AP3D1_HUMAN - dbPTM
AP3D1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP3D1_HUMAN
UniProt AC O14617
Protein Name AP-3 complex subunit delta-1
Gene Name AP3D1
Organism Homo sapiens (Human).
Sequence Length 1153
Subcellular Localization Cytoplasm. Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. Involved in process of CD8+ T-cell and NK cell degranulation. [PubMed: 26744459 In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals (By similarity]
Protein Sequence MALKMVKGSIDRMFDKNLQDLVRGIRNHKEDEAKYISQCIDEIKQELKQDNIAVKANAVCKLTYLQMLGYDISWAAFNIIEVMSASKFTFKRIGYLAASQSFHEGTDVIMLTTNQIRKDLSSPSQYDTGVALTGLSCFVTPDLARDLANDIMTLMSHTKPYIRKKAVLIMYKVFLKYPESLRPAFPRLKEKLEDPDPGVQSAAVNVICELARRNPKNYLSLAPLFFKLMTSSTNNWVLIKIIKLFGALTPLEPRLGKKLIEPLTNLIHSTSAMSLLYECVNTVIAVLISLSSGMPNHSASIQLCVQKLRILIEDSDQNLKYLGLLAMSKILKTHPKSVQSHKDLILQCLDDKDESIRLRALDLLYGMVSKKNLMEIVKKLMTHVDKAEGTTYRDELLTKIIDICSQSNYQYITNFEWYISILVELTRLEGTRHGHLIAAQMLDVAIRVKAIRKFAVSQMSALLDSAHLLASSTQRNGICEVLYAAAWICGEFSEHLQEPHHTLEAMLRPRVTTLPGHIQAVYVQNVVKLYASILQQKEQAGEAEGAQAVTQLMVDRLPQFVQSADLEVQERASCILQLVKHIQKLQAKDVPVAEEVSALFAGELNPVAPKAQKKVPVPEGLDLDAWINEPLSDSESEDERPRAVFHEEEQRRPKHRPSEADEEELARRREARKQEQANNPFYIKSSPSPQKRYQDTPGVEHIPVVQIDLSVPLKVPGLPMSDQYVKLEEERRHRQKLEKDKRRKKRKEKEKKGKRRHSSLPTESDEDIAPAQQVDIVTEEMPENALPSDEDDKDPNDPYRALDIDLDKPLADSEKLPIQKHRNTETSKSPEKDVPMVEKKSKKPKKKEKKHKEKERDKEKKKEKEKKKSPKPKKKKHRKEKEERTKGKKKSKKQPPGSEEAAGEPVQNGAPEEEQLPPESSYSLLAENSYVKMTCDIRGSLQEDSQVTVAIVLENRSSSILKGMELSVLDSLNARMARPQGSSVHDGVPVPFQLPPGVSNEAQYVFTIQSIVMAQKLKGTLSFIAKNDEGATHEKLDFRLHFSCSSYLITTPCYSDAFAKLLESGDLSMSSIKVDGIRMSFQNLLAKICFHHHFSVVERVDSCASMYSRSIQGHHVCLLVKKGENSVSVDGKCSDSTLLSNLLEEMKATLAKC
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------MALKMVKGS
------CCHHHHCHH
27.4822814378
4Ubiquitination----MALKMVKGSID
----CCHHHHCHHHH
49.0224816145
4 (in isoform 5)Ubiquitination-49.02-
7Ubiquitination-MALKMVKGSIDRMF
-CCHHHHCHHHHHHH
43.3629967540
7 (in isoform 5)Ubiquitination-43.36-
9PhosphorylationALKMVKGSIDRMFDK
CHHHHCHHHHHHHHH
18.6526846344
16UbiquitinationSIDRMFDKNLQDLVR
HHHHHHHHHHHHHHH
48.5722817900
16 (in isoform 1)Ubiquitination-48.5721890473
16 (in isoform 2)Ubiquitination-48.5721890473
16 (in isoform 3)Ubiquitination-48.5721890473
16 (in isoform 4)Ubiquitination-48.5721890473
16 (in isoform 5)Ubiquitination-48.5721890473
34UbiquitinationNHKEDEAKYISQCID
CCCHHHHHHHHHHHH
40.8632015554
35PhosphorylationHKEDEAKYISQCIDE
CCHHHHHHHHHHHHH
16.9223532336
44UbiquitinationSQCIDEIKQELKQDN
HHHHHHHHHHHHHCC
35.3529967540
44 (in isoform 5)Ubiquitination-35.35-
48UbiquitinationDEIKQELKQDNIAVK
HHHHHHHHHCCHHHH
55.6533845483
55UbiquitinationKQDNIAVKANAVCKL
HHCCHHHHHHHHHHH
27.2229967540
55 (in isoform 5)Ubiquitination-27.22-
164UbiquitinationHTKPYIRKKAVLIMY
CCCHHHHHHHHHHHH
35.21-
165UbiquitinationTKPYIRKKAVLIMYK
CCHHHHHHHHHHHHH
33.60-
172UbiquitinationKAVLIMYKVFLKYPE
HHHHHHHHHHHHCHH
14.7722817900
176AcetylationIMYKVFLKYPESLRP
HHHHHHHHCHHHHCC
47.50129103
176UbiquitinationIMYKVFLKYPESLRP
HHHHHHHHCHHHHCC
47.5022817900
176 (in isoform 1)Ubiquitination-47.5021890473
176 (in isoform 4)Ubiquitination-47.5021890473
176 (in isoform 5)Ubiquitination-47.5021890473
180PhosphorylationVFLKYPESLRPAFPR
HHHHCHHHHCCCCHH
25.7720860994
189UbiquitinationRPAFPRLKEKLEDPD
CCCCHHHHHHHCCCC
54.83-
189 (in isoform 5)Ubiquitination-54.83-
191UbiquitinationAFPRLKEKLEDPDPG
CCHHHHHHHCCCCCC
56.4429967540
191 (in isoform 5)Ubiquitination-56.44-
208GlutathionylationSAAVNVICELARRNP
HHHHHHHHHHHHHCC
2.8222555962
216UbiquitinationELARRNPKNYLSLAP
HHHHHCCCCHHHHHH
62.8721963094
264PhosphorylationKKLIEPLTNLIHSTS
HHHHHHHHHHHHHHC
38.4025332170
269PhosphorylationPLTNLIHSTSAMSLL
HHHHHHHHHCHHHHH
19.6425332170
270PhosphorylationLTNLIHSTSAMSLLY
HHHHHHHHCHHHHHH
13.3246165117
271PhosphorylationTNLIHSTSAMSLLYE
HHHHHHHCHHHHHHH
25.6225332170
328PhosphorylationYLGLLAMSKILKTHP
HHHHHHHHHHHHHCC
15.7820860994
332UbiquitinationLAMSKILKTHPKSVQ
HHHHHHHHHCCCCHH
48.5429967540
336UbiquitinationKILKTHPKSVQSHKD
HHHHHCCCCHHHCHH
56.5129967540
342UbiquitinationPKSVQSHKDLILQCL
CCCHHHCHHHHHHHC
60.5229967540
352AcetylationILQCLDDKDESIRLR
HHHHCCCCCHHHHHH
64.1627452117
352UbiquitinationILQCLDDKDESIRLR
HHHHCCCCCHHHHHH
64.1629967540
352 (in isoform 5)Ubiquitination-64.16-
355PhosphorylationCLDDKDESIRLRALD
HCCCCCHHHHHHHHH
24.1246165111
365PhosphorylationLRALDLLYGMVSKKN
HHHHHHHHHHCCHHH
15.5220068231
369PhosphorylationDLLYGMVSKKNLMEI
HHHHHHCCHHHHHHH
29.0820068231
370UbiquitinationLLYGMVSKKNLMEIV
HHHHHCCHHHHHHHH
33.98-
371MalonylationLYGMVSKKNLMEIVK
HHHHCCHHHHHHHHH
48.0526320211
378UbiquitinationKNLMEIVKKLMTHVD
HHHHHHHHHHHHHHH
45.9433845483
379UbiquitinationNLMEIVKKLMTHVDK
HHHHHHHHHHHHHHH
32.37-
386AcetylationKLMTHVDKAEGTTYR
HHHHHHHHHCCCCHH
47.457662841
409PhosphorylationDICSQSNYQYITNFE
HHHHHCCCEEECCHH
14.1324043423
411PhosphorylationCSQSNYQYITNFEWY
HHHCCCEEECCHHHH
10.1924043423
413PhosphorylationQSNYQYITNFEWYIS
HCCCEEECCHHHHHH
28.9924043423
418PhosphorylationYITNFEWYISILVEL
EECCHHHHHHHHHHH
4.2424043423
420PhosphorylationTNFEWYISILVELTR
CCHHHHHHHHHHHHC
8.3224043423
426PhosphorylationISILVELTRLEGTRH
HHHHHHHHCCCCCCC
21.5024043423
463UbiquitinationVSQMSALLDSAHLLA
HHHHHHHHHHHHHHC
4.9724816145
511UbiquitinationEAMLRPRVTTLPGHI
HHHHCCCCCCCCCCE
5.4824816145
521UbiquitinationLPGHIQAVYVQNVVK
CCCCEEHEHHHHHHH
2.4924816145
537UbiquitinationYASILQQKEQAGEAE
HHHHHHHHHHHCCCC
38.54-
553SulfoxidationAQAVTQLMVDRLPQF
HHHHHHHHHHCHHHH
1.8030846556
580AcetylationSCILQLVKHIQKLQA
HHHHHHHHHHHHHHC
43.5125953088
580UbiquitinationSCILQLVKHIQKLQA
HHHHHHHHHHHHHHC
43.5124816145
584AcetylationQLVKHIQKLQAKDVP
HHHHHHHHHHCCCCC
41.8025953088
584UbiquitinationQLVKHIQKLQAKDVP
HHHHHHHHHHCCCCC
41.8029967540
588UbiquitinationHIQKLQAKDVPVAEE
HHHHHHCCCCCHHHH
46.4229967540
597PhosphorylationVPVAEEVSALFAGEL
CCHHHHHHHHHCCCC
23.6418669648
610UbiquitinationELNPVAPKAQKKVPV
CCCCCCCHHCCCCCC
54.4330230243
610 (in isoform 5)Ubiquitination-54.43-
613UbiquitinationPVAPKAQKKVPVPEG
CCCCHHCCCCCCCCC
61.67-
632PhosphorylationAWINEPLSDSESEDE
HHHCCCCCCCCCCCC
50.2122617229
632 (in isoform 5)Phosphorylation-50.2118669648
634PhosphorylationINEPLSDSESEDERP
HCCCCCCCCCCCCCC
39.3822617229
634 (in isoform 5)Phosphorylation-39.3818669648
636PhosphorylationEPLSDSESEDERPRA
CCCCCCCCCCCCCCC
55.0622617229
636 (in isoform 5)Phosphorylation-55.0618669648
658PhosphorylationRRPKHRPSEADEEEL
CCCCCCCCHHCHHHH
45.4329255136
673UbiquitinationARRREARKQEQANNP
HHHHHHHHHHHHCCC
66.3029967540
682PhosphorylationEQANNPFYIKSSPSP
HHHCCCCCCCCCCCC
14.5421945579
684UbiquitinationANNPFYIKSSPSPQK
HCCCCCCCCCCCCHH
33.2432015554
685PhosphorylationNNPFYIKSSPSPQKR
CCCCCCCCCCCCHHC
37.6125159151
685 (in isoform 5)Phosphorylation-37.6118669648
686PhosphorylationNPFYIKSSPSPQKRY
CCCCCCCCCCCHHCC
25.1325159151
686 (in isoform 5)Phosphorylation-25.1318669648
688PhosphorylationFYIKSSPSPQKRYQD
CCCCCCCCCHHCCCC
41.7425159151
688 (in isoform 5)Phosphorylation-41.7418669648
691UbiquitinationKSSPSPQKRYQDTPG
CCCCCCHHCCCCCCC
57.3624816145
693PhosphorylationSPSPQKRYQDTPGVE
CCCCHHCCCCCCCCC
20.1326074081
696PhosphorylationPQKRYQDTPGVEHIP
CHHCCCCCCCCCCCC
13.3525159151
721PhosphorylationKVPGLPMSDQYVKLE
CCCCCCCCHHCHHHH
21.4425850435
724PhosphorylationGLPMSDQYVKLEEER
CCCCCHHCHHHHHHH
12.4472249951
726UbiquitinationPMSDQYVKLEEERRH
CCCHHCHHHHHHHHH
45.2932015554
736AcetylationEERRHRQKLEKDKRR
HHHHHHHHHHHHHHH
59.58129099
739UbiquitinationRHRQKLEKDKRRKKR
HHHHHHHHHHHHHHH
78.1124816145
749UbiquitinationRRKKRKEKEKKGKRR
HHHHHHHHHHHCCCC
77.2724816145
758PhosphorylationKKGKRRHSSLPTESD
HHCCCCCCCCCCCCC
31.5821955146
758 (in isoform 5)Phosphorylation-31.5818669648
759PhosphorylationKGKRRHSSLPTESDE
HCCCCCCCCCCCCCC
32.0421955146
759 (in isoform 5)Phosphorylation-32.0418669648
762PhosphorylationRRHSSLPTESDEDIA
CCCCCCCCCCCCCCC
54.1121955146
762 (in isoform 5)Phosphorylation-54.1118669648
764PhosphorylationHSSLPTESDEDIAPA
CCCCCCCCCCCCCCH
49.1021955146
764 (in isoform 5)Phosphorylation-49.1018669648
778PhosphorylationAQQVDIVTEEMPENA
HHHCEEECCCCCCCC
26.9321955146
785 (in isoform 2)Phosphorylation-21.1323663014
786 (in isoform 2)Phosphorylation-6.6823663014
787 (in isoform 2)Phosphorylation-37.0125159151
788PhosphorylationMPENALPSDEDDKDP
CCCCCCCCCCCCCCC
55.2521955146
788 (in isoform 5)Phosphorylation-55.2518669648
799PhosphorylationDKDPNDPYRALDIDL
CCCCCCHHHHHCCCC
16.0421955146
799 (in isoform 5)Phosphorylation-16.0418669648
801 (in isoform 2)Phosphorylation-12.0729514088
802 (in isoform 2)Phosphorylation-4.3629514088
808UbiquitinationALDIDLDKPLADSEK
HHCCCCCCCCCCCCC
49.5924816145
813PhosphorylationLDKPLADSEKLPIQK
CCCCCCCCCCCCCHH
30.9026074081
820UbiquitinationSEKLPIQKHRNTETS
CCCCCCHHCCCCCCC
45.3029967540
824PhosphorylationPIQKHRNTETSKSPE
CCHHCCCCCCCCCCC
40.3729255136
826PhosphorylationQKHRNTETSKSPEKD
HHCCCCCCCCCCCCC
39.1429255136
827PhosphorylationKHRNTETSKSPEKDV
HCCCCCCCCCCCCCC
25.5529255136
827 (in isoform 5)Phosphorylation-25.5518669648
828 (in isoform 2)Phosphorylation-76.9520201521
829PhosphorylationRNTETSKSPEKDVPM
CCCCCCCCCCCCCCC
37.7529255136
829 (in isoform 5)Phosphorylation-37.7518669648
836SulfoxidationSPEKDVPMVEKKSKK
CCCCCCCCCCCCCCC
6.4621406390
869PhosphorylationKEKEKKKSPKPKKKK
HHHHHHCCCCCCHHH
47.2218669648
876 (in isoform 5)Phosphorylation-58.4826657352
877 (in isoform 5)Phosphorylation-55.7326657352
878 (in isoform 5)Phosphorylation-58.6825849741
892 (in isoform 5)Phosphorylation-65.3926657352
897 (in isoform 5)Phosphorylation-55.1428348404
900 (in isoform 5)Phosphorylation-45.5828348404
931 (in isoform 5)Phosphorylation-3.2420201521
940PhosphorylationMTCDIRGSLQEDSQV
EEEECCCCCCCCCCE
19.6129978859
945PhosphorylationRGSLQEDSQVTVAIV
CCCCCCCCCEEEEEE
26.2929978859
948PhosphorylationLQEDSQVTVAIVLEN
CCCCCCEEEEEEEEC
9.1529978859
957PhosphorylationAIVLENRSSSILKGM
EEEEECCCCHHHCCC
39.7629978859
958PhosphorylationIVLENRSSSILKGME
EEEECCCCHHHCCCC
20.4022210691
959PhosphorylationVLENRSSSILKGMEL
EEECCCCHHHCCCCH
32.9424719451
964SulfoxidationSSSILKGMELSVLDS
CCHHHCCCCHHHHHH
4.4730846556
967PhosphorylationILKGMELSVLDSLNA
HHCCCCHHHHHHHHH
13.8221406692
971PhosphorylationMELSVLDSLNARMAR
CCHHHHHHHHHHHCC
21.2521406692
1020PhosphorylationMAQKLKGTLSFIAKN
HHHHHCCCEEEEEEC
20.0321406692
1022PhosphorylationQKLKGTLSFIAKNDE
HHHCCCEEEEEECCC
17.9124719451
1032PhosphorylationAKNDEGATHEKLDFR
EECCCCCCCCCEEEE
41.2320068231
1064PhosphorylationAFAKLLESGDLSMSS
HHHHHHHHCCCCCCC
37.2621406692
1068PhosphorylationLLESGDLSMSSIKVD
HHHHCCCCCCCEEEC
22.7421406692
1069SulfoxidationLESGDLSMSSIKVDG
HHHCCCCCCCEEECH
4.7821406390
1070PhosphorylationESGDLSMSSIKVDGI
HHCCCCCCCEEECHH
26.0721406692
1071PhosphorylationSGDLSMSSIKVDGIR
HCCCCCCCEEECHHH
20.1421406692
1132UbiquitinationNSVSVDGKCSDSTLL
CCEEECCCCCHHHHH
26.5429967540
1133GlutathionylationSVSVDGKCSDSTLLS
CEEECCCCCHHHHHH
7.1722555962
1137PhosphorylationDGKCSDSTLLSNLLE
CCCCCHHHHHHHHHH
36.3925338102
1194Ubiquitination------------------------------------------------
------------------------------------------------
29967540

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 AP3D1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP3D1_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 AP3D1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HTSF1_HUMANHTATSF1physical
22939629
CD11B_HUMANCDK11Bphysical
22939629
AP3B2_HUMANAP3B2physical
23144738
AP3S1_HUMANAP3S1physical
23144738
AP3M1_HUMANAP3M1physical
23144738
RUFY1_HUMANRUFY1physical
23144738
AP3S1_HUMANAP3S1physical
26344197
CDC73_HUMANCDC73physical
26344197
COPG1_HUMANCOPG1physical
26344197
RBM25_HUMANRBM25physical
26344197
VP33A_HUMANVPS33Aphysical
21411634
VP33B_HUMANVPS33Bphysical
21411634
CLH1_HUMANCLTCphysical
21411634
VPS11_MOUSEVps11physical
21411634
VPS18_MOUSEVps18physical
21411634
VPS39_HUMANVPS39physical
21411634
VPS41_HUMANVPS41physical
21411634

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 AP3D1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721, AND MASSSPECTROMETRY.
"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-632; SER-634; SER-636;SER-686; SER-688; SER-758; SER-759; THR-762; SER-764 AND SER-788, ANDMASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, 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 SER-632; SER-634; SER-636AND SER-658, AND MASS SPECTROMETRY.

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