AP180_RAT - dbPTM
AP180_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP180_RAT
UniProt AC Q05140
Protein Name Clathrin coat assembly protein AP180
Gene Name Snap91
Organism Rattus norvegicus (Rat).
Sequence Length 915
Subcellular Localization Cell membrane. Membrane, coated pit
Peripheral membrane protein
Cytoplasmic side. Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane.
Protein Description Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats..
Protein Sequence MSGQTLTDRIAAAQYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDFARVKKGADGVMRTMVPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVADEVGIDKGDIPDLTQAPSSLMETLEQHLNTLEGKKPGNNEGSGAPSPLSKSSPATTVTSPNSTPAKTIDTSPPVDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSGQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL
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
15PhosphorylationDRIAAAQYSVTGSAV
HHHHHHHCCCHHHHH		10.61-
16PhosphorylationRIAAAQYSVTGSAVA
HHHHHHCCCHHHHHH		10.92-
96PhosphorylationGNERFIQYLASRNTL
CCHHHHHHHHHCCCH		10.22-
107PhosphorylationRNTLFNLSNFLDKSG
CCCHHHHHHHHCCCC		27.0022673903
118PhosphorylationDKSGSHGYDMSTFIR
CCCCCCCCCHHHHHH		11.75-
134UbiquitinationYSRYLNEKAFSYRQM
HHHHHCHHCCHHHHH		54.37-
158PhosphorylationGADGVMRTMVPEKLL
CCCHHHHHCCCHHHH		12.3925575281
163AcetylationMRTMVPEKLLKSMPI
HHHCCCHHHHHCCCH		53.7222902405
238AcetylationKDALEIYKRFLTRMT
HHHHHHHHHHHHHHH		42.1922902405
296PhosphorylationKPGNNEGSGAPSPLS
CCCCCCCCCCCCCCC		26.1330411139
300PhosphorylationNEGSGAPSPLSKSSP
CCCCCCCCCCCCCCC		37.6330411139
303PhosphorylationSGAPSPLSKSSPATT
CCCCCCCCCCCCCCE		33.6028432305
305PhosphorylationAPSPLSKSSPATTVT
CCCCCCCCCCCCEEC		37.8727097102
306PhosphorylationPSPLSKSSPATTVTS
CCCCCCCCCCCEECC		23.4527097102
309PhosphorylationLSKSSPATTVTSPNS
CCCCCCCCEECCCCC		25.7828432305
310PhosphorylationSKSSPATTVTSPNST
CCCCCCCEECCCCCC		24.7227097102
310O-linked_GlycosylationSKSSPATTVTSPNST
CCCCCCCEECCCCCC		24.7221500857
312PhosphorylationSSPATTVTSPNSTPA
CCCCCEECCCCCCCC		36.0527097102
313PhosphorylationSPATTVTSPNSTPAK
CCCCEECCCCCCCCC		20.1130411139
316PhosphorylationTTVTSPNSTPAKTID
CEECCCCCCCCCCCC		38.8727097102
317PhosphorylationTVTSPNSTPAKTIDT
EECCCCCCCCCCCCC		33.6327097102
321PhosphorylationPNSTPAKTIDTSPPV
CCCCCCCCCCCCCCC		26.6227097102
324PhosphorylationTPAKTIDTSPPVDIF
CCCCCCCCCCCCEEE		39.0027097102
325PhosphorylationPAKTIDTSPPVDIFA
CCCCCCCCCCCEEEE		24.3727097102
333PhosphorylationPPVDIFATASAAAPV
CCCEEEEECCCCCCC		15.4727097102
593PhosphorylationLFGTDAFSSPPRGAS
CCCCCCCCCCCCCCC		43.5922673903
594PhosphorylationFGTDAFSSPPRGASP
CCCCCCCCCCCCCCC		32.2530240740
600 (in isoform 2)Phosphorylation-29.2927097102
600PhosphorylationSSPPRGASPVPESSL
CCCCCCCCCCCHHHH		29.2930240740
605 (in isoform 2)Phosphorylation-25.2827097102
606 (in isoform 2)Phosphorylation-28.2527097102
608 (in isoform 2)Phosphorylation-21.7727097102
613 (in isoform 2)Phosphorylation-37.9028551015
621 (in isoform 2)Phosphorylation-66.8828551015
624 (in isoform 2)Phosphorylation-45.0527097102
625 (in isoform 2)Phosphorylation-32.3227097102
627 (in isoform 2)Phosphorylation-19.8227097102
640PhosphorylationVDAFAAPSPASTASP
EHHHCCCCCCCCCCH		28.5030240740
646PhosphorylationPSPASTASPAKAESS
CCCCCCCCHHHHHHC		26.0230240740
771PhosphorylationGLGSDLDSSLASLVG
CCCCCHHHHHHHHHH		34.2522673903
772PhosphorylationLGSDLDSSLASLVGN
CCCCHHHHHHHHHHH		27.8522673903
775PhosphorylationDLDSSLASLVGNLGI
CHHHHHHHHHHHCCC		28.9622673903
783PhosphorylationLVGNLGISGTTSKKG
HHHHCCCCCCCCCCC		28.4322673903
785PhosphorylationGNLGISGTTSKKGDL
HHCCCCCCCCCCCCC		22.5522673903
786PhosphorylationNLGISGTTSKKGDLQ
HCCCCCCCCCCCCCE		41.9122673903
787PhosphorylationLGISGTTSKKGDLQW
CCCCCCCCCCCCCEE		32.0122673903
873MethylationMFAQPMMRPPFGAAA
EECCCCCCCCCCCCC		29.50-
873Asymmetric dimethylarginineMFAQPMMRPPFGAAA
EECCCCCCCCCCCCC		29.50-
884PhosphorylationGAAAVPGTQLSPSPT
CCCCCCCCCCCCCCC		21.9225575281
887PhosphorylationAVPGTQLSPSPTPAT
CCCCCCCCCCCCCCC		17.3225575281
889PhosphorylationPGTQLSPSPTPATQS
CCCCCCCCCCCCCCC		37.7225575281
891PhosphorylationTQLSPSPTPATQSPK
CCCCCCCCCCCCCCC		29.8725575281
894PhosphorylationSPSPTPATQSPKKPP
CCCCCCCCCCCCCCC		30.6825575281
896PhosphorylationSPTPATQSPKKPPAK
CCCCCCCCCCCCCCC		34.0430240740
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 AP180_RAT !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
310TPhosphorylation

21500857
310TPhosphorylation

21500857
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 AP180_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLCG1_RATPlcg1physical
11779129
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP180_RAT

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"A novel post-translational modification in nerve terminals: O-linkedN-acetylglucosamine phosphorylation.";
Graham M.E., Thaysen-Andersen M., Bache N., Craft G.E., Larsen M.R.,Packer N.H., Robinson P.J.;
J. Proteome Res. 10:2725-2733(2011).
Cited for: PROTEIN SEQUENCE OF 305-320 (ISOFORMS 1/2), PROTEIN SEQUENCE OF598-649 (ISOFORM 2), GLYCOSYLATION AT THR-310, PHOSPHORYLATION ATSER-313; SER-313; SER-600; SER-640 AND SER-646, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A novel post-translational modification in nerve terminals: O-linkedN-acetylglucosamine phosphorylation.";
Graham M.E., Thaysen-Andersen M., Bache N., Craft G.E., Larsen M.R.,Packer N.H., Robinson P.J.;
J. Proteome Res. 10:2725-2733(2011).
Cited for: PROTEIN SEQUENCE OF 305-320 (ISOFORMS 1/2), PROTEIN SEQUENCE OF598-649 (ISOFORM 2), GLYCOSYLATION AT THR-310, PHOSPHORYLATION ATSER-313; SER-313; SER-600; SER-640 AND SER-646, AND MASS SPECTROMETRY.

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