TPC12_HUMAN - dbPTM
TPC12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPC12_HUMAN
UniProt AC Q8WVT3
Protein Name Trafficking protein particle complex subunit 12 {ECO:0000305}
Gene Name TRAPPC12 {ECO:0000312|HGNC:HGNC:24284}
Organism Homo sapiens (Human).
Sequence Length 735
Subcellular Localization Endoplasmic reticulum-Golgi intermediate compartment . Nucleus . Mainly localizes to structures resembling the Golgi and a small amount is found in the nucleus.
Protein Description Component of the TRAPP complex, which is involved in endoplasmic reticulum to Golgi apparatus trafficking at a very early stage. [PubMed: 21525244]
Protein Sequence MEDAGGGEETPAPEAPHPPQLAPPEEQGLLFQEETIDLGGDEFGSEENETASEGSSPLADKLNEHMMESVLISDSPNSEGDAGDLGRVRDEAEPGGEGDPGPEPAGTPSPSGEADGDCAPEDAAPSSGGAPRQDAAREVPGSEAARPEQEPPVAEPVPVCTIFSQRAPPASGDGFEPQMVKSPSFGGASEASARTPPQVVQPSPSLSTFFGDTAASHSLASDFFDSFTTSAFISVSNPGAGSPAPASPPPLAVPGTEGRPEPVAMRGPQAAAPPASPEPFAHIQAVFAGSDDPFATALSMSEMDRRNDAWLPGEATRGVLRAVATQQRGAVFVDKENLTMPGLRFDNIQGDAVKDLMLRFLGEKAAAKRQVLNADSVEQSFVGLKQLISCRNWRAAVDLCGRLLTAHGQGYGKSGLLTSHTTDSLQLWFVRLALLVKLGLFQNAEMEFEPFGNLDQPDLYYEYYPHVYPGRRGSMVPFSMRILHAELQQYLGNPQESLDRLHKVKTVCSKILANLEQGLAEDGGMSSVTQEGRQASIRLWRSRLGRVMYSMANCLLLMKDYVLAVEAYHSVIKYYPEQEPQLLSGIGRISLQIGDIKTAEKYFQDVEKVTQKLDGLQGKIMVLMNSAFLHLGQNNFAEAHRFFTEILRMDPRNAVANNNAAVCLLYLGKLKDSLRQLEAMVQQDPRHYLHESVLFNLTTMYELESSRSMQKKQALLEAVAGKEGDSFNTQCLKLA
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
50PhosphorylationFGSEENETASEGSSP
CCCCCCCCCCCCCCH		47.2526074081
52PhosphorylationSEENETASEGSSPLA
CCCCCCCCCCCCHHH		50.3226074081
55PhosphorylationNETASEGSSPLADKL
CCCCCCCCCHHHHHH		25.4026074081
69PhosphorylationLNEHMMESVLISDSP
HHHHHHHHHEECCCC		12.3427080861
73PhosphorylationMMESVLISDSPNSEG
HHHHHEECCCCCCCC		28.0728270605
75PhosphorylationESVLISDSPNSEGDA
HHHEECCCCCCCCCC		21.1328270605
78PhosphorylationLISDSPNSEGDAGDL
EECCCCCCCCCCCCC		46.4728270605
107PhosphorylationPGPEPAGTPSPSGEA
CCCCCCCCCCCCCCC		23.7723927012
109PhosphorylationPEPAGTPSPSGEADG
CCCCCCCCCCCCCCC		31.3830278072
111PhosphorylationPAGTPSPSGEADGDC
CCCCCCCCCCCCCCC		54.3130278072
126PhosphorylationAPEDAAPSSGGAPRQ
CCCCCCCCCCCCCCH		36.5728450419
127PhosphorylationPEDAAPSSGGAPRQD
CCCCCCCCCCCCCHH		39.9428450419
171PhosphorylationSQRAPPASGDGFEPQ
ECCCCCCCCCCCCCC		43.1022210691
179SulfoxidationGDGFEPQMVKSPSFG
CCCCCCCCCCCCCCC		6.3221406390
181UbiquitinationGFEPQMVKSPSFGGA
CCCCCCCCCCCCCCC		51.84-
182PhosphorylationFEPQMVKSPSFGGAS
CCCCCCCCCCCCCCC		17.8629255136
184PhosphorylationPQMVKSPSFGGASEA
CCCCCCCCCCCCCCC		43.5529255136
189PhosphorylationSPSFGGASEASARTP
CCCCCCCCCCCCCCC		36.6530266825
192PhosphorylationFGGASEASARTPPQV
CCCCCCCCCCCCCCC		17.7724702127
195PhosphorylationASEASARTPPQVVQP
CCCCCCCCCCCCCCC		38.7529460479
234PhosphorylationFTTSAFISVSNPGAG
CCCEEEEEECCCCCC		17.0326074081
236PhosphorylationTSAFISVSNPGAGSP
CEEEEEECCCCCCCC		30.4326074081
242PhosphorylationVSNPGAGSPAPASPP
ECCCCCCCCCCCCCC		19.8426074081
247PhosphorylationAGSPAPASPPPLAVP
CCCCCCCCCCCCCCC		36.5626074081
256PhosphorylationPPLAVPGTEGRPEPV
CCCCCCCCCCCCCCC		29.2426074081
276PhosphorylationQAAAPPASPEPFAHI
CCCCCCCCCCCCCEE		35.2526657352
290PhosphorylationIQAVFAGSDDPFATA
EEEHHCCCCCHHHHH		35.1024117733
335UbiquitinationRGAVFVDKENLTMPG
CCCEEECCCCCCCCC		43.11-
354UbiquitinationNIQGDAVKDLMLRFL
CCCCHHHHHHHHHHH		47.0321890473
364UbiquitinationMLRFLGEKAAAKRQV
HHHHHCHHHHHHCCC		41.34-
364AcetylationMLRFLGEKAAAKRQV
HHHHHCHHHHHHCCC		41.3425953088
376PhosphorylationRQVLNADSVEQSFVG
CCCCCCCCHHHHHCH		25.7425072903
380PhosphorylationNADSVEQSFVGLKQL
CCCCHHHHHCHHHHH		14.3725072903
385UbiquitinationEQSFVGLKQLISCRN
HHHHCHHHHHHHCCC		36.81-
460PhosphorylationNLDQPDLYYEYYPHV
CCCCCCCCEEECCCC		11.1327461979
461PhosphorylationLDQPDLYYEYYPHVY
CCCCCCCEEECCCCC		12.5427461979
474PhosphorylationVYPGRRGSMVPFSMR
CCCCCCCCCCCCHHH		18.1324719451
505UbiquitinationLDRLHKVKTVCSKIL
HHHHHHHHHHHHHHH		39.79-
510UbiquitinationKVKTVCSKILANLEQ
HHHHHHHHHHHHHHH		36.29-
574PhosphorylationAYHSVIKYYPEQEPQ
HHHHHHHHCCCCCCC		17.09-
575PhosphorylationYHSVIKYYPEQEPQL
HHHHHHHCCCCCCCH		8.69-
584PhosphorylationEQEPQLLSGIGRISL
CCCCCHHCCCCEEEE		36.64-
590PhosphorylationLSGIGRISLQIGDIK
HCCCCEEEEEECCHH		16.9222985185
597UbiquitinationSLQIGDIKTAEKYFQ
EEEECCHHHHHHHHH		46.55-
598PhosphorylationLQIGDIKTAEKYFQD
EEECCHHHHHHHHHH		40.14-
601UbiquitinationGDIKTAEKYFQDVEK
CCHHHHHHHHHHHHH		49.2321890473
608UbiquitinationKYFQDVEKVTQKLDG
HHHHHHHHHHHHHCC		50.89-
612UbiquitinationDVEKVTQKLDGLQGK
HHHHHHHHHCCCCHH		38.90-
712UbiquitinationSSRSMQKKQALLEAV
CCCCHHHHHHHHHHH		24.74-
722UbiquitinationLLEAVAGKEGDSFNT
HHHHHHCCCCCCCHH		49.11-
733UbiquitinationSFNTQCLKLA-----
CCHHHHHHCC-----		50.42-
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 TPC12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPC12_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 TPC12_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TPPC4_HUMANTRAPPC4physical
21525244
TPC10_HUMANTRAPPC10physical
21525244
TPC11_HUMANTRAPPC11physical
21525244
TPC12_HUMANTRAPPC12physical
21525244
TPC6B_HUMANTRAPPC6Bphysical
21525244
TPC6A_HUMANTRAPPC6Aphysical
21525244
TPPC8_HUMANTRAPPC8physical
21525244
TPPC4_HUMANTRAPPC4physical
26186194
CEP55_HUMANCEP55physical
26186194
TPC11_HUMANTRAPPC11physical
26186194
TPPC8_HUMANTRAPPC8physical
26186194
TPC6B_HUMANTRAPPC6Bphysical
26186194
TPPC1_HUMANTRAPPC1physical
26186194
TPC6A_HUMANTRAPPC6Aphysical
26186194
TPPC3_HUMANTRAPPC3physical
26186194
TPPC5_HUMANTRAPPC5physical
26186194
EDRF1_HUMANEDRF1physical
26186194
TPC2L_HUMANTRAPPC2Lphysical
26186194
TPC2A_HUMANTRAPPC2physical
26186194
TPC2B_HUMANTRAPPC2physical
26186194
TPC11_HUMANTRAPPC11physical
28514442
CEP55_HUMANCEP55physical
28514442
TPPC8_HUMANTRAPPC8physical
28514442
TPC6A_HUMANTRAPPC6Aphysical
28514442
EDRF1_HUMANEDRF1physical
28514442
TPPC4_HUMANTRAPPC4physical
28514442
TPC6B_HUMANTRAPPC6Bphysical
28514442
TPPC3_HUMANTRAPPC3physical
28514442
TPC2L_HUMANTRAPPC2Lphysical
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 TPC12_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-184, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-184, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND MASSSPECTROMETRY.

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