AP4AT_HUMAN - dbPTM
AP4AT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP4AT_HUMAN
UniProt AC Q96N21
Protein Name AP-4 complex accessory subunit Tepsin {ECO:0000305}
Gene Name TEPSIN {ECO:0000303|PubMed:22472443, ECO:0000312|HGNC:HGNC:26458}
Organism Homo sapiens (Human).
Sequence Length 525
Subcellular Localization Golgi apparatus, trans-Golgi network membrane
Peripheral membrane protein . Cytoplasmic vesicle . Cytoplasm, cytosol . Extensively colocalizes with AP-4 which mediates the recruitment of TEPSIN to the trans-Golgi network.
Protein Description Associates with the adapter-like complex 4 (AP-4) and may therefore play a role in vesicular trafficking of proteins at the trans-Golgi network..
Protein Sequence MAAAPPLRDRLSFLHRLPILLKGTSDDDVPCPGYLFEEIAKISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNSAFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSDTVLPLAPSQPLGTPPATGMGSQARPHSTLQGFGYSKEHGRTAVRHQPGQAGGGWDELDSGPSSQNSSQNSDLSRVSDSGSHSGSDSHSGASREPGDLAERVEVVALSDCQQELSLVRTVTRGPRAFLSREEAQHFIKACGLLNCEAVLQLLTCHLRGTSECTQLRALCAIASLGSSDLLPQEHILLRTRPWLQELSMGSPGPVTNKATKILRHFEASCGQLSPARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVFLQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPAPGDPSEAEARLAESRRWRPERIPGGTDSPKRGPSSCAWSRDSLFAGMELVACPRLVGAGAAAGESCPDAPRAPQTSSQRTAAKEPPGSEPSAFAFLNA
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
12PhosphorylationPPLRDRLSFLHRLPI
CCHHHHHHHHHHHCC		27.0220873877
22UbiquitinationHRLPILLKGTSDDDV
HHHCCCCCCCCCCCC		57.6129967540
23 (in isoform 2)Phosphorylation-30.3528450419
25 (in isoform 2)Phosphorylation-47.9428450419
32 (in isoform 2)Phosphorylation-28.5220068231
33 (in isoform 2)Phosphorylation-38.1920068231
43 (in isoform 2)Phosphorylation-22.0922210691
51 (in isoform 2)Phosphorylation-24.4725159151
53 (in isoform 2)Phosphorylation-2.9328450419
54 (in isoform 2)Phosphorylation-5.5228450419
170UbiquitinationLQGFGYSKEHGRTAV
CCCCCCCCCCCCCEE		45.29-
201PhosphorylationGPSSQNSSQNSDLSR
CCCCCCCCCCCCCCC		40.71-
248PhosphorylationSDCQQELSLVRTVTR
HHHHHHHHHHHHHCC		24.8624719451
252PhosphorylationQELSLVRTVTRGPRA
HHHHHHHHHCCCCCC		20.8127174698
254PhosphorylationLSLVRTVTRGPRAFL
HHHHHHHCCCCCCCC		29.3327174698
262PhosphorylationRGPRAFLSREEAQHF
CCCCCCCCHHHHHHH		31.06-
322PhosphorylationQEHILLRTRPWLQEL
HHHHHHHCCHHHHHH		40.8423403867
330PhosphorylationRPWLQELSMGSPGPV
CHHHHHHHCCCCCCC		21.9823927012
333PhosphorylationLQELSMGSPGPVTNK
HHHHHCCCCCCCCHH		20.3123401153
338PhosphorylationMGSPGPVTNKATKIL
CCCCCCCCHHHHHHH		33.8523927012
340AcetylationSPGPVTNKATKILRH
CCCCCCHHHHHHHHH		48.3325953088
340MalonylationSPGPVTNKATKILRH
CCCCCCHHHHHHHHH		48.3326320211
351PhosphorylationILRHFEASCGQLSPA
HHHHHHHHCCCCCCC		16.1623403867
356PhosphorylationEASCGQLSPARGTSA
HHHCCCCCCCCCCCC		14.5022167270
395PhosphorylationQVFLQPLSSTPVSSR
EEEEEECCCCCCCCC		38.5628348404
396PhosphorylationVFLQPLSSTPVSSRS
EEEEECCCCCCCCCC		44.4028348404
397PhosphorylationFLQPLSSTPVSSRSP
EEEECCCCCCCCCCC		25.0828348404
400PhosphorylationPLSSTPVSSRSPAPS
ECCCCCCCCCCCCCC		22.6522210691
401PhosphorylationLSSTPVSSRSPAPSS
CCCCCCCCCCCCCCC		36.6932645325
403PhosphorylationSTPVSSRSPAPSSGM
CCCCCCCCCCCCCCC		27.6229978859
407PhosphorylationSSRSPAPSSGMPSSP
CCCCCCCCCCCCCCC		41.4529978859
408PhosphorylationSRSPAPSSGMPSSPV
CCCCCCCCCCCCCCC		37.7429978859
412PhosphorylationAPSSGMPSSPVPTPP
CCCCCCCCCCCCCCC		38.0828348404
413PhosphorylationPSSGMPSSPVPTPPP
CCCCCCCCCCCCCCC		24.8528985074
417PhosphorylationMPSSPVPTPPPDASP
CCCCCCCCCCCCCCC		48.9724719451
423PhosphorylationPTPPPDASPIPAPGD
CCCCCCCCCCCCCCC		30.6429978859
453PhosphorylationPERIPGGTDSPKRGP
CCCCCCCCCCCCCCC		38.9429255136
455PhosphorylationRIPGGTDSPKRGPSS
CCCCCCCCCCCCCCC		31.9629255136
457UbiquitinationPGGTDSPKRGPSSCA
CCCCCCCCCCCCCCC		74.1429967540
492PhosphorylationAGAAAGESCPDAPRA
CCHHCCCCCCCCCCC		29.9928555341
503PhosphorylationAPRAPQTSSQRTAAK
CCCCCCCCCCCCCCC		21.1628555341
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 AP4AT_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP4AT_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 AP4AT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
HNRPC_HUMANHNRNPCphysical
26496610
GRP78_HUMANHSPA5physical
26496610
IMDH2_HUMANIMPDH2physical
26496610
TNPO1_HUMANTNPO1physical
26496610
LAMA2_HUMANLAMA2physical
26496610
RL10_HUMANRPL10physical
26496610
BACD2_HUMANTNFAIP1physical
26496610
RBM10_HUMANRBM10physical
26496610
BAP1_HUMANBAP1physical
26496610
M2OM_HUMANSLC25A11physical
26496610
AP4M1_HUMANAP4M1physical
26496610
SCAM3_HUMANSCAMP3physical
26496610
SF3A1_HUMANSF3A1physical
26496610
YMEL1_HUMANYME1L1physical
26496610
SF3B2_HUMANSF3B2physical
26496610
AP4S1_HUMANAP4S1physical
26496610
AP4E1_HUMANAP4E1physical
26496610
SF3B1_HUMANSF3B1physical
26496610
UNC50_HUMANUNC50physical
26496610
NARF_HUMANNARFphysical
26496610
RT18B_HUMANMRPS18Bphysical
26496610
MED31_HUMANMED31physical
26496610
STK26_HUMANSTK26physical
26496610
KI16B_HUMANKIF16Bphysical
26496610
DERL1_HUMANDERL1physical
26496610
ISCA1_HUMANISCA1physical
26496610
ASCC2_HUMANASCC2physical
26496610
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 AP4AT_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-356 ANDSER-455, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 (ISOFORM 2),AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND MASSSPECTROMETRY.

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