SEC63_MOUSE - dbPTM
SEC63_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEC63_MOUSE
UniProt AC Q8VHE0
Protein Name Translocation protein SEC63 homolog
Gene Name Sec63
Organism Mus musculus (Mouse).
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 MAGQQFQYDDSGNTFFYFLTSFVGLIVIPATYYLWPRDQNAEQIRLKNIRKVYGRCMWYRLRLLKPQPNIIPTVKKIVLLAGWALFLFLAYKVSKTDREYQEYNPYEVLNLDPGATVAEIKKQYRLLSLKYHPDKGGDEVMFMRIAKAYAALTDEESRKNWEEFGNPDGPQATSFGIALPAWIVDQKNSILVLLVYGLAFMVILPVVVGSWWYRSIRYSGDQILIRTTQIYTYFVYKTRNMDMKRLIMVLAGASEFDPQYNKDSTSRPTDNILIPQLIREIGSINLKKNEPPLTCPYSLKARVLLLSHLARMKIPETLEEDQQFMLKKCPALLQEMVNVICQLIIMARSREEREFRAPTLASLENCMKLSQMAVQGLQQFKSPLLQLPHIEEDNLRRVSNHKKYKIKTIQDLVSLKESDRHSLLHFLEDEKYEEVMAVLGSFPYVTMDIKSQVLDDEDSNNITVGSLVTVLVKLTRQTMAEVFEKEQSICAAEEQPTEDGQSDANKIKAKGGWQQKNKGPKKMPKSKKKKPLKKKPTTVPLPQAKQQKQKQANGVVGSEAAIKEEEDDISDKGSDSEEEETNRDSQSEKEDGSDRESDREQDEKQSKDDEAEWQELQQSIQRKERALLETKSKITHPVYSLYFPEEKQEWWWLYIADRKEQTLISMPYHVCTLKDTEEVELKFPAPGKPGNYQYTVFLRSDSYMGLDQIKPLKLEVHEAKPVPENHPQWDTAIEGDEDQEDSEGFEDSFEEEEEEEEGGD
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
41UbiquitinationLWPRDQNAEQIRLKN
CCCCCCCHHHHHHHH		12.3927667366
50UbiquitinationQIRLKNIRKVYGRCM
HHHHHHHHHHHHHHH		31.6127667366
147UbiquitinationVMFMRIAKAYAALTD
EHHHHHHHHHHHCCC		39.2922790023
179UbiquitinationATSFGIALPAWIVDQ
CCCCEEEECCHHHCC		2.5527667366
187UbiquitinationPAWIVDQKNSILVLL
CCHHHCCCCHHHHHH		48.4727667366
267UbiquitinationYNKDSTSRPTDNILI
CCCCCCCCCCCCCHH		37.9227667366
276UbiquitinationTDNILIPQLIREIGS
CCCCHHHHHHHHHCC		42.3927667366
283PhosphorylationQLIREIGSINLKKNE
HHHHHHCCCCCCCCC		17.6129176673
287UbiquitinationEIGSINLKKNEPPLT
HHCCCCCCCCCCCCC		49.4127667366
307PhosphorylationKARVLLLSHLARMKI
HHHHHHHHHHHHCCC		19.2017203969
327UbiquitinationEDQQFMLKKCPALLQ
HHHHHHHHHCHHHHH		40.3127667366
366S-palmitoylationTLASLENCMKLSQMA
HHHHHHHHHHHHHHH		1.5328526873
368UbiquitinationASLENCMKLSQMAVQ
HHHHHHHHHHHHHHH		47.3822790023
381UbiquitinationVQGLQQFKSPLLQLP
HHHHHHHCCCHHCCC		46.9922790023
405UbiquitinationVSNHKKYKIKTIQDL
HHCCCCCCCEEHHHH		46.7527667366
407UbiquitinationNHKKYKIKTIQDLVS
CCCCCCCEEHHHHHH		35.1122790023
416UbiquitinationIQDLVSLKESDRHSL
HHHHHHCCHHHCCHH		47.9022790023
432PhosphorylationHFLEDEKYEEVMAVL
HHHCCCCHHHHHHHH		18.4428059163
488PhosphorylationEVFEKEQSICAAEEQ
HHHHHHHHHHHHCCC		22.2625521595
493UbiquitinationEQSICAAEEQPTEDG
HHHHHHHCCCCCCCC		38.3427667366
510MalonylationDANKIKAKGGWQQKN
HHHHHHHCCCHHHCC		53.6126320211
526PhosphorylationGPKKMPKSKKKKPLK
CCCCCCCCCCCCCCC		43.7822802335
537PhosphorylationKPLKKKPTTVPLPQA
CCCCCCCCCCCCHHH		49.67-
544UbiquitinationTTVPLPQAKQQKQKQ
CCCCCHHHHHHHHHH		15.0827667366
545UbiquitinationTVPLPQAKQQKQKQA
CCCCHHHHHHHHHHH		48.2727667366
558PhosphorylationQANGVVGSEAAIKEE
HHCCCCCCHHHHHHC		16.6822817900
570PhosphorylationKEEEDDISDKGSDSE
HHCCCCCCCCCCCCH		40.0223375375
574PhosphorylationDDISDKGSDSEEEET
CCCCCCCCCCHHHHH		43.6425195567
576PhosphorylationISDKGSDSEEEETNR
CCCCCCCCHHHHHCC		48.9125195567
581PhosphorylationSDSEEEETNRDSQSE
CCCHHHHHCCCCHHH		38.5423375375
585PhosphorylationEEETNRDSQSEKEDG
HHHHCCCCHHHCCCC		32.1625195567
587PhosphorylationETNRDSQSEKEDGSD
HHCCCCHHHCCCCCC		55.3725195567
593PhosphorylationQSEKEDGSDRESDRE
HHHCCCCCCCCHHHH		45.9025521595
597PhosphorylationEDGSDRESDREQDEK
CCCCCCCHHHHHHHH		42.7525521595
606PhosphorylationREQDEKQSKDDEAEW
HHHHHHHCHHHHHHH		49.4721743459
632UbiquitinationRALLETKSKITHPVY
HHHHHCHHCCCCCEE		36.3927667366
633UbiquitinationALLETKSKITHPVYS
HHHHCHHCCCCCEEE		53.8622790023
688UbiquitinationLKFPAPGKPGNYQYT
EECCCCCCCCCEEEE		49.0122790023
710UbiquitinationYMGLDQIKPLKLEVH
CCCCCCCCCEEEEEE		38.3722790023
731PhosphorylationENHPQWDTAIEGDED
CCCCCCCCCCCCCCC		26.9523140645
742PhosphorylationGDEDQEDSEGFEDSF
CCCCCCCCCCCCHHC		38.5821743459
748PhosphorylationDSEGFEDSFEEEEEE
CCCCCCHHCHHHHHH		27.6221743459
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 SEC63_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEC63_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SEC63_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEC63_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593 AND SER-597, ANDMASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory