SEC62_HUMAN - dbPTM
SEC62_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEC62_HUMAN
UniProt AC Q99442
Protein Name Translocation protein SEC62
Gene Name SEC62
Organism Homo sapiens (Human).
Sequence Length 399
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Required for preprotein translocation..
Protein Sequence MAERRRHKKRIQEVGEPSKEEKAVAKYLRFNCPTKSTNMMGHRVDYFIASKAVDCLLDSKWAKAKKGEEALFTTRESVVDYCNRLLKKQFFHRALKVMKMKYDKDIKKEKDKGKAESGKEEDKKSKKENIKDEKTKKEKEKKKDGEKEESKKEETPGTPKKKETKKKFKLEPHDDQVFLDGNEVYVWIYDPVHFKTFVMGLILVIAVIAATLFPLWPAEMRVGVYYLSVGAGCFVASILLLAVARCILFLIIWLITGGRHHFWFLPNLTADVGFIDSFRPLYTHEYKGPKADLKKDEKSETKKQQKSDSEEKSDSEKKEDEEGKVGPGNHGTEGSGGERHSDTDSDRREDDRSQHSSGNGNDFEMITKEELEQQTDGDCEEDEEEENDGETPKSSHEKS
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
9UbiquitinationAERRRHKKRIQEVGE
HHHHHHHHHHHHHCC		48.92-
19AcetylationQEVGEPSKEEKAVAK
HHHCCCCHHHHHHHH		79.2826051181
19UbiquitinationQEVGEPSKEEKAVAK
HHHCCCCHHHHHHHH		79.2821906983
22UbiquitinationGEPSKEEKAVAKYLR
CCCCHHHHHHHHHHH		49.61-
26UbiquitinationKEEKAVAKYLRFNCP
HHHHHHHHHHHHCCC		37.91-
27PhosphorylationEEKAVAKYLRFNCPT
HHHHHHHHHHHCCCC		8.0523828894
35UbiquitinationLRFNCPTKSTNMMGH
HHHCCCCCCCCCCCC		40.19-
35MalonylationLRFNCPTKSTNMMGH
HHHCCCCCCCCCCCC		40.1926320211
46PhosphorylationMMGHRVDYFIASKAV
CCCCCCCHHHHHHHH		8.2725884760
50PhosphorylationRVDYFIASKAVDCLL
CCCHHHHHHHHHHHH		19.1428152594
51AcetylationVDYFIASKAVDCLLD
CCHHHHHHHHHHHHC		43.3326051181
51UbiquitinationVDYFIASKAVDCLLD
CCHHHHHHHHHHHHC		43.3321906983
60UbiquitinationVDCLLDSKWAKAKKG
HHHHHCCHHHHCCCC		51.33-
63UbiquitinationLLDSKWAKAKKGEEA
HHCCHHHHCCCCCCC		60.67-
65UbiquitinationDSKWAKAKKGEEALF
CCHHHHCCCCCCCCC		61.68-
66UbiquitinationSKWAKAKKGEEALFT
CHHHHCCCCCCCCCC		76.142190698
73PhosphorylationKGEEALFTTRESVVD
CCCCCCCCCHHHHHH		26.2922210691
74PhosphorylationGEEALFTTRESVVDY
CCCCCCCCHHHHHHH		25.7122210691
81PhosphorylationTRESVVDYCNRLLKK
CHHHHHHHHHHHHHH		4.6822210691
88UbiquitinationYCNRLLKKQFFHRAL
HHHHHHHHHHHHHHH		52.92-
110AcetylationDKDIKKEKDKGKAES
CCCHHHHHHCCCCCC		73.88130211
114AcetylationKKEKDKGKAESGKEE
HHHHHCCCCCCCCHH		55.5119822365
117PhosphorylationKDKGKAESGKEEDKK
HHCCCCCCCCHHHHH		61.0926657352
119AcetylationKGKAESGKEEDKKSK
CCCCCCCCHHHHHHH		68.1819822375
123AcetylationESGKEEDKKSKKENI
CCCCHHHHHHHHHCC		63.3319822385
125PhosphorylationGKEEDKKSKKENIKD
CCHHHHHHHHHCCCC		55.4929514088
134UbiquitinationKENIKDEKTKKEKEK
HHCCCCHHHHHHHHH		75.64-
135O-linked_GlycosylationENIKDEKTKKEKEKK
HCCCCHHHHHHHHHC		45.3530620550
141AcetylationKTKKEKEKKKDGEKE
HHHHHHHHCCCCCHH		75.977262011
143AcetylationKKEKEKKKDGEKEES
HHHHHHCCCCCHHHH		80.28130215
150PhosphorylationKDGEKEESKKEETPG
CCCCHHHHHCCCCCC		50.5529255136
155PhosphorylationEESKKEETPGTPKKK
HHHHCCCCCCCCCCH		28.2729255136
158PhosphorylationKKEETPGTPKKKETK
HCCCCCCCCCCHHHC		32.8929255136
1602-HydroxyisobutyrylationEETPGTPKKKETKKK
CCCCCCCCCHHHCCC		76.06-
237PhosphorylationGAGCFVASILLLAVA
CCHHHHHHHHHHHHH		14.41-
307PhosphorylationETKKQQKSDSEEKSD
HHHHHHHCCCHHCCH		41.8726657352
309PhosphorylationKKQQKSDSEEKSDSE
HHHHHCCCHHCCHHH		55.5423911959
313PhosphorylationKSDSEEKSDSEKKED
HCCCHHCCHHHHHHC		50.0417137347
315PhosphorylationDSEEKSDSEKKEDEE
CCHHCCHHHHHHCCC		59.4130576142
332PhosphorylationVGPGNHGTEGSGGER
CCCCCCCCCCCCCCC		29.6229255136
335PhosphorylationGNHGTEGSGGERHSD
CCCCCCCCCCCCCCC		37.0829255136
341PhosphorylationGSGGERHSDTDSDRR
CCCCCCCCCCCCCCC		48.7229255136
343PhosphorylationGGERHSDTDSDRRED
CCCCCCCCCCCCCCC		40.1829255136
345PhosphorylationERHSDTDSDRREDDR
CCCCCCCCCCCCCHH		34.8029255136
353PhosphorylationDRREDDRSQHSSGNG
CCCCCHHHHCCCCCC		38.9623401153
356PhosphorylationEDDRSQHSSGNGNDF
CCHHHHCCCCCCCCC		32.1029255136
357PhosphorylationDDRSQHSSGNGNDFE
CHHHHCCCCCCCCCE		33.8730266825
367PhosphorylationGNDFEMITKEELEQQ
CCCCEECCHHHHHHC		30.9723927012
375PhosphorylationKEELEQQTDGDCEED
HHHHHHCCCCCCCCC		41.4625159151
391PhosphorylationEEENDGETPKSSHEK
HHCCCCCCCCCCCCC		41.3623927012
394PhosphorylationNDGETPKSSHEKS--
CCCCCCCCCCCCC--		37.8221712546
395PhosphorylationDGETPKSSHEKS---
CCCCCCCCCCCC---		41.6228165663
399PhosphorylationPKSSHEKS-------
CCCCCCCC-------		42.3323312004
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 SEC62_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEC62_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 SEC62_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEC62_YEASTSEC62genetic
20071467
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 SEC62_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-158 AND SER-313, ANDMASS SPECTROMETRY.
"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 THR-375, AND MASSSPECTROMETRY.

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