PACS2_HUMAN - dbPTM
PACS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PACS2_HUMAN
UniProt AC Q86VP3
Protein Name Phosphofurin acidic cluster sorting protein 2
Gene Name PACS2
Organism Homo sapiens (Human).
Sequence Length 889
Subcellular Localization Endoplasmic reticulum . Mitochondrion .
Protein Description Multifunctional sorting protein that controls the endoplasmic reticulum (ER)-mitochondria communication, including the apposition of mitochondria with the ER and ER homeostasis. In addition, in response to apoptotic inducer, translocates BIB to mitochondria, which initiates a sequence of events including the formation of mitochondrial truncated BID, the release of cytochrome c, the activation of caspase-3 thereby causing cell death. May also be involved in ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments..
Protein Sequence MAERGRLGLPGAPGALNTPVPMNLFATWEVDGSSPSCVPRLCSLTLKKLVVFKELEKELISVVIAVKMQGSKRILRSHEIVLPPSGQVETDLALTFSLQYPHFLKREGNKLQIMLQRRKRYKNRTILGYKTLAAGSISMAEVMQHPSEGGQVLSLCSSIKEAPVKAAEIWIASLSSQPIDHEDSTMQAGPKAKSTDNYSEEEYESFSSEQEASDDAVQGQDLDEDDFDVGKPKKQRRSIVRTTSMTRQQNFKQKVVALLRRFKVSDEVLDSEQDPAEHIPEAEEDLDLLYDTLDMEHPSDSGPDMEDDDSVLSTPKPKLRPYFEGLSHSSSQTEIGSIHSARSHKEPPSPADVPEKTRSLGGRQPSDSVSDTVALGVPGPREHPGQPEDSPEAEASTLDVFTERLPPSGRITKTESLVIPSTRSEGKQAGRRGRSTSLKERQAARPQNERANSLDNERCPDARSQLQIPRKTVYDQLNHILISDDQLPENIILVNTSDWQGQFLSDVLQRHTLPVVCTCSPADVQAAFSTIVSRIQRYCNCNSQPPTPVKIAVAGAQHYLSAILRLFVEQLSHKTPDWLGYMRFLVIPLGSHPVARYLGSVDYRYNNFFQDLAWRDLFNKLEAQSAVQDTPDIVSRITQYIAGANCAHQLPIAEAMLTYKQKSPDEESSQKFIPFVGVVKVGIVEPSSATSGDSDDAAPSGSGTLSSTPPSASPAAKEASPTPPSSPSVSGGLSSPSQGVGAELMGLQVDYWTAAQPADRKRDAEKKDLPVTKNTLKCTFRSLQVSRLPSSGEAAATPTMSMTVVTKEKNKKVMFLPKKAKDKDVESKSQCIEGISRLICTARQQQNMLRVLIDGVECSDVKFFQLAAQWSSHVKHFPICIFGHSKATF
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
43PhosphorylationSCVPRLCSLTLKKLV
CHHHHHHHCHHHHHH		29.0424719451
125PhosphorylationRKRYKNRTILGYKTL
HHHHCCCEECCHHHH		29.9220873877
171 (in isoform 4)Phosphorylation-1.9927251275
171PhosphorylationVKAAEIWIASLSSQP
CCHHHHHHHHCCCCC		1.9927251275
184PhosphorylationQPIDHEDSTMQAGPK
CCCCCCCCCCCCCCC		23.8524719451
185PhosphorylationPIDHEDSTMQAGPKA
CCCCCCCCCCCCCCC		26.1424719451
238PhosphorylationKPKKQRRSIVRTTSM
CCHHHHHHHHHHCHH		27.85-
242PhosphorylationQRRSIVRTTSMTRQQ
HHHHHHHHCHHHHHH		16.6022210691
244PhosphorylationRSIVRTTSMTRQQNF
HHHHHHCHHHHHHHH		19.97-
246PhosphorylationIVRTTSMTRQQNFKQ
HHHHCHHHHHHHHHH		25.70-
247 (in isoform 3)Phosphorylation-27.6927251275
299PhosphorylationTLDMEHPSDSGPDME
HCCCCCCCCCCCCCC		46.4425921289
301PhosphorylationDMEHPSDSGPDMEDD
CCCCCCCCCCCCCCC		57.4725921289
322PhosphorylationPKPKLRPYFEGLSHS
CCCCCCCCCCCCCCC		14.0827080861
327PhosphorylationRPYFEGLSHSSSQTE
CCCCCCCCCCCCCCC		31.9827080861
329PhosphorylationYFEGLSHSSSQTEIG
CCCCCCCCCCCCCCC		28.4526699800
330PhosphorylationFEGLSHSSSQTEIGS
CCCCCCCCCCCCCCC		22.5030576142
331PhosphorylationEGLSHSSSQTEIGSI
CCCCCCCCCCCCCCC		44.1026657352
333PhosphorylationLSHSSSQTEIGSIHS
CCCCCCCCCCCCCCC		31.3626699800
337PhosphorylationSSQTEIGSIHSARSH
CCCCCCCCCCCCCCC		23.8423312004
340PhosphorylationTEIGSIHSARSHKEP
CCCCCCCCCCCCCCC		24.5723312004
343PhosphorylationGSIHSARSHKEPPSP
CCCCCCCCCCCCCCC		38.3325849741
349PhosphorylationRSHKEPPSPADVPEK
CCCCCCCCCCCCCHH		43.3625159151
359PhosphorylationDVPEKTRSLGGRQPS
CCCHHHHCCCCCCCC		36.2828270605
366PhosphorylationSLGGRQPSDSVSDTV
CCCCCCCCCCHHHCE		33.8925159151
368PhosphorylationGGRQPSDSVSDTVAL
CCCCCCCCHHHCEEE		28.0529978859
370PhosphorylationRQPSDSVSDTVALGV
CCCCCCHHHCEEECC		31.3629978859
372PhosphorylationPSDSVSDTVALGVPG
CCCCHHHCEEECCCC		10.5229978859
390PhosphorylationHPGQPEDSPEAEAST
CCCCCCCCCCHHHHC		23.9929255136
396PhosphorylationDSPEAEASTLDVFTE
CCCCHHHHCHHHHHH		22.4729255136
397PhosphorylationSPEAEASTLDVFTER
CCCHHHHCHHHHHHC		33.7420068231
412PhosphorylationLPPSGRITKTESLVI
CCCCCCCCCCEEEEE		30.4728450419
414O-linked_GlycosylationPSGRITKTESLVIPS
CCCCCCCCEEEEECC		23.3530379171
414PhosphorylationPSGRITKTESLVIPS
CCCCCCCCEEEEECC		23.3530266825
416PhosphorylationGRITKTESLVIPSTR
CCCCCCEEEEECCCC		32.9223401153
421PhosphorylationTESLVIPSTRSEGKQ
CEEEEECCCCCCCCC		25.9029978859
422O-linked_GlycosylationESLVIPSTRSEGKQA
EEEEECCCCCCCCCC		32.6230379171
422PhosphorylationESLVIPSTRSEGKQA
EEEEECCCCCCCCCC		32.6227080861
435PhosphorylationQAGRRGRSTSLKERQ
CCCCCCCCCCHHHHH		25.7724706070
436PhosphorylationAGRRGRSTSLKERQA
CCCCCCCCCHHHHHH		36.4023312004
437PhosphorylationGRRGRSTSLKERQAA
CCCCCCCCHHHHHHC		38.4026699800
453PhosphorylationPQNERANSLDNERCP
CCCHHHHHCCCCCCC		35.7923401153
687PhosphorylationKVGIVEPSSATSGDS
EEEEECCCCCCCCCC		21.0629116813
688PhosphorylationVGIVEPSSATSGDSD
EEEECCCCCCCCCCC		46.4029116813
690PhosphorylationIVEPSSATSGDSDDA
EECCCCCCCCCCCCC		34.8829116813
691PhosphorylationVEPSSATSGDSDDAA
ECCCCCCCCCCCCCC		40.0830278072
694PhosphorylationSSATSGDSDDAAPSG
CCCCCCCCCCCCCCC		40.7030278072
698PhosphorylationSGDSDDAAPSGSGTL
CCCCCCCCCCCCCCC		13.0424719451
700PhosphorylationDSDDAAPSGSGTLSS
CCCCCCCCCCCCCCC		40.6430278072
702PhosphorylationDDAAPSGSGTLSSTP
CCCCCCCCCCCCCCC		32.7030278072
704PhosphorylationAAPSGSGTLSSTPPS
CCCCCCCCCCCCCCC		25.7629514088
706PhosphorylationPSGSGTLSSTPPSAS
CCCCCCCCCCCCCCC		31.8130278072
707PhosphorylationSGSGTLSSTPPSASP
CCCCCCCCCCCCCCC		48.3129514088
708PhosphorylationGSGTLSSTPPSASPA
CCCCCCCCCCCCCCC		35.5229514088
709PhosphorylationSGTLSSTPPSASPAA
CCCCCCCCCCCCCCH		23.8527251275
711PhosphorylationTLSSTPPSASPAAKE
CCCCCCCCCCCCHHH		42.4529449344
713PhosphorylationSSTPPSASPAAKEAS
CCCCCCCCCCHHHCC		21.2926330541
720PhosphorylationSPAAKEASPTPPSSP
CCCHHHCCCCCCCCC		30.3324275569
722PhosphorylationAAKEASPTPPSSPSV
CHHHCCCCCCCCCCC		45.3928348404
723PhosphorylationAKEASPTPPSSPSVS
HHHCCCCCCCCCCCC		30.1127251275
730PhosphorylationPPSSPSVSGGLSSPS
CCCCCCCCCCCCCCC		31.3322210691
737PhosphorylationSGGLSSPSQGVGAEL
CCCCCCCCCCCCHHH		41.3322210691
766AcetylationDRKRDAEKKDLPVTK
HHHCHHHHCCCCCCC		53.9919813403
767AcetylationRKRDAEKKDLPVTKN
HHCHHHHCCCCCCCH		56.8819813411
772PhosphorylationEKKDLPVTKNTLKCT
HHCCCCCCCHHHHEE		19.3526074081
773AcetylationKKDLPVTKNTLKCTF
HCCCCCCCHHHHEEE		48.4419813419
775PhosphorylationDLPVTKNTLKCTFRS
CCCCCCHHHHEEEEE		29.2026074081
777AcetylationPVTKNTLKCTFRSLQ
CCCCHHHHEEEEECE		29.237695397
779PhosphorylationTKNTLKCTFRSLQVS
CCHHHHEEEEECEEE		22.0926074081
782PhosphorylationTLKCTFRSLQVSRLP
HHHEEEEECEEEECC		20.9724719451
786PhosphorylationTFRSLQVSRLPSSGE
EEEECEEEECCCCCC		18.3526074081
790PhosphorylationLQVSRLPSSGEAAAT
CEEEECCCCCCCCCC		56.4120068231
791PhosphorylationQVSRLPSSGEAAATP
EEEECCCCCCCCCCC		38.4220068231
797PhosphorylationSSGEAAATPTMSMTV
CCCCCCCCCCEEEEE		17.9920068231
799PhosphorylationGEAAATPTMSMTVVT
CCCCCCCCEEEEEEE		19.9520068231
801PhosphorylationAAATPTMSMTVVTKE
CCCCCCEEEEEEECC		17.4920068231
803PhosphorylationATPTMSMTVVTKEKN
CCCCEEEEEEECCCC		12.4324719451
806PhosphorylationTMSMTVVTKEKNKKV
CEEEEEEECCCCCEE		29.2020068231
859PhosphorylationLIDGVECSDVKFFQL
EECCCCCCCCCHHHH		31.7530576142
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
437SPhosphorylationKinaseAKT1P31749
PSP
-KUbiquitinationE3 ubiquitin ligaseBIRC2Q13490
PMID:24633224
-KUbiquitinationE3 ubiquitin ligaseBIRC3Q13489
PMID:24633224
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PACS2_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 PACS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BIRC2_HUMANBIRC2physical
24633224
BIRC3_HUMANBIRC3physical
24633224
TRAF2_HUMANTRAF2physical
24633224
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 PACS2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASSSPECTROMETRY.

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