位置:首页 > 蛋白库 > EPHB2_HUMAN
EPHB2_HUMAN
ID   EPHB2_HUMAN             Reviewed;        1055 AA.
AC   P29323; O43477; Q5T0U6; Q5T0U7; Q5T0U8;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 5.
DT   03-AUG-2022, entry version 247.
DE   RecName: Full=Ephrin type-B receptor 2;
DE            EC=2.7.10.1;
DE   AltName: Full=Developmentally-regulated Eph-related tyrosine kinase;
DE   AltName: Full=ELK-related tyrosine kinase;
DE   AltName: Full=EPH tyrosine kinase 3;
DE   AltName: Full=EPH-like kinase 5;
DE            Short=EK5;
DE            Short=hEK5;
DE   AltName: Full=Renal carcinoma antigen NY-REN-47;
DE   AltName: Full=Tyrosine-protein kinase TYRO5;
DE   AltName: Full=Tyrosine-protein kinase receptor EPH-3;
DE   Contains:
DE     RecName: Full=EphB2/CTF1 {ECO:0000250|UniProtKB:P54763};
DE   Contains:
DE     RecName: Full=EphB2/CTF2 {ECO:0000250|UniProtKB:P54763};
DE   Flags: Precursor;
GN   Name=EPHB2; Synonyms=DRT, EPHT3, EPTH3, ERK, HEK5, TYRO5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=8033077;
RA   Kiyokawa E., Takai S., Tanaka M., Iwase T., Suzuki M., Xiang Y.Y.,
RA   Naito Y., Yamada K., Sugimura H., Kino I.;
RT   "Overexpression of ERK, an EPH family receptor protein tyrosine kinase, in
RT   various human tumors.";
RL   Cancer Res. 54:3645-3650(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Fetal brain;
RX   PubMed=8589679; DOI=10.1093/hmg/4.11.2033;
RA   Ikegaki N., Tang X.X., Liu X.-G., Biegel J.A., Allen C., Yoshioka A.,
RA   Sulman E.P., Brodeur G.M., Pleasure D.E.;
RT   "Molecular characterization and chromosomal localization of DRT (EPHT3): a
RT   developmentally regulated human protein-tyrosine kinase gene of the EPH
RT   family.";
RL   Hum. Mol. Genet. 4:2033-2045(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=9696046; DOI=10.1038/sj.onc.1201960;
RA   Tang X.X., Pleasure D.E., Brodeur G.M., Ikegaki N.;
RT   "A variant transcript encoding an isoform of the human protein tyrosine
RT   kinase EPHB2 is generated by alternative splicing and alternative use of
RT   polyadenylation signals.";
RL   Oncogene 17:521-526(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 15-986 (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=7898931;
RA   Fox G.M., Holst P.L., Chute H.T., Lindberg R.A., Janssen A.M., Basu R.,
RA   Welcher A.A.;
RT   "cDNA cloning and tissue distribution of five human EPH-like receptor
RT   protein-tyrosine kinases.";
RL   Oncogene 10:897-905(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 509-986 (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=7601466; DOI=10.1016/0888-7543(95)80224-a;
RA   Saito T., Seki N., Matsuda Y., Kitahara M., Murata M., Kanda N., Nomura N.,
RA   Yamamoto T., Hori T.-A.;
RT   "Identification of the human ERK gene as a putative receptor tyrosine
RT   kinase and its chromosomal localization to 1p36.1: a comparative mapping of
RT   human, mouse, and rat chromosomes.";
RL   Genomics 26:382-384(1995).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 640-986 (ISOFORM 2).
RC   TISSUE=Gastric carcinoma;
RX   PubMed=7688222; DOI=10.1006/bbrc.1993.1878;
RA   Iwase T., Tanaka M., Suzuki M., Naito Y., Sugimura H., Kino I.;
RT   "Identification of protein-tyrosine kinase genes preferentially expressed
RT   in embryo stomach and gastric cancer.";
RL   Biochem. Biophys. Res. Commun. 194:698-705(1993).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 652-712.
RX   PubMed=1648701;
RA   Chan J., Watt V.M.;
RT   "eek and erk, new members of the eph subclass of receptor protein-tyrosine
RT   kinases.";
RL   Oncogene 6:1057-1061(1991).
RN   [9]
RP   NOMENCLATURE.
RX   PubMed=9267020; DOI=10.1016/s0092-8674(00)80500-0;
RG   Eph nomenclature committee;
RT   "Unified nomenclature for Eph family receptors and their ligands, the
RT   ephrins.";
RL   Cell 90:403-404(1997).
RN   [10]
RP   IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC   TISSUE=Renal cell carcinoma;
RX   PubMed=10508479;
RX   DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA   Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA   Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA   Old L.J.;
RT   "Antigens recognized by autologous antibody in patients with renal-cell
RT   carcinoma.";
RL   Int. J. Cancer 83:456-464(1999).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983 (ISOFORM 2),
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984 (ISOFORM 3), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [13]
RP   POLYUBIQUITINATION, AND INTERACTION WITH SPSB1 AND SPSB4.
RX   PubMed=28931592; DOI=10.1091/mbc.e17-07-0450;
RA   Okumura F., Joo-Okumura A., Obara K., Petersen A., Nishikimi A., Fukui Y.,
RA   Nakatsukasa K., Kamura T.;
RT   "Ubiquitin ligase SPSB4 diminishes cell repulsive responses mediated by
RT   EphB2.";
RL   Mol. Biol. Cell 28:3532-3541(2017).
RN   [14]
RP   UBIQUITINATION BY RNF186, AND MUTAGENESIS OF LYS-787 AND LYS-891.
RX   PubMed=33280498; DOI=10.1080/15548627.2020.1851496;
RA   Zhang H., Cui Z., Cheng D., Du Y., Guo X., Gao R., Chen J., Sun W., He R.,
RA   Ma X., Peng Q., Martin B.N., Yan W., Rong Y., Wang C.;
RT   "RNF186 regulates EFNB1 (ephrin B1)-EPHB2-induced autophagy in the colonic
RT   epithelial cells for the maintenance of intestinal homeostasis.";
RL   Autophagy 17:3030-3047(2021).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 910-986 (ISOFORM SHORT).
RX   PubMed=9933164; DOI=10.1126/science.283.5403.833;
RA   Thanos C.D., Goodwill K.E., Bowie J.U.;
RT   "Oligomeric structure of the human EphB2 receptor SAM domain.";
RL   Science 283:833-836(1999).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-195 OF HOMODIMER IN COMPLEX
RP   WITH ANTAGONISTIC PEPTIDE, DISULFIDE BOND, AND SUBUNIT.
RX   PubMed=17897949; DOI=10.1074/jbc.m706340200;
RA   Chrencik J.E., Brooun A., Recht M.I., Nicola G., Davis L.K., Abagyan R.,
RA   Widmer H., Pasquale E.B., Kuhn P.;
RT   "Three-dimensional structure of the EphB2 receptor in complex with an
RT   antagonistic peptide reveals a novel mode of inhibition.";
RL   J. Biol. Chem. 282:36505-36513(2007).
RN   [17]
RP   VARIANTS PROSTATE CANCER HIS-199; SER-279; ASN-679 AND MET-909, AND
RP   FUNCTION AS A TUMOR SUPPRESSOR.
RX   PubMed=15300251; DOI=10.1038/ng1408;
RA   Huusko P., Ponciano-Jackson D., Wolf M., Kiefer J.A., Azorsa D.O.,
RA   Tuzmen S., Weaver D., Robbins C., Moses T., Allinen M., Hautaniemi S.,
RA   Chen Y., Elkahloun A., Basik M., Bova G.S., Bubendorf L., Lugli A.,
RA   Sauter G., Schleutker J., Ozcelik H., Elowe S., Pawson T., Trent J.M.,
RA   Carpten J.D., Kallioniemi O.-P., Mousses S.;
RT   "Nonsense-mediated decay microarray analysis identifies mutations of EPHB2
RT   in human prostate cancer.";
RL   Nat. Genet. 36:979-983(2004).
RN   [18]
RP   VARIANTS PROSTATE CANCER SER-279; ALA-650 AND VAL-883.
RX   PubMed=16155194; DOI=10.1136/jmg.2005.035790;
RA   Kittles R.A., Baffoe-Bonnie A.B., Moses T.Y., Robbins C.M., Ahaghotu C.,
RA   Huusko P., Pettaway C., Vijayakumar S., Bennett J., Hoke G., Mason T.,
RA   Weinrich S., Trent J.M., Collins F.S., Mousses S., Bailey-Wilson J.,
RA   Furbert-Harris P., Dunston G., Powell I.J., Carpten J.D.;
RT   "A common nonsense mutation in EphB2 is associated with prostate cancer
RT   risk in African American men with a positive family history.";
RL   J. Med. Genet. 43:507-511(2006).
RN   [19]
RP   VARIANTS [LARGE SCALE ANALYSIS] SER-279; GLY-289; VAL-361; ASN-678 AND
RP   TRP-844.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [20]
RP   VARIANT BDPLT22 CYS-745, INVOLVEMENT IN BDPLT22, AND FUNCTION.
RX   PubMed=30213874; DOI=10.1182/blood-2018-04-845644;
RA   Berrou E., Soukaseum C., Favier R., Adam F., Elaib Z., Kauskot A.,
RA   Bordet J.C., Ballerini P., Loyau S., Feng M., Dias K., Muheidli A.,
RA   Girault S., Nurden A.T., Turro E., Ouwehand W.H., Denis C.V.,
RA   Jandrot-Perrus M., Rosa J.P., Nurden P., Bryckaert M.;
RT   "A mutation of the human EPHB2 gene leads to a major platelet functional
RT   defect.";
RL   Blood 132:2067-2077(2018).
CC   -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously
CC       transmembrane ephrin-B family ligands residing on adjacent cells,
CC       leading to contact-dependent bidirectional signaling into neighboring
CC       cells. The signaling pathway downstream of the receptor is referred to
CC       as forward signaling while the signaling pathway downstream of the
CC       ephrin ligand is referred to as reverse signaling. Functions in axon
CC       guidance during development. Involved in the guidance of commissural
CC       axons, that form a major interhemispheric connection between the 2
CC       temporal lobes of the cerebral cortex. Also involved in guidance of
CC       contralateral inner ear efferent growth cones at the midline and of
CC       retinal ganglion cell axons to the optic disk. In addition to axon
CC       guidance, also regulates dendritic spines development and maturation
CC       and stimulates the formation of excitatory synapses. Upon activation by
CC       EFNB1, abolishes the ARHGEF15-mediated negative regulation on
CC       excitatory synapse formation. Controls other aspects of development
CC       including angiogenesis, palate development and in inner ear development
CC       through regulation of endolymph production. Forward and reverse
CC       signaling through the EFNB2/EPHB2 complex regulate movement and
CC       adhesion of cells that tubularize the urethra and septate the cloaca.
CC       May function as a tumor suppressor. May be involved in the regulation
CC       of platelet activation and blood coagulation (PubMed:30213874).
CC       {ECO:0000269|PubMed:15300251, ECO:0000269|PubMed:30213874}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SUBUNIT: Heterotetramer upon binding of the ligand (By similarity). The
CC       heterotetramer is composed of an ephrin dimer and a receptor dimer
CC       (PubMed:17897949). Interacts (via PDZ-binding motif) with GRIP1 and
CC       PICK1 (via PDZ domain) (By similarity). Interacts with ARHGEF15;
CC       mediates ARHGEF15 phosphorylation, ubiquitination and degradation by
CC       the proteasome (By similarity). Interacts with AQP1; involved in
CC       endolymph production in the inner ear (By similarity). Interacts with
CC       SPSB1 and SPSB4 (PubMed:28931592). The phosphorylated form interacts
CC       with RASA1 (via SH2 domain 1) (By similarity). Interacts with EFNA5 (By
CC       similarity). Interacts with SH2D3C (By similarity).
CC       {ECO:0000250|UniProtKB:P54763, ECO:0000269|PubMed:17897949,
CC       ECO:0000269|PubMed:28931592}.
CC   -!- INTERACTION:
CC       P29323; P49790: NUP153; NbExp=2; IntAct=EBI-1059294, EBI-286779;
CC       P29323-3; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-25838727, EBI-6165897;
CC       P29323-3; P21964-2: COMT; NbExp=3; IntAct=EBI-25838727, EBI-10200977;
CC       P29323-3; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-25838727, EBI-1055254;
CC       P29323-3; O14832: PHYH; NbExp=3; IntAct=EBI-25838727, EBI-721853;
CC       P29323-3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25838727, EBI-5235340;
CC       P29323-3; Q13148: TARDBP; NbExp=6; IntAct=EBI-25838727, EBI-372899;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Cell projection, axon {ECO:0000250}. Cell projection, dendrite
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=EPHB2v, Long;
CC         IsoId=P29323-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P29323-2; Sequence=VSP_003016, VSP_003017;
CC       Name=3;
CC         IsoId=P29323-3; Sequence=VSP_015713, VSP_003016, VSP_003017;
CC   -!- TISSUE SPECIFICITY: Brain, heart, lung, kidney, placenta, pancreas,
CC       liver and skeletal muscle. Preferentially expressed in fetal brain.
CC   -!- PTM: Autophosphorylated; ligand binding stimulates autophosphorylation
CC       on tyrosine residues. {ECO:0000250|UniProtKB:P54763}.
CC   -!- PTM: Polyubiquitinated; ligand binding stimulates ubiquitination
CC       (PubMed:28931592). Ubiquitinated by RNF186 at Lys-891, mainly through
CC       'Lys-27'-linked polyubiquitin chains (PubMed:33280498).
CC       {ECO:0000269|PubMed:28931592, ECO:0000269|PubMed:33280498}.
CC   -!- PTM: Ligand binding induces cleavage by matrix metalloproteinases
CC       (MMPs) such as MMP7/MMP9, producing an EphB2/N-terminal fragment (NTF)
CC       and a C-terminal long fragment (EphB2-LF). EphB2-LF is further cleaved
CC       by MMPs, producing EphB2/CTF1 which is further cleaved by the
CC       PS1/gamma-secretase producing EphB2/CTF2.
CC       {ECO:0000250|UniProtKB:P54763}.
CC   -!- DISEASE: Prostate cancer (PC) [MIM:176807]: A malignancy originating in
CC       tissues of the prostate. Most prostate cancers are adenocarcinomas that
CC       develop in the acini of the prostatic ducts. Other rare histopathologic
CC       types of prostate cancer that occur in approximately 5% of patients
CC       include small cell carcinoma, mucinous carcinoma, prostatic ductal
CC       carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal
CC       cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell
CC       carcinoma and neuroendocrine carcinoma. {ECO:0000269|PubMed:15300251,
CC       ECO:0000269|PubMed:16155194}. Note=The gene represented in this entry
CC       may be involved in disease pathogenesis. EPHB2 mutations have been
CC       found in a prostate cancer cell line derived from a brain metastasis.
CC   -!- DISEASE: Bleeding disorder, platelet-type, 22 (BDPLT22) [MIM:618462]:
CC       An autosomal recessive disorder characterized by increased bleeding
CC       tendency due to platelet dysfunction. Clinical features include
CC       epistaxis, hematomas, bleeding after minor injuries, and menorrhagia.
CC       {ECO:0000269|PubMed:30213874}. Note=The disease may be caused by
CC       variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D31661; BAA06506.1; -; mRNA.
DR   EMBL; L41939; AAA99310.1; -; mRNA.
DR   EMBL; AF025304; AAB94602.1; -; mRNA.
DR   EMBL; AL035704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL158086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL512444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L36643; AAA74244.1; -; mRNA.
DR   EMBL; D37827; BAA07073.1; -; mRNA.
DR   EMBL; D14717; BAA03537.1; -; mRNA.
DR   EMBL; X59292; CAA41981.1; -; Genomic_DNA.
DR   CCDS; CCDS229.2; -. [P29323-2]
DR   CCDS; CCDS230.1; -. [P29323-3]
DR   CCDS; CCDS81279.1; -. [P29323-1]
DR   PIR; A57174; A57174.
DR   PIR; I78842; I78842.
DR   RefSeq; NP_001296122.1; NM_001309193.1. [P29323-1]
DR   RefSeq; NP_004433.2; NM_004442.7. [P29323-3]
DR   RefSeq; NP_059145.2; NM_017449.4. [P29323-2]
DR   PDB; 1B4F; X-ray; 1.95 A; A/B/C/D/E/F/G/H=908-985.
DR   PDB; 1F0M; X-ray; 2.20 A; A=908-985.
DR   PDB; 2QBX; X-ray; 2.30 A; A/B=20-196.
DR   PDB; 3ZFM; X-ray; 2.27 A; A=604-898.
DR   PDBsum; 1B4F; -.
DR   PDBsum; 1F0M; -.
DR   PDBsum; 2QBX; -.
DR   PDBsum; 3ZFM; -.
DR   AlphaFoldDB; P29323; -.
DR   BMRB; P29323; -.
DR   SMR; P29323; -.
DR   BioGRID; 108362; 74.
DR   DIP; DIP-1162N; -.
DR   IntAct; P29323; 17.
DR   MINT; P29323; -.
DR   STRING; 9606.ENSP00000363763; -.
DR   BindingDB; P29323; -.
DR   ChEMBL; CHEMBL3290; -.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR   DrugCentral; P29323; -.
DR   GuidetoPHARMACOLOGY; 1831; -.
DR   GlyGen; P29323; 4 sites.
DR   iPTMnet; P29323; -.
DR   PhosphoSitePlus; P29323; -.
DR   SwissPalm; P29323; -.
DR   BioMuta; EPHB2; -.
DR   DMDM; 76803654; -.
DR   CPTAC; CPTAC-2786; -.
DR   EPD; P29323; -.
DR   jPOST; P29323; -.
DR   MassIVE; P29323; -.
DR   MaxQB; P29323; -.
DR   PaxDb; P29323; -.
DR   PeptideAtlas; P29323; -.
DR   PRIDE; P29323; -.
DR   ProteomicsDB; 54540; -. [P29323-1]
DR   ProteomicsDB; 54541; -. [P29323-2]
DR   ProteomicsDB; 54542; -. [P29323-3]
DR   Antibodypedia; 30106; 673 antibodies from 41 providers.
DR   DNASU; 2048; -.
DR   Ensembl; ENST00000374630.8; ENSP00000363761.3; ENSG00000133216.17. [P29323-2]
DR   Ensembl; ENST00000374632.7; ENSP00000363763.3; ENSG00000133216.17. [P29323-3]
DR   Ensembl; ENST00000400191.7; ENSP00000383053.3; ENSG00000133216.17. [P29323-1]
DR   GeneID; 2048; -.
DR   KEGG; hsa:2048; -.
DR   MANE-Select; ENST00000374630.8; ENSP00000363761.3; NM_017449.5; NP_059145.2. [P29323-2]
DR   UCSC; uc001bge.4; human. [P29323-1]
DR   CTD; 2048; -.
DR   DisGeNET; 2048; -.
DR   GeneCards; EPHB2; -.
DR   HGNC; HGNC:3393; EPHB2.
DR   HPA; ENSG00000133216; Tissue enhanced (intestine).
DR   MalaCards; EPHB2; -.
DR   MIM; 176807; phenotype.
DR   MIM; 600997; gene.
DR   MIM; 603688; phenotype.
DR   MIM; 618462; phenotype.
DR   neXtProt; NX_P29323; -.
DR   OpenTargets; ENSG00000133216; -.
DR   Orphanet; 1331; Familial prostate cancer.
DR   PharmGKB; PA27825; -.
DR   VEuPathDB; HostDB:ENSG00000133216; -.
DR   eggNOG; KOG0196; Eukaryota.
DR   GeneTree; ENSGT00940000155503; -.
DR   InParanoid; P29323; -.
DR   OMA; GAINCIC; -.
DR   PhylomeDB; P29323; -.
DR   TreeFam; TF315608; -.
DR   BRENDA; 2.7.10.1; 2681.
DR   PathwayCommons; P29323; -.
DR   Reactome; R-HSA-2682334; EPH-Ephrin signaling.
DR   Reactome; R-HSA-373760; L1CAM interactions.
DR   Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-HSA-3928664; Ephrin signaling.
DR   Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR   SignaLink; P29323; -.
DR   SIGNOR; P29323; -.
DR   BioGRID-ORCS; 2048; 10 hits in 1113 CRISPR screens.
DR   ChiTaRS; EPHB2; human.
DR   EvolutionaryTrace; P29323; -.
DR   GeneWiki; EPH_receptor_B2; -.
DR   GenomeRNAi; 2048; -.
DR   Pharos; P29323; Tchem.
DR   PRO; PR:P29323; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P29323; protein.
DR   Bgee; ENSG00000133216; Expressed in ganglionic eminence and 163 other tissues.
DR   ExpressionAtlas; P29323; baseline and differential.
DR   Genevisible; P29323; HS.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0098794; C:postsynapse; TAS:ARUK-UCL.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0001540; F:amyloid-beta binding; ISS:ARUK-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008046; F:axon guidance receptor activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; ISS:ARUK-UCL.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0005005; F:transmembrane-ephrin receptor activity; ISS:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR   GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
DR   GO; GO:0042113; P:B cell activation; IMP:ARUK-UCL.
DR   GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IBA:GO_Central.
DR   GO; GO:0071679; P:commissural neuron axon guidance; ISS:UniProtKB.
DR   GO; GO:0022038; P:corpus callosum development; ISS:UniProtKB.
DR   GO; GO:0060996; P:dendritic spine development; ISS:UniProtKB.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0021934; P:hindbrain tangential cell migration; IEA:Ensembl.
DR   GO; GO:0042472; P:inner ear morphogenesis; ISS:UniProtKB.
DR   GO; GO:0007612; P:learning; ISS:ARUK-UCL.
DR   GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; IEA:Ensembl.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; IMP:ARUK-UCL.
DR   GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:ARUK-UCL.
DR   GO; GO:1904782; P:negative regulation of NMDA glutamate receptor activity; ISS:ARUK-UCL.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:ARUK-UCL.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:ARUK-UCL.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:ARUK-UCL.
DR   GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
DR   GO; GO:0106028; P:neuron projection retraction; IEA:Ensembl.
DR   GO; GO:0021631; P:optic nerve morphogenesis; IEA:Ensembl.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:ARUK-UCL.
DR   GO; GO:0030335; P:positive regulation of cell migration; IGI:ARUK-UCL.
DR   GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
DR   GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:ARUK-UCL.
DR   GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR   GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:ARUK-UCL.
DR   GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; ISS:ARUK-UCL.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:ARUK-UCL.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR   GO; GO:0031915; P:positive regulation of synaptic plasticity; ISS:ARUK-UCL.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:ARUK-UCL.
DR   GO; GO:0097104; P:postsynaptic membrane assembly; IEA:Ensembl.
DR   GO; GO:2000822; P:regulation of behavioral fear response; IEA:Ensembl.
DR   GO; GO:0030193; P:regulation of blood coagulation; IMP:UniProtKB.
DR   GO; GO:0050878; P:regulation of body fluid levels; ISS:UniProtKB.
DR   GO; GO:0051489; P:regulation of filopodium assembly; IEA:Ensembl.
DR   GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISS:ARUK-UCL.
DR   GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR   GO; GO:2000316; P:regulation of T-helper 17 type immune response; IEA:Ensembl.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
DR   GO; GO:0060021; P:roof of mouth development; ISS:UniProtKB.
DR   GO; GO:0120192; P:tight junction assembly; IEA:Ensembl.
DR   GO; GO:0099557; P:trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission; IEA:Ensembl.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   GO; GO:0001655; P:urogenital system development; ISS:UniProtKB.
DR   GO; GO:0110077; P:vesicle-mediated intercellular transport; IEA:Ensembl.
DR   CDD; cd10477; EphR_LBD_B2; 1.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 1.10.150.50; -; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR027936; Eph_TM.
DR   InterPro; IPR034238; EphB2_rcpt_lig-bd.
DR   InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR   InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR   Pfam; PF14575; EphA2_TM; 1.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   Pfam; PF07699; Ephrin_rec_like; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS51550; EPH_LBD; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR   PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW   Cell projection; Developmental protein; Disease variant; Disulfide bond;
KW   Glycoprotein; Isopeptide bond; Kinase; Membrane; Neurogenesis;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   Signal; Transferase; Transmembrane; Transmembrane helix; Tumor suppressor;
KW   Tyrosine-protein kinase; Ubl conjugation.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..1055
FT                   /note="Ephrin type-B receptor 2"
FT                   /id="PRO_0000016827"
FT   CHAIN           536..986
FT                   /note="EphB2/CTF1"
FT                   /evidence="ECO:0000250|UniProtKB:P54763"
FT                   /id="PRO_0000445961"
FT   CHAIN           562..986
FT                   /note="EphB2/CTF2"
FT                   /evidence="ECO:0000250|UniProtKB:P54763"
FT                   /id="PRO_0000445962"
FT   TOPO_DOM        19..543
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        544..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        565..1055
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          20..202
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT   DOMAIN          324..434
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          435..530
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          621..884
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          913..977
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   REGION          990..1055
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           984..986
FT                   /note="PDZ-binding (in isoform 2)"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        999..1049
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        746
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         627..635
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         653
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   SITE            535..536
FT                   /note="Cleavage; by a metalloproteinase"
FT                   /evidence="ECO:0000250|UniProtKB:P54763"
FT   SITE            561..562
FT                   /note="Cleavage; by gamma-secretase/PS1"
FT                   /evidence="ECO:0000250|UniProtKB:P54763"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        482
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        62..184
FT                   /evidence="ECO:0000269|PubMed:17897949"
FT   DISULFID        97..107
FT                   /evidence="ECO:0000269|PubMed:17897949"
FT   CROSSLNK        891
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:33280498"
FT   VAR_SEQ         568
FT                   /note="R -> RR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:8589679"
FT                   /id="VSP_015713"
FT   VAR_SEQ         986
FT                   /note="G -> V (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:7601466,
FT                   ECO:0000303|PubMed:7688222, ECO:0000303|PubMed:7898931,
FT                   ECO:0000303|PubMed:8033077, ECO:0000303|PubMed:8589679"
FT                   /id="VSP_003016"
FT   VAR_SEQ         987..1055
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:7601466,
FT                   ECO:0000303|PubMed:7688222, ECO:0000303|PubMed:7898931,
FT                   ECO:0000303|PubMed:8033077, ECO:0000303|PubMed:8589679"
FT                   /id="VSP_003017"
FT   VARIANT         199
FT                   /note="R -> H (in prostate cancer; dbSNP:rs201754821)"
FT                   /evidence="ECO:0000269|PubMed:15300251"
FT                   /id="VAR_032853"
FT   VARIANT         279
FT                   /note="A -> S (in prostate cancer; dbSNP:rs35882952)"
FT                   /evidence="ECO:0000269|PubMed:15300251,
FT                   ECO:0000269|PubMed:16155194, ECO:0000269|PubMed:17344846"
FT                   /id="VAR_032854"
FT   VARIANT         289
FT                   /note="C -> G"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042172"
FT   VARIANT         361
FT                   /note="I -> V (in dbSNP:rs56180036)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042173"
FT   VARIANT         650
FT                   /note="V -> A (in prostate cancer; dbSNP:rs142173175)"
FT                   /evidence="ECO:0000269|PubMed:16155194"
FT                   /id="VAR_032855"
FT   VARIANT         678
FT                   /note="D -> N (in dbSNP:rs28936395)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042174"
FT   VARIANT         679
FT                   /note="H -> N (in prostate cancer)"
FT                   /evidence="ECO:0000269|PubMed:15300251"
FT                   /id="VAR_032856"
FT   VARIANT         745
FT                   /note="R -> C (in BDPLT22; dbSNP:rs761749948)"
FT                   /evidence="ECO:0000269|PubMed:30213874"
FT                   /id="VAR_082702"
FT   VARIANT         844
FT                   /note="R -> W (in dbSNP:rs55826626)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042175"
FT   VARIANT         883
FT                   /note="M -> V (in prostate cancer; dbSNP:rs372653137)"
FT                   /evidence="ECO:0000269|PubMed:16155194"
FT                   /id="VAR_032857"
FT   VARIANT         909
FT                   /note="I -> M (in prostate cancer)"
FT                   /evidence="ECO:0000269|PubMed:15300251"
FT                   /id="VAR_032858"
FT   MUTAGEN         787
FT                   /note="K->R: No loss of ubiquitination by RNF186."
FT                   /evidence="ECO:0000269|PubMed:33280498"
FT   MUTAGEN         891
FT                   /note="K->R: Complete loss of ubiquitination by RNF186."
FT                   /evidence="ECO:0000269|PubMed:33280498"
FT   CONFLICT        1..20
FT                   /note="MALRRLGAALLLLPLLAAVE -> MWVPVLALPVCTYA (in Ref. 1;
FT                   BAA06506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="G -> D (in Ref. 1; BAA06506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        476
FT                   /note="K -> KQ (in Ref. 1; BAA06506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        495..496
FT                   /note="Missing (in Ref. 5; AAA74244)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        532
FT                   /note="E -> D (in Ref. 1; BAA06506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        589
FT                   /note="M -> I (in Ref. 5; AAA74244)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        671
FT                   /note="A -> R (in Ref. 7; BAA03537)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        788
FT                   /note="I -> F (in Ref. 5; AAA74244)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        853
FT                   /note="S -> A (in Ref. 1; BAA06506, 6; BAA07073 and 7;
FT                   BAA03537)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        923
FT                   /note="E -> K (in Ref. 1; BAA06506, 6; BAA07073 and 7;
FT                   BAA03537)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        958
FT                   /note="V -> L (in Ref. 2; AAA99310)"
FT                   /evidence="ECO:0000305"
FT   STRAND          21..25
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   STRAND          44..49
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   STRAND          55..61
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   STRAND          84..94
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   STRAND          111..120
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   STRAND          135..141
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   STRAND          155..166
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   STRAND          171..183
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   STRAND          185..194
FT                   /evidence="ECO:0007829|PDB:2QBX"
FT   HELIX           618..620
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   STRAND          621..626
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   STRAND          635..640
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   STRAND          648..655
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   HELIX           661..674
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   STRAND          685..689
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   STRAND          691..700
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   HELIX           707..712
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   TURN            713..716
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   HELIX           720..739
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   HELIX           749..751
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   STRAND          752..754
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   STRAND          760..762
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   HELIX           790..792
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   HELIX           795..800
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   HELIX           805..820
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   TURN            826..829
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   HELIX           832..840
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   HELIX           853..862
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   HELIX           873..885
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   HELIX           887..890
FT                   /evidence="ECO:0007829|PDB:3ZFM"
FT   HELIX           918..924
FT                   /evidence="ECO:0007829|PDB:1B4F"
FT   HELIX           928..930
FT                   /evidence="ECO:0007829|PDB:1B4F"
FT   HELIX           931..936
FT                   /evidence="ECO:0007829|PDB:1B4F"
FT   HELIX           942..945
FT                   /evidence="ECO:0007829|PDB:1B4F"
FT   HELIX           950..955
FT                   /evidence="ECO:0007829|PDB:1B4F"
FT   HELIX           961..982
FT                   /evidence="ECO:0007829|PDB:1B4F"
FT   MOD_RES         P29323-2:983
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         P29323-3:984
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
SQ   SEQUENCE   1055 AA;  117493 MW;  4F8BFEDC45986483 CRC64;
     MALRRLGAAL LLLPLLAAVE ETLMDSTTAT AELGWMVHPP SGWEEVSGYD ENMNTIRTYQ
     VCNVFESSQN NWLRTKFIRR RGAHRIHVEM KFSVRDCSSI PSVPGSCKET FNLYYYEADF
     DSATKTFPNW MENPWVKVDT IAADESFSQV DLGGRVMKIN TEVRSFGPVS RSGFYLAFQD
     YGGCMSLIAV RVFYRKCPRI IQNGAIFQET LSGAESTSLV AARGSCIANA EEVDVPIKLY
     CNGDGEWLVP IGRCMCKAGF EAVENGTVCR GCPSGTFKAN QGDEACTHCP INSRTTSEGA
     TNCVCRNGYY RADLDPLDMP CTTIPSAPQA VISSVNETSL MLEWTPPRDS GGREDLVYNI
     ICKSCGSGRG ACTRCGDNVQ YAPRQLGLTE PRIYISDLLA HTQYTFEIQA VNGVTDQSPF
     SPQFASVNIT TNQAAPSAVS IMHQVSRTVD SITLSWSQPD QPNGVILDYE LQYYEKELSE
     YNATAIKSPT NTVTVQGLKA GAIYVFQVRA RTVAGYGRYS GKMYFQTMTE AEYQTSIQEK
     LPLIIGSSAA GLVFLIAVVV IAIVCNRRGF ERADSEYTDK LQHYTSGHMT PGMKIYIDPF
     TYEDPNEAVR EFAKEIDISC VKIEQVIGAG EFGEVCSGHL KLPGKREIFV AIKTLKSGYT
     EKQRRDFLSE ASIMGQFDHP NVIHLEGVVT KSTPVMIITE FMENGSLDSF LRQNDGQFTV
     IQLVGMLRGI AAGMKYLADM NYVHRDLAAR NILVNSNLVC KVSDFGLSRF LEDDTSDPTY
     TSALGGKIPI RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM TNQDVINAIE
     QDYRLPPPMD CPSALHQLML DCWQKDRNHR PKFGQIVNTL DKMIRNPNSL KAMAPLSSGI
     NLPLLDRTIP DYTSFNTVDE WLEAIKMGQY KESFANAGFT SFDVVSQMMM EDILRVGVTL
     AGHQKKILNS IQVMRAQMNQ IQSVEGQPLA RRPRATGRTK RCQPRDVTKK TCNSNDGKKK
     GMGKKKTDPG RGREIQGIFF KEDSHKESND CSCGG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024