EPHA5_HUMAN - dbPTM
EPHA5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPHA5_HUMAN
UniProt AC P54756
Protein Name Ephrin type-A receptor 5
Gene Name EPHA5
Organism Homo sapiens (Human).
Sequence Length 1037
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell projection, axon . Cell projection, dendrite .
Protein Description Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A 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. Among GPI-anchored ephrin-A ligands, EFNA5 most probably constitutes the cognate/functional ligand for EPHA5. Functions as an axon guidance molecule during development and may be involved in the development of the retinotectal, entorhino-hippocampal and hippocamposeptal pathways. Together with EFNA5 plays also a role in synaptic plasticity in adult brain through regulation of synaptogenesis. In addition to its function in the nervous system, the interaction of EPHA5 with EFNA5 mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion (By similarity)..
Protein Sequence MRGSGPRGAGRRRPPSGGGDTPITPASLAGCYSAPRRAPLWTCLLLCAALRTLLASPSNEVNLLDSRTVMGDLGWIAFPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGASRIFIELKFTLRDCNSLPGGLGTCKETFNMYYFESDDQNGRNIKENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLSKKGFYLAFQDVGACIALVSVRVYYKKCPSVVRHLAVFPDTITGADSSQLLEVSGSCVNHSVTDEPPKMHCSAEGEWLVPIGKCMCKAGYEEKNGTCQVCRPGFFKASPHIQSCGKCPPHSYTHEEASTSCVCEKDYFRRESDPPTMACTRPPSAPRNAISNVNETSVFLEWIPPADTGGRKDVSYYIACKKCNSHAGVCEECGGHVRYLPRQSGLKNTSVMMVDLLAHTNYTFEIEAVNGVSDLSPGARQYVSVNVTTNQAAPSPVTNVKKGKIAKNSISLSWQEPDRPNGIILEYEIKYFEKDQETSYTIIKSKETTITAEGLKPASVYVFQIRARTAAGYGVFSRRFEFETTPVFAASSDQSQIPVIAVSVTVGVILLAVVIGVLLSGSCCECGCGRASSLCAVAHPSLIWRCGYSKAKQDPEEEKMHFHNGHIKLPGVRTYIDPHTYEDPNQAVHEFAKEIEASCITIERVIGAGEFGEVCSGRLKLPGKRELPVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIHLEGVVTKSKPVMIVTEYMENGSLDTFLKKNDGQFTVIQLVGMLRGISAGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAFRKFTSASDVWSYGIVMWEVVSYGERPYWEMTNQDVIKAVEEGYRLPSPMDCPAALYQLMLDCWQKERNSRPKFDEIVNMLDKLIRNPSSLKTLVNASCRVSNLLAEHSPLGSGAYRSVGEWLEAIKMGRYTEIFMENGYSSMDAVAQVTLEDLRRLGVTLVGHQKKIMNSLQEMKVQLVNGMVPL
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
4Phosphorylation----MRGSGPRGAGR
----CCCCCCCCCCC
52.43-
66PhosphorylationNEVNLLDSRTVMGDL
CCCCCCCCCCCCCCE
29.8020068231
133PhosphorylationIFIELKFTLRDCNSL
EEEEEEEEECCCCCC
21.2124719451
197PhosphorylationDRVMKLNTEVRDVGP
HHEEECCCEEEECCC
46.42-
225PhosphorylationGACIALVSVRVYYKK
HHHHHEEEEEHHHHC
12.6924719451
264N-linked_GlycosylationEVSGSCVNHSVTDEP
EEECCEECCCCCCCC
26.50UniProtKB CARBOHYD
295PhosphorylationKCMCKAGYEEKNGTC
HEEEECCCCCCCCEE
26.2720068231
299N-linked_GlycosylationKAGYEEKNGTCQVCR
ECCCCCCCCEEEECC
55.04UniProtKB CARBOHYD
301PhosphorylationGYEEKNGTCQVCRPG
CCCCCCCEEEECCCC
14.79-
313PhosphorylationRPGFFKASPHIQSCG
CCCCCCCCCCCCCCC
20.01-
318PhosphorylationKASPHIQSCGKCPPH
CCCCCCCCCCCCCCC
25.00-
333PhosphorylationSYTHEEASTSCVCEK
CCCCCCCCCCEEECH
24.9222496350
351PhosphorylationRRESDPPTMACTRPP
CCCCCCCCCCCCCCC
23.8425332170
369N-linked_GlycosylationRNAISNVNETSVFLE
CCCCCCCCCCEEEEE
51.59UniProtKB CARBOHYD
387UbiquitinationPADTGGRKDVSYYIA
CCCCCCCCCEEEEEE
66.80-
423N-linked_GlycosylationPRQSGLKNTSVMMVD
CCCCCCCCCEEEEEE
42.50UniProtKB CARBOHYD
436N-linked_GlycosylationVDLLAHTNYTFEIEA
EEECCCCCEEEEEEE
24.79UniProtKB CARBOHYD
461N-linked_GlycosylationARQYVSVNVTTNQAA
CEEEEEEEEECCCCC
20.22UniProtKB CARBOHYD
523PhosphorylationTIIKSKETTITAEGL
EEEECCCEEEEECCC
27.5130576142
524PhosphorylationIIKSKETTITAEGLK
EEECCCEEEEECCCC
19.8830576142
526PhosphorylationKSKETTITAEGLKPA
ECCCEEEEECCCCCC
19.3030576142
649PhosphorylationIKLPGVRTYIDPHTY
CCCCCCEEEECCCCC
23.5622322096
650PhosphorylationKLPGVRTYIDPHTYE
CCCCCEEEECCCCCC
7.8622322096
655PhosphorylationRTYIDPHTYEDPNQA
EEEECCCCCCCHHHH
33.7126356563
656PhosphorylationTYIDPHTYEDPNQAV
EEECCCCCCCHHHHH
18.4622322096
673PhosphorylationFAKEIEASCITIERV
HHHHHHHHCEEEEEE
8.02-
676PhosphorylationEIEASCITIERVIGA
HHHHHCEEEEEEECC
22.55-
699UbiquitinationGRLKLPGKRELPVAI
CCCCCCCCCCCCEEE
40.54-
708PhosphorylationELPVAIKTLKVGYTE
CCCEEEEEEECCCCH
26.2122461510
710UbiquitinationPVAIKTLKVGYTEKQ
CEEEEEEECCCCHHH
38.55-
713PhosphorylationIKTLKVGYTEKQRRD
EEEEECCCCHHHCCC
18.0822461510
755PhosphorylationPVMIVTEYMENGSLD
CEEEEEEEECCCCCC
10.6018547520
790PhosphorylationGISAGMKYLSDMGYV
HHHHHHHHHHHCCCC
11.5322817900
796PhosphorylationKYLSDMGYVHRDLAA
HHHHHCCCCCHHHHH
6.09-
817PhosphorylationSNLVCKVSDFGLSRV
CCEEEEECHHCCHHH
16.83-
822PhosphorylationKVSDFGLSRVLEDDP
EECHHCCHHHCCCCC
22.2619369195
833PhosphorylationEDDPEAAYTTRGGKI
CCCCCHHCCCCCCCC
18.7227273156
834PhosphorylationDDPEAAYTTRGGKIP
CCCCHHCCCCCCCCC
12.8025159151
835PhosphorylationDPEAAYTTRGGKIPI
CCCHHCCCCCCCCCC
18.0325159151
856PhosphorylationAIAFRKFTSASDVWS
HEECCCCCCHHHHHH
26.81-
873PhosphorylationIVMWEVVSYGERPYW
EEEEEEEECCCCCCE
32.37-
879PhosphorylationVSYGERPYWEMTNQD
EECCCCCCEECCCHH
21.8829978859
883PhosphorylationERPYWEMTNQDVIKA
CCCCEECCCHHHHHH
20.4329978859
953PhosphorylationVNASCRVSNLLAEHS
HHHHHHHHHHHHHCC
11.4720068231
960PhosphorylationSNLLAEHSPLGSGAY
HHHHHHCCCCCCCCC
17.2122199227
964PhosphorylationAEHSPLGSGAYRSVG
HHCCCCCCCCCCHHH
28.1220068231
967PhosphorylationSPLGSGAYRSVGEWL
CCCCCCCCCHHHHHH
13.6220068231
982PhosphorylationEAIKMGRYTEIFMEN
HHHHCCCCEEEEEEC
11.73-

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 EPHA5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPHA5_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 EPHA5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAT3_HUMANSTAT3physical
15485908
DUS21_HUMANDUSP21physical
28065597

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPHA5_HUMAN

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Related Literatures of Post-Translational Modification

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