EPB42_MOUSE - dbPTM
EPB42_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPB42_MOUSE
UniProt AC P49222
Protein Name Erythrocyte membrane protein band 4.2
Gene Name Epb42
Organism Mus musculus (Mouse).
Sequence Length 691
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side. Cytoplasm, cytoskeleton. Cytoplasmic surface of erythrocyte membranes.
Protein Description Probably plays an important role in the regulation of erythrocyte shape and mechanical properties..
Protein Sequence MGQALSIKSCDFHAAENNEEHYTKAISSQHLTLRRGQSFTITLNFRAPTHTFLSALKKVALIAQTGEQPSKINKTQAIFPISSLGDQKGWSAAVEERDAQHWTVSVTTPVDAVIGHYSLLLQVSGKKQYPLGQFTLLFNPWNRDDAVFLQNEAERTEYVLNQNGFIYLGTADCIQEEPWDFGQFEKDVMDLSLKLLSMDKQVKDWNQPAHVARVVGALLHALKKKSVLPISQTQAAQEGALLYKRRGSVPILRQWLTGQGRAVYETQAWVSAAVACTVLRCLGIPARVVTTFDSAQGTVGSLLVDEYYNEEGLQNGEGQRGHIWVFQTSVECWMNRPDLSQGYGGWQILHPRAPNGAGVLGSCSLVPVRAVKEGELQLDPAVPELFAAVNASCVVWKCCEDGKLELTNSNRKDVGNCISTKVVGSDRCEDITQNYKYPAGSLQEKEVLEKVQKERLKLGKDNGMCPPSCEPWDPLHMFFEASSSIPLSGDGQLSVTLINPTDEEKKVHLVIGAQALYYNGVLAAGLWSKKQLFMLKPNQVMRLSTNLSFSCFEQTPPENSFLRVTAMARYSHTSLSCFAQENMAIGKPDLIIEMPKRAAQYRPLTVSVRMHNSLEAPMQNCIISIFGRGLIHREKRYGLGSLWPGSSLHTQFQFTPTHLGLQRLTVEVDCDMFQNLTGYRSVLVVAPEVSV
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
2Myristoylation------MGQALSIKS
------CCCCCEEEC
22.82-
49PhosphorylationTLNFRAPTHTFLSAL
EEEEECCCHHHHHHH
32.3428576409
51PhosphorylationNFRAPTHTFLSALKK
EEECCCHHHHHHHHH
28.8428576409
200UbiquitinationLKLLSMDKQVKDWNQ
HHHHCCCHHCCCCCC
48.6422790023
223UbiquitinationGALLHALKKKSVLPI
HHHHHHHHHCCCCCC
59.9622790023
225UbiquitinationLLHALKKKSVLPISQ
HHHHHHHCCCCCCCH
44.1822790023
226PhosphorylationLHALKKKSVLPISQT
HHHHHHCCCCCCCHH
37.45-
243PhosphorylationAQEGALLYKRRGSVP
HHHCCCCEEECCCCC
11.87-
248PhosphorylationLLYKRRGSVPILRQW
CCEEECCCCCEEEHH
23.9422817900
403UbiquitinationWKCCEDGKLELTNSN
EEECCCCCEEECCCC
51.62-
544PhosphorylationPNQVMRLSTNLSFSC
HHHEEEEECCCEEEC
12.6021454597
545PhosphorylationNQVMRLSTNLSFSCF
HHEEEEECCCEEECC
44.7821454597
548PhosphorylationMRLSTNLSFSCFEQT
EEEECCCEEECCCCC
19.7221454597
550PhosphorylationLSTNLSFSCFEQTPP
EECCCEEECCCCCCC
17.9621454597
555PhosphorylationSFSCFEQTPPENSFL
EEECCCCCCCCCCCC
33.3421454597
570PhosphorylationRVTAMARYSHTSLSC
HHEEEEECCCCHHHH
8.6822817900
571PhosphorylationVTAMARYSHTSLSCF
HEEEEECCCCHHHHH
18.0921082442
573PhosphorylationAMARYSHTSLSCFAQ
EEEECCCCHHHHHHH
25.9821082442
574PhosphorylationMARYSHTSLSCFAQE
EEECCCCHHHHHHHC
16.9221082442
576PhosphorylationRYSHTSLSCFAQENM
ECCCCHHHHHHHCCC
13.6221183079

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 EPB42_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPB42_MOUSE !!

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 EPB42_MOUSE !!

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

Oops, there are no PPI records of EPB42_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPB42_MOUSE

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Related Literatures of Post-Translational Modification

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