AP3B2_HUMAN - dbPTM
AP3B2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP3B2_HUMAN
UniProt AC Q13367
Protein Name AP-3 complex subunit beta-2
Gene Name AP3B2
Organism Homo sapiens (Human).
Sequence Length 1082
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 MSAAPAYSEDKGGSAGPGEPEYGHDPASGGIFSSDYKRHDDLKEMLDTNKDSLKLEAMKRIVAMIARGKNASDLFPAVVKNVACKNIEVKKLVYVYLVRYAEEQQDLALLSISTFQRGLKDPNQLIRASALRVLSSIRVPIIVPIMMLAIKEAASDMSPYVRKTAAHAIPKLYSLDSDQKDQLIEVIEKLLADKTTLVAGSVVMAFEEVCPERIDLIHKNYRKLCNLLIDVEEWGQVVIISMLTRYARTQFLSPTQNESLLEENAEKAFYGSEEDEAKGAGSEETAAAAAPSRKPYVMDPDHRLLLRNTKPLLQSRSAAVVMAVAQLYFHLAPKAEVGVIAKALVRLLRSHSEVQYVVLQNVATMSIKRRGMFEPYLKSFYIRSTDPTQIKILKLEVLTNLANETNIPTVLREFQTYIRSMDKDFVAATIQAIGRCATNIGRVRDTCLNGLVQLLSNRDELVVAESVVVIKKLLQMQPAQHGEIIKHLAKLTDNIQVPMARASILWLIGEYCEHVPRIAPDVLRKMAKSFTAEEDIVKLQVINLAAKLYLTNSKQTKLLTQYVLSLAKYDQNYDIRDRARFTRQLIVPSEQGGALSRHAKKLFLAPKPAPVLESSFKDRDHFQLGSLSHLLNAKATGYQELPDWPEEAPDPSVRNVEVPEWTKCSNREKRKEKEKPFYSDSEGESGPTESADSDPESESESDSKSSSESGSGESSSESDNEDQDEDEEKGRGSESEQSEEDGKRKTKKKVPERKGEASSSDEGSDSSSSSSESEMTSESEEEQLEPASWSRKTPPSSKSAPATKEISLLDLEDFTPPSVQPVSPPAIVSTSLAADLEGLTLTDSTLVPSLLSPVSGVGRQELLHRVAGEGLAVDYTFSRQPFSGDPHMVSVHIHFSNSSDTPIKGLHVGTPKLPAGISIQEFPEIESLAPGESATAVMGINFCDSTQAANFQLCTQTRQFYVSIQPPVGELMAPVFMSENEFKKEQGKLMGMNEITEKLMLPDTCRSDHIVVQKVTATANLGRVPCGTSDEYRFAGRTLTGGSLVLLTLDARPAGAAQLTVNSEKMVIGTMLVKDVIQALTQ
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
54AcetylationDTNKDSLKLEAMKRI
HCCHHHHHHHHHHHH		48.5125953088
94PhosphorylationIEVKKLVYVYLVRYA
CCHHHHHEEHHHHHC		8.2025332170
96PhosphorylationVKKLVYVYLVRYAEE
HHHHHEEHHHHHCHH		5.0425332170
100PhosphorylationVYVYLVRYAEEQQDL
HEEHHHHHCHHHHHH		15.7525332170
135PhosphorylationASALRVLSSIRVPII
HHHHHHHHCCCCCCH		22.3630301811
136PhosphorylationSALRVLSSIRVPIIV
HHHHHHHCCCCCCHH		15.3925954137
158PhosphorylationKEAASDMSPYVRKTA
HHHHHCCCHHHHHHH		20.3330576142
160PhosphorylationAASDMSPYVRKTAAH
HHHCCCHHHHHHHHH		12.9430576142
164PhosphorylationMSPYVRKTAAHAIPK
CCHHHHHHHHHHCCH		20.6530576142
255PhosphorylationRTQFLSPTQNESLLE
HHHCCCCCCCHHHHH		40.4227732954
259PhosphorylationLSPTQNESLLEENAE
CCCCCCHHHHHHHHH		45.8927732954
270PhosphorylationENAEKAFYGSEEDEA
HHHHHHHCCCHHHHH		25.3019690332
272PhosphorylationAEKAFYGSEEDEAKG
HHHHHCCCHHHHHCC		26.8328787133
282PhosphorylationDEAKGAGSEETAAAA
HHHCCCCCHHHHHHH		31.5522617229
285PhosphorylationKGAGSEETAAAAAPS
CCCCCHHHHHHHCCC		19.9724114839
292PhosphorylationTAAAAAPSRKPYVMD
HHHHHCCCCCCCCCC		48.4828111955
366PhosphorylationLQNVATMSIKRRGMF
EECEEEECHHHCCCC		22.1724719451
376PhosphorylationRRGMFEPYLKSFYIR
HCCCCHHHHHHEEEC		21.4022210691
420PhosphorylationEFQTYIRSMDKDFVA
HHHHHHHHCCHHHHH		23.0646165063
438PhosphorylationQAIGRCATNIGRVRD
HHHHHHHHHHHHHHH		30.8722210691
456PhosphorylationNGLVQLLSNRDELVV
HHHHHHHCCCCCEEH		38.1150565809
472UbiquitinationESVVVIKKLLQMQPA
EHHHHHHHHHCCCHH		43.22-
524MethylationRIAPDVLRKMAKSFT
CCCHHHHHHHHHHCC		26.93-
554UbiquitinationKLYLTNSKQTKLLTQ
HHHCCCCHHHHHHHH		65.15-
569PhosphorylationYVLSLAKYDQNYDIR
HHHHHHHCCCCCCHH		19.7028270605
573PhosphorylationLAKYDQNYDIRDRAR
HHHCCCCCCHHHHHH		13.7128270605
589PhosphorylationTRQLIVPSEQGGALS
EEEEECCHHHCCCCH		31.49113136279
596PhosphorylationSEQGGALSRHAKKLF
HHHCCCCHHHHHHHH		22.8346165069
733PhosphorylationDEEKGRGSESEQSEE
HHHCCCCCHHHHCHH		36.2720363803
735PhosphorylationEKGRGSESEQSEEDG
HCCCCCHHHHCHHHC		42.5020363803
738PhosphorylationRGSESEQSEEDGKRK
CCCHHHHCHHHCCCC		38.6120363803
764PhosphorylationASSSDEGSDSSSSSS
CCCCCCCCCCCCCCC		32.0730576142
766PhosphorylationSSDEGSDSSSSSSES
CCCCCCCCCCCCCCC		33.5430576142
768PhosphorylationDEGSDSSSSSSESEM
CCCCCCCCCCCCCCC		37.8950565801
777PhosphorylationSSESEMTSESEEEQL
CCCCCCCCCCHHHHC		37.5030576142
788PhosphorylationEEQLEPASWSRKTPP
HHHCCCCCCCCCCCC		35.9846165081
793PhosphorylationPASWSRKTPPSSKSA
CCCCCCCCCCCCCCC		39.0428176443
796PhosphorylationWSRKTPPSSKSAPAT
CCCCCCCCCCCCCCC		52.1525852190
797PhosphorylationSRKTPPSSKSAPATK
CCCCCCCCCCCCCCC		36.0825852190
901PhosphorylationHFSNSSDTPIKGLHV
EEECCCCCCCCEEEE		28.9446165087
957PhosphorylationNFQLCTQTRQFYVSI
CEEECCCCCEEEEEC		14.3246165093
1038PhosphorylationEYRFAGRTLTGGSLV
CCEECCEEECCCEEE		27.9622210691
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 AP3B2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP3B2_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 AP3B2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AP3B2_HUMAN !!
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 AP3B2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND MASSSPECTROMETRY.

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