EPHB1_HUMAN - dbPTM
EPHB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPHB1_HUMAN
UniProt AC P54762
Protein Name Ephrin type-B receptor 1
Gene Name EPHB1
Organism Homo sapiens (Human).
Sequence Length 984
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Early endosome membrane . Cell projection, dendrite .
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. Cognate/functional ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During nervous system development, regulates retinal axon guidance redirecting ipsilaterally ventrotemporal retinal ganglion cells axons at the optic chiasm midline. This probably requires repulsive interaction with EFNB2. In the adult nervous system together with EFNB3, regulates chemotaxis, proliferation and polarity of the hippocampus neural progenitors. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. May also regulate angiogenesis. More generally, may play a role in targeted cell migration and adhesion. Upon activation by EFNB1 and probably other ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively. Involved in the maintenance of the pool of satellite cells (muscle stem cells) by promoting their self-renewal and reducing their activation and differentiation (By similarity)..
Protein Sequence MALDYLLLLLLASAVAAMEETLMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPNVPGSCKETFNLYYYETDSVIATKKSAFWSEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYGACMSLLSVRVFFKKCPSIVQNFAVFPETMTGAESTSLVIARGTCIPNAEEVDVPIKLYCNGDGEWMVPIGRCTCKPGYEPENSVACKACPAGTFKASQEAEGCSHCPSNSRSPAEASPICTCRTGYYRADFDPPEVACTSVPSGPRNVISIVNETSIILEWHPPRETGGRDDVTYNIICKKCRADRRSCSRCDDNVEFVPRQLGLTECRVSISSLWAHTPYTFDIQAINGVSSKSPFPPQHVSVNITTNQAAPSTVPIMHQVSATMRSITLSWPQPEQPNGIILDYEIRYYEKEHNEFNSSMARSQTNTARIDGLRPGMVYVVQVRARTVAGYGKFSGKMCFQTLTDDDYKSELREQLPLIAGSAAAGVVFVVSLVAISIVCSRKRAYSKEAVYSDKLQHYSTGRGSPGMKIYIDPFTYEDPNEAVREFAKEIDVSFVKIEEVIGAGEFGEVYKGRLKLPGKREIYVAIKTLKAGYSEKQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLAEMNYVHRDLAARNILVNSNLVCKVSDFGLSRYLQDDTSDPTYTSSLGGKIPVRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPMDCPAALHQLMLDCWQKDRNSRPRFAEIVNTLDKMIRNPASLKTVATITAVPSQPLLDRSIPDFTAFTTVDDWLSAIKMVQYRDSFLTAGFTSLQLVTQMTSEDLLRIGITLAGHQKKILNSIHSMRVQISQSPTAMA
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
5Phosphorylation---MALDYLLLLLLA
---CHHHHHHHHHHH		10.4923663014
13PhosphorylationLLLLLLASAVAAMEE
HHHHHHHHHHHHHHH		24.2023663014
21PhosphorylationAVAAMEETLMDTRTA
HHHHHHHHHHCCCCC		17.6823663014
25PhosphorylationMEETLMDTRTATAEL
HHHHHHCCCCCCEEC		18.8923663014
57PhosphorylationENLNTIRTYQVCNVF
CCCCCEEEEEEEECC		17.9224043423
58PhosphorylationNLNTIRTYQVCNVFE
CCCCEEEEEEEECCC		6.7924043423
92PhosphorylationIYTEMRFTVRDCSSL
EEEEEEEEEECHHHC		12.3124719451
164PhosphorylationKVNTEVRSFGPLTRN
EECCCEECCCCCCCC		39.4727067055
169UbiquitinationVRSFGPLTRNGFYLA
EECCCCCCCCEEEEE		25.8121987572
169PhosphorylationVRSFGPLTRNGFYLA
EECCCCCCCCEEEEE		25.8127067055
264PhosphorylationPGYEPENSVACKACP
CCCCCCCCEECEECC		14.9426074081
285PhosphorylationSQEAEGCSHCPSNSR
CHHCCCCCCCCCCCC		38.6929083192
289PhosphorylationEGCSHCPSNSRSPAE
CCCCCCCCCCCCCCC		53.4829083192
291PhosphorylationCSHCPSNSRSPAEAS
CCCCCCCCCCCCCCC		38.1729083192
334N-linked_GlycosylationRNVISIVNETSIILE
CCEEEEEECCEEEEE		45.20UniProtKB CARBOHYD
395PhosphorylationECRVSISSLWAHTPY
EEEEEEHHHHCCCCE		26.68-
426N-linked_GlycosylationPPQHVSVNITTNQAA
CCCCEEEEEECCCCC		20.55UniProtKB CARBOHYD
480N-linked_GlycosylationEKEHNEFNSSMARSQ
HHHHCCCCHHHHHHH		27.31UniProtKB CARBOHYD
575PhosphorylationAYSKEAVYSDKLQHY
CCCCHHHHHCCCCCC		20.4220007894
582PhosphorylationYSDKLQHYSTGRGSP
HHCCCCCCCCCCCCC		8.5830108239
583PhosphorylationSDKLQHYSTGRGSPG
HCCCCCCCCCCCCCC		23.4330108239
584PhosphorylationDKLQHYSTGRGSPGM
CCCCCCCCCCCCCCC		24.5929514088
588PhosphorylationHYSTGRGSPGMKIYI
CCCCCCCCCCCEEEE		19.5430108239
592UbiquitinationGRGSPGMKIYIDPFT
CCCCCCCEEEECCCC		37.97-
594PhosphorylationGSPGMKIYIDPFTYE
CCCCCEEEECCCCCC		8.1821945579
599PhosphorylationKIYIDPFTYEDPNEA
EEEECCCCCCCHHHH		31.2421945579
600PhosphorylationIYIDPFTYEDPNEAV
EEECCCCCCCHHHHH		20.7921945579
634PhosphorylationAGEFGEVYKGRLKLP
CCCCCCEECCCCCCC		11.9221082442
643UbiquitinationGRLKLPGKREIYVAI
CCCCCCCCCEEEEEE		44.94-
652PhosphorylationEIYVAIKTLKAGYSE
EEEEEEEHHHCCCCH		27.6426657352
658PhosphorylationKTLKAGYSEKQRRDF
EHHHCCCCHHHHHHH		37.0826657352
740PhosphorylationKYLAEMNYVHRDLAA
HHHHHCCCCCHHHHH		9.0520071362
754PhosphorylationARNILVNSNLVCKVS
HHCEEECCCEEEEEC		24.86-
759UbiquitinationVNSNLVCKVSDFGLS
ECCCEEEEECCCCHH		36.9821987572
761PhosphorylationSNLVCKVSDFGLSRY
CCEEEEECCCCHHHH		16.83-
766PhosphorylationKVSDFGLSRYLQDDT
EECCCCHHHHCCCCC		21.1819369195
768PhosphorylationSDFGLSRYLQDDTSD
CCCCHHHHCCCCCCC		12.8224927040
773PhosphorylationSRYLQDDTSDPTYTS
HHHCCCCCCCCCEEC		43.2330108239
774PhosphorylationRYLQDDTSDPTYTSS
HHCCCCCCCCCEECC		48.8928355574
777PhosphorylationQDDTSDPTYTSSLGG
CCCCCCCCEECCCCC		44.4130108239
778PhosphorylationDDTSDPTYTSSLGGK
CCCCCCCEECCCCCC		15.2615107421
779PhosphorylationDTSDPTYTSSLGGKI
CCCCCCEECCCCCCC		17.8330108239
780PhosphorylationTSDPTYTSSLGGKIP
CCCCCEECCCCCCCC		17.1030108239
781PhosphorylationSDPTYTSSLGGKIPV
CCCCEECCCCCCCCC		24.1930108239
791UbiquitinationGKIPVRWTAPEAIAY
CCCCCEEECCHHHHC		23.0521987572
798PhosphorylationTAPEAIAYRKFTSAS
ECCHHHHCCCCCCHH		14.28-
807UbiquitinationKFTSASDVWSYGIVM
CCCCHHHHHHHHEEE		3.2021987572
813UbiquitinationDVWSYGIVMWEVMSF
HHHHHHEEEEEEECC		2.9521987572
890PhosphorylationRNPASLKTVATITAV
CCHHHCCCEEEEEEC		22.2130108239
893PhosphorylationASLKTVATITAVPSQ
HHCCCEEEEEECCCC		17.9630108239
895PhosphorylationLKTVATITAVPSQPL
CCCEEEEEECCCCCC		19.7630108239
899PhosphorylationATITAVPSQPLLDRS
EEEEECCCCCCCCCC		37.5230108239
928PhosphorylationSAIKMVQYRDSFLTA
HHHHHHHCHHHHHHC		12.6515107421
968PhosphorylationHQKKILNSIHSMRVQ
HHHHHHHHHHHHEEE		20.4518187866
979PhosphorylationMRVQISQSPTAMA--
HEEEECCCCCCCC--		19.8918187866
981PhosphorylationVQISQSPTAMA----
EEECCCCCCCC----		34.0218187866
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
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:18034775
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPHB1_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 EPHB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPAC_HUMANACP1physical
9499402
GRB2_HUMANGRB2physical
8798570
GRB10_HUMANGRB10physical
8798570
NCK1_HUMANNCK1physical
9430661
CBL_HUMANCBLphysical
18034775
PTEN_HUMANPTENphysical
23118026
NHRF1_HUMANSLC9A3R1physical
23118026
CBL_HUMANCBLphysical
23118026
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 EPHB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968, AND MASSSPECTROMETRY.

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