ERD21_HUMAN - dbPTM
ERD21_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERD21_HUMAN
UniProt AC P24390
Protein Name ER lumen protein-retaining receptor 1
Gene Name KDELR1
Organism Homo sapiens (Human).
Sequence Length 212
Subcellular Localization Cytoplasmic vesicle, COPI-coated vesicle membrane
Multi-pass membrane protein . Endoplasmic reticulum membrane
Multi-pass membrane protein . Endoplasmic reticulum-Golgi intermediate compartment membrane .
Protein Description Required for the retention of luminal endoplasmic reticulum resident proteins via vesicular recycling. This receptor recognizes the C-terminal K-D-E-L motif. COPI-coated transport intermediates, either in the form of round vesicles or as tubular processes, mediate retrograde traffic of the KDEL receptor-ligand complexes. Also required for normal vesicular traffic through the Golgi..
Protein Sequence MNLFRFLGDLSHLLAIILLLLKIWKSRSCAGISGKSQVLFAVVFTARYLDLFTNYISLYNTCMKVVYIACSFTTVWLIYSKFKATYDGNHDTFRVEFLVVPTAILAFLVNHDFTPLEILWTFSIYLESVAILPQLFMVSKTGEAETITSHYLFALGVYRTLYLFNWIWRYHFEGFFDLIAIVAGLVQTVLYCDFFYLYITKVLKGKKLSLPA
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
61PhosphorylationNYISLYNTCMKVVYI
HHHHHHHHHHHHHHH
10.62-
64UbiquitinationSLYNTCMKVVYIACS
HHHHHHHHHHHHHHC
30.6033845483
81UbiquitinationTVWLIYSKFKATYDG
HHHHHHHHHHEEECC
33.6322817900
83UbiquitinationWLIYSKFKATYDGNH
HHHHHHHHEEECCCC
43.4822817900
83UbiquitinationWLIYSKFKATYDGNH
HHHHHHHHEEECCCC
43.4821890473
141PhosphorylationQLFMVSKTGEAETIT
HHHCCCCCCCCEEHH
32.5225954137
146PhosphorylationSKTGEAETITSHYLF
CCCCCCEEHHHHHHH
36.2825954137
148PhosphorylationTGEAETITSHYLFAL
CCCCEEHHHHHHHHH
19.5121406692
149PhosphorylationGEAETITSHYLFALG
CCCEEHHHHHHHHHH
13.2921406692
151PhosphorylationAETITSHYLFALGVY
CEEHHHHHHHHHHHH
11.8625954137
158PhosphorylationYLFALGVYRTLYLFN
HHHHHHHHHHHHHHH
8.9721406692
191PhosphorylationGLVQTVLYCDFFYLY
HHHHHHHHHCHHHHH
5.9022817900
196PhosphorylationVLYCDFFYLYITKVL
HHHHCHHHHHHHHHH
9.8922817900
198PhosphorylationYCDFFYLYITKVLKG
HHCHHHHHHHHHHCC
8.6522817900
209PhosphorylationVLKGKKLSLPA----
HHCCCCCCCCC----
40.9828355574

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
209SPhosphorylationKinasePRKACAP17612
GPS
209SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
209SPhosphorylation

14517323

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 ERD21_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARFG1_HUMANARFGAP1physical
9405360
ERD21_HUMANKDELR1physical
9405360
UBE3A_HUMANUBE3Aphysical
28514442
UBL7_HUMANUBL7physical
28514442
MINY1_HUMANFAM63Aphysical
28514442
VPS36_HUMANVPS36physical
28514442
TAXB1_HUMANTAX1BP1physical
28514442
TRAD1_HUMANTRAFD1physical
28514442
UCHL5_HUMANUCHL5physical
28514442
PSD11_HUMANPSMD11physical
28514442
UBQL4_HUMANUBQLN4physical
28514442
NPL4_HUMANNPLOC4physical
28514442
PSD12_HUMANPSMD12physical
28514442
PSMD6_HUMANPSMD6physical
28514442
UBQL1_HUMANUBQLN1physical
28514442
RN115_HUMANRNF115physical
28514442
PSMD4_HUMANPSMD4physical
28514442

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 ERD21_HUMAN

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Related Literatures of Post-Translational Modification

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