SPCS1_HUMAN - dbPTM
SPCS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPCS1_HUMAN
UniProt AC Q9Y6A9
Protein Name Signal peptidase complex subunit 1
Gene Name SPCS1
Organism Homo sapiens (Human).
Sequence Length 102
Subcellular Localization Microsome membrane
Multi-pass membrane protein. Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum..
Protein Sequence MLEHLSSLPTQMDYKGQKLAEQMFQGIILFSAIVGFIYGYVAEQFGWTVYIVMAGFAFSCLLTLPPWPIYRRHPLKWLPVQESSTDDKKPGERKIKRHAKNN
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
14PhosphorylationSLPTQMDYKGQKLAE
CCCCCCCHHCHHHHH
50.33-
15AcetylationLPTQMDYKGQKLAEQ
CCCCCCHHCHHHHHH
33.6526051181
15UbiquitinationLPTQMDYKGQKLAEQ
CCCCCCHHCHHHHHH
33.65-
18UbiquitinationQMDYKGQKLAEQMFQ
CCCHHCHHHHHHHHH
28.82-
76UbiquitinationIYRRHPLKWLPVQES
CCCCCCCCCCCCCCC
23.64-
82UbiquitinationLKWLPVQESSTDDKK
CCCCCCCCCCCCCCC
51.0721890473
83PhosphorylationKWLPVQESSTDDKKP
CCCCCCCCCCCCCCC
24.5130266825
84PhosphorylationWLPVQESSTDDKKPG
CCCCCCCCCCCCCCC
33.1830266825
85UbiquitinationLPVQESSTDDKKPGE
CCCCCCCCCCCCCCH
59.3322817900
85PhosphorylationLPVQESSTDDKKPGE
CCCCCCCCCCCCCCH
59.3330266825
882-HydroxyisobutyrylationQESSTDDKKPGERKI
CCCCCCCCCCCHHHH
53.68-
88MalonylationQESSTDDKKPGERKI
CCCCCCCCCCCHHHH
53.6826320211
89UbiquitinationESSTDDKKPGERKIK
CCCCCCCCCCHHHHH
32.17-
89AcetylationESSTDDKKPGERKIK
CCCCCCCCCCHHHHH
32.1725953088
89MalonylationESSTDDKKPGERKIK
CCCCCCCCCCHHHHH
32.1726320211
94AcetylationDKKPGERKIKRHAKN
CCCCCHHHHHHHHHC
1.397290171
100AcetylationRKIKRHAKNN-----
HHHHHHHHCC-----
2.787290181
143Ubiquitination------------------------------------------------
------------------------------------------------
51.6523000965
150Phosphorylation-------------------------------------------------------
-------------------------------------------------------
22.8024719451
151Phosphorylation--------------------------------------------------------
--------------------------------------------------------
34.7927251275
155Malonylation------------------------------------------------------------
------------------------------------------------------------
64.7726320211
156Malonylation-------------------------------------------------------------
-------------------------------------------------------------
66.3126320211
156Ubiquitination-------------------------------------------------------------
-------------------------------------------------------------
66.31-

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 SPCS1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPCS1_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 SPCS1_HUMAN !!

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

Oops, there are no PPI records of SPCS1_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 SPCS1_HUMAN

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Related Literatures of Post-Translational Modification

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