PLAP_HUMAN - dbPTM
PLAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLAP_HUMAN
UniProt AC Q9Y263
Protein Name Phospholipase A-2-activating protein
Gene Name PLAA
Organism Homo sapiens (Human).
Sequence Length 795
Subcellular Localization Nucleus . Cytoplasm . Cell junction, synapse . Recruited to damaged lysosomes decorated with K48-linked ubiquitin chains.
Protein Description Plays a role in protein ubiquitination, sorting and degradation through its association with VCP. [PubMed: 27753622 Involved in ubiquitin-mediated membrane proteins trafficking to late endosomes in an ESCRT-dependent manner, and hence plays a role in synaptic vesicle recycling (By similarity May play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes]
Protein Sequence MTSGATRYRLSCSLRGHELDVRGLVCCAYPPGAFVSVSRDRTTRLWAPDSPNRSFTEMHCMSGHSNFVSCVCIIPSSDIYPHGLIATGGNDHNICIFSLDSPMPLYILKGHKNTVCSLSSGKFGTLLSGSWDTTAKVWLNDKCMMTLQGHTAAVWAVKILPEQGLMLTGSADKTVKLWKAGRCERTFSGHEDCVRGLAILSETEFLSCANDASIRRWQITGECLEVYYGHTNYIYSISVFPNCRDFVTTAEDRSLRIWKHGECAQTIRLPAQSIWCCCVLDNGDIVVGASDGIIRVFTESEDRTASAEEIKAFEKELSHATIDSKTGDLGDINAEQLPGREHLNEPGTREGQTRLIRDGEKVEAYQWSVSEGRWIKIGDVVGSSGANQQTSGKVLYEGKEFDYVFSIDVNEGGPSYKLPYNTSDDPWLTAYNFLQKNDLNPMFLDQVAKFIIDNTKGQMLGLGNPSFSDPFTGGGRYVPGSSGSSNTLPTADPFTGAGRYVPGSASMGTTMAGVDPFTGNSAYRSAASKTMNIYFPKKEAVTFDQANPTQILGKLKELNGTAPEEKKLTEDDLILLEKILSLICNSSSEKPTVQQLQILWKAINCPEDIVFPALDILRLSIKHPSVNENFCNEKEGAQFSSHLINLLNPKGKPANQLLALRTFCNCFVGQAGQKLMMSQRESLMSHAIELKSGSNKNIHIALATLALNYSVCFHKDHNIEGKAQCLSLISTILEVVQDLEATFRLLVALGTLISDDSNAVQLAKSLGVDSQIKKYSSVSEPAKVSECCRFILNLL
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------MTSGATRYR
------CCCCCCEEE		35.5520860994
3Phosphorylation-----MTSGATRYRL
-----CCCCCCEEEE		25.7320860994
6Phosphorylation--MTSGATRYRLSCS
--CCCCCCEEEEEEE		31.58-
8PhosphorylationMTSGATRYRLSCSLR
CCCCCCEEEEEEECC		16.1430631047
13PhosphorylationTRYRLSCSLRGHELD
CEEEEEEECCCCEEE		20.0930631047
50PhosphorylationTRLWAPDSPNRSFTE
CCEECCCCCCCCCCE		24.0230266825
112UbiquitinationLYILKGHKNTVCSLS
EEEECCCCCEEEECC		64.0829967540
122UbiquitinationVCSLSSGKFGTLLSG
EEECCCCCCCEECCC		42.4432015554
125PhosphorylationLSSGKFGTLLSGSWD
CCCCCCCEECCCCCC		27.8827067055
173UbiquitinationMLTGSADKTVKLWKA
EEECCCCCCEEEEEC		55.7429967540
176UbiquitinationGSADKTVKLWKAGRC
CCCCCCEEEEECCCC		54.5927667366
179UbiquitinationDKTVKLWKAGRCERT
CCCEEEEECCCCCCC		51.9427667366
186PhosphorylationKAGRCERTFSGHEDC
ECCCCCCCCCCCHHH		10.4023312004
188PhosphorylationGRCERTFSGHEDCVR
CCCCCCCCCCHHHHH		38.3323312004
259UbiquitinationDRSLRIWKHGECAQT
HCCEEEEECCHHHCC		39.0821906983
303MethylationVFTESEDRTASAEEI
EEECCCCCCCCHHHH		28.30115487723
311UbiquitinationTASAEEIKAFEKELS
CCCHHHHHHHHHHHH		50.7523000965
311AcetylationTASAEEIKAFEKELS
CCCHHHHHHHHHHHH		50.7525953088
315UbiquitinationEEIKAFEKELSHATI
HHHHHHHHHHHCCEE		58.4623000965
315MalonylationEEIKAFEKELSHATI
HHHHHHHHHHHCCEE		58.4626320211
315AcetylationEEIKAFEKELSHATI
HHHHHHHHHHHCCEE		58.4623236377
318PhosphorylationKAFEKELSHATIDSK
HHHHHHHHCCEECCC		16.5027251275
325UbiquitinationSHATIDSKTGDLGDI
HCCEECCCCCCCCCC		53.4221906983
326PhosphorylationHATIDSKTGDLGDIN
CCEECCCCCCCCCCC		39.6228857561
361UbiquitinationRLIRDGEKVEAYQWS
EEEECCCEEEEEEEE		51.4029967540
376UbiquitinationVSEGRWIKIGDVVGS
ECCCCEEEEEEEECC		33.4123000965
383PhosphorylationKIGDVVGSSGANQQT
EEEEEECCCCCCCCC		17.6223403867
384PhosphorylationIGDVVGSSGANQQTS
EEEEECCCCCCCCCC		35.6823403867
390PhosphorylationSSGANQQTSGKVLYE
CCCCCCCCCCEEEEC		29.6823403867
391PhosphorylationSGANQQTSGKVLYEG
CCCCCCCCCEEEECC		32.0723403867
393UbiquitinationANQQTSGKVLYEGKE
CCCCCCCEEEECCCE		28.9123000965
396PhosphorylationQTSGKVLYEGKEFDY
CCCCEEEECCCEEEE		26.1428270605
399UbiquitinationGKVLYEGKEFDYVFS
CEEEECCCEEEEEEE		43.1823000965
403PhosphorylationYEGKEFDYVFSIDVN
ECCCEEEEEEEEECC		14.5528270605
406PhosphorylationKEFDYVFSIDVNEGG
CEEEEEEEEECCCCC		14.0828270605
415PhosphorylationDVNEGGPSYKLPYNT
ECCCCCCCCCCCCCC		37.8725627689
436UbiquitinationTAYNFLQKNDLNPMF
HHHHHHHHCCCCHHH		55.3523503661
449UbiquitinationMFLDQVAKFIIDNTK
HHHHHHHHHHCCCCC		37.9333845483
456AcetylationKFIIDNTKGQMLGLG
HHHCCCCCCCEECCC		54.097407777
456UbiquitinationKFIIDNTKGQMLGLG
HHHCCCCCCCEECCC		54.0923000965
459SulfoxidationIDNTKGQMLGLGNPS
CCCCCCCEECCCCCC		4.3421406390
466PhosphorylationMLGLGNPSFSDPFTG
EECCCCCCCCCCCCC		41.1928857561
468PhosphorylationGLGNPSFSDPFTGGG
CCCCCCCCCCCCCCC		49.0328555341
477PhosphorylationPFTGGGRYVPGSSGS
CCCCCCCCCCCCCCC		17.8030242111
481PhosphorylationGGRYVPGSSGSSNTL
CCCCCCCCCCCCCCC		26.0030242111
482PhosphorylationGRYVPGSSGSSNTLP
CCCCCCCCCCCCCCC		48.9226657352
484PhosphorylationYVPGSSGSSNTLPTA
CCCCCCCCCCCCCCC		23.5126657352
485PhosphorylationVPGSSGSSNTLPTAD
CCCCCCCCCCCCCCC		37.0430242111
487PhosphorylationGSSGSSNTLPTADPF
CCCCCCCCCCCCCCC		35.7430242111
490PhosphorylationGSSNTLPTADPFTGA
CCCCCCCCCCCCCCC		46.9727251275
495PhosphorylationLPTADPFTGAGRYVP
CCCCCCCCCCCCCCC		31.3530242111
500PhosphorylationPFTGAGRYVPGSASM
CCCCCCCCCCCCCCC		15.3021945579
504PhosphorylationAGRYVPGSASMGTTM
CCCCCCCCCCCCCCC		15.8821945579
506PhosphorylationRYVPGSASMGTTMAG
CCCCCCCCCCCCCCC		21.3121945579
506UbiquitinationRYVPGSASMGTTMAG
CCCCCCCCCCCCCCC		21.3123000965
509PhosphorylationPGSASMGTTMAGVDP
CCCCCCCCCCCCCCC		12.5421945579
510PhosphorylationGSASMGTTMAGVDPF
CCCCCCCCCCCCCCC		10.1721945579
514UbiquitinationMGTTMAGVDPFTGNS
CCCCCCCCCCCCCCH		6.4929967540
515UbiquitinationGTTMAGVDPFTGNSA
CCCCCCCCCCCCCHH		31.5129967540
518PhosphorylationMAGVDPFTGNSAYRS
CCCCCCCCCCHHHHH		40.6221945579
521PhosphorylationVDPFTGNSAYRSAAS
CCCCCCCHHHHHHHC		28.2021945579
523PhosphorylationPFTGNSAYRSAASKT
CCCCCHHHHHHHCCE		12.6221945579
529AcetylationAYRSAASKTMNIYFP
HHHHHHCCEEEEEEC		47.2519608861
529UbiquitinationAYRSAASKTMNIYFP
HHHHHHCCEEEEEEC		47.2523000965
531UbiquitinationRSAASKTMNIYFPKK
HHHHCCEEEEEECCC		3.1023503661
533UbiquitinationAASKTMNIYFPKKEA
HHCCEEEEEECCCCC		2.3227667366
537UbiquitinationTMNIYFPKKEAVTFD
EEEEEECCCCCEECC		54.0429967540
538UbiquitinationMNIYFPKKEAVTFDQ
EEEEECCCCCEECCC		51.6621906983
543UbiquitinationPKKEAVTFDQANPTQ
CCCCCEECCCCCHHH		5.4227667366
544UbiquitinationKKEAVTFDQANPTQI
CCCCEECCCCCHHHH		37.0029967540
554UbiquitinationNPTQILGKLKELNGT
CHHHHHHHHHHHCCC		53.6023503661
554AcetylationNPTQILGKLKELNGT
CHHHHHHHHHHHCCC		53.6023954790
554MalonylationNPTQILGKLKELNGT
CHHHHHHHHHHHCCC		53.6026320211
556UbiquitinationTQILGKLKELNGTAP
HHHHHHHHHHCCCCC		64.7427667366
566UbiquitinationNGTAPEEKKLTEDDL
CCCCCHHHCCCHHHH		51.9627667366
567UbiquitinationGTAPEEKKLTEDDLI
CCCCHHHCCCHHHHH		65.0122053931
590UbiquitinationICNSSSEKPTVQQLQ
HHCCCCCCCCHHHHH		48.1921906983
599UbiquitinationTVQQLQILWKAINCP
CHHHHHHHHHHCCCC		2.1823000965
605GlutathionylationILWKAINCPEDIVFP
HHHHHCCCCHHHHHH		2.9722555962
611UbiquitinationNCPEDIVFPALDILR
CCCHHHHHHHHHHHH		2.7532015554
622UbiquitinationDILRLSIKHPSVNEN
HHHHHHCCCCCCCCC		46.1923000965
627UbiquitinationSIKHPSVNENFCNEK
HCCCCCCCCCCCCHH		42.7129967540
629UbiquitinationKHPSVNENFCNEKEG
CCCCCCCCCCCHHHH		41.3822505724
634UbiquitinationNENFCNEKEGAQFSS
CCCCCCHHHHCHHHH		47.6732015554
650UbiquitinationLINLLNPKGKPANQL
HHHHHCCCCCCHHHH		77.7429967540
652UbiquitinationNLLNPKGKPANQLLA
HHHCCCCCCHHHHHH		47.2722505724
652MalonylationNLLNPKGKPANQLLA
HHHCCCCCCHHHHHH		47.2726320211
668UbiquitinationRTFCNCFVGQAGQKL
HHHHHHHHHHHHHHH		6.3929967540
678PhosphorylationAGQKLMMSQRESLMS
HHHHHHHHHHHHHHH		16.48-
682PhosphorylationLMMSQRESLMSHAIE
HHHHHHHHHHHHHHH		31.4029083192
691AcetylationMSHAIELKSGSNKNI
HHHHHHHCCCCCCCH		39.7220167786
691UbiquitinationMSHAIELKSGSNKNI
HHHHHHHCCCCCCCH		39.722190698
750UbiquitinationFRLLVALGTLISDDS
HHHHHHHHHHHCCCC		14.5627667366
751UbiquitinationRLLVALGTLISDDSN
HHHHHHHHHHCCCCC		23.0529967540
760UbiquitinationISDDSNAVQLAKSLG
HCCCCCHHHHHHHCC		5.8429967540
773UbiquitinationLGVDSQIKKYSSVSE
CCCCHHHHHCCCCCC		37.7127667366
774UbiquitinationGVDSQIKKYSSVSEP
CCCHHHHHCCCCCCC		52.5829967540
776PhosphorylationDSQIKKYSSVSEPAK
CHHHHHCCCCCCCHH		32.8920860994
783UbiquitinationSSVSEPAKVSECCRF
CCCCCCHHHHHHHHH		57.9429967540
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 PLAP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLAP_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 PLAP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_HUMANVCPphysical
19887378
UBC_HUMANUBCphysical
19423704
PDIA3_HUMANPDIA3physical
22484374
CAV1_HUMANCAV1physical
22484374
NSF1C_HUMANNSFL1Cphysical
22863883
PARP6_HUMANPARP6physical
22863883
PCNA_HUMANPCNAphysical
22863883
TBB2A_HUMANTUBB2Aphysical
22863883
EFTU_HUMANTUFMphysical
22863883
TWF2_HUMANTWF2physical
22863883
UBXN1_HUMANUBXN1physical
22863883
UBXN1_HUMANUBXN1physical
25416956
BASP1_HUMANBASP1physical
26344197
XPO2_HUMANCSE1Lphysical
26344197
FPPS_HUMANFDPSphysical
26344197
PAK2_HUMANPAK2physical
26344197
SF01_HUMANSF1physical
26344197
XPP1_HUMANXPNPEP1physical
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 PLAP_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-529, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY.

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