SPCS3_HUMAN - dbPTM
SPCS3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPCS3_HUMAN
UniProt AC P61009
Protein Name Signal peptidase complex subunit 3
Gene Name SPCS3
Organism Homo sapiens (Human).
Sequence Length 180
Subcellular Localization Microsome membrane
Single-pass type II membrane protein . Endoplasmic reticulum membrane
Single-pass type II membrane protein .
Protein Description Component of the microsomal signal peptidase complex which removes signal peptides and other N-terminal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum..
Protein Sequence MNTVLSRANSLFAFSLSVMAALTFGCFITTAFKDRSVPVRLHVSRIMLKNVEDFTGPRERSDLGFITFDITADLENIFDWNVKQLFLYLSAEYSTKNNALNQVVLWDKIVLRGDNPKLLLKDMKTKYFFFDDGNGLKGNRNVTLTLSWNVVPNAGILPLVTGSGHVSVPFPDTYEITKSY
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
3Phosphorylation-----MNTVLSRANS
-----CCCHHHHHHH
22.8624043423
6Phosphorylation--MNTVLSRANSLFA
--CCCHHHHHHHHHH
25.6324043423
10PhosphorylationTVLSRANSLFAFSLS
CHHHHHHHHHHHHHH
24.7124043423
15PhosphorylationANSLFAFSLSVMAAL
HHHHHHHHHHHHHHH
19.1224043423
17PhosphorylationSLFAFSLSVMAALTF
HHHHHHHHHHHHHHH
14.5124043423
23PhosphorylationLSVMAALTFGCFITT
HHHHHHHHHCHHHHH
17.1624043423
29PhosphorylationLTFGCFITTAFKDRS
HHHCHHHHHHCCCCC
7.5724043423
30PhosphorylationTFGCFITTAFKDRSV
HHCHHHHHHCCCCCC
25.8624043423
49UbiquitinationHVSRIMLKNVEDFTG
EEEEEEECCHHHCCC
41.3827667366
49AcetylationHVSRIMLKNVEDFTG
EEEEEEECCHHHCCC
41.3827452117
492-HydroxyisobutyrylationHVSRIMLKNVEDFTG
EEEEEEECCHHHCCC
41.38-
55PhosphorylationLKNVEDFTGPRERSD
ECCHHHCCCCCCCCC
59.6124719451
71PhosphorylationGFITFDITADLENIF
CEEEEEEECCHHHHC
18.90-
108UbiquitinationNQVVLWDKIVLRGDN
CCEEEEEEEEECCCC
24.1122817900
117UbiquitinationVLRGDNPKLLLKDMK
EECCCCCCEEEECCC
59.0022817900
121UbiquitinationDNPKLLLKDMKTKYF
CCCCEEEECCCCCEE
56.6022817900
1212-HydroxyisobutyrylationDNPKLLLKDMKTKYF
CCCCEEEECCCCCEE
56.60-
124UbiquitinationKLLLKDMKTKYFFFD
CEEEECCCCCEEEEE
52.5822817900
125PhosphorylationLLLKDMKTKYFFFDD
EEEECCCCCEEEEEC
25.0827174698
126UbiquitinationLLKDMKTKYFFFDDG
EEECCCCCEEEEECC
34.2421906983
1262-HydroxyisobutyrylationLLKDMKTKYFFFDDG
EEECCCCCEEEEECC
34.24-
126AcetylationLLKDMKTKYFFFDDG
EEECCCCCEEEEECC
34.2427452117
127PhosphorylationLKDMKTKYFFFDDGN
EECCCCCEEEEECCC
15.7325693802
137UbiquitinationFDDGNGLKGNRNVTL
EECCCCCCCCCEEEE
56.3827667366
141N-linked_GlycosylationNGLKGNRNVTLTLSW
CCCCCCCEEEEEEEE
34.8219159218

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 SPCS3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPCS3_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 SPCS3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SPCS3_HUMAN !!

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 SPCS3_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-141, AND MASSSPECTROMETRY.

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