SEC63_HUMAN - dbPTM
SEC63_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEC63_HUMAN
UniProt AC Q9UGP8
Protein Name Translocation protein SEC63 homolog
Gene Name SEC63
Organism Homo sapiens (Human).
Sequence Length 760
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Required for integral membrane and secreted preprotein translocation across the endoplasmic reticulum membrane..
Protein Sequence MAGQQFQYDDSGNTFFYFLTSFVGLIVIPATYYLWPRDQNAEQIRLKNIRKVYGRCMWYRLRLLKPQPNIIPTVKKIVLLAGWALFLFLAYKVSKTDREYQEYNPYEVLNLDPGATVAEIKKQYRLLSLKYHPDKGGDEVMFMRIAKAYAALTDEESRKNWEEFGNPDGPQATSFGIALPAWIVDQKNSILVLLVYGLAFMVILPVVVGSWWYRSIRYSGDQILIRTTQIYTYFVYKTRNMDMKRLIMVLAGASEFDPQYNKDATSRPTDNILIPQLIREIGSINLKKNEPPLTCPYSLKARVLLLSHLARMKIPETLEEDQQFMLKKCPALLQEMVNVICQLIVMARNREEREFRAPTLASLENCMKLSQMAVQGLQQFKSPLLQLPHIEEDNLRRVSNHKKYKIKTIQDLVSLKESDRHTLLHFLEDEKYEEVMAVLGSFPYVTMDIKSQVLDDEDSNNITVGSLVTVLVKLTRQTMAEVFEKEQSICAAEEQPAEDGQGETNKNRTKGGWQQKSKGPKKTAKSKKKKPLKKKPTPVLLPQSKQQKQKQANGVVGNEAAVKEDEEEVSDKGSDSEEEETNRDSQSEKDDGSDRDSDREQDEKQNKDDEAEWQELQQSIQRKERALLETKSKITHPVYSLYFPEEKQEWWWLYIADRKEQTLISMPYHVCTLKDTEEVELKFPAPGKPGNYQYTVFLRSDSYMGLDQIKPLKLEVHEAKPVPENHPQWDTAIEGDEDQEDSEGFEDSFEEEEEEEEDDD
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
75UbiquitinationPNIIPTVKKIVLLAG
CCCCHHHHHHHHHHH		38.98-
76UbiquitinationNIIPTVKKIVLLAGW
CCCHHHHHHHHHHHH		33.44-
106PhosphorylationEYQEYNPYEVLNLDP
HHHHCCCCCCCCCCC		18.29-
121UbiquitinationGATVAEIKKQYRLLS
CCCHHHHHHHHEEHH		25.90-
128PhosphorylationKKQYRLLSLKYHPDK
HHHHEEHHCEECCCC		27.6624719451
1302-HydroxyisobutyrylationQYRLLSLKYHPDKGG
HHEEHHCEECCCCCC		37.83-
130UbiquitinationQYRLLSLKYHPDKGG
HHEEHHCEECCCCCC		37.8321890473
135UbiquitinationSLKYHPDKGGDEVMF
HCEECCCCCCCEEHH		70.0621890473
147UbiquitinationVMFMRIAKAYAALTD
EHHHHHHHHHHHCCC		39.2921890473
1472-HydroxyisobutyrylationVMFMRIAKAYAALTD
EHHHHHHHHHHHCCC		39.29-
149PhosphorylationFMRIAKAYAALTDEE
HHHHHHHHHHCCCHH		7.5324719451
153PhosphorylationAKAYAALTDEESRKN
HHHHHHCCCHHHHHC		36.32-
157PhosphorylationAALTDEESRKNWEEF
HHCCCHHHHHCHHHH		46.6524719451
218PhosphorylationWWYRSIRYSGDQILI
HHHHHCCCCCCEEEE		18.4824719451
219PhosphorylationWYRSIRYSGDQILIR
HHHHCCCCCCEEEEE		26.5024719451
231PhosphorylationLIRTTQIYTYFVYKT
EEEEEEEEEEEEEEC		5.8824719451
265PhosphorylationPQYNKDATSRPTDNI
CCCCCCCCCCCCCCC		35.0920068231
266PhosphorylationQYNKDATSRPTDNIL
CCCCCCCCCCCCCCH		37.6720068231
269PhosphorylationKDATSRPTDNILIPQ
CCCCCCCCCCCHHHH		40.3420068231
283PhosphorylationQLIREIGSINLKKNE
HHHHHHCCCCCCCCC		17.6120068231
287UbiquitinationEIGSINLKKNEPPLT
HHCCCCCCCCCCCCC		49.41-
288UbiquitinationIGSINLKKNEPPLTC
HCCCCCCCCCCCCCC		70.48-
294PhosphorylationKKNEPPLTCPYSLKA
CCCCCCCCCCCCHHH		19.7423403867
297PhosphorylationEPPLTCPYSLKARVL
CCCCCCCCCHHHHHH		28.8723403867
298PhosphorylationPPLTCPYSLKARVLL
CCCCCCCCHHHHHHH		14.4524719451
300UbiquitinationLTCPYSLKARVLLLS
CCCCCCHHHHHHHHH		28.3621890473
3002-HydroxyisobutyrylationLTCPYSLKARVLLLS
CCCCCCHHHHHHHHH		28.36-
307PhosphorylationKARVLLLSHLARMKI
HHHHHHHHHHHHCCC		19.2019060867
313UbiquitinationLSHLARMKIPETLEE
HHHHHHCCCCCCHHH		49.94-
327UbiquitinationEDQQFMLKKCPALLQ
HHHHHHHHHCHHHHH		40.31-
368UbiquitinationASLENCMKLSQMAVQ
HHHHHHHHHHHHHHH		47.38-
381UbiquitinationVQGLQQFKSPLLQLP
HHHHHHHCCCHHCCC		46.9921890473
402MethylationLRRVSNHKKYKIKTI
CHHHHCCCCCCCEEH		63.15-
402TrimethylationLRRVSNHKKYKIKTI
CHHHHCCCCCCCEEH		63.15-
403TrimethylationRRVSNHKKYKIKTIQ
HHHHCCCCCCCEEHH		44.20-
403MethylationRRVSNHKKYKIKTIQ
HHHHCCCCCCCEEHH		44.20-
407UbiquitinationNHKKYKIKTIQDLVS
CCCCCCCEEHHHHHH		35.1121890473
408PhosphorylationHKKYKIKTIQDLVSL
CCCCCCEEHHHHHHC		27.6122210691
414PhosphorylationKTIQDLVSLKESDRH
EEHHHHHHCCHHCCC		40.8122210691
4162-HydroxyisobutyrylationIQDLVSLKESDRHTL
HHHHHHCCHHCCCHH		47.90-
416UbiquitinationIQDLVSLKESDRHTL
HHHHHHCCHHCCCHH		47.90-
416AcetylationIQDLVSLKESDRHTL
HHHHHHCCHHCCCHH		47.9027452117
451PhosphorylationYVTMDIKSQVLDDED
EEEEEEHHHCCCCCC		26.34-
475PhosphorylationVTVLVKLTRQTMAEV
HHHHHHHHHHHHHHH		18.27-
478PhosphorylationLVKLTRQTMAEVFEK
HHHHHHHHHHHHHHH		18.30-
488PhosphorylationEVFEKEQSICAAEEQ
HHHHHHHHCCEEECC		22.2621815630
506UbiquitinationDGQGETNKNRTKGGW
CCCCCCCCCCCCCCH		56.05-
510UbiquitinationETNKNRTKGGWQQKS
CCCCCCCCCCHHCCC		52.79-
517PhosphorylationKGGWQQKSKGPKKTA
CCCHHCCCCCCCCCC		38.2123684312
527AcetylationPKKTAKSKKKKPLKK
CCCCCCCCCCCCCCC		68.8370999
537PhosphorylationKPLKKKPTPVLLPQS
CCCCCCCCCCCCCCC		34.6025159151
544PhosphorylationTPVLLPQSKQQKQKQ
CCCCCCCCHHHHHHH		30.4125159151
570PhosphorylationKEDEEEVSDKGSDSE
CCCHHHHCCCCCCCH		36.5625849741
574PhosphorylationEEVSDKGSDSEEEET
HHHCCCCCCCHHHHC		43.6429255136
576PhosphorylationVSDKGSDSEEEETNR
HCCCCCCCHHHHCCC		48.9129255136
585PhosphorylationEEETNRDSQSEKDDG
HHHCCCCCCCCCCCC		32.1625627689
593PhosphorylationQSEKDDGSDRDSDRE
CCCCCCCCCCCCHHH		36.1529255136
597PhosphorylationDDGSDRDSDREQDEK
CCCCCCCCHHHHHHH		39.1929255136
607UbiquitinationEQDEKQNKDDEAEWQ
HHHHHHCHHCHHHHH		65.15-
623UbiquitinationLQQSIQRKERALLET
HHHHHHHHHHHHHHC		34.87-
6312-HydroxyisobutyrylationERALLETKSKITHPV
HHHHHHCHHCCCCCE		40.14-
631UbiquitinationERALLETKSKITHPV
HHHHHHCHHCCCCCE		40.14-
633UbiquitinationALLETKSKITHPVYS
HHHHCHHCCCCCEEE		53.8621890473
642PhosphorylationTHPVYSLYFPEEKQE
CCCEEEEECCHHHHC		15.90-
6592-HydroxyisobutyrylationWLYIADRKEQTLISM
EEEEEECCCCEEEEC		55.51-
688UbiquitinationLKFPAPGKPGNYQYT
EECCCCCCCCCEEEE		49.0121890473
692PhosphorylationAPGKPGNYQYTVFLR
CCCCCCCEEEEEEEE		14.60-
694PhosphorylationGKPGNYQYTVFLRSD
CCCCCEEEEEEEECC		8.43-
695PhosphorylationKPGNYQYTVFLRSDS
CCCCEEEEEEEECCC		6.83-
700PhosphorylationQYTVFLRSDSYMGLD
EEEEEEECCCCCCCC		32.8123312004
702PhosphorylationTVFLRSDSYMGLDQI
EEEEECCCCCCCCCC		20.4723312004
703PhosphorylationVFLRSDSYMGLDQIK
EEEECCCCCCCCCCC		10.5323312004
710UbiquitinationYMGLDQIKPLKLEVH
CCCCCCCCCEEEEEE		38.3721890473
742PhosphorylationGDEDQEDSEGFEDSF
CCCCCCCCCCCCCCC		38.5818669648
748PhosphorylationDSEGFEDSFEEEEEE
CCCCCCCCCHHHHHH		27.6218669648
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
574SPhosphorylationKinaseCK2A1P68400
PSP
574SPhosphorylationKinaseCK2BP67870
PSP
576SPhosphorylationKinaseCK2A1P68400
PSP
576SPhosphorylationKinaseCK2BP67870
PSP
748SPhosphorylationKinaseCK2A1P68400
PSP
748SPhosphorylationKinaseCK2BP67870
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEC63_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 SEC63_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACADM_HUMANACADMphysical
26344197
RS5_HUMANRPS5physical
26344197
GRP78_HUMANHSPA5physical
26085089
Drug and Disease Associations
Kegg Disease
H00545 Polycystic liver disease
OMIM Disease
174050Polycystic liver disease (PCLD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEC63_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-742 AND SER-748, ANDMASS SPECTROMETRY.

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