSGYEIKGPRA
CCCEECCEEECCCCC		13.6324719451
132 (in isoform 2)Phosphorylation-3.72-
133PhosphorylationKLNIQSLSPVKKKKM
EEECCCCCCCCCCCC		32.6624719451
145 (in isoform 2)Phosphorylation-9.84-
361PhosphorylationALKMPRLSFPRFGAR
HHHCCCCCCCCCCHH		34.1924719451
424PhosphorylationLPTIKMPSLGIGVSG
CCCCCCCCCCCCCCC		35.4124114839
430PhosphorylationPSLGIGVSGPEVKVP
CCCCCCCCCCCCCCC		43.3423312004
552PhosphorylationEVQLPKVSEMKLPEV
CCCCCCCCCCCCCCC		37.7929449344
560PhosphorylationEMKLPEVSEVAVPEV
CCCCCCCCEEECCCC		25.3729449344
805PhosphorylationGFKMPKMTMPKLGRA
CCCCCCCCCCCCCCC		36.1329759185
900PhosphorylationEVGFRVPSVEIVTPQ
ECCEECCCEEEECCC		29.53-
932PhosphorylationVKPSSKFSLPKFGLS
CCCCCCCCCCCCCCC		47.7224719451
965PhosphorylationKVSKFAISLPKARVG
EEEEEEECCCHHHHC		34.8821815630
1004PhosphorylationSLDAHLPSGKVEVAG
CEECCCCCCCEEECC		58.5724719451
1082PhosphorylationEVQGDRASPGEKAES
EECCCCCCCCCCCCC		34.0428857561
1089PhosphorylationSPGEKAESTAVQLKI
CCCCCCCCCEEEECC		26.9024702127
1090PhosphorylationPGEKAESTAVQLKIP
CCCCCCCCEEEECCC		23.5024702127
1119PhosphorylationAEGAVAVSGMQLSGL
CCCEEEEECEEECCC		20.86-
1328PhosphorylationEEGEKAKSPKLRLPR
HCCCCCCCCCCCCCC		31.9320068231
1349PhosphorylationEMVTGEGSPSPEEEE
HCCCCCCCCCHHHHH		20.22-
1351PhosphorylationVTGEGSPSPEEEEEE
CCCCCCCCHHHHHHH		46.79-
1363PhosphorylationEEEEEEGSGEGASGR
HHHHHCCCCCCCCCC		36.63-
1387PhosphorylationRVGLAAPSKASRGQE
CCEEECCCCCCCCCC		35.8123403867
1401PhosphorylationEGDAAPKSPVREKSP
CCCCCCCCCCCCCCC		27.8028857561
1407PhosphorylationKSPVREKSPKFRFPR
CCCCCCCCCCCCCCC		28.6823911959
1416PhosphorylationKFRFPRVSLSPKARS
CCCCCCCCCCCCCCC		25.1424719451
1418PhosphorylationRFPRVSLSPKARSGS
CCCCCCCCCCCCCCC		19.4924719451
1423PhosphorylationSLSPKARSGSGDQEE
CCCCCCCCCCCCCCC		42.0228796482
1425PhosphorylationSPKARSGSGDQEEGG
CCCCCCCCCCCCCCC		40.2128796482
1439PhosphorylationGLRVRLPSVGFSETG
CEEEECCCCCCCCCC		39.1928857561
1445PhosphorylationPSVGFSETGAPGPAR
CCCCCCCCCCCCCCC		37.13-
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRAX_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DAG1_HUMANDAG1physical
11430802
DRP2_HUMANDRP2physical
11430802
PRAX_HUMANPRXphysical
11430802
Drug and Disease Associations
Kegg Disease
H00264 Charcot-Marie-Tooth disease (CMT); Hereditary motor and sensory neuropathy; Peroneal muscular atroph
OMIM Disease
145900Dejerine-Sottas syndrome (DSS)
614895Charcot-Marie-Tooth disease 4F (CMT4F)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRAX_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1328, AND MASSSPECTROMETRY.

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