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Ephrin type-A receptor 8 (EC 2.7.10.1) (EPH- and ELK-related kinase) (EPH-like kinase 3) (EK3) (hEK3) (Tyrosine-protein kinase receptor EEK)

 EPHA8_HUMAN             Reviewed;        1005 AA.
P29322; Q6IN80; Q8IUX6; Q9NUA9; Q9P269;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 2.
23-MAY-2018, entry version 194.
RecName: Full=Ephrin type-A receptor 8;
EC=2.7.10.1;
AltName: Full=EPH- and ELK-related kinase;
AltName: Full=EPH-like kinase 3;
Short=EK3;
Short=hEK3;
AltName: Full=Tyrosine-protein kinase receptor EEK;
Flags: Precursor;
Name=EPHA8; Synonyms=EEK, HEK3, KIAA1459;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-1005 (ISOFORM 1), AND
VARIANT GLN-612.
TISSUE=Brain;
PubMed=10819331; DOI=10.1093/dnares/7.2.143;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:143-150(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 706-726.
PubMed=1648701;
Chan J., Watt V.M.;
"eek and erk, new members of the eph subclass of receptor protein-
tyrosine kinases.";
Oncogene 6:1057-1061(1991).
[5]
NOMENCLATURE.
PubMed=9267020;
Eph nomenclature committee;
"Unified nomenclature for Eph family receptors and their ligands, the
ephrins.";
Cell 90:403-404(1997).
[6]
INTERACTION WITH FYN.
PubMed=10498895; DOI=10.1038/sj.onc.1202917;
Choi S., Park S.;
"Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates
Fyn binding to the Tyr-615 site by enhancing tyrosine kinase
activity.";
Oncogene 18:5413-5422(1999).
[7]
INTERACTION WITH PIK3CG.
PubMed=11416136; DOI=10.1128/MCB.21.14.4579-4597.2001;
Gu C., Park S.;
"The EphA8 receptor regulates integrin activity through p110gamma
phosphatidylinositol-3 kinase in a tyrosine kinase activity-
independent manner.";
Mol. Cell. Biol. 21:4579-4597(2001).
[8]
INTERACTION WITH ANKS1B.
PubMed=17875921; DOI=10.1128/MCB.00794-07;
Shin J., Gu C., Park E., Park S.;
"Identification of phosphotyrosine binding domain-containing proteins
as novel downstream targets of the EphA8 signaling function.";
Mol. Cell. Biol. 27:8113-8126(2007).
[9]
INTERACTION WITH TIAM1.
PubMed=20496116; DOI=10.1007/s10059-010-0075-2;
Yoo S., Shin J., Park S.;
"EphA8-ephrinA5 signaling and clathrin-mediated endocytosis is
regulated by Tiam-1, a Rac-specific guanine nucleotide exchange
factor.";
Mol. Cells 29:603-609(2010).
[10]
STRUCTURE BY NMR OF 437-534 AND 932-1000.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the second FN3 domain and of sterile alpha
motif (SAM) domain of EPH receptor A8 protein.";
Submitted (NOV-2005) to the PDB data bank.
[11]
VARIANTS [LARGE SCALE ANALYSIS] SER-45; LEU-60; LYS-123; CYS-179;
LEU-198 AND LEU-860.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI-
anchored ephrin-A family ligands residing on adjacent cells,
leading to contact-dependent bidirectional signaling into
neighboring cells. The signaling pathway downstream of the
receptor is referred to as forward signaling while the signaling
pathway downstream of the ephrin ligand is referred to as reverse
signaling. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are
able to activate EPHA8 through phosphorylation. With EFNA5 may
regulate integrin-mediated cell adhesion and migration on
fibronectin substrate but also neurite outgrowth. During
development of the nervous system plays also a role in axon
guidance. Downstream effectors of the EPHA8 signaling pathway
include FYN which promotes cell adhesion upon activation by EPHA8
and the MAP kinases in the stimulation of neurite outgrowth (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Heterotetramer upon binding of the ligand. The
heterotetramer is composed of an ephrin dimer and a receptor
dimer. Oligomerization is probably required to induce biological
responses. May also form heterodimers with other ephrin receptors
(By similarity). Interacts with FYN; possible downstream effector
of EPHA8 in regulation of cell adhesion. Interacts with PIK3CG;
regulates integrin-mediated cell adhesion to substrate. Interacts
with TIAM1; regulates clathrin-mediated endocytosis of EPHA8.
Interacts with ANKS1A and ANKS1B; EPHA8 kinase activity-
independent but stimulated by EPHA8 ubiquitination. {ECO:0000250,
ECO:0000269|PubMed:10498895, ECO:0000269|PubMed:11416136,
ECO:0000269|PubMed:17875921, ECO:0000269|PubMed:20496116}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:O09127}; Single-pass type I membrane
protein {ECO:0000255}. Cell projection
{ECO:0000250|UniProtKB:O09127}. Early endosome membrane
{ECO:0000250|UniProtKB:O09127}. Note=Undergoes clathrin-mediated
endocytosis upon EFNA5-binding and is targeted to early endosomes.
{ECO:0000250|UniProtKB:O09127}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P29322-1; Sequence=Displayed;
Name=2;
IsoId=P29322-2; Sequence=VSP_041946, VSP_041947;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylated. Phosphorylation is stimulated upon binding of
its ligands including EFNA2, EFNA3 and EFNA5. Autophosphorylation
on Tyr-616 is critical for association with FYN.
Autophosphorylation on Tyr-839 modulates tyrosine kinase activity
(By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor
stability and activity through proteasomal degradation. ANKS1A
prevents ubiquitination and degradation (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=CAA41980.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AL035703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC038796; AAH38796.1; -; mRNA.
EMBL; BC072417; AAH72417.2; -; mRNA.
EMBL; AB040892; BAA95983.1; -; mRNA.
EMBL; X59291; CAA41980.1; ALT_INIT; Genomic_DNA.
CCDS; CCDS225.1; -. [P29322-1]
CCDS; CCDS30626.1; -. [P29322-2]
PIR; S23361; S23361.
RefSeq; NP_001006944.1; NM_001006943.2. [P29322-2]
RefSeq; NP_065387.1; NM_020526.4. [P29322-1]
UniGene; Hs.283613; -.
PDB; 1UCV; NMR; -; A=933-1000.
PDB; 1X5L; NMR; -; A=437-534.
PDB; 3KUL; X-ray; 2.15 A; A/B=602-909.
PDBsum; 1UCV; -.
PDBsum; 1X5L; -.
PDBsum; 3KUL; -.
ProteinModelPortal; P29322; -.
SMR; P29322; -.
BioGrid; 108360; 12.
IntAct; P29322; 9.
MINT; P29322; -.
STRING; 9606.ENSP00000166244; -.
BindingDB; P29322; -.
ChEMBL; CHEMBL4134; -.
GuidetoPHARMACOLOGY; 1828; -.
iPTMnet; P29322; -.
PhosphoSitePlus; P29322; -.
BioMuta; EPHA8; -.
DMDM; 19857975; -.
EPD; P29322; -.
MaxQB; P29322; -.
PaxDb; P29322; -.
PeptideAtlas; P29322; -.
PRIDE; P29322; -.
DNASU; 2046; -.
Ensembl; ENST00000166244; ENSP00000166244; ENSG00000070886. [P29322-1]
Ensembl; ENST00000374644; ENSP00000363775; ENSG00000070886. [P29322-2]
GeneID; 2046; -.
KEGG; hsa:2046; -.
UCSC; uc001bfw.4; human. [P29322-1]
CTD; 2046; -.
DisGeNET; 2046; -.
EuPathDB; HostDB:ENSG00000070886.10; -.
GeneCards; EPHA8; -.
HGNC; HGNC:3391; EPHA8.
HPA; CAB009660; -.
HPA; HPA031433; -.
MIM; 176945; gene.
neXtProt; NX_P29322; -.
OpenTargets; ENSG00000070886; -.
PharmGKB; PA27823; -.
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118975; -.
HOGENOM; HOG000233856; -.
HOVERGEN; HBG062180; -.
InParanoid; P29322; -.
KO; K05109; -.
OMA; YEKDKEM; -.
OrthoDB; EOG091G00W0; -.
PhylomeDB; P29322; -.
TreeFam; TF315608; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-2682334; EPH-Ephrin signaling.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
SignaLink; P29322; -.
SIGNOR; P29322; -.
EvolutionaryTrace; P29322; -.
GeneWiki; EPHA8; -.
GenomeRNAi; 2046; -.
PRO; PR:P29322; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000070886; -.
CleanEx; HS_EPHA8; -.
Genevisible; P29322; HS.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005004; F:GPI-linked ephrin receptor activity; ISS:UniProtKB.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:0016322; P:neuron remodeling; ISS:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0006929; P:substrate-dependent cell migration; ISS:UniProtKB.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR027936; Eph_TM.
InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
InterPro; IPR020691; EphrinA_rcpt8.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
PANTHER; PTHR24416:SF339; PTHR24416:SF339; 1.
Pfam; PF14575; EphA2_TM; 1.
Pfam; PF01404; Ephrin_lbd; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00536; SAM_1; 1.
PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00615; EPH_lbd; 1.
SMART; SM01411; Ephrin_rec_like; 1.
SMART; SM00060; FN3; 2.
SMART; SM00454; SAM; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS51550; EPH_LBD; 1.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell adhesion;
Cell membrane; Cell projection; Complete proteome;
Developmental protein; Endosome; Glycoprotein; Kinase; Membrane;
Neurogenesis; Nucleotide-binding; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Repeat; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
Ubl conjugation.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 1005 Ephrin type-A receptor 8.
/FTId=PRO_0000016822.
TOPO_DOM 28 542 Extracellular. {ECO:0000255}.
TRANSMEM 543 563 Helical. {ECO:0000255}.
TOPO_DOM 564 1005 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 209 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 328 438 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 439 534 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 635 896 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 930 994 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 641 649 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 564 570 Mediates interaction with ANKS1A and
ANKS1B. {ECO:0000250}.
REGION 589 644 Mediates interaction with PIK3CG and
required for endocytosis. {ECO:0000250}.
MOTIF 1003 1005 PDZ-binding. {ECO:0000255}.
COMPBIAS 191 325 Cys-rich.
ACT_SITE 760 760 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 667 667 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 616 616 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:O09127}.
MOD_RES 839 839 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:O09127}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 407 407 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 432 432 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 439 495 APSQVVVIRQERAGQTSVSLLWQEPEQPNGIILEYEIKYYE
KDKEMQSYSTLKAVTT -> GRRRNSVPQRPGPPASPASDP
SRDQSSAGDVLWAFRQVPLWPCAPHQDPELEALHCL (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041946.
VAR_SEQ 496 1005 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041947.
VARIANT 45 45 G -> S (in dbSNP:rs45498698).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042153.
VARIANT 60 60 V -> L (in dbSNP:rs56402644).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042154.
VARIANT 123 123 N -> K (in a breast infiltrating ductal
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042155.
VARIANT 179 179 R -> C (in a gastric adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042156.
VARIANT 198 198 R -> L (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042157.
VARIANT 321 321 P -> L (in dbSNP:rs56656925).
/FTId=VAR_061292.
VARIANT 444 444 V -> M (in dbSNP:rs2295021).
/FTId=VAR_022107.
VARIANT 612 612 E -> Q (in dbSNP:rs999765).
{ECO:0000269|PubMed:10819331}.
/FTId=VAR_024514.
VARIANT 860 860 P -> L (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042158.
CONFLICT 237 237 S -> L (in Ref. 3; BAA95983).
{ECO:0000305}.
STRAND 456 460 {ECO:0000244|PDB:1X5L}.
STRAND 472 482 {ECO:0000244|PDB:1X5L}.
STRAND 488 499 {ECO:0000244|PDB:1X5L}.
STRAND 507 510 {ECO:0000244|PDB:1X5L}.
STRAND 512 516 {ECO:0000244|PDB:1X5L}.
STRAND 527 530 {ECO:0000244|PDB:1X5L}.
HELIX 632 634 {ECO:0000244|PDB:3KUL}.
STRAND 635 643 {ECO:0000244|PDB:3KUL}.
TURN 644 646 {ECO:0000244|PDB:3KUL}.
STRAND 647 654 {ECO:0000244|PDB:3KUL}.
STRAND 662 669 {ECO:0000244|PDB:3KUL}.
HELIX 675 688 {ECO:0000244|PDB:3KUL}.
STRAND 699 703 {ECO:0000244|PDB:3KUL}.
HELIX 705 707 {ECO:0000244|PDB:3KUL}.
STRAND 710 714 {ECO:0000244|PDB:3KUL}.
HELIX 721 726 {ECO:0000244|PDB:3KUL}.
TURN 727 730 {ECO:0000244|PDB:3KUL}.
HELIX 734 753 {ECO:0000244|PDB:3KUL}.
HELIX 763 765 {ECO:0000244|PDB:3KUL}.
STRAND 766 768 {ECO:0000244|PDB:3KUL}.
STRAND 774 776 {ECO:0000244|PDB:3KUL}.
HELIX 802 804 {ECO:0000244|PDB:3KUL}.
HELIX 807 812 {ECO:0000244|PDB:3KUL}.
HELIX 817 832 {ECO:0000244|PDB:3KUL}.
TURN 833 835 {ECO:0000244|PDB:3KUL}.
TURN 838 841 {ECO:0000244|PDB:3KUL}.
HELIX 844 852 {ECO:0000244|PDB:3KUL}.
HELIX 865 874 {ECO:0000244|PDB:3KUL}.
HELIX 879 881 {ECO:0000244|PDB:3KUL}.
HELIX 885 897 {ECO:0000244|PDB:3KUL}.
HELIX 935 941 {ECO:0000244|PDB:1UCV}.
HELIX 945 947 {ECO:0000244|PDB:1UCV}.
HELIX 948 953 {ECO:0000244|PDB:1UCV}.
HELIX 959 962 {ECO:0000244|PDB:1UCV}.
HELIX 967 973 {ECO:0000244|PDB:1UCV}.
HELIX 978 995 {ECO:0000244|PDB:1UCV}.
SEQUENCE 1005 AA; 111003 MW; 6FBF85535E4212B3 CRC64;
MAPARGRLPP ALWVVTAAAA AATCVSAARG EVNLLDTSTI HGDWGWLTYP AHGWDSINEV
DESFQPIHTY QVCNVMSPNQ NNWLRTSWVP RDGARRVYAE IKFTLRDCNS MPGVLGTCKE
TFNLYYLESD RDLGASTQES QFLKIDTIAA DESFTGADLG VRRLKLNTEV RSVGPLSKRG
FYLAFQDIGA CLAILSLRIY YKKCPAMVRN LAAFSEAVTG ADSSSLVEVR GQCVRHSEER
DTPKMYCSAE GEWLVPIGKC VCSAGYEERR DACVACELGF YKSAPGDQLC ARCPPHSHSA
APAAQACHCD LSYYRAALDP PSSACTRPPS APVNLISSVN GTSVTLEWAP PLDPGGRSDI
TYNAVCRRCP WALSRCEACG SGTRFVPQQT SLVQASLLVA NLLAHMNYSF WIEAVNGVSD
LSPEPRRAAV VNITTNQAAP SQVVVIRQER AGQTSVSLLW QEPEQPNGII LEYEIKYYEK
DKEMQSYSTL KAVTTRATVS GLKPGTRYVF QVRARTSAGC GRFSQAMEVE TGKPRPRYDT
RTIVWICLTL ITGLVVLLLL LICKKRHCGY SKAFQDSDEE KMHYQNGQAP PPVFLPLHHP
PGKLPEPQFY AEPHTYEEPG RAGRSFTREI EASRIHIEKI IGSGDSGEVC YGRLRVPGQR
DVPVAIKALK AGYTERQRRD FLSEASIMGQ FDHPNIIRLE GVVTRGRLAM IVTEYMENGS
LDTFLRTHDG QFTIMQLVGM LRGVGAGMRY LSDLGYVHRD LAARNVLVDS NLVCKVSDFG
LSRVLEDDPD AAYTTTGGKI PIRWTAPEAI AFRTFSSASD VWSFGVVMWE VLAYGERPYW
NMTNRDVISS VEEGYRLPAP MGCPHALHQL MLDCWHKDRA QRPRFSQIVS VLDALIRSPE
SLRATATVSR CPPPAFVRSC FDLRGGSGGG GGLTVGDWLD SIRMGRYRDH FAAGGYSSLG
MVLRMNAQDV RALGITLMGH QKKILGSIQT MRAQLTSTQG PRRHL


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