AP3B1_HUMAN - dbPTM
AP3B1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP3B1_HUMAN
UniProt AC O00203
Protein Name AP-3 complex subunit beta-1
Gene Name AP3B1
Organism Homo sapiens (Human).
Sequence Length 1094
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 MSSNSFPYNEQSGGGEATELGQEATSTISPSGAFGLFSSDLKKNEDLKQMLESNKDSAKLDAMKRIVGMIAKGKNASELFPAVVKNVASKNIEIKKLVYVYLVRYAEEQQDLALLSISTFQRALKDPNQLIRASALRVLSSIRVPIIVPIMMLAIKEASADLSPYVRKNAAHAIQKLYSLDPEQKEMLIEVIEKLLKDKSTLVAGSVVMAFEEVCPDRIDLIHKNYRKLCNLLVDVEEWGQVVIIHMLTRYARTQFVSPWKEGDELEDNGKNFYESDDDQKEKTDKKKKPYTMDPDHRLLIRNTKPLLQSRNAAVVMAVAQLYWHISPKSEAGIISKSLVRLLRSNREVQYIVLQNIATMSIQRKGMFEPYLKSFYVRSTDPTMIKTLKLEILTNLANEANISTLLREFQTYVKSQDKQFAAATIQTIGRCATNILEVTDTCLNGLVCLLSNRDEIVVAESVVVIKKLLQMQPAQHGEIIKHMAKLLDSITVPVARASILWLIGENCERVPKIAPDVLRKMAKSFTSEDDLVKLQILNLGAKLYLTNSKQTKLLTQYILNLGKYDQNYDIRDRTRFIRQLIVPNVKSGALSKYAKKIFLAQKPAPLLESPFKDRDHFQLGTLSHTLNIKATGYLELSNWPEVAPDPSVRNVEVIELAKEWTPAGKAKQENSAKKFYSESEEEEDSSDSSSDSESESGSESGEQGESGEEGDSNEDSSEDSSSEQDSESGRESGLENKRTAKRNSKAKGKSDSEDGEKENEKSKTSDSSNDESSSIEDSSSDSESESEPESESESRRVTKEKEKKTKQDRTPLTKDVSLLDLDDFNPVSTPVALPTPALSPSLMADLEGLHLSTSSSVISVSTPAFVPTKTHVLLHRMSGKGLAAHYFFPRQPCIFGDKMVSIQITLNNTTDRKIENIHIGEKKLPIGMKMHVFNPIDSLEPEGSITVSMGIDFCDSTQTASFQLCTKDDCFNVNIQPPVGELLLPVAMSEKDFKKEQGVLTGMNETSAVIIAAPQNFTPSVIFQKVVNVANVGAVPSGQDNIHRFAAKTVHSGSLMLVTVELKEGSTAQLIINTEKTVIGSVLLRELKPVLSQG
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
2Phosphorylation------MSSNSFPYN
------CCCCCCCCC		49.9122210691
8PhosphorylationMSSNSFPYNEQSGGG
CCCCCCCCCCCCCCC		29.3522210691
25PhosphorylationTELGQEATSTISPSG
CHHHHHHCCCCCCCH		26.1726074081
26PhosphorylationELGQEATSTISPSGA
HHHHHHCCCCCCCHH		30.6926074081
27PhosphorylationLGQEATSTISPSGAF
HHHHHCCCCCCCHHH		22.5626074081
29PhosphorylationQEATSTISPSGAFGL
HHHCCCCCCCHHHHH		17.0725159151
31PhosphorylationATSTISPSGAFGLFS
HCCCCCCCHHHHHCC		35.6426074081
38PhosphorylationSGAFGLFSSDLKKNE
CHHHHHCCCCCCCCH		28.1626074081
39PhosphorylationGAFGLFSSDLKKNED
HHHHHCCCCCCCCHH		39.3626074081
53PhosphorylationDLKQMLESNKDSAKL
HHHHHHHHCHHHHHH		45.2623403867
57PhosphorylationMLESNKDSAKLDAMK
HHHHCHHHHHHHHHH		28.9830243723
74MalonylationVGMIAKGKNASELFP
HHHHHCCCCHHHHHH		48.9426320211
76UbiquitinationMIAKGKNASELFPAV
HHHCCCCHHHHHHHH		14.10-
77PhosphorylationIAKGKNASELFPAVV
HHCCCCHHHHHHHHH		44.2028857561
89PhosphorylationAVVKNVASKNIEIKK
HHHHHHHCCCCCHHH		23.1950565793
90UbiquitinationVVKNVASKNIEIKKL
HHHHHHCCCCCHHHH		52.81-
90MalonylationVVKNVASKNIEIKKL
HHHHHHCCCCCHHHH		52.8126320211
99PhosphorylationIEIKKLVYVYLVRYA
CCHHHHHHHHHHHHC		8.2025332170
101PhosphorylationIKKLVYVYLVRYAEE
HHHHHHHHHHHHCHH		5.0425332170
105PhosphorylationVYVYLVRYAEEQQDL
HHHHHHHHCHHHHHH		15.7525332170
119UbiquitinationLALLSISTFQRALKD
HHHHHHHHHHHHCCC		23.32-
125UbiquitinationSTFQRALKDPNQLIR
HHHHHHCCCHHHHHH		70.88-
140PhosphorylationASALRVLSSIRVPII
HHHHHHHHCCCCCCH		22.3630301811
141PhosphorylationSALRVLSSIRVPIIV
HHHHHHHCCCCCCHH		15.3925954137
163PhosphorylationKEASADLSPYVRKNA
HHHCCCCCHHHHHHH		18.0928152594
165PhosphorylationASADLSPYVRKNAAH
HCCCCCHHHHHHHHH		14.9828152594
168UbiquitinationDLSPYVRKNAAHAIQ
CCCHHHHHHHHHHHH		40.6821906983
168 (in isoform 1)Ubiquitination-40.6821890473
176UbiquitinationNAAHAIQKLYSLDPE
HHHHHHHHHHCCCHH		43.19-
187SulfoxidationLDPEQKEMLIEVIEK
CCHHHHHHHHHHHHH		6.1830846556
200PhosphorylationEKLLKDKSTLVAGSV
HHHHCCCCCCCCHHH		36.7927732954
201PhosphorylationKLLKDKSTLVAGSVV
HHHCCCCCCCCHHHH		30.8722210691
206PhosphorylationKSTLVAGSVVMAFEE
CCCCCCHHHHHHHHH		11.2027732954
254PhosphorylationMLTRYARTQFVSPWK
HHHHHHHHCCCCCCC		20.4223312004
258PhosphorylationYARTQFVSPWKEGDE
HHHHCCCCCCCCCCC		26.7423312004
274PhosphorylationEDNGKNFYESDDDQK
CCCCCCCCCCCCCHH		24.7430278072
276PhosphorylationNGKNFYESDDDQKEK
CCCCCCCCCCCHHHC		34.6529255136
284PhosphorylationDDDQKEKTDKKKKPY
CCCHHHCCCCCCCCC		54.8923403867
292PhosphorylationDKKKKPYTMDPDHRL
CCCCCCCCCCCCCCC		24.5146165045
293SulfoxidationKKKKPYTMDPDHRLL
CCCCCCCCCCCCCCE		6.0930846556
305MalonylationRLLIRNTKPLLQSRN
CCEECCCHHHHHCHH		36.9026320211
336PhosphorylationKSEAGIISKSLVRLL
CCCCCHHCHHHHHHH		17.8024719451
337MalonylationSEAGIISKSLVRLLR
CCCCHHCHHHHHHHH		37.0826320211
379PhosphorylationLKSFYVRSTDPTMIK
HHHEEECCCCHHHHH		27.4122210691
380PhosphorylationKSFYVRSTDPTMIKT
HHEEECCCCHHHHHH		35.1222210691
383PhosphorylationYVRSTDPTMIKTLKL
EECCCCHHHHHHHHH		34.0522210691
414UbiquitinationREFQTYVKSQDKQFA
HHHHHHHHHCCHHHH		31.80-
414MalonylationREFQTYVKSQDKQFA
HHHHHHHHHCCHHHH		31.8026320211
414AcetylationREFQTYVKSQDKQFA
HHHHHHHHHCCHHHH		31.8025953088
463UbiquitinationIVVAESVVVIKKLLQ
EEEEEHHHHHHHHHC		5.26-
467UbiquitinationESVVVIKKLLQMQPA
EHHHHHHHHHCCCHH		43.22-
474UbiquitinationKLLQMQPAQHGEIIK
HHHCCCHHHHHHHHH		9.34-
503UbiquitinationRASILWLIGENCERV
HHHHHHHHCCCCCCC		4.38-
512UbiquitinationENCERVPKIAPDVLR
CCCCCCCCCCHHHHH		48.9521890473
512MalonylationENCERVPKIAPDVLR
CCCCCCCCCCHHHHH		48.9526320211
512 (in isoform 1)Ubiquitination-48.9521890473
519MethylationKIAPDVLRKMAKSFT
CCCHHHHHHHHHHCC		26.93-
523UbiquitinationDVLRKMAKSFTSEDD
HHHHHHHHHCCCHHH		42.4721890473
523 (in isoform 1)Ubiquitination-42.4721890473
524PhosphorylationVLRKMAKSFTSEDDL
HHHHHHHHCCCHHHH		24.9923186163
526PhosphorylationRKMAKSFTSEDDLVK
HHHHHHCCCHHHHHH		37.9923186163
527PhosphorylationKMAKSFTSEDDLVKL
HHHHHCCCHHHHHHH		36.7022985185
533UbiquitinationTSEDDLVKLQILNLG
CCHHHHHHHHHHHHC		41.81-
547UbiquitinationGAKLYLTNSKQTKLL
CCEEEECCHHHHHHH		44.61-
549UbiquitinationKLYLTNSKQTKLLTQ
EEEECCHHHHHHHHH		65.15-
552UbiquitinationLTNSKQTKLLTQYIL
ECCHHHHHHHHHHHH		38.7221890473
552AcetylationLTNSKQTKLLTQYIL
ECCHHHHHHHHHHHH		38.7225953088
552 (in isoform 1)Ubiquitination-38.7221890473
553UbiquitinationTNSKQTKLLTQYILN
CCHHHHHHHHHHHHH		7.70-
555PhosphorylationSKQTKLLTQYILNLG
HHHHHHHHHHHHHHC		29.7524719451
557PhosphorylationQTKLLTQYILNLGKY
HHHHHHHHHHHHCCC		11.3524719451
563AcetylationQYILNLGKYDQNYDI
HHHHHHCCCCCCCCC		49.1466724541
564PhosphorylationYILNLGKYDQNYDIR
HHHHHCCCCCCCCCH		22.4428270605
568PhosphorylationLGKYDQNYDIRDRTR
HCCCCCCCCCHHHHH		13.7128270605
592AcetylationVKSGALSKYAKKIFL
CCCCHHHHHHHHHHH		50.5119608861
592UbiquitinationVKSGALSKYAKKIFL
CCCCHHHHHHHHHHH		50.5119608861
592MalonylationVKSGALSKYAKKIFL
CCCCHHHHHHHHHHH		50.5126320211
596UbiquitinationALSKYAKKIFLAQKP
HHHHHHHHHHHHCCC		30.4421890473
596MalonylationALSKYAKKIFLAQKP
HHHHHHHHHHHHCCC		30.4426320211
596 (in isoform 1)Ubiquitination-30.4421890473
602UbiquitinationKKIFLAQKPAPLLES
HHHHHHCCCCCCCCC		37.2221890473
602 (in isoform 1)Ubiquitination-37.2221890473
609PhosphorylationKPAPLLESPFKDRDH
CCCCCCCCCCCCCCC		35.2919664994
609UbiquitinationKPAPLLESPFKDRDH
CCCCCCCCCCCCCCC		35.29-
621PhosphorylationRDHFQLGTLSHTLNI
CCCCCHHCEECCCEE		33.4168727759
623PhosphorylationHFQLGTLSHTLNIKA
CCCHHCEECCCEEEE		17.7928857561
625PhosphorylationQLGTLSHTLNIKATG
CHHCEECCCEEEECE		20.3728857561
647PhosphorylationPEVAPDPSVRNVEVI
CCCCCCCCCCCEEHH		40.88113299245
658UbiquitinationVEVIELAKEWTPAGK
EEHHHHHHHCCCCCH		67.4221890473
658 (in isoform 1)Ubiquitination-67.4221890473
661PhosphorylationIELAKEWTPAGKAKQ
HHHHHHCCCCCHHCC		12.3521712546
665UbiquitinationKEWTPAGKAKQENSA
HHCCCCCHHCCCCCH		55.29-
671O-linked_GlycosylationGKAKQENSAKKFYSE
CHHCCCCCHHHCCCC		40.4930379171
750PhosphorylationNSKAKGKSDSEDGEK
HHHCCCCCCCCCCCH		55.8527794612
752PhosphorylationKAKGKSDSEDGEKEN
HCCCCCCCCCCCHHC		44.6827794612
765PhosphorylationENEKSKTSDSSNDES
HCHHCCCCCCCCCCC		38.9530576142
767PhosphorylationEKSKTSDSSNDESSS
HHCCCCCCCCCCCCC		30.7022468782
768PhosphorylationKSKTSDSSNDESSSI
HCCCCCCCCCCCCCC		53.9830576142
773PhosphorylationDSSNDESSSIEDSSS
CCCCCCCCCCCCCCC		33.0330576142
778PhosphorylationESSSIEDSSSDSESE
CCCCCCCCCCCCCCC		20.9630576142
779PhosphorylationSSSIEDSSSDSESES
CCCCCCCCCCCCCCC		50.9530576142
782PhosphorylationIEDSSSDSESESEPE
CCCCCCCCCCCCCCC		44.9930576142
810PhosphorylationKKTKQDRTPLTKDVS
HCCCCCCCCCCCCCC		30.8228985074
813PhosphorylationKQDRTPLTKDVSLLD
CCCCCCCCCCCCCCC		26.8029396449
817PhosphorylationTPLTKDVSLLDLDDF
CCCCCCCCCCCCCCC		33.0926074081
839PhosphorylationALPTPALSPSLMADL
CCCCCCCCHHHHHHC		17.9726074081
841PhosphorylationPTPALSPSLMADLEG
CCCCCCHHHHHHCCC		27.6626074081
862PhosphorylationSSVISVSTPAFVPTK
CCEEEECCCCCCCCC		19.2430804307
905PhosphorylationKMVSIQITLNNTTDR
EEEEEEEEECCCCCC		13.6820860994
909PhosphorylationIQITLNNTTDRKIEN
EEEEECCCCCCCEEE		29.0620860994
9222-HydroxyisobutyrylationENIHIGEKKLPIGMK
EEEEECCCCCCCCCE		55.16-
1077PhosphorylationLIINTEKTVIGSVLL
EEECCCCHHHHHHHH		15.8946165039
1081PhosphorylationTEKTVIGSVLLRELK
CCCHHHHHHHHHHHH		9.8551460367
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP3B1_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 AP3B1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARF5_HUMANARF5physical
11926829
ARF6_HUMANARF6physical
11926829
AP3D1_HUMANAP3D1physical
22939629
AP3S1_HUMANAP3S1physical
22939629
AP3D1_HUMANAP3D1physical
22863883
AP3M1_HUMANAP3M1physical
22863883
AP3S1_HUMANAP3S1physical
22863883
COG3_HUMANCOG3physical
22863883
LRSM1_HUMANLRSAM1physical
25380047
AP3D1_HUMANAP3D1physical
26344197
AP3S1_HUMANAP3S1physical
26344197
CDC73_HUMANCDC73physical
26344197
JMJD6_HUMANJMJD6physical
26344197
PELP1_HUMANPELP1physical
26344197
EAF1_HUMANEAF1physical
27173435
DDX20_HUMANDDX20physical
27173435
DPOD1_HUMANPOLD1physical
27173435
MFAP1_HUMANMFAP1physical
27173435
NAF1_HUMANNAF1physical
27173435
ATRX_HUMANATRXphysical
27173435
RBM14_HUMANRBM14physical
27173435
CC154_HUMANCCDC154physical
27173435
MCM3_HUMANMCM3physical
27173435
PR38A_HUMANPRPF38Aphysical
27173435
Drug and Disease Associations
Kegg Disease
H00166 Hermansky-Pudlak syndrome (HPS)
OMIM Disease
608233Hermansky-Pudlak syndrome 2 (HPS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP3B1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-592, AND MASS SPECTROMETRY.
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-276, 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-276; SER-609 ANDTHR-661, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND MASSSPECTROMETRY.
"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-276, 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-276 AND SER-609, ANDMASS SPECTROMETRY.

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