AP1M2_HUMAN - dbPTM
AP1M2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP1M2_HUMAN
UniProt AC Q9Y6Q5
Protein Name AP-1 complex subunit mu-2
Gene Name AP1M2
Organism Homo sapiens (Human).
Sequence Length 423
Subcellular Localization Golgi apparatus. Cytoplasmic vesicle, clathrin-coated 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 Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules..
Protein Sequence MSASAVFILDVKGKPLISRNYKGDVAMSKIEHFMPLLVQREEEGALAPLLSHGQVHFLWIKHSNLYLVATTSKNANASLVYSFLYKTIEVFCEYFKELEEESIRDNFVIVYELLDELMDFGFPQTTDSKILQEYITQQSNKLETGKSRVPPTVTNAVSWRSEGIKYKKNEVFIDVIESVNLLVNANGSVLLSEIVGTIKLKVFLSGMPELRLGLNDRVLFELTGRSKNKSVELEDVKFHQCVRLSRFDNDRTISFIPPDGDFELMSYRLSTQVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANGVEISVPVPSDADSPRFKTSVGSAKYVPERNVVIWSIKSFPGGKEYLMRAHFGLPSVEKEEVEGRPPIGVKFEIPYFTVSGIQVRYMKIIEKSGYQALPWVRYITQSGDYQLRTS
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------MSASAVFIL
------CCCEEEEEE		30.8250565775
4Phosphorylation----MSASAVFILDV
----CCCEEEEEEEE		20.0550565781
14UbiquitinationFILDVKGKPLISRNY
EEEEECCCCCCCCCC		30.8221906983
14 (in isoform 2)Ubiquitination-30.8221906983
14 (in isoform 1)Ubiquitination-30.8221906983
22UbiquitinationPLISRNYKGDVAMSK
CCCCCCCCCCCCHHH		52.7821906983
22 (in isoform 2)Ubiquitination-52.7821906983
22 (in isoform 1)Ubiquitination-52.7821906983
28PhosphorylationYKGDVAMSKIEHFMP
CCCCCCHHHHHHHHH		22.2728348404
29UbiquitinationKGDVAMSKIEHFMPL
CCCCCHHHHHHHHHH		38.7421906983
29 (in isoform 2)Ubiquitination-38.7421906983
29 (in isoform 1)Ubiquitination-38.7421906983
63PhosphorylationHFLWIKHSNLYLVAT
EEEEEECCCEEEEEE		24.4325627689
70PhosphorylationSNLYLVATTSKNANA
CCEEEEEEECCCCCH		24.9172266281
134PhosphorylationDSKILQEYITQQSNK
CHHHHHHHHHHHCCC		9.0529759185
136PhosphorylationKILQEYITQQSNKLE
HHHHHHHHHHCCCCC		21.4729759185
141 (in isoform 1)Ubiquitination-53.6121906983
141 (in isoform 2)Ubiquitination-53.6121906983
141UbiquitinationYITQQSNKLETGKSR
HHHHHCCCCCCCCCC		53.6121906983
146 (in isoform 2)Ubiquitination-42.3721906983
146 (in isoform 1)Ubiquitination-42.3721906983
146UbiquitinationSNKLETGKSRVPPTV
CCCCCCCCCCCCCCH		42.3721906983
152PhosphorylationGKSRVPPTVTNAVSW
CCCCCCCCHHHHCCC		33.619573089
154PhosphorylationSRVPPTVTNAVSWRS
CCCCCCHHHHCCCCC		21.6828188228
178PhosphorylationVFIDVIESVNLLVNA
EEEEEHHHCCEEECC		12.75113334349
192PhosphorylationANGSVLLSEIVGTIK
CCCCCHHHEEEEEEE		22.5527251275
197PhosphorylationLLSEIVGTIKLKVFL
HHHEEEEEEEEEEHH		12.2128060719
201 (in isoform 1)Ubiquitination-26.4121906983
201UbiquitinationIVGTIKLKVFLSGMP
EEEEEEEEEHHCCCC		26.4121906983
201 (in isoform 2)Ubiquitination-26.4121906983
223PhosphorylationDRVLFELTGRSKNKS
CEEEEEEECCCCCCC		24.2928188228
223 (in isoform 2)Phosphorylation-24.2927050516
226 (in isoform 2)Phosphorylation-41.7624719451
229 (in isoform 2)Ubiquitination-60.6621906983
229 (in isoform 1)Ubiquitination-60.6621906983
229UbiquitinationLTGRSKNKSVELEDV
EECCCCCCCEEEECC		60.6621906983
231 (in isoform 2)Ubiquitination-11.8321906983
237UbiquitinationSVELEDVKFHQCVRL
CEEEECCEEEEEEEE		49.83-
266PhosphorylationDGDFELMSYRLSTQV
CCCCEEEEEEECCCC		21.52102782477
267PhosphorylationGDFELMSYRLSTQVK
CCCEEEEEEECCCCC		11.1225850435
274UbiquitinationYRLSTQVKPLIWIES
EEECCCCCCEEEHHH		25.04-
276 (in isoform 2)Ubiquitination-4.14-
296UbiquitinationSRVEIMVKAKGQFKK
CCEEEEEEECCCCCC		27.3121906983
296 (in isoform 1)Ubiquitination-27.3121906983
298UbiquitinationVEIMVKAKGQFKKQS
EEEEEEECCCCCCEE		47.75-
298 (in isoform 2)Ubiquitination-47.7521906983
303 (in isoform 1)Ubiquitination-49.4421906983
303UbiquitinationKAKGQFKKQSVANGV
EECCCCCCEEECCCC		49.4421906983
305PhosphorylationKGQFKKQSVANGVEI
CCCCCCEEECCCCEE		31.8828111955
305 (in isoform 2)Ubiquitination-31.8821906983
313PhosphorylationVANGVEISVPVPSDA
ECCCCEEEEECCCCC		13.5828111955
318PhosphorylationEISVPVPSDADSPRF
EEEEECCCCCCCCCC		45.7428111955
322PhosphorylationPVPSDADSPRFKTSV
ECCCCCCCCCCCCCC		21.5028111955
326MethylationDADSPRFKTSVGSAK
CCCCCCCCCCCCCCE		40.96-
326 (in isoform 1)Ubiquitination-40.9621906983
326UbiquitinationDADSPRFKTSVGSAK
CCCCCCCCCCCCCCE		40.9621906983
328 (in isoform 2)Ubiquitination-25.6821906983
333 (in isoform 1)Ubiquitination-48.7721906983
333UbiquitinationKTSVGSAKYVPERNV
CCCCCCCEEECCCCE		48.7721906983
335 (in isoform 2)Ubiquitination-3.8021906983
364PhosphorylationRAHFGLPSVEKEEVE
HEECCCCCCCHHHCC		48.2054887435
367 (in isoform 1)Ubiquitination-57.9521906983
367UbiquitinationFGLPSVEKEEVEGRP
CCCCCCCHHHCCCCC		57.9521906983
369 (in isoform 2)Ubiquitination-57.8621906983
379 (in isoform 1)Ubiquitination-31.8721906983
379UbiquitinationGRPPIGVKFEIPYFT
CCCCCCCEEEECEEE		31.8721906983
381 (in isoform 2)Ubiquitination-37.0221906983
388PhosphorylationEIPYFTVSGIQVRYM
EECEEEEECCEEEEE		27.4130631047
396UbiquitinationGIQVRYMKIIEKSGY
CCEEEEEEHHHHHCC		31.432190698
396 (in isoform 1)Ubiquitination-31.4321906983
398 (in isoform 2)Ubiquitination-4.5621906983
400UbiquitinationRYMKIIEKSGYQALP
EEEEHHHHHCCCCCC		38.48-
400 (in isoform 1)Ubiquitination-38.4821906983
401PhosphorylationYMKIIEKSGYQALPW
EEEHHHHHCCCCCCC		29.9128152594
402 (in isoform 2)Ubiquitination-29.6421906983
403PhosphorylationKIIEKSGYQALPWVR
EHHHHHCCCCCCCEE		9.5628152594
411PhosphorylationQALPWVRYITQSGDY
CCCCCEEEECCCCCE		9.9428152594
413PhosphorylationLPWVRYITQSGDYQL
CCCEEEECCCCCEEE		14.0328152594
415PhosphorylationWVRYITQSGDYQLRT
CEEEECCCCCEEEEC		25.6128152594
418PhosphorylationYITQSGDYQLRTS--
EECCCCCEEEECC--		16.9928152594
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 AP1M2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP1M2_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 AP1M2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EHD2_HUMANEHD2physical
15182197
SCNNG_HUMANSCNN1Gphysical
17381423
SCNNA_HUMANSCNN1Aphysical
16574660
SCNNB_HUMANSCNN1Bphysical
16574660
BLMH_HUMANBLMHphysical
21163940
LOXL4_HUMANLOXL4physical
21163940
RAB3A_HUMANRAB3Aphysical
21163940
RAB3D_HUMANRAB3Dphysical
21163940
AP1S2_HUMANAP1S2physical
26186194
AP1S1_HUMANAP1S1physical
26186194
AP1S3_HUMANAP1S3physical
26186194
AP1G2_HUMANAP1G2physical
26186194
AP1B1_HUMANAP1B1physical
26186194
AP2B1_HUMANAP2B1physical
26186194
TMF1_HUMANTMF1physical
26186194
HTR5B_HUMANHEATR5Bphysical
26186194
AP1G1_HUMANAP1G1physical
26186194
HECD1_HUMANHECTD1physical
26186194
RIPK1_HUMANRIPK1physical
26186194
NECP1_HUMANNECAP1physical
26186194
AP1B1_HUMANAP1B1physical
26344197
AP1G1_HUMANAP1G1physical
26344197
AP2B1_HUMANAP2B1physical
26344197
MON1A_HUMANMON1Aphysical
26344197
AP1S2_HUMANAP1S2physical
28514442
AP1S1_HUMANAP1S1physical
28514442
AP1G2_HUMANAP1G2physical
28514442
AP1B1_HUMANAP1B1physical
28514442
AP1G1_HUMANAP1G1physical
28514442
TMF1_HUMANTMF1physical
28514442
AP1S3_HUMANAP1S3physical
28514442
AP2B1_HUMANAP2B1physical
28514442
AFTIN_HUMANAFTPHphysical
28514442
HTR5B_HUMANHEATR5Bphysical
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 AP1M2_HUMAN

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Related Literatures of Post-Translational Modification

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