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Protein
Submitted name:

Eph receptor B3 (Predicted)

Gene

Ephb3

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Protein predictedi

Functioni

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.SAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei660 – 6601ATPUniRule annotation
Active sitei753 – 7531Proton acceptorUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi634 – 6429ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. axon guidance receptor activity Source: Ensembl
  3. ephrin receptor activity Source: InterPro

GO - Biological processi

  1. angiogenesis Source: Ensembl
  2. axonal fasciculation Source: Ensembl
  3. cell migration Source: Ensembl
  4. central nervous system projection neuron axonogenesis Source: Ensembl
  5. corpus callosum development Source: Ensembl
  6. dendritic spine morphogenesis Source: Ensembl
  7. digestive tract morphogenesis Source: Ensembl
  8. palate development Source: Ensembl
  9. positive regulation of synapse assembly Source: Ensembl
  10. protein autophosphorylation Source: Ensembl
  11. regulation of axonogenesis Source: Ensembl
  12. regulation of Cdc42 GTPase activity Source: Ensembl
  13. regulation of cell-cell adhesion Source: Ensembl
  14. regulation of Rac GTPase activity Source: Ensembl
  15. retinal ganglion cell axon guidance Source: Ensembl
  16. substrate adhesion-dependent cell spreading Source: Ensembl
  17. thymus development Source: Ensembl
  18. urogenital system development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, ReceptorSAAS annotationImported, Transferase, Tyrosine-protein kinaseSAAS annotation

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_277188. EPHB-mediated forward signaling.
REACT_299172. Ephrin signaling.
REACT_313117. EPH-ephrin mediated repulsion of cells.
REACT_348379. EPH-Ephrin signaling.

Names & Taxonomyi

Protein namesi
Submitted name:
Eph receptor B3 (Predicted)Imported
Submitted name:
Protein Ephb3Imported
Gene namesi
Name:Ephb3Imported
Synonyms:Ephb3_predictedImported
ORF Names:rCG_36502Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi1305602. Ephb3.

Subcellular locationi

GO - Cellular componenti

  1. integral component of plasma membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Family & Domainsi

Sequence similaritiesi

Contains SAM (sterile alpha motif) domain.SAAS annotation
Contains protein kinase domain.SAAS annotation

Keywords - Domaini

RepeatSAAS annotation, Transmembrane, Transmembrane helixSAAS annotation

Phylogenomic databases

GeneTreeiENSGT00760000118975.
InParanoidiD3ZH39.
KOiK05112.
OMAiNLRPKFA.
OrthoDBiEOG7VTDM6.
PhylomeDBiD3ZH39.
TreeFamiTF315608.

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.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
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.
PF00536. SAM_1. 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.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 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]

Sequencei

Sequence statusi: Complete.

D3ZH39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGARPPPGL LPLLAPLLLP LLLPAGCRAL EETLMDTKWV TSELAWTSHP
60 70 80 90 100
ESGWEEVSGY DEAMNPIRTY QVCNVRESSQ NNWLRTGFIW RREVQRVYVE
110 120 130 140 150
LKFTVRDCNS IPNIPGSCKE TFNLFYYEAD SDVASASSPF WMENPYVKVD
160 170 180 190 200
TIAPDESFSR LDAGRVNTKV RSFGPLSKAG FYLAFQDQGA CMSLISVRAF
210 220 230 240 250
YKKCASTTAG FALFPETLTG AEPTSLVIAP GTCIANAVEV SVPLKLYCNG
260 270 280 290 300
DGEWMVPVGA CTCATGHEPA AKETQCRACP PGSYKAKQGE GPCLPCPPNS
310 320 330 340 350
RTTSPAASIC TCHNNFYRAD SDTADSACTT VPSPPRGVIS NVNETSLILE
360 370 380 390 400
WSEPRDLGGR DDLLYNVICK KCRGSSGAGG PATCSRCDDN VEFEPRQLGL
410 420 430 440 450
TERRVHISHL LAHTRYTFEV QAVNGVSGKS PLPPRYAAVN ITTNQAAPSE
460 470 480 490 500
VPTLHLHSSS GSSLTLSWAP PERPNGVILD YEMKYFEKSK GIASTVTSQK
510 520 530 540 550
NSVQLDGLQP DARYVVQVRA RTVAGYGQYS RPAEFETTSE RGSGAQQLQE
560 570 580 590 600
QLPLIVGSTV AGFVFMVVVV VIALVCLRKQ RQGPDAEYTE KLQQYVAPRM
610 620 630 640 650
KVYIDPFTYE DPNEAVREFA KEIDVSCVKI EEVIGAGEFG EVCRGRLKLP
660 670 680 690 700
GRREVFVAIK TLKVGYTERQ RRDFLSEASI MGQFDHPNII RLEGVVTKSR
710 720 730 740 750
PVMILTEFME NCALDSFLRL NDGQFTVIQL VGMLRGIAAG MKYLSEMNYV
760 770 780 790 800
HRDLAARNIL VNSNLVCKVS DFGLSRFLED DPSDPTYTSS LGGKIPIRWT
810 820 830 840 850
APEAIAYRKF TSASDVWSYG IVMWEVMSYG ERPYWDMSNQ DVINAVEQDY
860 870 880 890 900
RLPPPMDCPT ALHQLMLDCW VRDRNLRPKF SQIVNTLDKL IRNAASLKVI
910 920 930 940 950
ASAPSGMSQP LLDRTVPDYT TFTTVGDWLD AIKMGRYKES FVGAGFASFD
960 970 980 990 1000
LVAQMTAEDL LRIGVTLAGH QKKILSSIQD MRLQMNQTLP VQEVCPKPLH
1010 1020 1030 1040
IEDGLEEGVI SPPQMPQGPG LPALQSGIFT TQIWLCFSSG GPGRVGWG
Length:1,048
Mass (Da):115,537
Last modified:April 20, 2010 - v1
Checksum:i340974E05953244D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06069444 Genomic DNA. No translation available.
CH473999 Genomic DNA. Translation: EDL78031.1.
RefSeqiNP_001099338.1. NM_001105868.1.
UniGeneiRn.131133.

Genome annotation databases

EnsembliENSRNOT00000044896; ENSRNOP00000039489; ENSRNOG00000031801.
GeneIDi287989.
KEGGirno:287989.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06069444 Genomic DNA. No translation available.
CH473999 Genomic DNA. Translation: EDL78031.1.
RefSeqiNP_001099338.1. NM_001105868.1.
UniGeneiRn.131133.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000044896; ENSRNOP00000039489; ENSRNOG00000031801.
GeneIDi287989.
KEGGirno:287989.

Organism-specific databases

CTDi2049.
RGDi1305602. Ephb3.

Phylogenomic databases

GeneTreeiENSGT00760000118975.
InParanoidiD3ZH39.
KOiK05112.
OMAiNLRPKFA.
OrthoDBiEOG7VTDM6.
PhylomeDBiD3ZH39.
TreeFamiTF315608.

Enzyme and pathway databases

ReactomeiREACT_277188. EPHB-mediated forward signaling.
REACT_299172. Ephrin signaling.
REACT_313117. EPH-ephrin mediated repulsion of cells.
REACT_348379. EPH-Ephrin signaling.

Miscellaneous databases

NextBioi627371.

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.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
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.
PF00536. SAM_1. 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.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Ensembl
    Submitted (JUN-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiD3ZH39_RAT
AccessioniPrimary (citable) accession number: D3ZH39
Entry historyi
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: April 1, 2015
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.