SSRB_HUMAN - dbPTM
SSRB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSRB_HUMAN
UniProt AC P43308
Protein Name Translocon-associated protein subunit beta
Gene Name SSR2
Organism Homo sapiens (Human).
Sequence Length 183
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein.
Protein Description TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins..
Protein Sequence MRLLSFVVLALFAVTQAEEGARLLASKSLLNRYAVEGRDLTLQYNIYNVGSSAALDVELSDDSFPPEDFGIVSGMLNVKWDRIAPASNVSHTVVLRPLKAGYFNFTSATITYLAQEDGPVVIGSTSAPGQGGILAQREFDRRFSPHFLDWAAFGVMTLPSIGIPLLLWYSSKRKYDTPKTKKN
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
27UbiquitinationGARLLASKSLLNRYA
HHHHHHCHHHHHHHH
39.2421963094
272-HydroxyisobutyrylationGARLLASKSLLNRYA
HHHHHHCHHHHHHHH
39.24-
32MethylationASKSLLNRYAVEGRD
HCHHHHHHHHHCCCC
22.28115917889
46UbiquitinationDLTLQYNIYNVGSSA
CEEEEEEEEECCCCE
1.9421906983
87O-linked_GlycosylationWDRIAPASNVSHTVV
CEEECCCCCCCEEEE
36.3830059200
88N-linked_GlycosylationDRIAPASNVSHTVVL
EEECCCCCCCEEEEE
41.2212754519
90O-linked_GlycosylationIAPASNVSHTVVLRP
ECCCCCCCEEEEECE
20.0730059200
104N-linked_GlycosylationPLKAGYFNFTSATIT
EECCCCCEECEEEEE
30.7012754519
125O-linked_GlycosylationGPVVIGSTSAPGQGG
CCEEEECCCCCCCCC
24.56OGP
157PhosphorylationWAAFGVMTLPSIGIP
HHHHCCCCCHHCCCC
32.8627251275
160PhosphorylationFGVMTLPSIGIPLLL
HCCCCCHHCCCCHHH
36.2427251275
169PhosphorylationGIPLLLWYSSKRKYD
CCCHHHHHHCCCCCC
11.7527251275
171PhosphorylationPLLLWYSSKRKYDTP
CHHHHHHCCCCCCCC
22.3027251275
177PhosphorylationSSKRKYDTPKTKKN-
HCCCCCCCCCCCCC-
24.4821857030
182UbiquitinationYDTPKTKKN------
CCCCCCCCC------
73.4624816145
201Ubiquitination-------------------------
-------------------------
24816145

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 SSRB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSRB_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 SSRB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRPRA_HUMANSRPRphysical
3021779
RPN1_HUMANRPN1physical
26344197
QCR2_HUMANUQCRC2physical
26344197

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 SSRB_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-88 AND ASN-104, AND MASSSPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-88 AND ASN-104.

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