RER1_HUMAN - dbPTM
RER1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RER1_HUMAN
UniProt AC O15258
Protein Name Protein RER1
Gene Name RER1
Organism Homo sapiens (Human).
Sequence Length 196
Subcellular Localization Golgi apparatus membrane
Multi-pass membrane protein.
Protein Description Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment..
Protein Sequence MSEGDSVGESVHGKPSVVYRFFTRLGQIYQSWLDKSTPYTAVRWVVTLGLSFVYMIRVYLLQGWYIVTYALGIYHLNLFIAFLSPKVDPSLMEDSDDGPSLPTKQNEEFRPFIRRLPEFKFWHAATKGILVAMVCTFFDAFNVPVFWPILVMYFIMLFCITMKRQIKHMIKYRYIPFTHGKRRYRGKEDAGKAFAS
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
2Phosphorylation------MSEGDSVGE
------CCCCCCCCC
50.7329255136
2Acetylation------MSEGDSVGE
------CCCCCCCCC
50.7320068231
6Phosphorylation--MSEGDSVGESVHG
--CCCCCCCCCCCCC
42.7622167270
10PhosphorylationEGDSVGESVHGKPSV
CCCCCCCCCCCCHHH
17.3122167270
14MalonylationVGESVHGKPSVVYRF
CCCCCCCCHHHHHHH
21.1726320211
14UbiquitinationVGESVHGKPSVVYRF
CCCCCCCCHHHHHHH
21.1721890473
16PhosphorylationESVHGKPSVVYRFFT
CCCCCCHHHHHHHHH
27.9229396449
19PhosphorylationHGKPSVVYRFFTRLG
CCCHHHHHHHHHHHH
10.2729396449
35UbiquitinationIYQSWLDKSTPYTAV
HHHHHHCCCCCCHHH
54.8021906983
54PhosphorylationTLGLSFVYMIRVYLL
HHHHHHHHHHHHHHH
5.70-
59PhosphorylationFVYMIRVYLLQGWYI
HHHHHHHHHHCHHHH
7.58-
84PhosphorylationNLFIAFLSPKVDPSL
HHHHHHHCCCCCHHH
19.07-
90PhosphorylationLSPKVDPSLMEDSDD
HCCCCCHHHCCCCCC
35.5730266825
92SulfoxidationPKVDPSLMEDSDDGP
CCCCHHHCCCCCCCC
6.7121406390
95PhosphorylationDPSLMEDSDDGPSLP
CHHHCCCCCCCCCCC
25.0529255136
100PhosphorylationEDSDDGPSLPTKQNE
CCCCCCCCCCCCCCH
53.1330266825
103PhosphorylationDDGPSLPTKQNEEFR
CCCCCCCCCCCHHCH
51.0223927012
171UbiquitinationRQIKHMIKYRYIPFT
HHHHHHHHHCCCCCC
18.99-
174PhosphorylationKHMIKYRYIPFTHGK
HHHHHHCCCCCCCCC
15.1728152594
181UbiquitinationYIPFTHGKRRYRGKE
CCCCCCCCCCCCCCC
26.5421890473
192UbiquitinationRGKEDAGKAFAS---
CCCCCCHHHCCC---
41.89-

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 RER1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RER1_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 RER1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MIC60_HUMANIMMTphysical
16169070
HAP1_HUMANHAP1physical
16169070
SH3G3_HUMANSH3GL3physical
16169070
PMP22_HUMANPMP22physical
25385046
STX12_HUMANSTX12physical
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 RER1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-95, AND MASSSPECTROMETRY.

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