AP3B1_MOUSE - dbPTM
AP3B1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP3B1_MOUSE
UniProt AC Q9Z1T1
Protein Name AP-3 complex subunit beta-1
Gene Name Ap3b1
Organism Mus musculus (Mouse).
Sequence Length 1105
Subcellular Localization Cytoplasmic vesicle, clathrin-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Golgi apparatus. Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex..
Protein Description Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. 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..
Protein Sequence MSSNSFAYNEQSGGGEAAELGQEATSTISPSGAFGLFSSDWKKNEDLKQMLESNKDSAKLDAMKRIVGMIAKGKNASELFPAVVKNVASKNIEIKKLVYVYLVRYAEEQQDLALLSISTFQRALKDPNQLIRASALRVLSSIRVPIIVPVMMLAIKEASADLSPYVRKNAAHAIQKLYSLDPEQKEMLIEVIEKLLKDKSTLVAGSVVMAFEEVCPDRIDLIHRNYRKLCNLLVDVEEWGQVVIIHMLTRYARTQFVSPWREDGGLEDNEKNFYESEEEEEEKEKSSRKKSYAMDPDHRLLIRNTKPLLQSRNAAVVMAVAQLYWHISPKSEAGVISKSLVRLLRSNREVQYIVLQNIATMSIERKGMFEPYLKSFYVRSTDPTMIKTLKLEILTNLANEANISTLLREFQTYVRSQDKQFAAATIQTIGRCATSISEVTDTCLNGLVCLLSNRDEIVVAESVVVIKKLLQMQPAQHGEIIRHMAKLLDSITVPVARASILWLIGENCERVPKIAPDVLRKMAKSFTSEDDLVKLQILNLAAKLYLTNSKQTKLLTQYILNLGKYDQNYDIRDRTRFIRQLIVPNEKSGALSKYAKKIFLAPKPAPLLESPFKDRDRFQLGTLSHTLNIKASGYLELSNWPEVAPDPSVRNVEVIESAKEWTPLGKTKKEKPMKKFYSESEEEEDEDEDEDEEEEEKEDEDENPSDSSSDSESGSGSESGDTGTEDSSEDSSSGQDSETGSQAEAERQKVAKRNSKTKRKSDSENREKKNENSKASESSSEESSSMEDSSSESESESGSDSEPAPRNVAPAKERKPQQERHPPSKDVFLLDLDDFNPVSTPVALPTPALSPSLIADLEGLNLSTSSSVINVSTPVFVPTKTHELLHRMHGKGLAAHYCFPRQPCIFSDKMVSVQITLTNTSDRKIENIHIGGKGLPVGMQMHAFHPIDSLEPKGSVTVSVGIDFCDSTQTASFQLCTKDDCFNVTLQPPVGELLSPVAMSEKDFKKEQGTLTGMNETSATLIAAPQNFTPSMILQKVVNVANLGAVPSSQDNVHRFAARTVHSGSLMLVTVELKEGSTAQLIINTEKTVIGSVLLRELKPVLSQG
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
48SuccinylationWKKNEDLKQMLESNK
CCCCHHHHHHHHHCH		46.0826388266
74AcetylationVGMIAKGKNASELFP
HHHHHCCCCHHHHHH		48.9422902405
125AcetylationSTFQRALKDPNQLIR
HHHHHHCCCHHHHHH		70.8823806337
140PhosphorylationASALRVLSSIRVPII
HHHHHHHHCCCCCCH		22.3625159016
141PhosphorylationSALRVLSSIRVPIIV
HHHHHHHCCCCCCHH		15.3925159016
274PhosphorylationEDNEKNFYESEEEEE
CCCCCCCCCCHHHHH		28.1225521595
276PhosphorylationNEKNFYESEEEEEEK
CCCCCCCCHHHHHHH		38.6424925903
291PhosphorylationEKSSRKKSYAMDPDH
HHHHHHHHHCCCCCH		22.5925266776
292PhosphorylationKSSRKKSYAMDPDHR
HHHHHHHHCCCCCHH		18.1529472430
338MalonylationSEAGVISKSLVRLLR
CHHCHHCHHHHHHHH		36.3626320211
395PhosphorylationTLKLEILTNLANEAN
HHHHHHHHHHHHHCC		33.5728494245
404PhosphorylationLANEANISTLLREFQ
HHHHCCHHHHHHHHH		16.8928494245
405PhosphorylationANEANISTLLREFQT
HHHCCHHHHHHHHHH		26.4728494245
513UbiquitinationENCERVPKIAPDVLR
CCCCCCCCCCHHHHH		48.9522790023
550UbiquitinationKLYLTNSKQTKLLTQ
HHHHCCCHHHHHHHH		65.1522790023
587UbiquitinationQLIVPNEKSGALSKY
HHHCCCCCCCCHHHH		61.9122790023
588PhosphorylationLIVPNEKSGALSKYA
HHCCCCCCCCHHHHH		24.1023737553
592PhosphorylationNEKSGALSKYAKKIF
CCCCCCHHHHHHHHH		24.0823737553
593MalonylationEKSGALSKYAKKIFL
CCCCCHHHHHHHHHC		50.5126320211
603UbiquitinationKKIFLAPKPAPLLES
HHHHCCCCCCCCCCC		48.4822790023
610PhosphorylationKPAPLLESPFKDRDR
CCCCCCCCCCCCCCC		35.2926824392
657PhosphorylationRNVEVIESAKEWTPL
CCEEEHHHCCCCCCC		33.2526525534
662PhosphorylationIESAKEWTPLGKTKK
HHHCCCCCCCCCCCC		15.1027180971
677PhosphorylationEKPMKKFYSESEEEE
CCCCHHHCCCCCCCC		22.0223737553
678PhosphorylationKPMKKFYSESEEEED
CCCHHHCCCCCCCCC		37.4725521595
680PhosphorylationMKKFYSESEEEEDED
CHHHCCCCCCCCCCC		44.3525521595
761PhosphorylationNSKTKRKSDSENREK
HHHCCCCCHHHHHHH		50.8630352176
763PhosphorylationKTKRKSDSENREKKN
HCCCCCHHHHHHHHH		43.8123375375
912PhosphorylationIFSDKMVSVQITLTN
ECCCCEEEEEEEEEC		12.5726160508
916PhosphorylationKMVSVQITLTNTSDR
CEEEEEEEEECCCCC		15.5026160508
918PhosphorylationVSVQITLTNTSDRKI
EEEEEEEECCCCCEE		28.0026160508
920PhosphorylationVQITLTNTSDRKIEN
EEEEEECCCCCEEEE		27.1126160508
921PhosphorylationQITLTNTSDRKIENI
EEEEECCCCCEEEEE		37.1726160508
1010PhosphorylationDFKKEQGTLTGMNET
HHHHHHCCCCCCCCC		22.3551460357
1092PhosphorylationTEKTVIGSVLLRELK
CCCHHHHHHHHHHHH		9.8551460365
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 AP3B1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP3B1_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 AP3B1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AP3B1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP3B1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-276, AND MASSSPECTROMETRY.
"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-276, AND MASSSPECTROMETRY.
"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-276, AND MASSSPECTROMETRY.

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