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O15197

- EPHB6_HUMAN

UniProt

O15197 - EPHB6_HUMAN

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Protein
Ephrin type-B receptor 6
Gene
EPHB6
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 6849ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. calcium ion homeostasis Source: Ensembl
  2. parathyroid hormone secretion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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: Chromosome 7

Organism-specific databases

HGNCiHGNC:3396. EPHB6.

Subcellular locationi

Isoform 3 : Secreted Inferred

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 594563Extracellular Reviewed prediction
Add
BLAST
Transmembranei595 – 61521Helical; Reviewed prediction
Add
BLAST
Topological domaini616 – 1021406Cytoplasmic Reviewed prediction
Add
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 Publication
Add
BLAST
Chaini32 – 1021990Ephrin type-B receptor 6
PRO_0000016837Add
BLAST

Amino acid modifications

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

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.

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

ArrayExpressiO15197.
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. 5 interactions.
IntActiO15197. 7 interactions.
MINTiMINT-1392963.
STRINGi9606.ENSP00000376684.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 237205Eph LBD
Add
BLAST
Domaini369 – 486118Fibronectin type-III 1
Add
BLAST
Domaini487 – 58296Fibronectin type-III 2
Add
BLAST
Domaini670 – 919250Protein kinase
Add
BLAST
Domaini948 – 101265SAM
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1019 – 10213PDZ-binding Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi166 – 17611Poly-Ser
Add
BLAST
Compositional biasi219 – 366148Cys-rich
Add
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

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. Fibronectin_type3.
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

MATEGAAQLG NRVAGMVCSL WVLLLVSSVL ALEEVLLDTT GETSEIGWLT     50
YPPGGWDEVS VLDDQRRLTR TFEACHVAGA PPGTGQDNWL QTHFVERRGA 100
QRAHIRLHFS VRACSSLGVS GGTCRETFTL YYRQAEEPDS PDSVSSWHLK 150
RWTKVDTIAA DESFPSSSSS SSSSSSAAWA VGPHGAGQRA GLQLNVKERS 200
FGPLTQRGFY VAFQDTGACL ALVAVRLFSY TCPAVLRSFA SFPETQASGA 250
GGASLVAAVG TCVAHAEPEE DGVGGQAGGS PPRLHCNGEG KWMVAVGGCR 300
CQPGYQPARG DKACQACPRG LYKSSAGNAP CSPCPARSHA PNPAAPVCPC 350
LEGFYRASSD PPEAPCTGPP SAPQELWFEV QGSALMLHWR LPRELGGRGD 400
LLFNVVCKEC EGRQEPASGG GGTCHRCRDE VHFDPRQRGL TESRVLVGGL 450
RAHVPYILEV QAVNGVSELS PDPPQAAAIN VSTSHEVPSA VPVVHQVSRA 500
SNSITVSWPQ PDQTNGNILD YQLRYYDQAE DESHSFTLTS ETNTATVTQL 550
SPGHIYGFQV RARTAAGHGP YGGKVYFQTL PQGELSSQLP ERLSLVIGSI 600
LGALAFLLLA AITVLAVVFQ RKRRGTGYTE QLQQYSSPGL GVKYYIDPST 650
YEDPCQAIRE LAREVDPAYI KIEEVIGTGS FGEVRQGRLQ PRGRREQTVA 700
IQALWAGGAE SLQMTFLGRA AVLGQFQHPN ILRLEGVVTK SRPLMVLTEF 750
MELGPLDSFL RQREGQFSSL QLVAMQRGVA AAMQYLSSFA FVHRSLSAHS 800
VLVNSHLVCK VARLGHSPQG PSCLLRWAAP EVIAHGKHTT SSDVWSFGIL 850
MWEVMSYGER PYWDMSEQEV LNAIEQEFRL PPPPGCPPGL HLLMLDTWQK 900
DRARRPHFDQ LVAAFDKMIR KPDTLQAGGD PGERPSQALL TPVALDFPCL 950
DSPQAWLSAI GLECYQDNFS KFGLCTFSDV AQLSLEDLPA LGITLAGHQK 1000
KLLHHIQLLQ QHLRQQGSVE V 1021
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.
The sequence AAI10608.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAP20939.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA21560.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence EAL23775.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence EAW51902.1 differs from that shown. Reason: Erroneous gene model prediction.

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.
VSP_037496Add
BLAST
Alternative sequencei487 – 54054VPSAV…FTLTS → GELFSLAFRIPCLRSFEPPS LLLISSLVHPCRPPLKADPA PRDSYPHNNFPFAL in isoform 3.
VSP_037497Add
BLAST
Alternative sequencei541 – 1021481Missing in isoform 3.
VSP_037498Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. [O15197-1]
ENST00000442129; ENSP00000410789; ENSG00000106123. [O15197-1]
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:
EMBL
GenBank
DDBJ
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 .
PIRi JC5526.
RefSeqi NP_001267724.2. NM_001280795.2.
NP_004436.4. NM_004445.5.
UniGenei Hs.380089.

3D structure databases

ProteinModelPortali O15197.
SMRi O15197. Positions 31-587, 621-926, 956-1007.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108365. 5 interactions.
IntActi O15197. 7 interactions.
MINTi MINT-1392963.
STRINGi 9606.ENSP00000376684.

Chemistry

BindingDBi O15197.
ChEMBLi CHEMBL5836.
GuidetoPHARMACOLOGYi 1834.

PTM databases

PhosphoSitei O15197.

Proteomic databases

PaxDbi O15197.
PRIDEi O15197.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000392957 ; ENSP00000376684 ; ENSG00000106123 . [O15197-1 ]
ENST00000442129 ; ENSP00000410789 ; ENSG00000106123 . [O15197-1 ]
GeneIDi 2051.
KEGGi hsa:2051.
UCSCi uc003wbs.3. human. [O15197-1 ]

Organism-specific databases

CTDi 2051.
GeneCardsi GC07P142552.
HGNCi HGNC:3396. EPHB6.
HPAi HPA001351.
MIMi 602757. gene.
neXtProti NX_O15197.
PharmGKBi PA27828.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi O15197.
KOi K05114.
OMAi EQAVAIQ.
OrthoDBi EOG7VTDM6.
PhylomeDBi O15197.
TreeFami TF314013.

Miscellaneous databases

ChiTaRSi EPHB6. human.
GeneWikii EPHB6.
GenomeRNAii 2051.
NextBioi 8339.
PROi O15197.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15197.
Bgeei O15197.
CleanExi HS_EPHB6.
Genevestigatori O15197.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProi IPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
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 ]
Pfami PF14575. 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 ]
PIRSFi PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEi PS51550. 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 ]
ProtoNeti Search...

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: July 9, 2014
This is version 157 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

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