PDXD1_MOUSE - dbPTM
PDXD1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDXD1_MOUSE
UniProt AC Q99K01
Protein Name Pyridoxal-dependent decarboxylase domain-containing protein 1
Gene Name Pdxdc1
Organism Mus musculus (Mouse).
Sequence Length 787
Subcellular Localization
Protein Description
Protein Sequence MDASLEKIADPTLAEMGKNLKEAMRMLEKSPRRTEEENGKKPVSEDIPGPLQGSGQDMVSILQLVQNLMHGDEDEEPQSTRIQNIGEQGHMALLGHSLGAYISTLDKEKLRKLTTRILSDTTLWLRRIFRYENGCAYFHEEEREGLAKICRLAIHSRYEDFVVDGFNVLYNKKPVIYLSAAARPGLGQYLCNQLGLPFPCLCRVPCNTMFGSQHQMDVAFLEKLIKDDVERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLALGYVSSSVLAATKCDSMTLTPGLWLGLPAVPAVTLYKHDDPALTLVAGLTSNKPADKLRALPLWLSLQYLGLDGIVERIKHACHLSQRLQESLKKVDHIKILVEDELSSPVVVFRFFQELPASDSAFKAVPVSNIAPAAVGRERHSCDALNRWLGEQLKQLVPQCGLTVIDLEVDGTCVRFSPLMTAEGLGTRGEDVDQLITCIQSKLPVLTCTLQLREEFKQEVEGTAGLLYVDDPNWPGIGVVRYEHANDDDTSLKSDPEGEKIHTGLLKKLNELESDLTFKIGPEYKSMKSCIYIGMASDDVDVSELVETIAVTAREIEENSRLLENMTEVVRKGIQEAQVQLQKANEERLLEEGVLRQIPVVGSVLNWFSPVQASQKGRSFNLTAGSLESTEYTYVHKVQGTGVTPPPTPLGTRSKQRLPGQKPFKRSLRGSDAVSETSSVSHIEDLEKVEQLSSGLEHDNLEAHSPEQPPRATDLTARQTEALQNQAQHQEDDHSQVEELERLR
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
4Phosphorylation----MDASLEKIADP
----CCCHHHHHCCH		32.56-
18UbiquitinationPTLAEMGKNLKEAMR
HHHHHHHHHHHHHHH		58.7722790023
18 (in isoform 4)Ubiquitination-58.7722790023
30PhosphorylationAMRMLEKSPRRTEEE
HHHHHHHCCCCCHHH		17.7926824392
212PhosphorylationPCNTMFGSQHQMDVA
CCCCCCCCHHHCHHH		17.1417203969
335 (in isoform 4)Ubiquitination-41.8122790023
335UbiquitinationTSNKPADKLRALPLW
CCCCCHHHHHHHHHH		41.8122790023
386PhosphorylationILVEDELSSPVVVFR
EEEECCCCCCEEEEE		30.4626745281
387PhosphorylationLVEDELSSPVVVFRF
EEECCCCCCEEEEEE		34.0526745281
406 (in isoform 4)Ubiquitination-48.4622790023
406UbiquitinationPASDSAFKAVPVSNI
CCCCCCCEEEEHHHC		48.4622790023
424PhosphorylationAVGRERHSCDALNRW
HHCCHHHCHHHHHHH		21.66-
491S-nitrosocysteineSKLPVLTCTLQLREE
CCCCCEEEEHHHHHH		2.90-
491S-nitrosylationSKLPVLTCTLQLREE
CCCCCEEEEHHHHHH		2.9020925432
536 (in isoform 4)Ubiquitination-53.2122790023
536UbiquitinationNDDDTSLKSDPEGEK
CCCCCCCCCCCCCCC		53.2122790023
537PhosphorylationDDDTSLKSDPEGEKI
CCCCCCCCCCCCCCC		64.79-
551 (in isoform 4)Ubiquitination-57.4222790023
551UbiquitinationIHTGLLKKLNELESD
CCHHHHHHHHHHCCC		57.4222790023
562 (in isoform 4)Ubiquitination-41.3322790023
562UbiquitinationLESDLTFKIGPEYKS
HCCCCEEECCHHHHC		41.3322790023
610PhosphorylationSRLLENMTEVVRKGI
HHHHHHHHHHHHHHH		36.89-
626UbiquitinationEAQVQLQKANEERLL
HHHHHHHHHCHHHHH		62.8722790023
626 (in isoform 4)Ubiquitination-62.8722790023
652PhosphorylationGSVLNWFSPVQASQK
CHHHCCCCCCCHHHC		18.7726745281
662PhosphorylationQASQKGRSFNLTAGS
CHHHCCCCEEECCCC		27.4429899451
666PhosphorylationKGRSFNLTAGSLEST
CCCCEEECCCCCCCC		30.0329899451
669PhosphorylationSFNLTAGSLESTEYT
CEEECCCCCCCCEEE		26.8829899451
672PhosphorylationLTAGSLESTEYTYVH
ECCCCCCCCEEEEEE		31.6521183079
684PhosphorylationYVHKVQGTGVTPPPT
EEEEEECCCCCCCCC		16.0425521595
687PhosphorylationKVQGTGVTPPPTPLG
EEECCCCCCCCCCCC		31.2727087446
691PhosphorylationTGVTPPPTPLGTRSK
CCCCCCCCCCCCCCC		36.6027087446
691 (in isoform 4)Phosphorylation-36.6025266776
691 (in isoform 3)Phosphorylation-36.6029514104
695PhosphorylationPPPTPLGTRSKQRLP
CCCCCCCCCCCCCCC		39.1822942356
710PhosphorylationGQKPFKRSLRGSDAV
CCCCCCCCCCCCCCC		24.0226643407
714PhosphorylationFKRSLRGSDAVSETS
CCCCCCCCCCCCCCC		18.9027742792
718PhosphorylationLRGSDAVSETSSVSH
CCCCCCCCCCCCCHH		36.5625521595
720PhosphorylationGSDAVSETSSVSHIE
CCCCCCCCCCCHHHH		20.8527087446
721PhosphorylationSDAVSETSSVSHIED
CCCCCCCCCCHHHHH		25.3727087446
722PhosphorylationDAVSETSSVSHIEDL
CCCCCCCCCHHHHHH		34.7525521595
724PhosphorylationVSETSSVSHIEDLEK
CCCCCCCHHHHHHHH		22.2425521595
736PhosphorylationLEKVEQLSSGLEHDN
HHHHHHHHHCCCCCC		23.2727087446
737PhosphorylationEKVEQLSSGLEHDNL
HHHHHHHHCCCCCCC		56.8627087446
748PhosphorylationHDNLEAHSPEQPPRA
CCCCCCCCCCCCCCC		36.8625521595
756PhosphorylationPEQPPRATDLTARQT
CCCCCCCCCCCHHHH		32.5926643407
759PhosphorylationPPRATDLTARQTEAL
CCCCCCCCHHHHHHH		23.7026643407
778PhosphorylationQHQEDDHSQVEELER
HHCCCCHHHHHHHHH		42.8028576409
778 (in isoform 2)Phosphorylation-42.8025338131
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
691TPhosphorylationKinaseMAPK1P63085
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDXD1_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 PDXD1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PDXD1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDXD1_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-718, AND MASSSPECTROMETRY.
"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 THR-687; SER-718 ANDSER-722, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND MASSSPECTROMETRY.
"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 THR-687, AND MASSSPECTROMETRY.

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