EPHB6_HUMAN - dbPTM
EPHB6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPHB6_HUMAN
UniProt AC O15197
Protein Name Ephrin type-B receptor 6
Gene Name EPHB6
Organism Homo sapiens (Human).
Sequence Length 1021
Subcellular Localization Membrane
Single-pass type I membrane protein.
Isoform 3: Secreted .
Protein Description Kinase-defective receptor for members of the ephrin-B family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimulation with ephrin-B2..
Protein Sequence MATEGAAQLGNRVAGMVCSLWVLLLVSSVLALEEVLLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEACHVAGAPPGTGQDNWLQTHFVERRGAQRAHIRLHFSVRACSSLGVSGGTCRETFTLYYRQAEEPDSPDSVSSWHLKRWTKVDTIAADESFPSSSSSSSSSSSAAWAVGPHGAGQRAGLQLNVKERSFGPLTQRGFYVAFQDTGACLALVAVRLFSYTCPAVLRSFASFPETQASGAGGASLVAAVGTCVAHAEPEEDGVGGQAGGSPPRLHCNGEGKWMVAVGGCRCQPGYQPARGDKACQACPRGLYKSSAGNAPCSPCPARSHAPNPAAPVCPCLEGFYRASSDPPEAPCTGPPSAPQELWFEVQGSALMLHWRLPRELGGRGDLLFNVVCKECEGRQEPASGGGGTCHRCRDEVHFDPRQRGLTESRVLVGGLRAHVPYILEVQAVNGVSELSPDPPQAAAINVSTSHEVPSAVPVVHQVSRASNSITVSWPQPDQTNGNILDYQLRYYDQAEDESHSFTLTSETNTATVTQLSPGHIYGFQVRARTAAGHGPYGGKVYFQTLPQGELSSQLPERLSLVIGSILGALAFLLLAAITVLAVVFQRKRRGTGYTEQLQQYSSPGLGVKYYIDPSTYEDPCQAIRELAREVDPAYIKIEEVIGTGSFGEVRQGRLQPRGRREQTVAIQALWAGGAESLQMTFLGRAAVLGQFQHPNILRLEGVVTKSRPLMVLTEFMELGPLDSFLRQREGQFSSLQLVAMQRGVAAAMQYLSSFAFVHRSLSAHSVLVNSHLVCKVARLGHSPQGPSCLLRWAAPEVIAHGKHTTSSDVWSFGILMWEVMSYGERPYWDMSEQEVLNAIEQEFRLPPPPGCPPGLHLLMLDTWQKDRARRPHFDQLVAAFDKMIRKPDTLQAGGDPGERPSQALLTPVALDFPCLDSPQAWLSAIGLECYQDNFSKFGLCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQLLQQHLRQQGSVEV
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
140PhosphorylationRQAEEPDSPDSVSSW
EECCCCCCCCCCCHH		41.1229083192
143PhosphorylationEEPDSPDSVSSWHLK
CCCCCCCCCCHHHHH		27.5529083192
145PhosphorylationPDSPDSVSSWHLKRW
CCCCCCCCHHHHHCC		31.4929083192
146PhosphorylationDSPDSVSSWHLKRWT
CCCCCCCHHHHHCCE		19.1629083192
153PhosphorylationSWHLKRWTKVDTIAA
HHHHHCCEECCEEEC		25.8129083192
154MethylationWHLKRWTKVDTIAAD
HHHHCCEECCEEECC		31.02-
168PhosphorylationDESFPSSSSSSSSSS
CCCCCCCCCCCCCCC		38.28-
169PhosphorylationESFPSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
170PhosphorylationSFPSSSSSSSSSSSA
CCCCCCCCCCCCCCC		35.87-
171PhosphorylationFPSSSSSSSSSSSAA
CCCCCCCCCCCCCCE		35.87-
171O-linked_GlycosylationFPSSSSSSSSSSSAA
CCCCCCCCCCCCCCE		35.87OGP
172O-linked_GlycosylationPSSSSSSSSSSSAAW
CCCCCCCCCCCCCEE		35.87OGP
173O-linked_GlycosylationSSSSSSSSSSSAAWA
CCCCCCCCCCCCEEE		35.87OGP
174O-linked_GlycosylationSSSSSSSSSSAAWAV
CCCCCCCCCCCEEEE		30.20OGP
175O-linked_GlycosylationSSSSSSSSSAAWAVG
CCCCCCCCCCEEEEC		26.41OGP
176O-linked_GlycosylationSSSSSSSSAAWAVGP
CCCCCCCCCEEEECC		24.77OGP
480N-linked_GlycosylationPPQAAAINVSTSHEV
CCCCEEEECCCCCCC		19.57UniProtKB CARBOHYD
489O-linked_GlycosylationSTSHEVPSAVPVVHQ
CCCCCCCCCCCCEEE		47.26OGP
514O-linked_GlycosylationSWPQPDQTNGNILDY
EECCCCCCCCCEEEE		53.10OGP
544O-linked_GlycosylationTLTSETNTATVTQLS
EEECCCCEEEEEEEC		31.00OGP
546O-linked_GlycosylationTSETNTATVTQLSPG
ECCCCEEEEEEECCC		23.27OGP
548O-linked_GlycosylationETNTATVTQLSPGHI
CCCEEEEEEECCCEE		21.31OGP
551O-linked_GlycosylationTATVTQLSPGHIYGF
EEEEEEECCCEEEEE		21.01OGP
579O-linked_GlycosylationGGKVYFQTLPQGELS
CCEEEEEECCCCCHH		30.43OGP
635PhosphorylationYTEQLQQYSSPGLGV
CHHHHHHHCCCCCCC		9.7322817900
636PhosphorylationTEQLQQYSSPGLGVK
HHHHHHHCCCCCCCE		26.2223312004
637PhosphorylationEQLQQYSSPGLGVKY
HHHHHHCCCCCCCEE		20.3223312004
644PhosphorylationSPGLGVKYYIDPSTY
CCCCCCEEEECHHHC		11.8422817900
645PhosphorylationPGLGVKYYIDPSTYE
CCCCCEEEECHHHCC		7.9811713248
650PhosphorylationKYYIDPSTYEDPCQA
EEEECHHHCCCHHHH		36.0026356563
651PhosphorylationYYIDPSTYEDPCQAI
EEECHHHCCCHHHHH		23.7527259358
669PhosphorylationAREVDPAYIKIEEVI
HHHCCHHHEEEEEEE		14.2426356563
680PhosphorylationEEVIGTGSFGEVRQG
EEEECCCCCCHHHCC		29.8930576142
795PhosphorylationSFAFVHRSLSAHSVL
HHHHHHHCCCCHHHE		16.2923879269
800PhosphorylationHRSLSAHSVLVNSHL
HHCCCCHHHEECHHH		19.5023879269
817PhosphorylationKVARLGHSPQGPSCL
HHHHCCCCCCCCCHH		19.6823879269
1001UbiquitinationTLAGHQKKLLHHIQL
EEHHHHHHHHHHHHH		50.11-
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 EPHB6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPHB6_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 EPHB6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPHB4_HUMANEPHB4physical
20086179
REL_HUMANRELphysical
25416956
ITF2_HUMANTCF4physical
25416956
TRI39_HUMANTRIM39physical
25416956
NIF3L_HUMANNIF3L1physical
25416956
INCA1_HUMANINCA1physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
DUS18_HUMANDUSP18physical
28065597
DUS19_HUMANDUSP19physical
28065597
STYX_HUMANSTYXphysical
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 EPHB6_HUMAN

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Related Literatures of Post-Translational Modification

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