AP3D1_MOUSE - dbPTM
AP3D1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP3D1_MOUSE
UniProt AC O54774
Protein Name AP-3 complex subunit delta-1
Gene Name Ap3d1
Organism Mus musculus (Mouse).
Sequence Length 1199
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 (By similarity). Involved in process of CD8+ T-cell and NK cell degranulation (By similarity). 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. [PubMed: 21998198]
Protein Sequence MALKMVKGSIDRMFDKNLQDLVRGIRNHKEDEAKYISQCIDEIKQELKQDNIAVKANAVCKLTYLQMLGYDISWAAFNIIEVMSASKFTFKRVGYLAASQCFHEGTDVIMLTTNQIRKDLSSPSQYDTGVALTGLSCFVTPDLARDLANDIMTLMSHTKPYIRKKAVLIMYKVFLKYPESLRPAFPRLKEKLEDPDPGVQSAAVNVICELARRNPKNYLSLAPLFFKLMTSSTNNWVLIKIIKLFGALTPLEPRLGKKLIEPLTNLIHSTSAMSLLYECVNTVIAVLISLSSGMPNHSASIQLCVQKLRILIEDSDQNLKYLGLLAMSKILKTHPKSVQSHKDLILQCLDDKDESIRLRALDLLYGMVSKKNLMEIVKKLMTHVDKAEGTTYRDELLTKIIDICSQSNYQHITNFEWYISILVELTRLEGTRHGHLIAAQMLDVAIRVKAIRKFAVSQMSSLLDSAHLVASSTQRNGICEVLYAAAWICGEFSEHLQGPQQTLEAMLRPKVTTLPGHIQAVYVQNVVKLYASILQQKEQAADTEAAQEVTQLLVERLPQFVQSADLEVQERASCILQLVKHVQKLQAKGVPVAEEVSALFAGELNPVAPKAQKKVPVPEGLDLDAWINEPPSDSESEDEKPKAIFHEEEPRHTRRRQPEEDEEELARRREARKQEQANNPFYIKSSPSPQKRYQDAPGVEHIPVVQIDLSVPLKVPGMPMSDQYVKLEEQRRHRQRLEKDKKRKKKEKGKRRHSSLPTESDEDIAPAQRVDIITEEMPENALPSDEDDKDPNDPYRALDIDLDKPLADSEKLPVQKHRNAEAVKSPEKEGVLGVEKKSKKPKKKEKKTKEREREKKDKKGEDLDFWLSTTPPPAAAPIPAPSTEELAASTITSPKDECEVLKGEEEDHVDHDQERKSSRHKKKKHRKEKEKEERPRDKKKAKKKQVAPLENGAAAEEEEEPIPPMSSYCLLAESPYIKVTYDIQASLQKDSQVTVSIILENQSSSFLKNMELNVLDSLNTKMTRPEGSSVHDGVPVPFQLPPGVSNEAQFVFTIQSIVMAQKLKGTLSFIAKDDEGATHEKLDFRLHFSCSSYLITTPCYSDAFAKLLESGDLSMNSIKVDGISMSFQNLLAKICFYHHFSVVERVDSCASMYSRSIQGHHVCLLVKKGESSVSVDGKCSDATLLSSLLEEMKTTLAQC
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		27.48-
9PhosphorylationALKMVKGSIDRMFDK
CHHHHCHHHHHHHHH		18.6522324799
34UbiquitinationNHKEDEAKYISQCID
CCCHHHHHHHHHHHH		40.8622790023
48UbiquitinationDEIKQELKQDNIAVK
HHHHHHHHHCCHHHH		55.6527667366
220PhosphorylationRNPKNYLSLAPLFFK
HCCCCHHHHHHHHHH		16.4829899451
321PhosphorylationDSDQNLKYLGLLAMS
CCCCHHHHHHHHHHH		14.7923882026
352UbiquitinationILQCLDDKDESIRLR
HHHHCCCCCHHHHHH		64.1622790023
369PhosphorylationDLLYGMVSKKNLMEI
HHHHHHCCHHHHHHH		29.0828576409
390PhosphorylationHVDKAEGTTYRDELL
HHHHHCCCCHHHHHH		16.5021454597
610UbiquitinationELNPVAPKAQKKVPV
CCCCCCCHHCCCCCC		54.4322790023
613UbiquitinationPVAPKAQKKVPVPEG
CCCCHHCCCCCCCCC		61.67-
632PhosphorylationAWINEPPSDSESEDE
HHCCCCCCCCCCCCC		65.5721930439
634PhosphorylationINEPPSDSESEDEKP
CCCCCCCCCCCCCCC		47.5721930439
636PhosphorylationEPPSDSESEDEKPKA
CCCCCCCCCCCCCCC		55.0621082442
682PhosphorylationEQANNPFYIKSSPSP
HHHCCCCCCCCCCCC		14.5418779572
685PhosphorylationNNPFYIKSSPSPQKR
CCCCCCCCCCCCCCC		37.6126745281
686PhosphorylationNPFYIKSSPSPQKRY
CCCCCCCCCCCCCCC		25.1326745281
688PhosphorylationFYIKSSPSPQKRYQD
CCCCCCCCCCCCCCC		41.7426824392
724PhosphorylationGMPMSDQYVKLEEQR
CCCCCHHHHHHHHHH		12.4429514104
754PhosphorylationEKGKRRHSSLPTESD
HHCCCCCCCCCCCCC		31.5824925903
755PhosphorylationKGKRRHSSLPTESDE
HCCCCCCCCCCCCCC		32.0427087446
758PhosphorylationRRHSSLPTESDEDIA
CCCCCCCCCCCCCCC		54.1124925903
760PhosphorylationHSSLPTESDEDIAPA
CCCCCCCCCCCCCHH		49.1024925903
774PhosphorylationAQRVDIITEEMPENA
HHHHEEECCCCCCCC		26.6525619855
784PhosphorylationMPENALPSDEDDKDP
CCCCCCCCCCCCCCC		55.2524925903
795PhosphorylationDKDPNDPYRALDIDL
CCCCCCHHHHHCCCC		16.0424925903
825PhosphorylationRNAEAVKSPEKEGVL
CCCHHHCCHHHCCCC		31.5225521595
838PhosphorylationVLGVEKKSKKPKKKE
CCCCCCCCCCCCCHH		57.91-
868PhosphorylationEDLDFWLSTTPPPAA
CCCCCCCCCCCCCCC		22.3426239621
869PhosphorylationDLDFWLSTTPPPAAA
CCCCCCCCCCCCCCC		40.9426239621
870PhosphorylationLDFWLSTTPPPAAAP
CCCCCCCCCCCCCCC		30.3526824392
882PhosphorylationAAPIPAPSTEELAAS
CCCCCCCCHHHHHHH		51.0226643407
883PhosphorylationAPIPAPSTEELAAST
CCCCCCCHHHHHHHC		32.2126643407
889PhosphorylationSTEELAASTITSPKD
CHHHHHHHCCCCCHH		18.0926643407
890PhosphorylationTEELAASTITSPKDE
HHHHHHHCCCCCHHH		24.4526643407
892PhosphorylationELAASTITSPKDECE
HHHHHCCCCCHHHHE		38.7826643407
893PhosphorylationLAASTITSPKDECEV
HHHHCCCCCHHHHEE		26.5423649490
1066PhosphorylationMAQKLKGTLSFIAKD
HHHHHCCEEEEEEEC		20.0322871156
1068PhosphorylationQKLKGTLSFIAKDDE
HHHCCEEEEEEECCC		17.9122871156
1114PhosphorylationLLESGDLSMNSIKVD
HHHHCCCCCCEEEEC		22.21-
1117PhosphorylationSGDLSMNSIKVDGIS
HCCCCCCEEEECCCC		18.36-
1195PhosphorylationLLEEMKTTLAQC---
HHHHHHHHHHCC---		17.9918779572
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP3D1_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AP3D1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP3D1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-758 AND SER-760, ANDMASS SPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632; SER-634; SER-636;SER-760 AND SER-784, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754; THR-758; SER-760AND SER-784, AND MASS SPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-760, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755; THR-758; SER-760AND SER-784, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-760 AND SER-784, ANDMASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-760 AND SER-825, ANDMASS SPECTROMETRY.

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