PEX5R_MOUSE - dbPTM
PEX5R_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PEX5R_MOUSE
UniProt AC Q8C437
Protein Name PEX5-related protein
Gene Name Pex5l
Organism Mus musculus (Mouse).
Sequence Length 567
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Some fraction is membrane associated via its interaction with RAB8B..
Protein Description Accessory subunit of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, regulating their cell-surface expression and cyclic nucleotide dependence..
Protein Sequence MYQGHMQLVNEQQESRPLLSPSIDDFLCETKSEAIAKPVTSNTAVLTTGLDLLDLSEPVSQPQTKAKKSEPSSKSSSLKKKADGSDLISADAEQRAQALRGPETSSLDLDIQTQLEKWDDVKFHGDRTSKGHLMAERKSCSSRTGSKELLWSAEHRSQPELSTGKSALNSESASELELVAPAQARLTKEHRWGSALLSRNHSLEEEFERAKAAVESDTEFWDKMQAEWEEMARRNWISENQEAQNQVTVSASEKGYYFHTENPFKDWPGAFEEGLKRLKEGDLPVTILFMEAAILQDPGDAEAWQFLGITQAENENEQAAIVALQRCLELQPNNLKALMALAVSYTNTSHQQDACEALKNWIKQNPKYKYLVKNKKGSPGLTRRMSKSPVDSSVLEGVKELYLEAAHQNGDMIDPDLQTGLGVLFHLSGEFNRAIDAFNAALTVRPEDYSLWNRLGATLANGDRSEEAVEAYTRALEIQPGFIRSRYNLGISCINLGAYREAVSNFLTALSLQRKSRNQQQVPHPAISGNIWAALRIALSLMDQPELFQAANLGDLDVLLRAFNLDP
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
20PhosphorylationQESRPLLSPSIDDFL
HHHCCCCCCCHHHHH		25.0429899451
22PhosphorylationSRPLLSPSIDDFLCE
HCCCCCCCHHHHHHC		34.9629899451
38 (in isoform 3)Phosphorylation-26.1229899451
42 (in isoform 3)Phosphorylation-23.7729899451
43 (in isoform 3)Phosphorylation-20.2222807455
69PhosphorylationPQTKAKKSEPSSKSS
CCCCCCCCCCCCCCH		54.77-
72PhosphorylationKAKKSEPSSKSSSLK
CCCCCCCCCCCHHCC		46.47-
85PhosphorylationLKKKADGSDLISADA
CCHHCCCCCCCCCCH		29.7729899451
104PhosphorylationQALRGPETSSLDLDI
HHHHCCCCCCCCCCH		27.0925777480
105PhosphorylationALRGPETSSLDLDIQ
HHHCCCCCCCCCCHH		27.5225777480
106PhosphorylationLRGPETSSLDLDIQT
HHCCCCCCCCCCHHH		33.0725777480
113PhosphorylationSLDLDIQTQLEKWDD
CCCCCHHHHHHCCCC		35.1425777480
139PhosphorylationHLMAERKSCSSRTGS
CHHCCCCCCCCCCCC		26.00-
141PhosphorylationMAERKSCSSRTGSKE
HCCCCCCCCCCCCHH		29.91-
144PhosphorylationRKSCSSRTGSKELLW
CCCCCCCCCCHHHHH		47.9925177544
146PhosphorylationSCSSRTGSKELLWSA
CCCCCCCCHHHHHCH		23.5019060867
157PhosphorylationLWSAEHRSQPELSTG
HHCHHHCCCCCCCCC		52.5825521595
162PhosphorylationHRSQPELSTGKSALN
HCCCCCCCCCHHHHC		33.1922324799
163PhosphorylationRSQPELSTGKSALNS
CCCCCCCCCHHHHCC		62.3422324799
166PhosphorylationPELSTGKSALNSESA
CCCCCCHHHHCCCCH		39.0621454597
170PhosphorylationTGKSALNSESASELE
CCHHHHCCCCHHHHE		33.5029899451
172PhosphorylationKSALNSESASELELV
HHHHCCCCHHHHEEH		36.5929899451
174PhosphorylationALNSESASELELVAP
HHCCCCHHHHEEHHH		52.5829899451
194PhosphorylationTKEHRWGSALLSRNH
CHHHHHHHHHHHCCC		14.5827180971
198PhosphorylationRWGSALLSRNHSLEE
HHHHHHHHCCCCHHH		31.7022324799
202PhosphorylationALLSRNHSLEEEFER
HHHHCCCCHHHHHHH		40.8125521595
216PhosphorylationRAKAAVESDTEFWDK
HHHHHHHCCHHHHHH		43.1429899451
378PhosphorylationLVKNKKGSPGLTRRM
EECCCCCCCCCCCCC		25.3625521595
382PhosphorylationKKGSPGLTRRMSKSP
CCCCCCCCCCCCCCC		23.3429899451
386PhosphorylationPGLTRRMSKSPVDSS
CCCCCCCCCCCCCHH		28.3319060867
388PhosphorylationLTRRMSKSPVDSSVL
CCCCCCCCCCCHHHH		23.8925521595
392PhosphorylationMSKSPVDSSVLEGVK
CCCCCCCHHHHHHHH		23.6825521595
393PhosphorylationSKSPVDSSVLEGVKE
CCCCCCHHHHHHHHH		26.6820415495
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 PEX5R_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PEX5R_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 PEX5R_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADDA_MOUSEAdd1physical
28671696
AGO1_MOUSEAgo1physical
28671696
AGO2_MOUSEAgo2physical
28671696
AGO3_MOUSEAgo3physical
28671696
ANK2_MOUSEAnk2physical
28671696
AP2A1_MOUSEAp2a1physical
28671696
AP2A2_MOUSEAp2a2physical
28671696
AP2B1_MOUSEAp2b1physical
28671696
ARHG2_MOUSEArhgef2physical
28671696
KCC2A_MOUSECamk2aphysical
28671696
CSKI1_MOUSECaskin1physical
28671696
CAD11_MOUSECdh11physical
28671696
CADH2_MOUSECdh2physical
28671696
CTNA1_MOUSECtnna1physical
28671696
CTNA2_MOUSECtnna2physical
28671696
CTNB1_MOUSECtnnb1physical
28671696
CTND2_MOUSECtnnd2physical
28671696
CYFP2_MOUSECyfip2physical
28671696
DREB_MOUSEDbn1physical
28671696
GABR2_MOUSEGabbr2physical
28671696
GIT1_MOUSEGit1physical
28671696
HCN1_MOUSEHcn1physical
28671696
HCN2_MOUSEHcn2physical
28671696
HCN3_MOUSEHcn3physical
28671696
ICAM5_MOUSEIcam5physical
28671696
KCD16_MOUSEKctd16physical
28671696
MYH9_MOUSEMyh9physical
28671696
MYO5A_MOUSEMyo5aphysical
28671696
NCAN_MOUSENcanphysical
28671696
NCKP1_MOUSENckap1physical
28671696
PARD3_MOUSEPard3physical
28671696
PEX5_MOUSEPex5physical
28671696
PPR3F_MOUSEPpp1r3fphysical
28671696
SKT_MOUSEEtl4physical
28671696
S12A5_MOUSESlc12a5physical
28671696
S4A4_MOUSESlc4a4physical
28671696
SPTB2_MOUSESptbn1physical
28671696
TANC2_MOUSETanc2physical
28671696
TENR_MOUSETnrphysical
28671696
UN13A_MOUSEUnc13aphysical
28671696
WDR7_MOUSEWdr7physical
28671696
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PEX5R_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, AND MASSSPECTROMETRY.
"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-202, AND MASSSPECTROMETRY.

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