PLD1_HUMAN - dbPTM
PLD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLD1_HUMAN
UniProt AC Q13393
Protein Name Phospholipase D1
Gene Name PLD1
Organism Homo sapiens (Human).
Sequence Length 1074
Subcellular Localization Cytoplasm, perinuclear region. Endoplasmic reticulum membrane
Lipid-anchor
Cytoplasmic side. Golgi apparatus membrane
Lipid-anchor
Cytoplasmic side. Late endosome membrane
Lipid-anchor
Cytoplasmic side.
Protein Description Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity)..
Protein Sequence MSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEGEEVDYDVSPSDPKIQEVYIPFSAIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEPREMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDLGPKGIEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDHRFGSYAAIQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAMESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSISSIDSTSSYFNHYRSHHNLIHGLKPHFKLFHPSSESEQGLTRPHADTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLLPKSQTTAHELRYQVPGSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPVLAKEDPIRAEEELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
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
2Phosphorylation------MSLKNEPRV
------CCCCCCCCC		60.3926278961
11PhosphorylationKNEPRVNTSALQKIA
CCCCCCCHHHHHHHH		16.7229396449
12PhosphorylationNEPRVNTSALQKIAA
CCCCCCHHHHHHHHH		23.0625159151
16UbiquitinationVNTSALQKIAADMSN
CCHHHHHHHHHHHHH		34.85-
22PhosphorylationQKIAADMSNIIENLD
HHHHHHHHHHHHHCC		25.9821712546
42PhosphorylationFEGEEVDYDVSPSDP
ECCCCCCCCCCCCCC		24.3426657352
45PhosphorylationEEVDYDVSPSDPKIQ
CCCCCCCCCCCCCCE		18.7825159151
47PhosphorylationVDYDVSPSDPKIQEV
CCCCCCCCCCCCEEE		60.0729523821
50UbiquitinationDVSPSDPKIQEVYIP
CCCCCCCCCEEEEEE		63.11-
121UbiquitinationWQVKRKFKHFQEFHR
HHHHHHHHHHHHHHH		46.69-
132MethylationEFHRELLKYKAFIRI
HHHHHHHCCCEEEEC		58.28115975105
147PhosphorylationPIPTRRHTFRRQNVR
CCCCCCHHCCCCCCC		19.6110441128
162PhosphorylationEEPREMPSLPRSSEN
CCCCCCCCCCCCHHH		50.0930266825
189 (in isoform 1)Ubiquitination-43.3721890473
189 (in isoform 2)Ubiquitination-43.3721890473
189UbiquitinationQLEDYLTKILKMPMY
HHHHHHHHHHCCHHH		43.3721890473
189 (in isoform 3)Ubiquitination-43.3721890473
189 (in isoform 4)Ubiquitination-43.3721890473
240S-palmitoylationHRIPGLNCCGQGRAC
CCCCCCCCCCCCCHH		3.1212429840
241S-palmitoylationRIPGLNCCGQGRACY
CCCCCCCCCCCCHHH		4.4212429840
264PhosphorylationVKDSFLLYMKPDSGA
EECCEEEEECCCCCC		12.7722461510
294UbiquitinationGKKETETKYGIRIDN
CCCCCCCCCEEEEEC		34.94-
303PhosphorylationGIRIDNLSRTLILKC
EEEEECCCCEEEEEC		29.4923403867
305PhosphorylationRIDNLSRTLILKCNS
EEECCCCEEEEECCC		18.1223403867
406MethylationWRLDCILKRKAQQGV
EEEEEHHHHHHHHCC		31.76115975113
420PhosphorylationVRIFIMLYKEVELAL
CEEEEEEHHHHHHHH		6.4222817900
431PhosphorylationELALGINSEYTKRTL
HHHHCCCCHHHHHHH		30.02-
495PhosphorylationDDNEHRLTDVGSVKR
CCCCCEECCCCCEEE		28.7023663014
499PhosphorylationHRLTDVGSVKRVTSG
CEECCCCCEEECCCC		25.0623663014
501UbiquitinationLTDVGSVKRVTSGPS
ECCCCCEEECCCCCC		42.73-
504PhosphorylationVGSVKRVTSGPSLGS
CCCEEECCCCCCCCC		31.8123663014
505PhosphorylationGSVKRVTSGPSLGSL
CCEEECCCCCCCCCC		45.9426657352
508PhosphorylationKRVTSGPSLGSLPPA
EECCCCCCCCCCCHH		49.2226657352
511PhosphorylationTSGPSLGSLPPAAME
CCCCCCCCCCHHHHH		42.8923663014
519PhosphorylationLPPAAMESMESLRLK
CCHHHHHHHHHHCCC		18.1123663014
522PhosphorylationAAMESMESLRLKDKN
HHHHHHHHHCCCCCC		15.3323663014
540PhosphorylationQNLPIQKSIDDVDSK
CCCCCCCCHHHHHHH		18.1826657352
547UbiquitinationSIDDVDSKLKGIGKP
CHHHHHHHHCCCCCC		50.16-
558PhosphorylationIGKPRKFSKFSLYKQ
CCCCCCCCHHHHHHH		35.5120873877
559UbiquitinationGKPRKFSKFSLYKQL
CCCCCCCHHHHHHHH		41.95-
561PhosphorylationPRKFSKFSLYKQLHR
CCCCCHHHHHHHHHH		34.2325159151
586PhosphorylationSIDSTSSYFNHYRSH
CCCCCHHHHHHHHHH		14.25-
590PhosphorylationTSSYFNHYRSHHNLI
CHHHHHHHHHHCCCC		18.21-
610PhosphorylationHFKLFHPSSESEQGL
CCEEECCCCHHCCCC		37.8611171116
611PhosphorylationFKLFHPSSESEQGLT
CEEECCCCHHCCCCC		49.9811171116
613PhosphorylationLFHPSSESEQGLTRP
EECCCCHHCCCCCCC		36.8527080861
618PhosphorylationSESEQGLTRPHADTG
CHHCCCCCCCCCCCC		49.3227080861
624PhosphorylationLTRPHADTGSIRSLQ
CCCCCCCCCCCEEEE		33.3427080861
626PhosphorylationRPHADTGSIRSLQTG
CCCCCCCCCEEEECC		19.5427080861
629O-linked_GlycosylationADTGSIRSLQTGVGE
CCCCCCEEEECCCCC		24.1431492838
629PhosphorylationADTGSIRSLQTGVGE
CCCCCCEEEECCCCC		24.1423401153
632O-linked_GlycosylationGSIRSLQTGVGELHG
CCCEEEECCCCCCCC		38.8431492838
632PhosphorylationGSIRSLQTGVGELHG
CCCEEEECCCCCCCC		38.8430266825
641PhosphorylationVGELHGETRFWHGKD
CCCCCCEEEECCCCC		35.4429449344
641O-linked_GlycosylationVGELHGETRFWHGKD
CCCCCCEEEECCCCC		35.4431492838
662UbiquitinationKDWVQLDKPFADFID
CCCCCCCCCHHHHHH		51.10-
673PhosphorylationDFIDRYSTPRMPWHD
HHHHHCCCCCCCHHH		13.1324719451
688UbiquitinationIASAVHGKAARDVAR
HHHHHHHHHHHHHHH		24.80-
711PhosphorylationTKIMKSKYRSLSYPF
HHHHHHCCCCCCCCE		16.7220393185
796UbiquitinationDDKVVFNKIGDAIAQ
CCCEEEHHHHHHHHH		36.28-
807AcetylationAIAQRILKAHRENQK
HHHHHHHHHHHHCCC		39.517696529
832PhosphorylationPGFEGDISTGGGNAL
CCCCCCCCCCCHHHH		26.2423401153
833PhosphorylationGFEGDISTGGGNALQ
CCCCCCCCCCHHHHH		39.9323401153
847PhosphorylationQAIMHFNYRTMCRGE
HHHHHCCHHHHCCCC		13.4023401153
962 (in isoform 2)Ubiquitination-1.7721890473
1000UbiquitinationRNATIYDKVFRCLPN
CCCCHHHHHHHCCCC		26.7121890473
1000 (in isoform 1)Ubiquitination-26.7121890473
1027UbiquitinationINKPVLAKEDPIRAE
HCCCCCCCCCCCCCH		59.49-
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
505SPhosphorylationKinasePRKAA2P54646
GPS
610SPhosphorylationKinaseCSNK2A1P68400
GPS
611SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLD1_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 PLD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHOA_HUMANRHOAphysical
12593858
ACTB_RATActbphysical
11373276
AMPH_HUMANAMPHgenetic
10764771
BIN1_HUMANBIN1genetic
10764771
AMPH_HUMANAMPHphysical
10764771
SYUA_HUMANSNCAphysical
11821392
PEA15_HUMANPEA15physical
10926929
RHOA_HUMANRHOAphysical
11311142
PKN1_HUMANPKN1physical
11259428
ARF6_HUMANARF6physical
12379803
ACTG_HUMANACTG1physical
12388543
RHEB_HUMANRHEBphysical
18550814
HIF1A_HUMANHIF1Aphysical
25361009
VHL_HUMANVHLphysical
25361009
EGLN1_HUMANEGLN1physical
25361009
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLD1_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-629, AND MASSSPECTROMETRY.

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