USO1_HUMAN - dbPTM
USO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID USO1_HUMAN
UniProt AC O60763
Protein Name General vesicular transport factor p115
Gene Name USO1
Organism Homo sapiens (Human).
Sequence Length 962
Subcellular Localization Cytoplasm, cytosol . Golgi apparatus membrane
Peripheral membrane protein . Recycles between the cytosol and the Golgi apparatus during interphase. During interphase, the phosphorylated form is found exclusively in cytosol
the unphosphorylated for
Protein Description General vesicular transport factor required for intercisternal transport in the Golgi stack; it is required for transcytotic fusion and/or subsequent binding of the vesicles to the target membrane. May well act as a vesicular anchor by interacting with the target membrane and holding the vesicular and target membranes in proximity..
Protein Sequence MNFLRGVMGGQSAGPQHTEAETIQKLCDRVASSTLLDDRRNAVRALKSLSKKYRLEVGIQAMEHLIHVLQTDRSDSEIIGYALDTLYNIISNEEEEEVEENSTRQSEDLGSQFTEIFIKQQENVTLLLSLLEEFDFHVRWPGVKLLTSLLKQLGPQVQQIILVSPMGVSRLMDLLADSREVIRNDGVLLLQALTRSNGAIQKIVAFENAFERLLDIISEEGNSDGGIVVEDCLILLQNLLKNNNSNQNFFKEGSYIQRMKPWFEVGDENSGWSAQKVTNLHLMLQLVRVLVSPTNPPGATSSCQKAMFQCGLLQQLCTILMATGVPADILTETINTVSEVIRGCQVNQDYFASVNAPSNPPRPAIVVLLMSMVNERQPFVLRCAVLYCFQCFLYKNQKGQGEIVSTLLPSTIDATGNSVSAGQLLCGGLFSTDSLSNWCAAVALAHALQENATQKEQLLRVQLATSIGNPPVSLLQQCTNILSQGSKIQTRVGLLMLLCTWLSNCPIAVTHFLHNSANVPFLTGQIAENLGEEEQLVQGLCALLLGISIYFNDNSLESYMKEKLKQLIEKRIGKENFIEKLGFISKHELYSRASQKPQPNFPSPEYMIFDHEFTKLVKELEGVITKAIYKSSEEDKKEEEVKKTLEQHDNIVTHYKNMIREQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYSEGAQMNGIQPEEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAIVSARDSEQVAELKQELATLKSQLNSQSVEITKLQTEKQELLQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEEDELESGDQEDEDDESEDPGKDLDHI
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
5Methylation---MNFLRGVMGGQS
---CCCCCHHCCCCC		31.36115918209
8SulfoxidationMNFLRGVMGGQSAGP
CCCCCHHCCCCCCCC		5.7821406390
12PhosphorylationRGVMGGQSAGPQHTE
CHHCCCCCCCCCCCH		38.1728857561
25AcetylationTEAETIQKLCDRVAS
CHHHHHHHHHHHHHH		47.4326051181
25MalonylationTEAETIQKLCDRVAS
CHHHHHHHHHHHHHH		47.4326320211
25UbiquitinationTEAETIQKLCDRVAS
CHHHHHHHHHHHHHH		47.4323000965
25 (in isoform 2)Ubiquitination-47.43-
29MethylationTIQKLCDRVASSTLL
HHHHHHHHHHHCCHH		25.55115918201
32PhosphorylationKLCDRVASSTLLDDR
HHHHHHHHCCHHHHH		22.4616674116
33PhosphorylationLCDRVASSTLLDDRR
HHHHHHHCCHHHHHH		17.2128348404
34PhosphorylationCDRVASSTLLDDRRN
HHHHHHCCHHHHHHH		28.9228348404
39MethylationSSTLLDDRRNAVRAL
HCCHHHHHHHHHHHH		33.16115918205
47UbiquitinationRNAVRALKSLSKKYR
HHHHHHHHHHCHHHH		48.6529967540
48PhosphorylationNAVRALKSLSKKYRL
HHHHHHHHHCHHHHH		38.4329743597
50PhosphorylationVRALKSLSKKYRLEV
HHHHHHHCHHHHHHH		33.9020068231
74PhosphorylationHVLQTDRSDSEIIGY
HHHHCCCCCCHHHHH		48.5830576142
87PhosphorylationGYALDTLYNIISNEE
HHHHHHHHHHHCCCC		13.3530576142
102PhosphorylationEEEVEENSTRQSEDL
HHHHHHHCCCCCHHH		28.3930576142
111PhosphorylationRQSEDLGSQFTEIFI
CCCHHHHHHHHHHHH		29.4421712546
148PhosphorylationPGVKLLTSLLKQLGP
CHHHHHHHHHHHHCH		31.5124719451
164PhosphorylationVQQIILVSPMGVSRL
CCEEEEECCCHHHHH		13.0122210691
169PhosphorylationLVSPMGVSRLMDLLA
EECCCHHHHHHHHHH		17.61-
172SulfoxidationPMGVSRLMDLLADSR
CCHHHHHHHHHHHCC		3.1130846556
202AcetylationRSNGAIQKIVAFENA
HCCCHHHHHHHHHHH		32.7919608861
202UbiquitinationRSNGAIQKIVAFENA
HCCCHHHHHHHHHHH		32.7923000965
206UbiquitinationAIQKIVAFENAFERL
HHHHHHHHHHHHHHH		5.2921890473
206 (in isoform 2)Ubiquitination-5.29-
206UbiquitinationAIQKIVAFENAFERL
HHHHHHHHHHHHHHH		5.2921890473
245PhosphorylationNLLKNNNSNQNFFKE
HHHHCCCCCCCCCCC		41.7530622161
251MethylationNSNQNFFKEGSYIQR
CCCCCCCCCCHHHHH		57.96115980199
465PhosphorylationLLRVQLATSIGNPPV
HHHHHHHHHCCCCCH		29.48-
483PhosphorylationQQCTNILSQGSKIQT
HHHHHHHHCCCHHHH		28.79-
486PhosphorylationTNILSQGSKIQTRVG
HHHHHCCCHHHHHHH		20.96-
565MalonylationSYMKEKLKQLIEKRI
HHHHHHHHHHHHHHH		54.8726320211
580AcetylationGKENFIEKLGFISKH
CCCHHHHHHCCCCHH		49.4427452117
580UbiquitinationGKENFIEKLGFISKH
CCCHHHHHHCCCCHH		49.4433845483
584UbiquitinationFIEKLGFISKHELYS
HHHHHCCCCHHHHHH		5.2121890473
585PhosphorylationIEKLGFISKHELYSR
HHHHCCCCHHHHHHH		26.2121712546
587UbiquitinationKLGFISKHELYSRAS
HHCCCCHHHHHHHHC		24.4121890473
591PhosphorylationISKHELYSRASQKPQ
CCHHHHHHHHCCCCC		33.7121712546
591UbiquitinationISKHELYSRASQKPQ
CCHHHHHHHHCCCCC		33.7121890473
591UbiquitinationISKHELYSRASQKPQ
CCHHHHHHHHCCCCC		33.7121890473
594PhosphorylationHELYSRASQKPQPNF
HHHHHHHCCCCCCCC		37.3128857561
596UbiquitinationLYSRASQKPQPNFPS
HHHHHCCCCCCCCCC		43.0329967540
607SulfoxidationNFPSPEYMIFDHEFT
CCCCCCCEEECHHHH		2.0430846556
607UbiquitinationNFPSPEYMIFDHEFT
CCCCCCCEEECHHHH		2.0429967540
618MalonylationHEFTKLVKELEGVIT
HHHHHHHHHHHHHHH		68.0026320211
618UbiquitinationHEFTKLVKELEGVIT
HHHHHHHHHHHHHHH		68.0029967540
626AcetylationELEGVITKAIYKSSE
HHHHHHHHHHHHCCH		22.9723236377
626MalonylationELEGVITKAIYKSSE
HHHHHHHHHHHHCCH		22.9726320211
626UbiquitinationELEGVITKAIYKSSE
HHHHHHHHHHHHCCH		22.9723000965
629UbiquitinationGVITKAIYKSSEEDK
HHHHHHHHHCCHHHH		15.0729967540
630UbiquitinationVITKAIYKSSEEDKK
HHHHHHHHCCHHHHH		41.2023000965
633UbiquitinationKAIYKSSEEDKKEEE
HHHHHCCHHHHHHHH		76.8423000965
634UbiquitinationAIYKSSEEDKKEEEV
HHHHCCHHHHHHHHH		76.6623000965
637MalonylationKSSEEDKKEEEVKKT
HCCHHHHHHHHHHHH		80.7226320211
637UbiquitinationKSSEEDKKEEEVKKT
HCCHHHHHHHHHHHH		80.7223000965
637 (in isoform 2)Ubiquitination-80.72-
641UbiquitinationEDKKEEEVKKTLEQH
HHHHHHHHHHHHHHH		9.7323000965
642UbiquitinationDKKEEEVKKTLEQHD
HHHHHHHHHHHHHHH		43.2323000965
643UbiquitinationKKEEEVKKTLEQHDN
HHHHHHHHHHHHHHH		64.6123000965
644UbiquitinationKEEEVKKTLEQHDNI
HHHHHHHHHHHHHHH		29.7923000965
646UbiquitinationEEVKKTLEQHDNIVT
HHHHHHHHHHHHHHH		51.6123000965
647UbiquitinationEVKKTLEQHDNIVTH
HHHHHHHHHHHHHHH		52.9623000965
648UbiquitinationVKKTLEQHDNIVTHY
HHHHHHHHHHHHHHH		22.2523000965
649UbiquitinationKKTLEQHDNIVTHYK
HHHHHHHHHHHHHHH		46.3623000965
650UbiquitinationKTLEQHDNIVTHYKN
HHHHHHHHHHHHHHH		28.6223000965
653UbiquitinationEQHDNIVTHYKNMIR
HHHHHHHHHHHHHHH		18.7223000965
654UbiquitinationQHDNIVTHYKNMIRE
HHHHHHHHHHHHHHH		22.2223000965
654 (in isoform 2)Ubiquitination-22.22-
655PhosphorylationHDNIVTHYKNMIREQ
HHHHHHHHHHHHHHH		8.4918180459
670MethylationDLQLEELRQQVSTLK
HHCHHHHHHHHHHHH		28.32115918213
698UbiquitinationVSQIQQHKDQYNLLK
HHHHHHCHHHHEEEE		42.0429967540
705UbiquitinationKDQYNLLKIQLGKDN
HHHHEEEEEECCCCC		31.4123000965
709UbiquitinationNLLKIQLGKDNQHQG
EEEEEECCCCCCCCC		20.9221890473
710UbiquitinationLLKIQLGKDNQHQGS
EEEEECCCCCCCCCC		63.2023000965
712UbiquitinationKIQLGKDNQHQGSYS
EEECCCCCCCCCCCC		44.7321890473
714UbiquitinationQLGKDNQHQGSYSEG
ECCCCCCCCCCCCCC		39.9823000965
716UbiquitinationGKDNQHQGSYSEGAQ
CCCCCCCCCCCCCHH		26.8221890473
716 (in isoform 2)Ubiquitination-26.82-
716UbiquitinationGKDNQHQGSYSEGAQ
CCCCCCCCCCCCCHH		26.8221890473
717PhosphorylationKDNQHQGSYSEGAQM
CCCCCCCCCCCCHHH		20.9320068231
717UbiquitinationKDNQHQGSYSEGAQM
CCCCCCCCCCCCHHH		20.9323000965
718PhosphorylationDNQHQGSYSEGAQMN
CCCCCCCCCCCHHHC		19.9820068231
719PhosphorylationNQHQGSYSEGAQMNG
CCCCCCCCCCHHHCC		31.1120068231
721UbiquitinationHQGSYSEGAQMNGIQ
CCCCCCCCHHHCCCC		18.3723000965
743UbiquitinationREEIEELKRNQELLQ
HHHHHHHHHHHHHHH		53.2124816145
747UbiquitinationEELKRNQELLQSQLT
HHHHHHHHHHHHHHH		55.8024816145
750UbiquitinationKRNQELLQSQLTEKD
HHHHHHHHHHHHHHH		41.5824816145
751PhosphorylationRNQELLQSQLTEKDS
HHHHHHHHHHHHHHH		27.4222617229
754PhosphorylationELLQSQLTEKDSMIE
HHHHHHHHHHHHHHH		33.0922617229
754UbiquitinationELLQSQLTEKDSMIE
HHHHHHHHHHHHHHH		33.0924816145
758PhosphorylationSQLTEKDSMIENMKS
HHHHHHHHHHHHHHH		32.5021712546
766PhosphorylationMIENMKSSQTSGTNE
HHHHHHHHCCCCCCC		31.7722817901
771PhosphorylationKSSQTSGTNEQSSAI
HHHCCCCCCCCCHHE		35.0428555341
775PhosphorylationTSGTNEQSSAIVSAR
CCCCCCCCHHEEECC		18.6329978859
776PhosphorylationSGTNEQSSAIVSARD
CCCCCCCHHEEECCC		23.0028555341
780PhosphorylationEQSSAIVSARDSEQV
CCCHHEEECCCHHHH		16.0928555341
791AcetylationSEQVAELKQELATLK
HHHHHHHHHHHHHHH		32.9823236377
791UbiquitinationSEQVAELKQELATLK
HHHHHHHHHHHHHHH		32.9829967540
798UbiquitinationKQELATLKSQLNSQS
HHHHHHHHHHHHHCC		31.6232015554
799PhosphorylationQELATLKSQLNSQSV
HHHHHHHHHHHHCCE		42.9121406692
802UbiquitinationATLKSQLNSQSVEIT
HHHHHHHHHCCEEEE		30.3029967540
803PhosphorylationTLKSQLNSQSVEITK
HHHHHHHHCCEEEEH		32.2121406692
805PhosphorylationKSQLNSQSVEITKLQ
HHHHHHCCEEEEHHH		22.8721406692
809PhosphorylationNSQSVEITKLQTEKQ
HHCCEEEEHHHHHHH		16.5221406692
809UbiquitinationNSQSVEITKLQTEKQ
HHCCEEEEHHHHHHH		16.5232015554
815AcetylationITKLQTEKQELLQKT
EEHHHHHHHHHHHHH		53.0825953088
828PhosphorylationKTEAFAKSVEVQGET
HHHHHHHHCEECCEE		21.7827251275
843PhosphorylationETIIATKTTDVEGRL
EEEEEEEECCHHHHH		24.7127251275
844PhosphorylationTIIATKTTDVEGRLS
EEEEEEECCHHHHHH		39.3327251275
851PhosphorylationTDVEGRLSALLQETK
CCHHHHHHHHHHHHH		18.6030266825
857PhosphorylationLSALLQETKELKNEI
HHHHHHHHHHHHHHH		19.5030266825
858AcetylationSALLQETKELKNEIK
HHHHHHHHHHHHHHH		61.3725953088
858MalonylationSALLQETKELKNEIK
HHHHHHHHHHHHHHH		61.3726320211
858UbiquitinationSALLQETKELKNEIK
HHHHHHHHHHHHHHH		61.3732015554
868PhosphorylationKNEIKALSEERTAIK
HHHHHHHHHHHHHHH		42.1222210691
869UbiquitinationNEIKALSEERTAIKE
HHHHHHHHHHHHHHH		52.9632015554
872PhosphorylationKALSEERTAIKEQLD
HHHHHHHHHHHHHHH		35.6922210691
881PhosphorylationIKEQLDSSNSTIAIL
HHHHHHCCCCEEEEE		34.1725627689
890PhosphorylationSTIAILQTEKDKLEL
CEEEEEEEHHHCEEE		41.3722210691
894UbiquitinationILQTEKDKLELEITD
EEEEHHHCEEEEEEC		55.7329901268
904UbiquitinationLEITDSKKEQDDLLV
EEEECCCCHHCCEEE		65.6429967540
905UbiquitinationEITDSKKEQDDLLVL
EEECCCCHHCCEEEE		64.0829901268
915UbiquitinationDLLVLLADQDQKILS
CEEEEEECCCHHHHH		53.1929967540
919UbiquitinationLLADQDQKILSLKNK
EEECCCHHHHHHHHH		54.6321890473
922PhosphorylationDQDQKILSLKNKLKD
CCCHHHHHHHHHHHH		40.5524719451
923UbiquitinationQDQKILSLKNKLKDL
CCHHHHHHHHHHHHC		6.7621890473
926UbiquitinationKILSLKNKLKDLGHP
HHHHHHHHHHHCCCC		56.1621890473
930UbiquitinationLKNKLKDLGHPVEEE
HHHHHHHCCCCCCCH		6.9321890473
930UbiquitinationLKNKLKDLGHPVEEE
HHHHHHHCCCCCCCH		6.9321890473
942PhosphorylationEEEDELESGDQEDED
CCHHHHHCCCCCCCC		61.3622167270
952PhosphorylationQEDEDDESEDPGKDL
CCCCCCCCCCCCCCC		55.0523927012
953PhosphorylationEDEDDESEDPGKDLD
CCCCCCCCCCCCCCC		67.2032645325
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 USO1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of USO1_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 USO1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CA094_HUMANC1orf94physical
16189514
GOSR1_HUMANGOSR1physical
11927603
GOSR2_HUMANGOSR2physical
11927603
BET1_HUMANBET1physical
11927603
YKT6_HUMANYKT6physical
11927603
STX5_HUMANSTX5physical
11927603
SC22A_HUMANSEC22Aphysical
11927603
SCFD1_HUMANSCFD1physical
11927603
RAB1A_HUMANRAB1Aphysical
10903204
SCFD1_HUMANSCFD1physical
10903204
GOSR2_HUMANGOSR2physical
10903204
STX5_HUMANSTX5physical
10903204
USO1_HUMANUSO1physical
21147777
VINC_HUMANVCLphysical
22939629
XIAP_HUMANXIAPphysical
22939629
ZN593_HUMANZNF593physical
22939629
MYOME_HUMANPDE4DIPphysical
22792062
SC16A_HUMANSEC16Aphysical
22792062
KAPCA_HUMANPRKACAphysical
22792062
TRIPB_HUMANTRIP11physical
22792062
KAP3_HUMANPRKAR2Bphysical
22792062
CEP68_HUMANCEP68physical
22792062
F184A_HUMANFAM184Aphysical
22792062
GOGA2_HUMANGOLGA2physical
22792062
TRAF3_HUMANTRAF3physical
22792062
USO1_HUMANUSO1physical
25416956
AKAP9_HUMANAKAP9physical
25416956
DUS12_HUMANDUSP12physical
25416956
XPO7_HUMANXPO7physical
25416956
AT2L2_HUMANPHYKPLphysical
25416956
DPOE3_HUMANPOLE3physical
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 USO1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, AND MASS SPECTROMETRY.
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-942 AND SER-952, 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-942, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND MASSSPECTROMETRY.
"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-942 AND SER-952, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND MASSSPECTROMETRY.
"Phosphorylation of the vesicle docking protein p115 regulates itsassociation with the Golgi membrane.";
Sohda M., Misumi Y., Yano A., Takami N., Ikehara Y.;
J. Biol. Chem. 273:5385-5388(1998).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,MUTAGENESIS OF SER-942, AND PHOSPHORYLATION AT SER-942.

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