dbPTM

EPHB4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EPHB4_MOUSE
UniProt AC	P54761
Protein Name	Ephrin type-B receptor 4
Gene Name	Ephb4
Organism	Mus musculus (Mouse).
Sequence Length	987
Subcellular Localization	Cell membrane Single-pass type I membrane protein.
Protein Description	Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation form EFNB2-expressing cells. Plays also a role in postnatal blood vessel remodeling, morphogenesis and permeability and is thus important in the context of tumor angiogenesis..
Protein Sequence	MELRALLCWASLATALEETLLNTKLETADLKWVTYPQAEGQWEELSGLDEEQHSVRTYEVCDMKRPGGQAHWLRTGWVPRRGAVHVYATIRFTMMECLSLPRASRSCKETFTVFYYESEADTATAHTPAWMENPYIKVDTVAAEHLTRKRPGAEATGKVNIKTLRLGPLSKAGFYLAFQDQGACMALLSLHLFYKKCSWLITNLTYFPETVPRELVVPVAGSCVANAVPTANPSPSLYCREDGQWAEQQVTGCSCAPGYEAAESNKVCRACGQGTFKPQIGDESCLPCPANSHSNNIGSPVCLCRIGYYRARSDPRSSPCTTPPSAPRSVVHHLNGSTLRLEWSAPLESGGREDLTYAVRCRECRPGGSCLPCGGDMTFDPGPRDLVEPWVAIRGLRPDVTYTFEVAALNGVSTLATGPPPFEPVNVTTDREVPPAVSDIRVTRSSPSSLILSWAIPRAPSGAVLDYEVKYHEKGAEGPSSVRFLKTSENRAELRGLKRGASYLVQVRARSEAGYGPFGQEHHSQTQLDESESWREQLALIAGTAVVGVVLVLVVVIIAVLCLRKQSNGREVEYSDKHGQYLIGHGTKVYIDPFTYEDPNEAVREFAKEIDVSYVKIEEVIGAGEFGEVCRGRLKAPGKKESCVAIKTLKGGYTERQRREFLSEASIMGQFEHPNIIRLEGVVTNSVPVMILTEFMENGALDSFLRLNDGQFTVIQLVGMLRGIASGMRYLAEMSYVHRDLAARNILVNSNLVCKVSDFGLSRFLEENSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTSASDAWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPPDCPTSLHQLMLDCWQKDRNARPRFPQVVSALDKMIRNPASLKIVARENGGASHPLLDQRQPHYSAFGSVGEWLRAIKMGRYEESFAAAGFGSFEVVSQISAEDLLRIGVTLAGHQKKILASVQHMKSQAKPGAPGGTGGPAQQF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
140	Phosphorylation	NPYIKVDTVAAEHLT CCCEEEEHHHHHHHH	18.29	-
147	Phosphorylation	TVAAEHLTRKRPGAE HHHHHHHHCCCCCCC	35.73	-
203	N-linked_Glycosylation	KCSWLITNLTYFPET HHCHHHHCCCCCCCC	24.32	-
335	N-linked_Glycosylation	RSVVHHLNGSTLRLE CCEEEECCCCEEEEE	37.70	19656770
426	N-linked_Glycosylation	PPPFEPVNVTTDREV CCCCCCCCCCCCCCC	35.81	-
502	Phosphorylation	RGLKRGASYLVQVRA HHHHCCCEEEEEEEE	23.09	25521595
574	Phosphorylation	SNGREVEYSDKHGQY CCCCEEEEECCCCCE	27.61	22499769
575	Phosphorylation	NGREVEYSDKHGQYL CCCEEEEECCCCCEE	27.03	22499769
581	Phosphorylation	YSDKHGQYLIGHGTK EECCCCCEEECCCCE	12.60	22499769
587	Phosphorylation	QYLIGHGTKVYIDPF CEEECCCCEEEECCC	16.21	22499769
590	Phosphorylation	IGHGTKVYIDPFTYE ECCCCEEEECCCCCC	10.93	26824392
595	Phosphorylation	KVYIDPFTYEDPNEA EEEECCCCCCCCCHH	31.24	22499769
596	Phosphorylation	VYIDPFTYEDPNEAV EEECCCCCCCCCHHH	20.79	26824392
613	Phosphorylation	FAKEIDVSYVKIEEV HHHHCCCEEEEEEEE	22.06	22499769
614	Phosphorylation	AKEIDVSYVKIEEVI HHHCCCEEEEEEEEE	12.95	22499769
642	Phosphorylation	KAPGKKESCVAIKTL CCCCCCCCEEEEEEE	23.83	21454597
648	Phosphorylation	ESCVAIKTLKGGYTE CCEEEEEEECCCCCH	27.82	21454597
762	Phosphorylation	KVSDFGLSRFLEENS EECHHCHHHHHHHCC	22.74	20415495
769	Phosphorylation	SRFLEENSSDPTYTS HHHHHHCCCCCCEEC	39.12	27087446
770	Phosphorylation	RFLEENSSDPTYTSS HHHHHCCCCCCEECC	60.22	25521595
773	Phosphorylation	EENSSDPTYTSSLGG HHCCCCCCEECCCCC	44.41	25619855
774	Phosphorylation	ENSSDPTYTSSLGGK HCCCCCCEECCCCCC	15.26	27742792
775	Phosphorylation	NSSDPTYTSSLGGKI CCCCCCEECCCCCCC	17.83	25619855
776	Phosphorylation	SSDPTYTSSLGGKIP CCCCCEECCCCCCCC	17.10	25619855
777	Phosphorylation	SDPTYTSSLGGKIPI CCCCEECCCCCCCCE	24.19	25619855
872	Phosphorylation	PRFPQVVSALDKMIR CCHHHHHHHHHHHHC	25.02	22942356
906	Phosphorylation	LDQRQPHYSAFGSVG CCCCCCCCCCCCCHH	14.37	18515860
911	Phosphorylation	PHYSAFGSVGEWLRA CCCCCCCCHHHHHHH	22.09	-
943	Phosphorylation	FEVVSQISAEDLLRI EEEEEECCHHHHHHH	20.26	-
953	Phosphorylation	DLLRIGVTLAGHQKK HHHHHCEEEHHHHHH	12.99	25338131
980	Phosphorylation	KPGAPGGTGGPAQQF CCCCCCCCCCCCCCC	44.90	29514104

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 EPHB4_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EPHB4_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 EPHB4_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
ELF2_MOUSE	Elf2	physical	8954633

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EPHB4_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-335, AND MASSSPECTROMETRY.	19349973 [Abstract]
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation."; Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.; Mol. Cell. Proteomics 8:2555-2569(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-335, AND MASSSPECTROMETRY.	19656770 [Abstract]