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Protein

Ephrin type-B receptor 6

Gene

EPHB6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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-B2.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi676 – 6849ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ephrin receptor activity Source: ProtInc
  3. receptor activity Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_228085. EPHB-mediated forward signaling.
REACT_228170. EPH-Ephrin signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.
REACT_228226. Ephrin signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-B receptor 6
Alternative name(s):
HEP
Tyrosine-protein kinase-defective receptor EPH-6
Gene namesi
Name:EPHB6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:3396. EPHB6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 594563ExtracellularSequence AnalysisAdd
BLAST
Transmembranei595 – 61521HelicalSequence AnalysisAdd
BLAST
Topological domaini616 – 1021406CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. integral component of plasma membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27828.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 31311 PublicationAdd
BLAST
Chaini32 – 1021990Ephrin type-B receptor 6PRO_0000016837Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Ligand-binding increases phosphorylation on tyrosine residues. Phosphorylation on tyrosine residues is mediated by transphosphorylation by the catalytically active EPHB1 in a ligand-independent manner. Tyrosine phosphorylation of the receptor may act as a switch on the functional transition from cell adhesion/attraction to de-adhesion/repulsion.2 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiO15197.
PRIDEiO15197.

PTM databases

PhosphoSiteiO15197.

Expressioni

Tissue specificityi

Expressed in brain. Expressed in non invasive breast carcinoma cell lines (at protein level). Strong expression in brain and pancreas, and weak expression in other tissues, such as heart, placenta, lung, liver, skeletal muscle and kidney. Expressed in breast non invasive tumors but not in metastatic lesions. Isoform 3 is expressed in cell lines of glioblastomas, anaplastic astrocytomas, gliosarcomas and astrocytomas. Isoform 3 is not detected in normal tissues.3 Publications

Gene expression databases

BgeeiO15197.
CleanExiHS_EPHB6.
GenevestigatoriO15197.

Organism-specific databases

HPAiHPA001351.

Interactioni

Subunit structurei

Interacts with CBL and EPHB1. Interacts with FYN; this interaction takes place in a ligand-independent manner.2 Publications

Protein-protein interaction databases

BioGridi108365. 11 interactions.
IntActiO15197. 7 interactions.
MINTiMINT-1392963.
STRINGi9606.ENSP00000376684.

Structurei

3D structure databases

ProteinModelPortaliO15197.
SMRiO15197. Positions 31-587, 621-926, 956-1007.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 237205Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini369 – 486118Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini487 – 58296Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini670 – 919250Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini948 – 101265SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1019 – 10213PDZ-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi166 – 17611Poly-SerAdd
BLAST
Compositional biasi219 – 366148Cys-richAdd
BLAST
Compositional biasi881 – 8844Poly-Pro

Domaini

The protein kinase domain is predicted to be catalytically inactive. Its extracellular domain is capable of promoting cell adhesion and migration in response to low concentrations of ephrin-B2, but its cytoplasmic domain is essential for cell repulsion and inhibition of migration induced by high concentrations of ephrin-B2.

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation
Contains 1 Eph LBD (Eph ligand-binding) domain.PROSITE-ProRule annotation
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiO15197.
KOiK05114.
OMAiEQAVAIQ.
OrthoDBiEOG7VTDM6.
PhylomeDBiO15197.
TreeFamiTF314013.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PfamiPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07699. GCC2_GCC3. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15197-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATEGAAQLG NRVAGMVCSL WVLLLVSSVL ALEEVLLDTT GETSEIGWLT
60 70 80 90 100
YPPGGWDEVS VLDDQRRLTR TFEACHVAGA PPGTGQDNWL QTHFVERRGA
110 120 130 140 150
QRAHIRLHFS VRACSSLGVS GGTCRETFTL YYRQAEEPDS PDSVSSWHLK
160 170 180 190 200
RWTKVDTIAA DESFPSSSSS SSSSSSAAWA VGPHGAGQRA GLQLNVKERS
210 220 230 240 250
FGPLTQRGFY VAFQDTGACL ALVAVRLFSY TCPAVLRSFA SFPETQASGA
260 270 280 290 300
GGASLVAAVG TCVAHAEPEE DGVGGQAGGS PPRLHCNGEG KWMVAVGGCR
310 320 330 340 350
CQPGYQPARG DKACQACPRG LYKSSAGNAP CSPCPARSHA PNPAAPVCPC
360 370 380 390 400
LEGFYRASSD PPEAPCTGPP SAPQELWFEV QGSALMLHWR LPRELGGRGD
410 420 430 440 450
LLFNVVCKEC EGRQEPASGG GGTCHRCRDE VHFDPRQRGL TESRVLVGGL
460 470 480 490 500
RAHVPYILEV QAVNGVSELS PDPPQAAAIN VSTSHEVPSA VPVVHQVSRA
510 520 530 540 550
SNSITVSWPQ PDQTNGNILD YQLRYYDQAE DESHSFTLTS ETNTATVTQL
560 570 580 590 600
SPGHIYGFQV RARTAAGHGP YGGKVYFQTL PQGELSSQLP ERLSLVIGSI
610 620 630 640 650
LGALAFLLLA AITVLAVVFQ RKRRGTGYTE QLQQYSSPGL GVKYYIDPST
660 670 680 690 700
YEDPCQAIRE LAREVDPAYI KIEEVIGTGS FGEVRQGRLQ PRGRREQTVA
710 720 730 740 750
IQALWAGGAE SLQMTFLGRA AVLGQFQHPN ILRLEGVVTK SRPLMVLTEF
760 770 780 790 800
MELGPLDSFL RQREGQFSSL QLVAMQRGVA AAMQYLSSFA FVHRSLSAHS
810 820 830 840 850
VLVNSHLVCK VARLGHSPQG PSCLLRWAAP EVIAHGKHTT SSDVWSFGIL
860 870 880 890 900
MWEVMSYGER PYWDMSEQEV LNAIEQEFRL PPPPGCPPGL HLLMLDTWQK
910 920 930 940 950
DRARRPHFDQ LVAAFDKMIR KPDTLQAGGD PGERPSQALL TPVALDFPCL
960 970 980 990 1000
DSPQAWLSAI GLECYQDNFS KFGLCTFSDV AQLSLEDLPA LGITLAGHQK
1010 1020
KLLHHIQLLQ QHLRQQGSVE V
Length:1,021
Mass (Da):110,700
Last modified:April 20, 2010 - v4
Checksum:iBF1D4D9BE34358A5
GO
Isoform 2 (identifier: O15197-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     16-292: Missing.

Show »
Length:744
Mass (Da):81,211
Checksum:i8BCF105B3B7A5B92
GO
Isoform 3 (identifier: O15197-3) [UniParc]FASTAAdd to Basket

Also known as: EphB6v

The sequence of this isoform differs from the canonical sequence as follows:
     487-540: VPSAVPVVHQ...DESHSFTLTS → GELFSLAFRI...YPHNNFPFAL
     541-1021: Missing.

Show »
Length:540
Mass (Da):57,498
Checksum:i3635871D1070FF27
GO

Sequence cautioni

The sequence AAD03058.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAI10608.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAP20939.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA21560.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EAL23775.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAW51902.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti122 – 1221G → S.2 Publications
Corresponds to variant rs8177173 [ dbSNP | Ensembl ].
VAR_019139
Natural varianti170 – 1701S → T.1 Publication
VAR_042190
Natural varianti221 – 2211A → V.1 Publication
VAR_042191
Natural varianti282 – 2821P → H.1 Publication
VAR_042192
Natural varianti282 – 2821P → R.1 Publication
Corresponds to variant rs8177143 [ dbSNP | Ensembl ].
VAR_019140
Natural varianti309 – 3091R → Q.1 Publication
Corresponds to variant rs55728646 [ dbSNP | Ensembl ].
VAR_042193
Natural varianti324 – 3241S → A.2 Publications
Corresponds to variant rs8177146 [ dbSNP | Ensembl ].
VAR_019141
Natural varianti332 – 3321S → L.1 Publication
Corresponds to variant rs35189999 [ dbSNP | Ensembl ].
VAR_042194
Natural varianti360 – 3601D → N in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036091
Natural varianti499 – 4991R → Q.1 Publication
Corresponds to variant rs8177175 [ dbSNP | Ensembl ].
VAR_019142
Natural varianti603 – 6031A → P in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036092
Natural varianti662 – 6621A → V.1 Publication
Corresponds to variant rs35984674 [ dbSNP | Ensembl ].
VAR_042195
Natural varianti719 – 7191R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036093
Natural varianti743 – 7431P → S in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
VAR_042196
Natural varianti813 – 8131R → H.1 Publication
VAR_042197
Natural varianti875 – 8751E → K in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_042198
Natural varianti930 – 9301D → G in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036094
Natural varianti993 – 9931I → V.1 Publication
VAR_042199

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei16 – 292277Missing in isoform 2. 1 PublicationVSP_037496Add
BLAST
Alternative sequencei487 – 54054VPSAV…FTLTS → GELFSLAFRIPCLRSFEPPS LLLISSLVHPCRPPLKADPA PRDSYPHNNFPFAL in isoform 3. 1 PublicationVSP_037497Add
BLAST
Alternative sequencei541 – 1021481Missing in isoform 3. 1 PublicationVSP_037498Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83492 mRNA. Translation: BAA21560.1. Different initiation.
AY280502 Genomic DNA. Translation: AAP20939.1. Different initiation.
AF107256 Genomic DNA. Translation: AAD03058.1. Different initiation.
AC104597 Genomic DNA. No translation available.
CH236959 Genomic DNA. Translation: EAL23775.1. Sequence problems.
CH471198 Genomic DNA. Translation: EAW51900.1.
CH471198 Genomic DNA. Translation: EAW51901.1.
CH471198 Genomic DNA. Translation: EAW51902.1. Sequence problems.
CH471198 Genomic DNA. Translation: EAW51903.1.
BC051028 mRNA. No translation available.
BC110606 mRNA. Translation: AAI10607.1.
BC110607 mRNA. Translation: AAI10608.2. Different initiation.
EU054308 mRNA. Translation: ABV55388.1.
PIRiJC5526.
RefSeqiNP_001267724.2. NM_001280795.2.
NP_004436.4. NM_004445.5.
UniGeneiHs.380089.

Genome annotation databases

EnsembliENST00000392957; ENSP00000376684; ENSG00000106123.
ENST00000442129; ENSP00000410789; ENSG00000106123.
GeneIDi2051.
KEGGihsa:2051.
UCSCiuc003wbs.3. human. [O15197-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83492 mRNA. Translation: BAA21560.1. Different initiation.
AY280502 Genomic DNA. Translation: AAP20939.1. Different initiation.
AF107256 Genomic DNA. Translation: AAD03058.1. Different initiation.
AC104597 Genomic DNA. No translation available.
CH236959 Genomic DNA. Translation: EAL23775.1. Sequence problems.
CH471198 Genomic DNA. Translation: EAW51900.1.
CH471198 Genomic DNA. Translation: EAW51901.1.
CH471198 Genomic DNA. Translation: EAW51902.1. Sequence problems.
CH471198 Genomic DNA. Translation: EAW51903.1.
BC051028 mRNA. No translation available.
BC110606 mRNA. Translation: AAI10607.1.
BC110607 mRNA. Translation: AAI10608.2. Different initiation.
EU054308 mRNA. Translation: ABV55388.1.
PIRiJC5526.
RefSeqiNP_001267724.2. NM_001280795.2.
NP_004436.4. NM_004445.5.
UniGeneiHs.380089.

3D structure databases

ProteinModelPortaliO15197.
SMRiO15197. Positions 31-587, 621-926, 956-1007.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108365. 11 interactions.
IntActiO15197. 7 interactions.
MINTiMINT-1392963.
STRINGi9606.ENSP00000376684.

Chemistry

BindingDBiO15197.
ChEMBLiCHEMBL5836.
GuidetoPHARMACOLOGYi1834.

PTM databases

PhosphoSiteiO15197.

Proteomic databases

PaxDbiO15197.
PRIDEiO15197.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392957; ENSP00000376684; ENSG00000106123.
ENST00000442129; ENSP00000410789; ENSG00000106123.
GeneIDi2051.
KEGGihsa:2051.
UCSCiuc003wbs.3. human. [O15197-1]

Organism-specific databases

CTDi2051.
GeneCardsiGC07P142552.
HGNCiHGNC:3396. EPHB6.
HPAiHPA001351.
MIMi602757. gene.
neXtProtiNX_O15197.
PharmGKBiPA27828.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiO15197.
KOiK05114.
OMAiEQAVAIQ.
OrthoDBiEOG7VTDM6.
PhylomeDBiO15197.
TreeFamiTF314013.

Enzyme and pathway databases

ReactomeiREACT_228085. EPHB-mediated forward signaling.
REACT_228170. EPH-Ephrin signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.
REACT_228226. Ephrin signaling.

Miscellaneous databases

ChiTaRSiEPHB6. human.
GeneWikiiEPHB6.
GenomeRNAii2051.
NextBioi8339.
PROiO15197.
SOURCEiSearch...

Gene expression databases

BgeeiO15197.
CleanExiHS_EPHB6.
GenevestigatoriO15197.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PfamiPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07699. GCC2_GCC3. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of a kinase-defective Eph-like receptor in the normal human brain."
    Matsuoka H., Iwata N., Ito M., Shimoyama M., Nagata A., Chihara K., Takai S., Matsui T.
    Biochem. Biophys. Res. Commun. 235:487-492(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. SeattleSNPs variation discovery resource
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-122; ARG-282; ALA-324 AND GLN-499.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  7. "Identification of EphB6 variant-derived epitope peptides recognized by cytotoxic T-lymphocytes from HLA-A24+ malignant glioma patients."
    Jin M., Komohara Y., Shichijo S., Harada M., Yamanaka R., Miyamoto S., Nikawa J., Itoh K., Yamada A.
    Oncol. Rep. 19:1277-1283(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-1021 (ISOFORM 3).
  8. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 32-46.
  9. "The kinase-null EphB6 receptor undergoes transphosphorylation in a complex with EphB1."
    Freywald A., Sharfe N., Roifman C.M.
    J. Biol. Chem. 277:3823-3828(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBL AND EPHB1, PHOSPHORYLATION.
  10. "The EphB6 receptor inhibits JNK activation in T lymphocytes and modulates T cell receptor-mediated responses."
    Freywald A., Sharfe N., Rashotte C., Grunberger T., Roifman C.M.
    J. Biol. Chem. 278:10150-10156(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Biphasic functions of the kinase-defective Ephb6 receptor in cell adhesion and migration."
    Matsuoka H., Obama H., Kelly M.L., Matsui T., Nakamoto M.
    J. Biol. Chem. 280:29355-29363(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FYN, PHOSPHORYLATION.
  12. "Erythropoietin-producing hepatocyte B6 variant-derived peptides with the ability to induce glioma-reactive cytotoxic T lymphocytes in human leukocyte antigen-A2+ glioma patients."
    Jin M., Komohara Y., Shichijo S., Yamanaka R., Nikawa J., Itoh K., Yamada A.
    Cancer Sci. 99:1656-1662(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  13. "EphB6 receptor significantly alters invasiveness and other phenotypic characteristics of human breast carcinoma cells."
    Fox B.P., Kandpal R.P.
    Oncogene 28:1706-1713(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  14. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-360; PRO-603; GLN-719 AND GLY-930.
  15. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-122; THR-170; VAL-221; HIS-282; GLN-309; ALA-324; LEU-332; VAL-662; SER-743; HIS-813; LYS-875 AND VAL-993.

Entry informationi

Entry nameiEPHB6_HUMAN
AccessioniPrimary (citable) accession number: O15197
Secondary accession number(s): A4D2I7
, A8CDT5, D3DXD3, Q2TB23, Q2TB24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 20, 2010
Last modified: February 4, 2015
This is version 162 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.