AP1M1_HUMAN - dbPTM
AP1M1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP1M1_HUMAN
UniProt AC Q9BXS5
Protein Name AP-1 complex subunit mu-1
Gene Name AP1M1
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 MSASAVYVLDLKGKVLICRNYRGDVDMSEVEHFMPILMEKEEEGMLSPILAHGGVRFMWIKHNNLYLVATSKKNACVSLVFSFLYKVVQVFSEYFKELEEESIRDNFVIIYELLDELMDFGYPQTTDSKILQEYITQEGHKLETGAPRPPATVTNAVSWRSEGIKYRKNEVFLDVIESVNLLVSANGNVLRSEIVGSIKMRVFLSGMPELRLGLNDKVLFDNTGRGKSKSVELEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLNTHVKPLIWIESVIEKHSHSRIEYMIKAKSQFKRRSTANNVEIHIPVPNDADSPKFKTTVGSVKWVPENSEIVWSIKSFPGGKEYLMRAHFGLPSVEAEDKEGKPPISVKFEIPYFTTSGIQVRYLKIIEKSGYQALPWVRYITQNGDYQLRTQ
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------MSASAVYVL
------CCCCEEEEE		30.8225003641
2Acetylation------MSASAVYVL
------CCCCEEEEE		30.8222223895
4Phosphorylation----MSASAVYVLDL
----CCCCEEEEEEC		15.8023532336
7Phosphorylation-MSASAVYVLDLKGK
-CCCCEEEEEECCCC		8.6023532336
12 (in isoform 2)Ubiquitination-57.25-
14UbiquitinationYVLDLKGKVLICRNY
EEEECCCCEEEECCC		32.08-
14 (in isoform 2)Ubiquitination-32.08-
28PhosphorylationYRGDVDMSEVEHFMP
CCCCCCHHHCHHHHH		33.7422210691
28O-linked_GlycosylationYRGDVDMSEVEHFMP
CCCCCCHHHCHHHHH		33.7429351928
47PhosphorylationKEEEGMLSPILAHGG
CCCCCCCHHHHHCCC		10.87102781351
72UbiquitinationLYLVATSKKNACVSL
EEEEEECCHHHHHHH		45.77-
134 (in isoform 2)Phosphorylation-9.0527642862
134PhosphorylationDSKILQEYITQEGHK
CHHHHHHHHHHCCCC		9.0531130153
141 (in isoform 2)Ubiquitination-59.90-
141UbiquitinationYITQEGHKLETGAPR
HHHHCCCCCCCCCCC		59.90-
144PhosphorylationQEGHKLETGAPRPPA
HCCCCCCCCCCCCCC		49.4324532841
152 (in isoform 2)Phosphorylation-33.3724719451
152PhosphorylationGAPRPPATVTNAVSW
CCCCCCCEEEHHCCC		33.3730266825
154PhosphorylationPRPPATVTNAVSWRS
CCCCCEEEHHCCCCC		17.0730266825
154 (in isoform 2)Phosphorylation-17.0727251275
158PhosphorylationATVTNAVSWRSEGIK
CEEEHHCCCCCCCCC		17.8630266825
165UbiquitinationSWRSEGIKYRKNEVF
CCCCCCCCCCCCEEH		50.27-
184PhosphorylationESVNLLVSANGNVLR
HHCCEEECCCCCEEC		18.9122210691
199UbiquitinationSEIVGSIKMRVFLSG
EEEEEEEEEEEECCC		23.50-
211 (in isoform 2)Ubiquitination-25.66-
217UbiquitinationLRLGLNDKVLFDNTG
EECCCCCEEEECCCC		39.5021890473
223PhosphorylationDKVLFDNTGRGKSKS
CEEEECCCCCCCCCC		30.0530266825
225MethylationVLFDNTGRGKSKSVE
EEECCCCCCCCCCEE		47.53-
227UbiquitinationFDNTGRGKSKSVELE
ECCCCCCCCCCEEHH		54.04-
229UbiquitinationNTGRGKSKSVELEDV
CCCCCCCCCEEHHHC		63.10-
229MalonylationNTGRGKSKSVELEDV
CCCCCCCCCEEHHHC		63.1026320211
229 (in isoform 2)Ubiquitination-63.10-
229UbiquitinationNTGRGKSKSVELEDV
CCCCCCCCCEEHHHC		63.1021890473
229AcetylationNTGRGKSKSVELEDV
CCCCCCCCCEEHHHC		63.1027452117
235 (in isoform 2)Phosphorylation-62.6224719451
237AcetylationSVELEDVKFHQCVRL
CEEHHHCEEEEEEEH		49.8325953088
237UbiquitinationSVELEDVKFHQCVRL
CEEHHHCEEEEEEEH		49.83-
241 (in isoform 2)Ubiquitination-1.12-
241 (in isoform 2)Malonylation-1.1226320211
249 (in isoform 2)Ubiquitination-41.16-
299PhosphorylationEYMIKAKSQFKRRST
HHHHHHHHHHCCCCC		45.7922333153
305PhosphorylationKSQFKRRSTANNVEI
HHHHCCCCCCCCEEE		35.5930266825
306PhosphorylationSQFKRRSTANNVEIH
HHHCCCCCCCCEEEE		31.4330266825
322PhosphorylationPVPNDADSPKFKTTV
CCCCCCCCCCCCCEE		31.5428985074
324AcetylationPNDADSPKFKTTVGS
CCCCCCCCCCCEECE		64.5425953088
324UbiquitinationPNDADSPKFKTTVGS
CCCCCCCCCCCEECE		64.5421890473
326MethylationDADSPKFKTTVGSVK
CCCCCCCCCEECEEE		49.79-
326UbiquitinationDADSPKFKTTVGSVK
CCCCCCCCCEECEEE		49.79-
331PhosphorylationKFKTTVGSVKWVPEN
CCCCEECEEEECCCC		19.0469213517
333UbiquitinationKTTVGSVKWVPENSE
CCEECEEEECCCCCE		44.14-
336UbiquitinationVGSVKWVPENSEIVW
ECEEEECCCCCEEEE		33.6621890473
336 (in isoform 2)Ubiquitination-33.66-
338 (in isoform 2)Ubiquitination-38.58-
345 (in isoform 2)Ubiquitination-2.25-
346UbiquitinationSEIVWSIKSFPGGKE
CEEEEEEEECCCCHH		40.2921890473
358 (in isoform 2)Ubiquitination-6.60-
358UbiquitinationGKEYLMRAHFGLPSV
CHHHHHHEECCCCCE		6.6021890473
370UbiquitinationPSVEAEDKEGKPPIS
CCEEECCCCCCCCCE		60.93-
396MalonylationGIQVRYLKIIEKSGY
CCEEEEEEEHHHHCC		32.4826320211
396AcetylationGIQVRYLKIIEKSGY
CCEEEEEEEHHHHCC		32.4822424773
396UbiquitinationGIQVRYLKIIEKSGY
CCEEEEEEEHHHHCC		32.48-
400UbiquitinationRYLKIIEKSGYQALP
EEEEEHHHHCCCCCC		38.4821890473
401PhosphorylationYLKIIEKSGYQALPW
EEEEHHHHCCCCCCE		29.9128152594
403PhosphorylationKIIEKSGYQALPWVR
EEHHHHCCCCCCEEE		9.5628152594
408 (in isoform 2)Ubiquitination-6.51-
408 (in isoform 2)Malonylation-6.5126320211
411PhosphorylationQALPWVRYITQNGDY
CCCCEEEEECCCCCE		9.9429496907
412 (in isoform 2)Ubiquitination-1.93-
412UbiquitinationALPWVRYITQNGDYQ
CCCEEEEECCCCCEE		1.9321890473
418PhosphorylationYITQNGDYQLRTQ--
EECCCCCEEEECC--		15.7329496907
421MethylationQNGDYQLRTQ-----
CCCCEEEECC-----		18.63-
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
144TPhosphorylationKinaseAAK1Q2M2I8
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP1M1_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 AP1M1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TIFA_HUMANTIFAphysical
16189514
FXR2_HUMANFXR2physical
16189514
RUN3A_HUMANRUNDC3Aphysical
16189514
LDOC1_HUMANLDOC1physical
16189514
ZBT8A_HUMANZBTB8Aphysical
16189514
AP1S2_HUMANAP1S2physical
22939629
AP1S1_HUMANAP1S1physical
22939629
MTF1_HUMANMTF1physical
19060904
LDOC1_HUMANLDOC1physical
19060904
FXR2_HUMANFXR2physical
25416956
DZIP3_HUMANDZIP3physical
25416956
TNIP1_HUMANTNIP1physical
25416956
IKZF1_HUMANIKZF1physical
25416956
SDCG3_HUMANSDCCAG3physical
25416956
RUN3A_HUMANRUNDC3Aphysical
25416956
ZBT43_HUMANZBTB43physical
25416956
ZBT44_HUMANZBTB44physical
25416956
HOOK2_HUMANHOOK2physical
25416956
LZTS2_HUMANLZTS2physical
25416956
TIFA_HUMANTIFAphysical
25416956
PNMA5_HUMANPNMA5physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
K1C40_HUMANKRT40physical
25416956
FAM9B_HUMANFAM9Bphysical
25416956
CE57L_HUMANCEP57L1physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
ZBT8A_HUMANZBTB8Aphysical
25416956
CORO7_HUMANCORO7physical
16905771
BRCA1_HUMANBRCA1physical
25184681
AP1B1_HUMANAP1B1physical
26344197
AP1G1_HUMANAP1G1physical
26344197
AP1S1_HUMANAP1S1physical
26344197
AP1S2_HUMANAP1S2physical
26344197
AP2B1_HUMANAP2B1physical
26344197
DCPS_HUMANDCPSphysical
26344197
AAKB1_HUMANPRKAB1physical
26344197
RNH2A_HUMANRNASEH2Aphysical
26344197
RNH2B_HUMANRNASEH2Bphysical
26344197
UBA1_HUMANUBA1physical
26344197
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 AP1M1_HUMAN

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Related Literatures of Post-Translational Modification

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