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O15197 (EPHB6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin type-B receptor 6
Alternative name(s):
HEP
Tyrosine-protein kinase-defective receptor EPH-6
Gene names
Name:EPHB6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1021 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11

Subunit structure

Interacts with CBL and EPHB1. Interacts with FYN; this interaction takes place in a ligand-independent manner. Ref.9 Ref.11

Subcellular location

Membrane; Single-pass type I membrane protein.

Isoform 3: Secreted Probable.

Tissue specificity

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. Ref.1 Ref.12 Ref.13

Domain

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.

Post-translational modification

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.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.

Contains 1 Eph LBD (Eph ligand-binding) domain.

Contains 2 fibronectin type-III domains.

Contains 1 protein kinase domain.

Contains 1 SAM (sterile alpha motif) domain.

Sequence caution

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.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15197-1)

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.
Isoform 2 (identifier: O15197-2)

The sequence of this isoform differs from the canonical sequence as follows:
     16-292: Missing.
Isoform 3 (identifier: O15197-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.8
Chain32 – 1021990Ephrin type-B receptor 6
PRO_0000016837

Regions

Topological domain32 – 594563Extracellular Potential
Transmembrane595 – 61521Helical; Potential
Topological domain616 – 1021406Cytoplasmic Potential
Domain33 – 237205Eph LBD
Domain369 – 486118Fibronectin type-III 1
Domain487 – 58296Fibronectin type-III 2
Domain670 – 919250Protein kinase
Domain948 – 101265SAM
Nucleotide binding676 – 6849ATP By similarity
Motif1019 – 10213PDZ-binding Potential
Compositional bias166 – 17611Poly-Ser
Compositional bias219 – 366148Cys-rich
Compositional bias881 – 8844Poly-Pro

Amino acid modifications

Glycosylation4801N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence16 – 292277Missing in isoform 2.
VSP_037496
Alternative sequence487 – 54054VPSAV…FTLTS → GELFSLAFRIPCLRSFEPPS LLLISSLVHPCRPPLKADPA PRDSYPHNNFPFAL in isoform 3.
VSP_037497
Alternative sequence541 – 1021481Missing in isoform 3.
VSP_037498
Natural variant1221G → S. Ref.2 Ref.15
Corresponds to variant rs8177173 [ dbSNP | Ensembl ].
VAR_019139
Natural variant1701S → T. Ref.15
VAR_042190
Natural variant2211A → V. Ref.15
VAR_042191
Natural variant2821P → H. Ref.15
VAR_042192
Natural variant2821P → R. Ref.2
Corresponds to variant rs8177143 [ dbSNP | Ensembl ].
VAR_019140
Natural variant3091R → Q. Ref.15
Corresponds to variant rs55728646 [ dbSNP | Ensembl ].
VAR_042193
Natural variant3241S → A. Ref.2 Ref.15
Corresponds to variant rs8177146 [ dbSNP | Ensembl ].
VAR_019141
Natural variant3321S → L. Ref.15
Corresponds to variant rs35189999 [ dbSNP | Ensembl ].
VAR_042194
Natural variant3601D → N in a colorectal cancer sample; somatic mutation. Ref.14
VAR_036091
Natural variant4991R → Q. Ref.2
Corresponds to variant rs8177175 [ dbSNP | Ensembl ].
VAR_019142
Natural variant6031A → P in a colorectal cancer sample; somatic mutation. Ref.14
VAR_036092
Natural variant6621A → V. Ref.15
Corresponds to variant rs35984674 [ dbSNP | Ensembl ].
VAR_042195
Natural variant7191R → Q in a colorectal cancer sample; somatic mutation. Ref.14
VAR_036093
Natural variant7431P → S in an ovarian mucinous carcinoma sample; somatic mutation. Ref.15
VAR_042196
Natural variant8131R → H. Ref.15
VAR_042197
Natural variant8751E → K in a glioblastoma multiforme sample; somatic mutation. Ref.15
VAR_042198
Natural variant9301D → G in a colorectal cancer sample; somatic mutation. Ref.14
VAR_036094
Natural variant9931I → V. Ref.15
VAR_042199

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 20, 2010. Version 4.
Checksum: BF1D4D9BE34358A5

FASTA1,021110,700
        10         20         30         40         50         60 
MATEGAAQLG NRVAGMVCSL WVLLLVSSVL ALEEVLLDTT GETSEIGWLT YPPGGWDEVS 

        70         80         90        100        110        120 
VLDDQRRLTR TFEACHVAGA PPGTGQDNWL QTHFVERRGA QRAHIRLHFS VRACSSLGVS 

       130        140        150        160        170        180 
GGTCRETFTL YYRQAEEPDS PDSVSSWHLK RWTKVDTIAA DESFPSSSSS SSSSSSAAWA 

       190        200        210        220        230        240 
VGPHGAGQRA GLQLNVKERS FGPLTQRGFY VAFQDTGACL ALVAVRLFSY TCPAVLRSFA 

       250        260        270        280        290        300 
SFPETQASGA GGASLVAAVG TCVAHAEPEE DGVGGQAGGS PPRLHCNGEG KWMVAVGGCR 

       310        320        330        340        350        360 
CQPGYQPARG DKACQACPRG LYKSSAGNAP CSPCPARSHA PNPAAPVCPC LEGFYRASSD 

       370        380        390        400        410        420 
PPEAPCTGPP SAPQELWFEV QGSALMLHWR LPRELGGRGD LLFNVVCKEC EGRQEPASGG 

       430        440        450        460        470        480 
GGTCHRCRDE VHFDPRQRGL TESRVLVGGL RAHVPYILEV QAVNGVSELS PDPPQAAAIN 

       490        500        510        520        530        540 
VSTSHEVPSA VPVVHQVSRA SNSITVSWPQ PDQTNGNILD YQLRYYDQAE DESHSFTLTS 

       550        560        570        580        590        600 
ETNTATVTQL SPGHIYGFQV RARTAAGHGP YGGKVYFQTL PQGELSSQLP ERLSLVIGSI 

       610        620        630        640        650        660 
LGALAFLLLA AITVLAVVFQ RKRRGTGYTE QLQQYSSPGL GVKYYIDPST YEDPCQAIRE 

       670        680        690        700        710        720 
LAREVDPAYI KIEEVIGTGS FGEVRQGRLQ PRGRREQTVA IQALWAGGAE SLQMTFLGRA 

       730        740        750        760        770        780 
AVLGQFQHPN ILRLEGVVTK SRPLMVLTEF MELGPLDSFL RQREGQFSSL QLVAMQRGVA 

       790        800        810        820        830        840 
AAMQYLSSFA FVHRSLSAHS VLVNSHLVCK VARLGHSPQG PSCLLRWAAP EVIAHGKHTT 

       850        860        870        880        890        900 
SSDVWSFGIL MWEVMSYGER PYWDMSEQEV LNAIEQEFRL PPPPGCPPGL HLLMLDTWQK 

       910        920        930        940        950        960 
DRARRPHFDQ LVAAFDKMIR KPDTLQAGGD PGERPSQALL TPVALDFPCL DSPQAWLSAI 

       970        980        990       1000       1010       1020 
GLECYQDNFS KFGLCTFSDV AQLSLEDLPA LGITLAGHQK KLLHHIQLLQ QHLRQQGSVE 


V 

« Hide

Isoform 2 [UniParc].

Checksum: 8BCF105B3B7A5B92
Show »

FASTA74481,211
Isoform 3 (EphB6v) [UniParc].

Checksum: 3635871D1070FF27
Show »

FASTA54057,498

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC5526.
RefSeqNP_001267724.2. NM_001280795.2.
NP_004436.4. NM_004445.5.
UniGeneHs.380089.

3D structure databases

ProteinModelPortalO15197.
SMRO15197. Positions 31-587, 621-926, 956-1007.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108365. 5 interactions.
IntActO15197. 7 interactions.
MINTMINT-1392963.
STRING9606.ENSP00000376684.

Chemistry

BindingDBO15197.
ChEMBLCHEMBL5836.
GuidetoPHARMACOLOGY1834.

PTM databases

PhosphoSiteO15197.

Proteomic databases

PaxDbO15197.
PRIDEO15197.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392957; ENSP00000376684; ENSG00000106123. [O15197-1]
ENST00000442129; ENSP00000410789; ENSG00000106123. [O15197-1]
GeneID2051.
KEGGhsa:2051.
UCSCuc003wbs.3. human. [O15197-1]

Organism-specific databases

CTD2051.
GeneCardsGC07P142552.
HGNCHGNC:3396. EPHB6.
HPAHPA001351.
MIM602757. gene.
neXtProtNX_O15197.
PharmGKBPA27828.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233856.
HOVERGENHBG062180.
InParanoidO15197.
KOK05114.
OMAEQAVAIQ.
OrthoDBEOG7VTDM6.
PhylomeDBO15197.
TreeFamTF314013.

Gene expression databases

ArrayExpressO15197.
BgeeO15197.
CleanExHS_EPHB6.
GenevestigatorO15197.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProIPR027936. 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]
PfamPF14575. 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]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEPS51550. 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]
ProtoNetSearch...

Other

ChiTaRSEPHB6. human.
GeneWikiEPHB6.
GenomeRNAi2051.
NextBio8339.
PROO15197.
SOURCESearch...

Entry information

Entry nameEPHB6_HUMAN
AccessionPrimary (citable) accession number: O15197
Secondary accession number(s): A4D2I7 expand/collapse secondary AC list , A8CDT5, D3DXD3, Q2TB23, Q2TB24
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM