PACS1_HUMAN - dbPTM
PACS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PACS1_HUMAN
UniProt AC Q6VY07
Protein Name Phosphofurin acidic cluster sorting protein 1
Gene Name PACS1
Organism Homo sapiens (Human).
Sequence Length 963
Subcellular Localization Golgi apparatus, trans-Golgi network . Localizes in the perinuclear region, probably the TGN.
Protein Description Coat protein that is involved in the localization of trans-Golgi network (TGN) membrane proteins that contain acidic cluster sorting motifs. Controls the endosome-to-Golgi trafficking of furin and mannose-6-phosphate receptor by connecting the acidic-cluster-containing cytoplasmic domain of these molecules with the adapter-protein complex-1 (AP-1) of endosomal clathrin-coated membrane pits. Involved in HIV-1 nef-mediated removal of MHC-I from the cell surface to the TGN..
Protein Sequence MAERGGAGGGPGGAGGGSGQRGSGVAQSPQQPPPQQQQQQPPQQPTPPKLAQATSSSSSTSAAAASSSSSSTSTSMAVAVASGSAPPGGPGPGRTPAPVQMNLYATWEVDRSSSSCVPRLFSLTLKKLVMLKEMDKDLNSVVIAVKLQGSKRILRSNEIVLPASGLVETELQLTFSLQYPHFLKRDANKLQIMLQRRKRYKNRTILGYKTLAVGLINMAEVMQHPNEGALVLGLHSNVKDVSVPVAEIKIYSLSSQPIDHEGIKSKLSDRSPDIDNYSEEEEESFSSEQEGSDDPLHGQDLFYEDEDLRKVKKTRRKLTSTSAITRQPNIKQKFVALLKRFKVSDEVGFGLEHVSREQIREVEEDLDELYDSLEMYNPSDSGPEMEETESILSTPKPKLKPFFEGMSQSSSQTEIGSLNSKGSLGKDTTSPMELAALEKIKSTWIKNQDDSLTETDTLEITDQDMFGDASTSLVVPEKVKTPMKSSKTDLQGSASPSKVEGVHTPRQKRSTPLKERQLSKPLSERTNSSDSERSPDLGHSTQIPRKVVYDQLNQILVSDAALPENVILVNTTDWQGQYVAELLQDQRKPVVCTCSTVEVQAVLSALLTRIQRYCNCNSSMPRPVKVAAVGGQSYLSSILRFFVKSLANKTSDWLGYMRFLIIPLGSHPVAKYLGSVDSKYSSSFLDSGWRDLFSRSEPPVSEQLDVAGRVMQYVNGAATTHQLPVAEAMLTCRHKFPDEDSYQKFIPFIGVVKVGLVEDSPSTAGDGDDSPVVSLTVPSTSPPSSSGLSRDATATPPSSPSMSSALAIVGSPNSPYGDVIGLQVDYWLGHPGERRREGDKRDASSKNTLKSVFRSVQVSRLPHSGEAQLSGTMAMTVVTKEKNKKVPTIFLSKKPREKEVDSKSQVIEGISRLICSAKQQQTMLRVSIDGVEWSDIKFFQLAAQWPTHVKHFPVGLFSGSKAT
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
2Acetylation------MAERGGAGG
------CCCCCCCCC
18.3919413330
4Methylation----MAERGGAGGGP
----CCCCCCCCCCC
39.03115387237
18PhosphorylationPGGAGGGSGQRGSGV
CCCCCCCCCCCCCCC
34.7225159151
23PhosphorylationGGSGQRGSGVAQSPQ
CCCCCCCCCCCCCCC
32.0823663014
28PhosphorylationRGSGVAQSPQQPPPQ
CCCCCCCCCCCCCCH
18.2225159151
46PhosphorylationQQPPQQPTPPKLAQA
CCCCCCCCCCHHHHH
48.1329255136
54PhosphorylationPPKLAQATSSSSSTS
CCHHHHHCCCCCCHH
19.6330576142
69PhosphorylationAAAASSSSSSTSTSM
HHHHHCCCCCCCCEE
30.2030576142
104PhosphorylationAPVQMNLYATWEVDR
CCEEEEEEEEEEECC
9.2929978859
104 (in isoform 2)Phosphorylation-9.2927642862
106PhosphorylationVQMNLYATWEVDRSS
EEEEEEEEEEECCCC
14.4929978859
112PhosphorylationATWEVDRSSSSCVPR
EEEEECCCCCCHHHH
30.06-
113PhosphorylationTWEVDRSSSSCVPRL
EEEECCCCCCHHHHH
27.45-
114PhosphorylationWEVDRSSSSCVPRLF
EEECCCCCCHHHHHH
29.07-
115PhosphorylationEVDRSSSSCVPRLFS
EECCCCCCHHHHHHH
22.53-
122PhosphorylationSCVPRLFSLTLKKLV
CHHHHHHHHHHHHHH
25.6524719451
124PhosphorylationVPRLFSLTLKKLVML
HHHHHHHHHHHHHHH
35.0220068231
132AcetylationLKKLVMLKEMDKDLN
HHHHHHHHHHCCCCC
32.667973175
151AcetylationAVKLQGSKRILRSNE
EEEECCCCEEEECCC
50.737973187
204PhosphorylationRKRYKNRTILGYKTL
HHHHCCCEECCHHHH
29.9220873877
249UbiquitinationSVPVAEIKIYSLSSQ
ECEEEEEEEEECCCC
27.39-
251PhosphorylationPVAEIKIYSLSSQPI
EEEEEEEEECCCCCC
9.8825159151
251 (in isoform 2)Phosphorylation-9.8827642862
252PhosphorylationVAEIKIYSLSSQPID
EEEEEEEECCCCCCC
25.8328152594
254PhosphorylationEIKIYSLSSQPIDHE
EEEEEECCCCCCCCH
22.4628152594
255PhosphorylationIKIYSLSSQPIDHEG
EEEEECCCCCCCCHH
45.31-
264UbiquitinationPIDHEGIKSKLSDRS
CCCCHHHHHHHCCCC
53.01-
266UbiquitinationDHEGIKSKLSDRSPD
CCHHHHHHHCCCCCC
47.19-
278DephosphorylationSPDIDNYSEEEEESF
CCCCCCCCHHHHHHH
44.8014633983
278PhosphorylationSPDIDNYSEEEEESF
CCCCCCCCHHHHHHH
44.8014633983
292PhosphorylationFSSEQEGSDDPLHGQ
HCCCCCCCCCCCCCC
37.7824275569
303PhosphorylationLHGQDLFYEDEDLRK
CCCCCCCCCCHHHHH
29.75-
317UbiquitinationKVKKTRRKLTSTSAI
HHHHHHHHHHCCCHH
53.47-
319PhosphorylationKKTRRKLTSTSAITR
HHHHHHHHCCCHHHC
32.7528450419
320PhosphorylationKTRRKLTSTSAITRQ
HHHHHHHCCCHHHCC
30.7025159151
321PhosphorylationTRRKLTSTSAITRQP
HHHHHHCCCHHHCCC
19.5528450419
322PhosphorylationRRKLTSTSAITRQPN
HHHHHCCCHHHCCCC
19.9019276368
325PhosphorylationLTSTSAITRQPNIKQ
HHCCCHHHCCCCHHH
23.9828450419
333UbiquitinationRQPNIKQKFVALLKR
CCCCHHHHHHHHHHH
36.48-
3392-HydroxyisobutyrylationQKFVALLKRFKVSDE
HHHHHHHHHCCCCCC
57.55-
339UbiquitinationQKFVALLKRFKVSDE
HHHHHHHHHCCCCCC
57.5521890473
339 (in isoform 1)Ubiquitination-57.5521890473
339 (in isoform 2)Ubiquitination-57.5521890473
344PhosphorylationLLKRFKVSDEVGFGL
HHHHCCCCCCCCCCC
28.7528555341
355PhosphorylationGFGLEHVSREQIREV
CCCCCCCCHHHHHHH
31.8225849741
370PhosphorylationEEDLDELYDSLEMYN
HHHHHHHHHHHHHHC
11.0528060719
370 (in isoform 2)Phosphorylation-11.0527642862
372PhosphorylationDLDELYDSLEMYNPS
HHHHHHHHHHHHCCC
16.8128060719
376PhosphorylationLYDSLEMYNPSDSGP
HHHHHHHHCCCCCCC
17.9728060719
379PhosphorylationSLEMYNPSDSGPEME
HHHHHCCCCCCCCHH
40.5518669648
379 (in isoform 2)Phosphorylation-40.5527642862
381PhosphorylationEMYNPSDSGPEMEET
HHHCCCCCCCCHHHH
61.6623898821
381 (in isoform 2)Phosphorylation-61.6627642862
388PhosphorylationSGPEMEETESILSTP
CCCCHHHHHHHHCCC
23.0228060719
388 (in isoform 2)Phosphorylation-23.0227642862
390PhosphorylationPEMEETESILSTPKP
CCHHHHHHHHCCCCC
35.9328060719
393PhosphorylationEETESILSTPKPKLK
HHHHHHHCCCCCCCC
40.7825841592
393 (in isoform 2)Phosphorylation-40.7827642862
394PhosphorylationETESILSTPKPKLKP
HHHHHHCCCCCCCCH
31.7028060719
394 (in isoform 2)Phosphorylation-31.7027642862
407PhosphorylationKPFFEGMSQSSSQTE
CHHHCCCCCCCCCCC
37.4517525332
409PhosphorylationFFEGMSQSSSQTEIG
HHCCCCCCCCCCCCC
25.3421712546
410PhosphorylationFEGMSQSSSQTEIGS
HCCCCCCCCCCCCCC
20.8723401153
411PhosphorylationEGMSQSSSQTEIGSL
CCCCCCCCCCCCCCC
46.5023401153
413PhosphorylationMSQSSSQTEIGSLNS
CCCCCCCCCCCCCCC
31.3630108239
417PhosphorylationSSQTEIGSLNSKGSL
CCCCCCCCCCCCCCC
30.0030108239
420PhosphorylationTEIGSLNSKGSLGKD
CCCCCCCCCCCCCCC
43.6222199227
423PhosphorylationGSLNSKGSLGKDTTS
CCCCCCCCCCCCCCC
37.3730108239
426AcetylationNSKGSLGKDTTSPME
CCCCCCCCCCCCHHH
58.1419827559
428PhosphorylationKGSLGKDTTSPMELA
CCCCCCCCCCHHHHH
32.4330266825
429PhosphorylationGSLGKDTTSPMELAA
CCCCCCCCCHHHHHH
40.7530266825
430PhosphorylationSLGKDTTSPMELAAL
CCCCCCCCHHHHHHH
25.0925159151
439UbiquitinationMELAALEKIKSTWIK
HHHHHHHHHHHHCCC
57.17-
443O-linked_GlycosylationALEKIKSTWIKNQDD
HHHHHHHHCCCCCCC
26.6329351928
451PhosphorylationWIKNQDDSLTETDTL
CCCCCCCCCCCCCEE
45.5427251275
453PhosphorylationKNQDDSLTETDTLEI
CCCCCCCCCCCEEEE
40.5727690223
455PhosphorylationQDDSLTETDTLEITD
CCCCCCCCCEEEECC
29.1127251275
457PhosphorylationDSLTETDTLEITDQD
CCCCCCCEEEECCHH
33.4427251275
481PhosphorylationVVPEKVKTPMKSSKT
ECCCCCCCCCCCCCC
31.4424719451
485PhosphorylationKVKTPMKSSKTDLQG
CCCCCCCCCCCCCCC
30.7128857561
486PhosphorylationVKTPMKSSKTDLQGS
CCCCCCCCCCCCCCC
33.7726074081
488PhosphorylationTPMKSSKTDLQGSAS
CCCCCCCCCCCCCCC
43.8423927012
493PhosphorylationSKTDLQGSASPSKVE
CCCCCCCCCCHHHCC
16.7725159151
495PhosphorylationTDLQGSASPSKVEGV
CCCCCCCCHHHCCCC
31.2523927012
497PhosphorylationLQGSASPSKVEGVHT
CCCCCCHHHCCCCCC
47.0023401153
504PhosphorylationSKVEGVHTPRQKRST
HHCCCCCCCCCCCCC
20.1223401153
510PhosphorylationHTPRQKRSTPLKERQ
CCCCCCCCCCCCHHH
41.2223312004
511PhosphorylationTPRQKRSTPLKERQL
CCCCCCCCCCCHHHC
36.3523312004
519PhosphorylationPLKERQLSKPLSERT
CCCHHHCCCCHHHCC
24.7223898821
520AcetylationLKERQLSKPLSERTN
CCHHHCCCCHHHCCC
59.5825953088
523PhosphorylationRQLSKPLSERTNSSD
HHCCCCHHHCCCCCC
33.2930576142
526PhosphorylationSKPLSERTNSSDSER
CCCHHHCCCCCCCCC
35.0923927012
526 (in isoform 2)Phosphorylation-35.0921406692
528PhosphorylationPLSERTNSSDSERSP
CHHHCCCCCCCCCCC
34.6025159151
528 (in isoform 2)Phosphorylation-34.6021406692
529PhosphorylationLSERTNSSDSERSPD
HHHCCCCCCCCCCCC
47.4225159151
529 (in isoform 2)Phosphorylation-47.4221406692
531PhosphorylationERTNSSDSERSPDLG
HCCCCCCCCCCCCCC
36.5423927012
531 (in isoform 2)Phosphorylation-36.5421406692
534PhosphorylationNSSDSERSPDLGHST
CCCCCCCCCCCCCCC
20.7929255136
534 (in isoform 2)Phosphorylation-20.7921406692
540O-linked_GlycosylationRSPDLGHSTQIPRKV
CCCCCCCCCCCCHHH
21.8729351928
540PhosphorylationRSPDLGHSTQIPRKV
CCCCCCCCCCCCHHH
21.8723927012
541PhosphorylationSPDLGHSTQIPRKVV
CCCCCCCCCCCHHHH
25.5023927012
549PhosphorylationQIPRKVVYDQLNQIL
CCCHHHHHHHHHHHH
10.85-
593PhosphorylationQRKPVVCTCSTVEVQ
CCCCEEEECCHHHHH
9.6227732954
595PhosphorylationKPVVCTCSTVEVQAV
CCEEEECCHHHHHHH
19.8227732954
596PhosphorylationPVVCTCSTVEVQAVL
CEEEECCHHHHHHHH
23.8827732954
613PhosphorylationLLTRIQRYCNCNSSM
HHHHHHHHHCCCCCC
3.31-
633PhosphorylationVAAVGGQSYLSSILR
EEEECCHHHHHHHHH
31.1728152594
634PhosphorylationAAVGGQSYLSSILRF
EEECCHHHHHHHHHH
11.6028152594
636PhosphorylationVGGQSYLSSILRFFV
ECCHHHHHHHHHHHH
13.7028152594
637PhosphorylationGGQSYLSSILRFFVK
CCHHHHHHHHHHHHH
24.0524719451
651PhosphorylationKSLANKTSDWLGYMR
HHHCCCCCHHHHCCE
28.53-
671AcetylationLGSHPVAKYLGSVDS
CCCCHHHHHHCCCCC
41.0425953088
672PhosphorylationGSHPVAKYLGSVDSK
CCCHHHHHHCCCCCH
13.42-
680PhosphorylationLGSVDSKYSSSFLDS
HCCCCCHHCHHHHCC
20.10-
687PhosphorylationYSSSFLDSGWRDLFS
HCHHHHCCCHHHHHH
42.26-
719PhosphorylationQYVNGAATTHQLPVA
HHHCCCCCCCCCCHH
25.0322210691
731PhosphorylationPVAEAMLTCRHKFPD
CHHHHHHHCCCCCCC
8.3922210691
760PhosphorylationKVGLVEDSPSTAGDG
EEEEECCCCCCCCCC
13.7722199227
762PhosphorylationGLVEDSPSTAGDGDD
EEECCCCCCCCCCCC
34.5422199227
763PhosphorylationLVEDSPSTAGDGDDS
EECCCCCCCCCCCCC
37.7422199227
770PhosphorylationTAGDGDDSPVVSLTV
CCCCCCCCCEEEEEE
25.0822199227
774PhosphorylationGDDSPVVSLTVPSTS
CCCCCEEEEEECCCC
20.6828450419
776PhosphorylationDSPVVSLTVPSTSPP
CCCEEEEEECCCCCC
23.9028450419
779PhosphorylationVVSLTVPSTSPPSSS
EEEEEECCCCCCCCC
36.8630278072
780PhosphorylationVSLTVPSTSPPSSSG
EEEEECCCCCCCCCC
38.9030278072
781PhosphorylationSLTVPSTSPPSSSGL
EEEECCCCCCCCCCC
38.8730278072
784PhosphorylationVPSTSPPSSSGLSRD
ECCCCCCCCCCCCCC
40.2928450419
785PhosphorylationPSTSPPSSSGLSRDA
CCCCCCCCCCCCCCC
33.9128450419
786PhosphorylationSTSPPSSSGLSRDAT
CCCCCCCCCCCCCCC
48.3628450419
789PhosphorylationPPSSSGLSRDATATP
CCCCCCCCCCCCCCC
31.4728450419
795PhosphorylationLSRDATATPPSSPSM
CCCCCCCCCCCCCCH
31.2327251275
798PhosphorylationDATATPPSSPSMSSA
CCCCCCCCCCCHHHH
56.9627251275
799PhosphorylationATATPPSSPSMSSAL
CCCCCCCCCCHHHHE
27.1127251275
814O-linked_GlycosylationAIVGSPNSPYGDVIG
ECCCCCCCCCCCCEE
23.9229351928
844PhosphorylationEGDKRDASSKNTLKS
CCCCCCCCCCHHHHH
46.24-
845PhosphorylationGDKRDASSKNTLKSV
CCCCCCCCCHHHHHH
31.48-
848PhosphorylationRDASSKNTLKSVFRS
CCCCCCHHHHHHHHH
39.02-
851PhosphorylationSSKNTLKSVFRSVQV
CCCHHHHHHHHHEEE
29.6023401153
855PhosphorylationTLKSVFRSVQVSRLP
HHHHHHHHEEECCCC
12.8729449344
859PhosphorylationVFRSVQVSRLPHSGE
HHHHEEECCCCCCCC
15.8229449344
870PhosphorylationHSGEAQLSGTMAMTV
CCCCCCCCCEEEEEE
21.8230387612
872PhosphorylationGEAQLSGTMAMTVVT
CCCCCCCEEEEEEEE
9.8130387612
884AcetylationVVTKEKNKKVPTIFL
EEECCCCCCCCEEEE
67.2418585905
903UbiquitinationREKEVDSKSQVIEGI
CHHHCCCHHHHHHHH
40.21-
918MalonylationSRLICSAKQQQTMLR
HHHHHCHHHHCCEEE
32.1426320211

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
278SPhosphorylationKinaseCSNK2A1P68400
GPS
278SPhosphorylationKinaseCK2-FAMILY-GPS
278SPhosphorylationKinaseCK2_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PACS1_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 PACS1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GGA3_HUMANGGA3physical
16977309
CSK21_HUMANCSNK2A1physical
16977309
SORL_HUMANSORL1physical
17855360
PTPRG_HUMANPTPRGphysical
27173435
FP100_HUMANC17orf70physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615009Mental retardation, autosomal dominant 17 (MRD17)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PACS1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-46, AND MASS SPECTROMETRY.
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-379; SER-381; SER-430;SER-495; THR-504; SER-528; SER-529 AND SER-534, AND MASS SPECTROMETRY.
"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-407 AND SER-410, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-46, AND MASS SPECTROMETRY.
"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 THR-46, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-251, AND MASSSPECTROMETRY.

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