EPB42_HUMAN - dbPTM
EPB42_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPB42_HUMAN
UniProt AC P16452
Protein Name Erythrocyte membrane protein band 4.2
Gene Name EPB42
Organism Homo sapiens (Human).
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 MGQALGIKSCDFQAARNNEEHHTKALSSRRLFVRRGQPFTIILYFRAPVRAFLPALKKVALTAQTGEQPSKINRTQATFPISSLGDRKWWSAVVEERDAQSWTISVTTPADAVIGHYSLLLQVSGRKQLLLGQFTLLFNPWNREDAVFLKNEAQRMEYLLNQNGLIYLGTADCIQAESWDFGQFEGDVIDLSLRLLSKDKQVEKWSQPVHVARVLGALLHFLKEQRVLPTPQTQATQEGALLNKRRGSVPILRQWLTGRGRPVYDGQAWVLAAVACTVLRCLGIPARVVTTFASAQGTGGRLLIDEYYNEEGLQNGEGQRGRIWIFQTSTECWMTRPALPQGYDGWQILHPSAPNGGGVLGSCDLVPVRAVKEGTLGLTPAVSDLFAAINASCVVWKCCEDGTLELTDSNTKYVGNNISTKGVGSDRCEDITQNYKYPEGSLQEKEVLERVEKEKMEREKDNGIRPPSLETASPLYLLLKAPSSLPLRGDAQISVTLVNHSEQEKAVQLAIGVQAVHYNGVLAAKLWRKKLHLTLSANLEKIITIGLFFSNFERNPPENTFLRLTAMATHSESNLSCFAQEDIAICRPHLAIKMPEKAEQYQPLTASVSLQNSLDAPMEDCVISILGRGLIHRERSYRFRSVWPENTMCAKFQFTPTHVGLQRLTVEVDCNMFQNLTNYKSVTVVAPELSA
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------MGQALGIKS
------CCCCCCCCC		22.821544941
2N-myristoyl glycine------MGQALGIKS
------CCCCCCCCC		22.82-
7 (in isoform 2)Phosphorylation-2.86-
10 (in isoform 2)Phosphorylation-5.2923025827
11 (in isoform 2)Phosphorylation-45.8727251275
23PhosphorylationRNNEEHHTKALSSRR
CCCHHHHHHHHHHCE		21.6624501219
27PhosphorylationEHHTKALSSRRLFVR
HHHHHHHHHCEEEEE		27.0224501219
28PhosphorylationHHTKALSSRRLFVRR
HHHHHHHHCEEEEEC		23.4424501219
82O-linked_GlycosylationTQATFPISSLGDRKW
EEEEEECHHHCCCCE		21.5412556529
192PhosphorylationEGDVIDLSLRLLSKD
CCHHHHHHHHHHCCC		14.0124719451
204UbiquitinationSKDKQVEKWSQPVHV
CCCCCCHHCCCCHHH		53.9730230243
230PhosphorylationKEQRVLPTPQTQATQ
HHCCCCCCCCCCCHH		24.7023025827
234UbiquitinationVLPTPQTQATQEGAL
CCCCCCCCCHHHHHH		36.8530230243
248PhosphorylationLLNKRRGSVPILRQW
HHHCCCCCCCHHHHH		23.9427273156
257PhosphorylationPILRQWLTGRGRPVY
CHHHHHHHCCCCCCC		23.1322210691
264PhosphorylationTGRGRPVYDGQAWVL
HCCCCCCCCHHHHHH		19.6222210691
291PhosphorylationIPARVVTTFASAQGT
CCHHHEEEHHHHCCC		12.95-
294PhosphorylationRVVTTFASAQGTGGR
HHEEEHHHHCCCCCE		19.55-
375PhosphorylationVRAVKEGTLGLTPAV
EECEEECCCCCCHHH		20.81-
403PhosphorylationWKCCEDGTLELTDSN
EEECCCCCEEEECCC		29.40-
407PhosphorylationEDGTLELTDSNTKYV
CCCCEEEECCCCCEE		28.18-
409PhosphorylationGTLELTDSNTKYVGN
CCEEEECCCCCEECC		40.96-
411PhosphorylationLELTDSNTKYVGNNI
EEEECCCCCEECCCC		27.92-
435PhosphorylationCEDITQNYKYPEGSL
HHHHHHHCCCCCCCC		11.3321951684
437PhosphorylationDITQNYKYPEGSLQE
HHHHHCCCCCCCCCH		8.9922985185
484PhosphorylationLLLKAPSSLPLRGDA
EHHCCCCCCCCCCCC		32.7124719451
560PhosphorylationERNPPENTFLRLTAM
CCCCCCCCCHHHHHE		23.53-
565PhosphorylationENTFLRLTAMATHSE
CCCCHHHHHEEECCC		14.14-
569PhosphorylationLRLTAMATHSESNLS
HHHHHEEECCCCCCE		16.9227251275
571PhosphorylationLTAMATHSESNLSCF
HHHEEECCCCCCEEE		38.0627251275
573PhosphorylationAMATHSESNLSCFAQ
HEEECCCCCCEEEEE		46.1927251275
593"N6,N6-dimethyllysine"CRPHLAIKMPEKAEQ
ECCEEEEECCCHHHH		42.68-
593MethylationCRPHLAIKMPEKAEQ
ECCEEEEECCCHHHH		42.68-
665PhosphorylationHVGLQRLTVEVDCNM
CCCCCEEEEEEECHH		19.4629759185
677PhosphorylationCNMFQNLTNYKSVTV
CHHCCCCCCCCEEEE		44.0129759185
681PhosphorylationQNLTNYKSVTVVAPE
CCCCCCCEEEEECCC		16.8023025827
690PhosphorylationTVVAPELSA------
EEECCCCCC------		30.2123025827
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
248SPhosphorylationKinasePKA-FAMILY-GPS
248SPhosphorylationKinasePKA-Uniprot
248SPhosphorylationKinasePKA_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPB42_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 EPB42_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANK2_HUMANANK2physical
2968981
B3AT_HUMANSLC4A1physical
7626035
S4A7_HUMANSLC4A7physical
28514442
HSP7C_HUMANHSPA8physical
28514442
SNX6_HUMANSNX6physical
28514442
Drug and Disease Associations
Kegg Disease
H00230 Hereditary spherocytosis (SPH)
OMIM Disease
612690Spherocytosis 5 (SPH5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPB42_HUMAN

loading...

Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Human erythrocyte protein 4.2, a high copy number membrane protein,is N-myristylated.";
Risinger M.A., Dotimas E.M., Cohen C.M.;
J. Biol. Chem. 267:5680-5685(1992).
Cited for: MYRISTOYLATION AT GLY-2.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory