41_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: 41_HUMAN
• UniProt AC: P11171
• Protein Name: Protein 4.1
• Gene Name: EPB41
• Organism: Homo sapiens (Human).
• Sequence Length: 864
• Subcellular Localization: Cytoplasm, cytoskeleton . Cytoplasm, cell cortex . Nucleus .
• Protein Description: Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. [PubMed: 23870127]
• Protein Sequence: MTTEKSLVTEAENSQHQQKEEGEEAINSGQQEPQQEESCQTAAEGDNWCEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLFSSFLKRPKSQVSEEEGKEVESDKEKGEGGQKEIEFGTSLDEEIILKAPIAAPEPELKTDPSLDLHSLSSAETQPAQEELREDPDFEIKEGEGLEECSKIEVKEESPQSKAETELKASQKPIRKHRNMHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAVDSADRSPRPTSAPAITQGQVAEGGVLDASAKKTVVPKAQKETVKAEVKKEDEPPEQAEPEPTEAWKVEKTHIEVTVPTSNGDQTQKLAEKTEDLIRMRKKKRERLDGENIYIRHSNLMLEDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQIPTGEGPPLVKTQTVTISDNANAVKSEIPTKDVPIVHTETKTITYEAAQTDDNSGDLDPGVLLTAQTITSETPSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPDMSVTKVVVHQETEIADE

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
88 (in isoform 1)	Ubiquitination	-	65.72	21890473
88 (in isoform 2)	Ubiquitination	-	65.72	21890473
88 (in isoform 5)	Ubiquitination	-	65.72	21890473
88 (in isoform 7)	Ubiquitination	-	65.72	21890473
224	Glutathionylation	LDDTVYECVVEKHAK CCCCHHHHHHHHHHC	1.97	22555962
228	Acetylation	VYECVVEKHAKGQDL HHHHHHHHHHCCHHH	36.93	25953088
506	Acetylation	KFLALGSKFRYSGRT HEEECCCCCCCCCCC	31.87	25953088

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
60	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
60	T	Phosphorylation	Kinase	CDK1	P06493	PSP
660	Y	Phosphorylation	Kinase	EGFR	P00533	Uniprot
679	S	Phosphorylation	Kinase	CDK1	P06493	PSP
712	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of 41_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of 41_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MYH9_HUMAN	MYH9	physical	17353931
SYVC_HUMAN	VARS	physical	17353931
PUR6_HUMAN	PAICS	physical	17353931
TAGL2_HUMAN	TAGLN2	physical	17353931
ECHM_HUMAN	ECHS1	physical	17353931
CALR_HUMAN	CALR	physical	17353931
PUR4_HUMAN	PFAS	physical	17353931
ZO2_HUMAN	TJP2	physical	10874042
NUMA1_HUMAN	NUMA1	physical	10189366
DYHC1_HUMAN	DYNC1H1	physical	10189366
DCTN1_HUMAN	DCTN1	physical	10189366
SPTN1_HUMAN	SPTAN1	physical	12044158
RWD2B_HUMAN	RWDD2B	physical	25416956
ZCH10_HUMAN	ZCCHC10	physical	25416956
SF3A3_HUMAN	SF3A3	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 611804: Elliptocytosis 1 (EL1)
• 266140: Hereditary pyropoikilocytosis (HPP)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-542, AND MASSSPECTROMETRY.
PubMed: 19690332

"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-188; SER-191; SER-555AND SER-712, AND MASS SPECTROMETRY.
PubMed: 18669648

"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712, AND MASSSPECTROMETRY.
PubMed: 18220336

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASSSPECTROMETRY.
PubMed: 17287340

"Mitotic regulation of protein 4.1R involves phosphorylation by cdc2kinase.";
Huang S.-C., Liu E.S., Chan S.-H., Munagala I.D., Cho H.T.,Jagadeeswaran R., Benz E.J. Jr.;
Mol. Biol. Cell 16:117-127(2005).
Cited for: MUTAGENESIS OF THR-60 AND SER-712, AND PHOSPHORYLATION AT THR-60 ANDSER-712.
PubMed: 15525677

"Identification of two cAMP-dependent phosphorylation sites onerythrocyte protein 4.1.";
Horne W.C., Prinz W.C., Tang E.K.;
Biochim. Biophys. Acta 1055:87-92(1990).
Cited for: PROTEIN SEQUENCE OF 534-541; 693-701 AND 793-794, AND PHOSPHORYLATIONAT SERINE RESIDUES.
PubMed: 2171679

"Phosphorylation of protein 4.1 on tyrosine-418 modulates its functionin vitro.";
Subrahmanyan G., Bertics P.J., Anderson R.A.;
Proc. Natl. Acad. Sci. U.S.A. 88:5222-5226(1991).
Cited for: PHOSPHORYLATION AT TYR-660 BY EGFR.
PubMed: 1647028