PDXD1_HUMAN - dbPTM
PDXD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDXD1_HUMAN
UniProt AC Q6P996
Protein Name Pyridoxal-dependent decarboxylase domain-containing protein 1
Gene Name PDXDC1
Organism Homo sapiens (Human).
Sequence Length 788
Subcellular Localization
Protein Description
Protein Sequence MDASLEKIADPTLAEMGKNLKEAVKMLEDSQRRTEEENGKKLISGDIPGPLQGSGQDMVSILQLVQNLMHGDEDEEPQSPRIQNIGEQGHMALLGHSLGAYISTLDKEKLRKLTTRILSDTTLWLCRIFRYENGCAYFHEEEREGLAKICRLAIHSRYEDFVVDGFNVLYNKKPVIYLSAAARPGLGQYLCNQLGLPFPCLCRVPCNTVFGSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLALGYVSSSVLAAAKCDSMTMTPGPWLGLPAVPAVTLYKHDDPALTLVAGLTSNKPTDKLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELSSPVVVFRFFQELPGSDPVFKAVPVPNMTPSGVGRERHSCDALNRWLGEQLKQLVPASGLTVMDLEAEGTCLRFSPLMTAAVLGTRGEDVDQLVACIESKLPVLCCTLQLREEFKQEVEATAGLLYVDDPNWSGIGVVRYEHANDDKSSLKSDPEGENIHAGLLKKLNELESDLTFKIGPEYKSMKSCLYVGMASDNVDAAELVETIAATAREIEENSRLLENMTEVVRKGIQEAQVELQKASEERLLEEGVLRQIPVVGSVLNWFSPVQALQKGRTFNLTAGSLESTEPIYVYKAQGAGVTLPPTPSGSRTKQRLPGQKPFKRSLRGSDALSETSSVSHIEDLEKVERLSSGPEQITLEASSTEGHPGAPSPQHTDQTEAFQKGVPHPEDDHSQVEGPESLR
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		32.5624719451
10UbiquitinationASLEKIADPTLAEMG
CHHHHHCCHHHHHHH		39.94-
12PhosphorylationLEKIADPTLAEMGKN
HHHHCCHHHHHHHHC		38.8621406692
18UbiquitinationPTLAEMGKNLKEAVK
HHHHHHHHCHHHHHH		58.77-
18UbiquitinationPTLAEMGKNLKEAVK
HHHHHHHHCHHHHHH		58.77-
21UbiquitinationAEMGKNLKEAVKMLE
HHHHHCHHHHHHHHH		53.68-
21UbiquitinationAEMGKNLKEAVKMLE
HHHHHCHHHHHHHHH		53.68-
25UbiquitinationKNLKEAVKMLEDSQR
HCHHHHHHHHHHHHH		44.83-
30PhosphorylationAVKMLEDSQRRTEEE
HHHHHHHHHHHHHHH		19.0625159151
44PhosphorylationENGKKLISGDIPGPL
HHCCCCCCCCCCCCC		40.6320068231
54PhosphorylationIPGPLQGSGQDMVSI
CCCCCCCCCHHHHHH		21.9620068231
57UbiquitinationPLQGSGQDMVSILQL
CCCCCCHHHHHHHHH		42.87-
60PhosphorylationGSGQDMVSILQLVQN
CCCHHHHHHHHHHHH		15.7920068231
79PhosphorylationDEDEEPQSPRIQNIG
CCCCCCCCCCCCCCH		27.1928192239
97PhosphorylationHMALLGHSLGAYIST
HHHHHHHHHHHHHHH		27.0527251275
107UbiquitinationAYISTLDKEKLRKLT
HHHHHCCHHHHHHHH		60.92-
121PhosphorylationTTRILSDTTLWLCRI
HHHHHHCHHHHHHHH		22.0324719451
135UbiquitinationIFRYENGCAYFHEEE
HHHCCCCCEECCHHH		4.12-
148UbiquitinationEEREGLAKICRLAIH
HHHHHHHHHHHHHHH		47.59-
161UbiquitinationIHSRYEDFVVDGFNV
HHHCCCCCEEECEEE		3.74-
198UbiquitinationCNQLGLPFPCLCRVP
HHHHCCCCCEEEECC		8.8521906983
199UbiquitinationNQLGLPFPCLCRVPC
HHHCCCCCEEEECCC		14.2921906983
203 (in isoform 2)Ubiquitination-23.5921906983
208PhosphorylationLCRVPCNTVFGSQHQ
EEECCCCCCCCCCHH		24.7527251275
212PhosphorylationPCNTVFGSQHQMDVA
CCCCCCCCCHHHHHH		17.0229396449
226UbiquitinationAFLEKLIKDDIERGR
HHHHHHHHHHHHCCC		60.8421906983
226 (in isoform 1)Ubiquitination-60.8421906983
240UbiquitinationRLPLLLVANAGTAAV
CCCEEEEECCCCCCC		10.50-
244UbiquitinationLLVANAGTAAVGHTD
EEEECCCCCCCCCHH		14.72-
252UbiquitinationAAVGHTDKIGRLKEL
CCCCCHHHHHHHHHH		48.49-
267UbiquitinationCEQYGIWLHVEGVNL
HHHHCCEEEEECCCH		2.83-
303UbiquitinationTMTPGPWLGLPAVPA
CCCCCCCCCCCCCCE		5.9321906983
304UbiquitinationMTPGPWLGLPAVPAV
CCCCCCCCCCCCCEE		26.2521906983
308 (in isoform 2)Ubiquitination-2.7121906983
315UbiquitinationVPAVTLYKHDDPALT
CCEEEEECCCCHHHH		43.61-
322PhosphorylationKHDDPALTLVAGLTS
CCCCHHHHHHEECCC		22.6920873877
328PhosphorylationLTLVAGLTSNKPTDK
HHHHEECCCCCCCHH		29.3620873877
329PhosphorylationTLVAGLTSNKPTDKL
HHHEECCCCCCCHHH		48.1520873877
331UbiquitinationVAGLTSNKPTDKLRA
HEECCCCCCCHHHHH		49.4121906983
331 (in isoform 1)Ubiquitination-49.4121906983
333PhosphorylationGLTSNKPTDKLRALP
ECCCCCCCHHHHHHH		47.5820873877
335UbiquitinationTSNKPTDKLRALPLW
CCCCCCHHHHHHHHH		42.21-
346UbiquitinationLPLWLSLQYLGLDGF
HHHHHHHHHHCCHHH		28.20-
358UbiquitinationDGFVERIKHACQLSQ
HHHHHHHHHHHHHHH		31.22-
372UbiquitinationQRLQESLKKVNYIKI
HHHHHHHHHCCEEEE		65.05-
378UbiquitinationLKKVNYIKILVEDEL
HHHCCEEEEEEECCC		21.4521906983
379UbiquitinationKKVNYIKILVEDELS
HHCCEEEEEEECCCC		3.6521906983
383 (in isoform 2)Ubiquitination-55.4421906983
386PhosphorylationILVEDELSSPVVVFR
EEEECCCCCCEEEEE		30.4628857561
387PhosphorylationLVEDELSSPVVVFRF
EEECCCCCCEEEEEE		34.0528857561
401PhosphorylationFFQELPGSDPVFKAV
EECCCCCCCCCCEEE		36.4825850435
406UbiquitinationPGSDPVFKAVPVPNM
CCCCCCCEEEECCCC		49.0221906983
406 (in isoform 1)Ubiquitination-49.0221906983
413SulfoxidationKAVPVPNMTPSGVGR
EEEECCCCCCCCCCC		4.8230846556
414PhosphorylationAVPVPNMTPSGVGRE
EEECCCCCCCCCCCH		22.4225159151
416PhosphorylationPVPNMTPSGVGRERH
ECCCCCCCCCCCHHH		36.6223403867
424PhosphorylationGVGRERHSCDALNRW
CCCCHHHCHHHHHHH		21.6624719451
445UbiquitinationQLVPASGLTVMDLEA
HHCCCCCCEEEEEEE		2.78-
460UbiquitinationEGTCLRFSPLMTAAV
CCCEEECHHHHHHHH		15.64-
460PhosphorylationEGTCLRFSPLMTAAV
CCCEEECHHHHHHHH		15.6421406692
464PhosphorylationLRFSPLMTAAVLGTR
EECHHHHHHHHHCCC		21.1021406692
470PhosphorylationMTAAVLGTRGEDVDQ
HHHHHHCCCCCCHHH		31.1921406692
471UbiquitinationTAAVLGTRGEDVDQL
HHHHHCCCCCCHHHH		44.71-
477UbiquitinationTRGEDVDQLVACIES
CCCCCHHHHHHHHHC		37.37-
500UbiquitinationLQLREEFKQEVEATA
HHCHHHHHHHHHHCC		49.15-
506O-linked_GlycosylationFKQEVEATAGLLYVD
HHHHHHHCCCEEEEC		14.0429351928
508UbiquitinationQEVEATAGLLYVDDP
HHHHHCCCEEEECCC		16.3221906983
509UbiquitinationEVEATAGLLYVDDPN
HHHHCCCEEEECCCC		2.6421906983
518O-linked_GlycosylationYVDDPNWSGIGVVRY
EECCCCCCCEEEEEE		27.4629351928
524UbiquitinationWSGIGVVRYEHANDD
CCCEEEEEEEECCCC		28.81-
525PhosphorylationSGIGVVRYEHANDDK
CCEEEEEEEECCCCH		10.6429449344
533PhosphorylationEHANDDKSSLKSDPE
EECCCCHHHCCCCCC		48.1520873877
534PhosphorylationHANDDKSSLKSDPEG
ECCCCHHHCCCCCCC		45.6220873877
535UbiquitinationANDDKSSLKSDPEGE
CCCCHHHCCCCCCCC		8.75-
536UbiquitinationNDDKSSLKSDPEGEN
CCCHHHCCCCCCCCC		55.552190698
536 (in isoform 1)Ubiquitination-55.5521906983
537PhosphorylationDDKSSLKSDPEGENI
CCHHHCCCCCCCCCC		64.7920873877
550UbiquitinationNIHAGLLKKLNELES
CCCHHHHHHHHHHCC		61.32-
551UbiquitinationIHAGLLKKLNELESD
CCHHHHHHHHHHCCC		57.42-
560PhosphorylationNELESDLTFKIGPEY
HHHCCCCEEECCHHH		28.0724719451
562UbiquitinationLESDLTFKIGPEYKS
HCCCCEEECCHHHCC		41.33-
567PhosphorylationTFKIGPEYKSMKSCL
EEECCHHHCCHHCCE		16.11-
568UbiquitinationFKIGPEYKSMKSCLY
EECCHHHCCHHCCEE		42.27-
572PhosphorylationPEYKSMKSCLYVGMA
HHHCCHHCCEEEECC		10.7427499020
609SulfoxidationNSRLLENMTEVVRKG
HHHHHHHHHHHHHHH		2.1721406390
615UbiquitinationNMTEVVRKGIQEAQV
HHHHHHHHHHHHHHH		49.08-
626UbiquitinationEAQVELQKASEERLL
HHHHHHHHHHHHHHH		67.51-
646PhosphorylationRQIPVVGSVLNWFSP
HHCCCCHHHHHCCCH		16.3024719451
652PhosphorylationGSVLNWFSPVQALQK
HHHHHCCCHHHHHHC		18.7725159151
659UbiquitinationSPVQALQKGRTFNLT
CHHHHHHCCCCEEEC		51.73-
662PhosphorylationQALQKGRTFNLTAGS
HHHHCCCCEEECCCC		26.0821945579
666PhosphorylationKGRTFNLTAGSLEST
CCCCEEECCCCCCCC		30.0321945579
669PhosphorylationTFNLTAGSLESTEPI
CEEECCCCCCCCCCE		26.8821945579
672PhosphorylationLTAGSLESTEPIYVY
ECCCCCCCCCCEEEE		43.2821945579
673PhosphorylationTAGSLESTEPIYVYK
CCCCCCCCCCEEEEE		36.0821945579
677PhosphorylationLESTEPIYVYKAQGA
CCCCCCEEEEEECCC		14.4021945579
679PhosphorylationSTEPIYVYKAQGAGV
CCCCEEEEEECCCCC		5.4321945579
680MethylationTEPIYVYKAQGAGVT
CCCEEEEEECCCCCC		24.96115974779
680UbiquitinationTEPIYVYKAQGAGVT
CCCEEEEEECCCCCC		24.96-
687PhosphorylationKAQGAGVTLPPTPSG
EECCCCCCCCCCCCC		32.4023403867
691PhosphorylationAGVTLPPTPSGSRTK
CCCCCCCCCCCCCCC		28.3125159151
693PhosphorylationVTLPPTPSGSRTKQR
CCCCCCCCCCCCCCC		52.4523403867
695PhosphorylationLPPTPSGSRTKQRLP
CCCCCCCCCCCCCCC		40.9125159151
697PhosphorylationPTPSGSRTKQRLPGQ
CCCCCCCCCCCCCCC		32.9725159151
705UbiquitinationKQRLPGQKPFKRSLR
CCCCCCCCCCCCCCC		59.33-
708UbiquitinationLPGQKPFKRSLRGSD
CCCCCCCCCCCCCCC		49.99-
710PhosphorylationGQKPFKRSLRGSDAL
CCCCCCCCCCCCCCC		24.0225159151
714PhosphorylationFKRSLRGSDALSETS
CCCCCCCCCCCCCCC		17.1825159151
718PhosphorylationLRGSDALSETSSVSH
CCCCCCCCCCCCCHH		40.3229255136
720PhosphorylationGSDALSETSSVSHIE
CCCCCCCCCCCHHHH		23.9529255136
721PhosphorylationSDALSETSSVSHIED
CCCCCCCCCCHHHHH		25.3729255136
722PhosphorylationDALSETSSVSHIEDL
CCCCCCCCCHHHHHH		34.7529255136
724PhosphorylationLSETSSVSHIEDLEK
CCCCCCCHHHHHHHH		22.2429255136
731UbiquitinationSHIEDLEKVERLSSG
HHHHHHHHHHHHCCC		57.61-
736PhosphorylationLEKVERLSSGPEQIT
HHHHHHHCCCCCEEE		39.2023401153
737PhosphorylationEKVERLSSGPEQITL
HHHHHHCCCCCEEEE		64.0622167270
743PhosphorylationSSGPEQITLEASSTE
CCCCCEEEEEECCCC		20.4522167270
747PhosphorylationEQITLEASSTEGHPG
CEEEEEECCCCCCCC		28.5430278072
748PhosphorylationQITLEASSTEGHPGA
EEEEEECCCCCCCCC		37.2130278072
749PhosphorylationITLEASSTEGHPGAP
EEEEECCCCCCCCCC		43.4130278072
757PhosphorylationEGHPGAPSPQHTDQT
CCCCCCCCCCCCCHH		36.3423401153
761PhosphorylationGAPSPQHTDQTEAFQ
CCCCCCCCCHHHHHH		25.2630278072
764PhosphorylationSPQHTDQTEAFQKGV
CCCCCCHHHHHHCCC		31.9030243723
779PhosphorylationPHPEDDHSQVEGPES
CCCCCCCCCCCCCCC		42.8029255136
786PhosphorylationSQVEGPESLR-----
CCCCCCCCCC-----		32.3623401153
788MethylationVEGPESLR-------
CCCCCCCC-------		54.49115486947
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 PDXD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDXD1_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 PDXD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VATH_HUMANATP6V1Hphysical
22863883
WDR44_HUMANWDR44physical
22863883
NSF1C_HUMANNSFL1Cphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDXD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-779, AND MASSSPECTROMETRY.
"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 THR-720; SER-721; SER-722;SER-724; SER-737 AND SER-779, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-691, AND MASSSPECTROMETRY.

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