AP3M1_HUMAN - dbPTM
AP3M1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP3M1_HUMAN
UniProt AC Q9Y2T2
Protein Name AP-3 complex subunit mu-1
Gene Name AP3M1
Organism Homo sapiens (Human).
Sequence Length 418
Subcellular Localization Golgi apparatus. Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex..
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. 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 MIHSLFLINCSGDIFLEKHWKSVVSQSVCDYFFEAQEKAADVENVPPVISTPHHYLISIYRDKLFFVSVIQTEVPPLFVIEFLHRVADTFQDYFGECSEAAIKDNVVIVYELLEEMLDNGFPLATESNILKELIKPPTILRSVVNSITGSSNVGDTLPTGQLSNIPWRRAGVKYTNNEAYFDVVEEIDAIIDKSGSTVFAEIQGVIDACIKLSGMPDLSLSFMNPRLLDDVSFHPCIRFKRWESERVLSFIPPDGNFRLISYRVSSQNLVAIPVYVKHSISFKENSSCGRFDITIGPKQNMGKTIEGITVTVHMPKVVLNMNLTPTQGSYTFDPVTKVLTWDVGKITPQKLPSLKGLVNLQSGAPKPEENPSLNIQFKIQQLAISGLKVNRLDMYGEKYKPFKGVKYVTKAGKFQVRT
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
25PhosphorylationKHWKSVVSQSVCDYF
HHHHHHHHHHHHHHH		18.00-
29GlutathionylationSVVSQSVCDYFFEAQ
HHHHHHHHHHHHHHH		4.2022555962
31PhosphorylationVSQSVCDYFFEAQEK
HHHHHHHHHHHHHHH		12.6822817900
135UbiquitinationNILKELIKPPTILRS
HHHHHHCCCCHHHHH		58.5321890473
146PhosphorylationILRSVVNSITGSSNV
HHHHHHHHHHCCCCC		15.2127251275
148PhosphorylationRSVVNSITGSSNVGD
HHHHHHHHCCCCCCC		30.7227251275
150PhosphorylationVVNSITGSSNVGDTL
HHHHHHCCCCCCCCC		15.3028857561
151PhosphorylationVNSITGSSNVGDTLP
HHHHHCCCCCCCCCC		36.5628348404
156PhosphorylationGSSNVGDTLPTGQLS
CCCCCCCCCCCCCCC		28.8028348404
173UbiquitinationPWRRAGVKYTNNEAY
CCCCCCCCCCCCCEE		45.50-
275PhosphorylationNLVAIPVYVKHSISF
CEEEEEEEEEEEEEE		9.8328152594
281PhosphorylationVYVKHSISFKENSSC
EEEEEEEEECCCCCC		33.0324719451
283AcetylationVKHSISFKENSSCGR
EEEEEEECCCCCCCC		49.5526051181
283UbiquitinationVKHSISFKENSSCGR
EEEEEEECCCCCCCC		49.55-
283MethylationVKHSISFKENSSCGR
EEEEEEECCCCCCCC		49.55-
283MalonylationVKHSISFKENSSCGR
EEEEEEECCCCCCCC		49.5526320211
286PhosphorylationSISFKENSSCGRFDI
EEEECCCCCCCCEEE		28.2629759185
287PhosphorylationISFKENSSCGRFDIT
EEECCCCCCCCEEEE		31.9729759185
298UbiquitinationFDITIGPKQNMGKTI
EEEEECCCCCCCCEE		49.44-
304PhosphorylationPKQNMGKTIEGITVT
CCCCCCCEEECEEEE		20.6624248375
309PhosphorylationGKTIEGITVTVHMPK
CCEEECEEEEEECCE		22.4524248375
311PhosphorylationTIEGITVTVHMPKVV
EEECEEEEEECCEEE		8.95-
330PhosphorylationLTPTQGSYTFDPVTK
CCCCCCCEECCCCCE		20.4624248375
345UbiquitinationVLTWDVGKITPQKLP
EEEEECCCCCCCCCC		43.16-
347PhosphorylationTWDVGKITPQKLPSL
EEECCCCCCCCCCCC		24.1325159151
350UbiquitinationVGKITPQKLPSLKGL
CCCCCCCCCCCCCCC		64.67-
350AcetylationVGKITPQKLPSLKGL
CCCCCCCCCCCCCCC		64.6725953088
353PhosphorylationITPQKLPSLKGLVNL
CCCCCCCCCCCCEEC		53.8224719451
355UbiquitinationPQKLPSLKGLVNLQS
CCCCCCCCCCEECCC		55.31-
385PhosphorylationKIQQLAISGLKVNRL
EEEEHHHCCCEECEE		32.2528060719
388UbiquitinationQLAISGLKVNRLDMY
EHHHCCCEECEEECC		40.77-
398UbiquitinationRLDMYGEKYKPFKGV
EEECCCCCCCCCCCC		54.9621890473
399PhosphorylationLDMYGEKYKPFKGVK
EECCCCCCCCCCCCE		21.42-
400UbiquitinationDMYGEKYKPFKGVKY
ECCCCCCCCCCCCEE		55.86-
406UbiquitinationYKPFKGVKYVTKAGK
CCCCCCCEEEEECEE		42.55-
413UbiquitinationKYVTKAGKFQVRT--
EEEEECEEEEECC--		37.17-
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 AP3M1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP3M1_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 AP3M1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP3D1_HUMANAP3D1physical
22863883
PSA7_HUMANPSMA7physical
22863883
PSB5_HUMANPSMB5physical
22863883
RSP14_HUMANRSPH14physical
25416956
ATRAP_HUMANAGTRAPphysical
25416956
SI1L2_HUMANSIPA1L2physical
25416956
TRIM9_HUMANTRIM9physical
25416956
AP3B1_HUMANAP3B1physical
26344197
AP3D1_HUMANAP3D1physical
26344197
BRD4_HUMANBRD4physical
26344197
AP3B2_HUMANAP3B2physical
28514442
AP3M2_HUMANAP3M2physical
28514442
FERM2_HUMANFERMT2physical
28514442
AP3S2_HUMANAP3S2physical
28514442
AP3B1_HUMANAP3B1physical
28514442
RABL6_HUMANRABL6physical
28514442
AP3D1_HUMANAP3D1physical
28514442
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 AP3M1_HUMAN

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Related Literatures of Post-Translational Modification

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