O15197 (EPHB6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ephrin type-B receptor 6

Alternative name(s):
HEP
Tyrosine-protein kinase-defective receptor EPH-6

Gene names

Name:

EPHB6

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1021 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Receptor
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ephrin receptor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Ref.8
	Chain	32 – 1021	990	Ephrin type-B receptor 6		PRO_0000016837
Regions
	Topological domain	32 – 594	563	Extracellular Potential
	Transmembrane	595 – 615	21	Helical; Potential
	Topological domain	616 – 1021	406	Cytoplasmic Potential
	Domain	33 – 237	205	Eph LBD
	Domain	369 – 478	110	Fibronectin type-III 1
	Domain	488 – 579	92	Fibronectin type-III 2
	Domain	670 – 919	250	Protein kinase
	Domain	948 – 1012	65	SAM
	Nucleotide binding	676 – 684	9	ATP By similarity
	Motif	1019 – 1021	3	PDZ-binding Potential
	Compositional bias	166 – 176	11	Poly-Ser
	Compositional bias	219 – 366	148	Cys-rich
	Compositional bias	881 – 884	4	Poly-Pro
Amino acid modifications
	Glycosylation	480	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	16 – 292	277	Missing in isoform 2.		VSP_037496
	Alternative sequence	487 – 540	54	VPSAV…FTLTS → GELFSLAFRIPCLRSFEPPS LLLISSLVHPCRPPLKADPA PRDSYPHNNFPFAL in isoform 3.		VSP_037497
	Alternative sequence	541 – 1021	481	Missing in isoform 3.		VSP_037498
	Natural variant	122	1	G → S. Ref.2 Ref.15 Corresponds to variant rs8177173 [ dbSNP | Ensembl ].		VAR_019139
	Natural variant	170	1	S → T. Ref.15		VAR_042190
	Natural variant	221	1	A → V. Ref.15		VAR_042191
	Natural variant	282	1	P → H. Ref.15		VAR_042192
	Natural variant	282	1	P → R. Ref.2 Corresponds to variant rs8177143 [ dbSNP | Ensembl ].		VAR_019140
	Natural variant	309	1	R → Q. Ref.15		VAR_042193
	Natural variant	324	1	S → A. Ref.2 Ref.15 Corresponds to variant rs8177146 [ dbSNP | Ensembl ].		VAR_019141
	Natural variant	332	1	S → L. Ref.15		VAR_042194
	Natural variant	360	1	D → N in a colorectal cancer sample; somatic mutation. Ref.14		VAR_036091
	Natural variant	499	1	R → Q. Ref.2 Corresponds to variant rs8177175 [ dbSNP | Ensembl ].		VAR_019142
	Natural variant	603	1	A → P in a colorectal cancer sample; somatic mutation. Ref.14		VAR_036092
	Natural variant	662	1	A → V. Ref.15		VAR_042195
	Natural variant	719	1	R → Q in a colorectal cancer sample; somatic mutation. Ref.14		VAR_036093
	Natural variant	743	1	P → S in an ovarian mucinous carcinoma sample; somatic mutation. Ref.15		VAR_042196
	Natural variant	813	1	R → H. Ref.15		VAR_042197
	Natural variant	875	1	E → K in a glioblastoma multiforme sample; somatic mutation. Ref.15		VAR_042198
	Natural variant	930	1	D → G in a colorectal cancer sample; somatic mutation. Ref.14		VAR_036094
	Natural variant	993	1	I → V. Ref.15		VAR_042199

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 20, 2010. Version 4. Checksum: BF1D4D9BE34358A5	FASTA	1,021	110,700
	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
	Isoform 2 [UniParc]. Checksum: 8BCF105B3B7A5B92	FASTA	744	81,211
	10 20 30 40 50 60 MATEGAAQLG NRVAGMVAVG GCRCQPGYQP ARGDKACQAC PRGLYKSSAG NAPCSPCPAR 70 80 90 100 110 120 SHAPNPAAPV CPCLEGFYRA SSDPPEAPCT GPPSAPQELW FEVQGSALML HWRLPRELGG 130 140 150 160 170 180 RGDLLFNVVC KECEGRQEPA SGGGGTCHRC RDEVHFDPRQ RGLTESRVLV GGLRAHVPYI 190 200 210 220 230 240 LEVQAVNGVS ELSPDPPQAA AINVSTSHEV PSAVPVVHQV SRASNSITVS WPQPDQTNGN 250 260 270 280 290 300 ILDYQLRYYD QAEDESHSFT LTSETNTATV TQLSPGHIYG FQVRARTAAG HGPYGGKVYF 310 320 330 340 350 360 QTLPQGELSS QLPERLSLVI GSILGALAFL LLAAITVLAV VFQRKRRGTG YTEQLQQYSS 370 380 390 400 410 420 PGLGVKYYID PSTYEDPCQA IRELAREVDP AYIKIEEVIG TGSFGEVRQG RLQPRGRREQ 430 440 450 460 470 480 TVAIQALWAG GAESLQMTFL GRAAVLGQFQ HPNILRLEGV VTKSRPLMVL TEFMELGPLD 490 500 510 520 530 540 SFLRQREGQF SSLQLVAMQR GVAAAMQYLS SFAFVHRSLS AHSVLVNSHL VCKVARLGHS 550 560 570 580 590 600 PQGPSCLLRW AAPEVIAHGK HTTSSDVWSF GILMWEVMSY GERPYWDMSE QEVLNAIEQE 610 620 630 640 650 660 FRLPPPPGCP PGLHLLMLDT WQKDRARRPH FDQLVAAFDK MIRKPDTLQA GGDPGERPSQ 670 680 690 700 710 720 ALLTPVALDF PCLDSPQAWL SAIGLECYQD NFSKFGLCTF SDVAQLSLED LPALGITLAG 730 740 HQKKLLHHIQ LLQQHLRQQG SVEV
	Isoform 3 (EphB6v) [UniParc]. Checksum: 3635871D1070FF27	FASTA	540	57,498
	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 VSTSHEGELF SLAFRIPCLR SFEPPSLLLI SSLVHPCRPP LKADPAPRDS YPHNNFPFAL

References

	« Hide 'large scale' referencesShow '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: 9207182] [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: 12853948] [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: 12690205] [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. , 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: 15489334] [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: 18425388] [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: 15340161] [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: 11713248] [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: 12517763] [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: 15955811] [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: 18754880] [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: 19234485] [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. , 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: 16959974] [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. , 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: 17344846] [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.

Web resources

SeattleSNPs

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.
IPI	IPI00005222. IPI00873336. IPI00915412.
PIR	JC5526.
RefSeq	NP_004436.2. NM_004445.3.
UniGene	Hs.380089.
3D structure databases
ProteinModelPortal	O15197.
SMR	O15197. Positions 28-584, 656-941, 949-1009.
ModBase	Search...
Protein-protein interaction databases
IntAct	O15197. 5 interactions.
MINT	MINT-1392963.
STRING	O15197.
PTM databases
PhosphoSite	O15197.
Proteomic databases
PRIDE	O15197.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000222847; ENSP00000222847; ENSG00000106123. ENST00000392957; ENSP00000376684; ENSG00000106123. ENST00000411471; ENSP00000409061; ENSG00000106123. ENST00000442129; ENSP00000410789; ENSG00000106123.
GeneID	2051.
KEGG	hsa:2051.
UCSC	uc003wbq.1. human.
Organism-specific databases
CTD	2051.
GeneCards	GC07P142552.
H-InvDB	HIX0007161.
HGNC	HGNC:3396. EPHB6.
HPA	HPA001351.
MIM	602757. gene.
neXtProt	NX_O15197.
PharmGKB	PA27828.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00570000078802.
HOGENOM	HBG755340.
HOVERGEN	HBG062180.
InParanoid	O15197.
OMA	FDKMIRK.
OrthoDB	EOG4PK272.
PhylomeDB	O15197.
Gene expression databases
ArrayExpress	O15197.
Bgee	O15197.
CleanEx	HS_EPHB6.
Genevestigator	O15197.
GermOnline	ENSG00000106123. Homo sapiens.
Family and domain databases
InterPro	IPR001090. Ephrin_rcpt_lig-bd. IPR003961. Fibronectin_type3. IPR008979. Galactose-bd-like. IPR013783. Ig-like_fold. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR001660. SAM. IPR013761. SAM/pointed. IPR011510. SAM_2. IPR001245. Ser-Thr/Tyr_kinase. IPR011641. Tyr-kin_ephrin_A/B_rcpt-like. IPR016257. Tyr_kinase_ephrin_rcpt. IPR001426. Tyr_kinase_rcpt_V_CS. [Graphical view]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 2 hits. G3DSA:1.10.150.50. SAM_type. 1 hit.
KO	K05114.
Pfam	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]
PIRSF	PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTS	PR00109. TYRKINASE.
SMART	SM00615. EPH_lbd. 1 hit. SM00060. FN3. 2 hits. SM00454. SAM. 1 hit. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 2 hits. SSF49785. Gal_bind_like. 1 hit. SSF56112. Kinase_like. 1 hit. SSF47769. SAM_homology. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
NextBio	8339.
SOURCE	Search...

Entry information

Entry name

EPHB6_HUMAN

Accession

Primary (citable) accession number: O15197
Secondary accession number(s): A4D2I7 , A8CDT5, D3DXD3, Q2TB23, Q2TB24

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	April 20, 2010
Last modified:	January 25, 2012
This is version 131 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.