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Ski oncogene (Proto-oncogene c-Ski)

 SKI_HUMAN               Reviewed;         728 AA.
P12755; Q5SYT7;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
22-NOV-2017, entry version 175.
RecName: Full=Ski oncogene;
AltName: Full=Proto-oncogene c-Ski;
Name=SKI;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2762147; DOI=10.1093/nar/17.14.5489;
Nomura N., Sasamoto S., Ishii S., Date T., Matsui M., Ishizaki R.;
"Isolation of human cDNA clones of ski and the ski-related gene,
sno.";
Nucleic Acids Res. 17:5489-5500(1989).
[2]
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).
[3]
INTERACTION WITH HIPK2; SMAD2; SMAD3 AND SMAD4.
PubMed=12874272; DOI=10.1074/jbc.M307112200;
Harada J., Kokura K., Kanei-Ishii C., Nomura T., Khan M.M., Kim Y.,
Ishii S.;
"Requirement of the co-repressor homeodomain-interacting protein
kinase 2 for ski-mediated inhibition of bone morphogenetic protein-
induced transcriptional activation.";
J. Biol. Chem. 278:38998-39005(2003).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[5]
FUNCTION, AND INTERACTION WITH PRDM16 AND SMAD3.
PubMed=19049980; DOI=10.1074/jbc.M808989200;
Takahata M., Inoue Y., Tsuda H., Imoto I., Koinuma D., Hayashi M.,
Ichikura T., Yamori T., Nagasaki K., Yoshida M., Matsuoka M.,
Morishita K., Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K.,
Imamura T.;
"SKI and MEL1 cooperate to inhibit transforming growth factor-beta
signal in gastric cancer cells.";
J. Biol. Chem. 284:3334-3344(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-432 AND
SER-720, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[8]
VARIANTS SGS LEU-31; VAL-32; PRO-32; CYS-34; VAL-34; SER-34; GLN-35;
SER-35; 94-SER--SER-97 DEL AND 95-ASP--SER-97 DEL.
PubMed=23103230; DOI=10.1016/j.ajhg.2012.10.002;
Carmignac V., Thevenon J., Ades L., Callewaert B., Julia S.,
Thauvin-Robinet C., Gueneau L., Courcet J.B., Lopez E., Holman K.,
Renard M., Plauchu H., Plessis G., De Backer J., Child A., Arno G.,
Duplomb L., Callier P., Aral B., Vabres P., Gigot N., Arbustini E.,
Grasso M., Robinson P.N., Goizet C., Baumann C., Di Rocco M.,
Sanchez Del Pozo J., Huet F., Jondeau G., Collod-Beroud G., Beroud C.,
Amiel J., Cormier-Daire V., Riviere J.B., Boileau C., De Paepe A.,
Faivre L.;
"In-frame mutations in exon 1 of SKI cause dominant Shprintzen-
Goldberg syndrome.";
Am. J. Hum. Genet. 91:950-957(2012).
[9]
VARIANTS SGS ARG-21; VAL-32; ASP-34; CYS-34; SER-34; SER-35;
95-ASP--SER-97 DEL; GLU-116 AND ARG-117.
PubMed=23023332; DOI=10.1038/ng.2421;
Doyle A.J., Doyle J.J., Bessling S.L., Maragh S., Lindsay M.E.,
Schepers D., Gillis E., Mortier G., Homfray T., Sauls K., Norris R.A.,
Huso N.D., Leahy D., Mohr D.W., Caulfield M.J., Scott A.F.,
Destree A., Hennekam R.C., Arn P.H., Curry C.J., Van Laer L.,
McCallion A.S., Loeys B.L., Dietz H.C.;
"Mutations in the TGF-beta repressor SKI cause Shprintzen-Goldberg
syndrome with aortic aneurysm.";
Nat. Genet. 44:1249-1254(2012).
[10]
VARIANTS SGS SER-35 AND GLU-116.
PubMed=24357594; DOI=10.1002/ajmg.a.36340;
FORGE Canada Consortium;
Au P.Y., Racher H.E., Graham J.M. Jr., Kramer N., Lowry R.B.,
Parboosingh J.S., Innes A.M.;
"De novo exon 1 missense mutations of SKI and Shprintzen-Goldberg
syndrome: two new cases and a clinical review.";
Am. J. Med. Genet. A 164A:676-684(2014).
[11]
VARIANTS SGS THR-28; LEU-31; VAL-32; VAL-34; ALA-34; ASP-34; SER-34
AND SER-35.
PubMed=24736733; DOI=10.1038/ejhg.2014.61;
Schepers D., Doyle A.J., Oswald G., Sparks E., Myers L., Willems P.J.,
Mansour S., Simpson M.A., Frysira H., Maat-Kievit A., Van Minkelen R.,
Hoogeboom J.M., Mortier G.R., Titheradge H., Brueton L., Starr L.,
Stark Z., Ockeloen C., Lourenco C.M., Blair E., Hobson E., Hurst J.,
Maystadt I., Destree A., Girisha K.M., Miller M., Dietz H.C.,
Loeys B., Van Laer L.;
"The SMAD-binding domain of SKI: a hotspot for de novo mutations
causing Shprintzen-Goldberg syndrome.";
Eur. J. Hum. Genet. 23:224-228(2015).
-!- FUNCTION: May play a role in terminal differentiation of skeletal
muscle cells but not in the determination of cells to the myogenic
lineage. Functions as a repressor of TGF-beta signaling.
{ECO:0000269|PubMed:19049980}.
-!- SUBUNIT: Interacts with SMAD2, SMAD3 and SMAD4. Interacts with
HIPK2. Part of a complex with HIPK2 and SMAD1/2/3. Interacts with
PRDM16 and SMAD3; the interaction with PRDM16 promotes the
recruitment SMAD3-HDAC1 complex on the promoter of TGF-beta target
genes. {ECO:0000269|PubMed:12874272, ECO:0000269|PubMed:19049980}.
-!- INTERACTION:
Q9QUI1:Fam89b (xeno); NbExp=6; IntAct=EBI-347281, EBI-6503100;
O75376:NCOR1; NbExp=4; IntAct=EBI-347281, EBI-347233;
Q60974:Ncor1 (xeno); NbExp=5; IntAct=EBI-347281, EBI-349004;
Q6ZSG1:RNF165; NbExp=2; IntAct=EBI-347281, EBI-2129206;
Q8VI24:Satb2 (xeno); NbExp=2; IntAct=EBI-347281, EBI-5737999;
Q96ST3:SIN3A; NbExp=3; IntAct=EBI-347281, EBI-347218;
Q15796:SMAD2; NbExp=10; IntAct=EBI-347281, EBI-1040141;
P84022:SMAD3; NbExp=8; IntAct=EBI-347281, EBI-347161;
Q13485:SMAD4; NbExp=13; IntAct=EBI-347281, EBI-347263;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- PTM: Ubiquitinated by RNF165, promoting proteasomal degradation,
leading to enhance the BMP-Smad signaling.
{ECO:0000250|UniProtKB:Q60698}.
-!- DISEASE: Shprintzen-Goldberg craniosynostosis syndrome (SGS)
[MIM:182212]: A very rare syndrome characterized by a marfanoid
habitus, craniosynostosis, characteristic dysmorphic facial
features, skeletal and cardiovascular abnormalities, mental
retardation, developmental delay and learning disabilities.
{ECO:0000269|PubMed:23023332, ECO:0000269|PubMed:23103230,
ECO:0000269|PubMed:24357594, ECO:0000269|PubMed:24736733}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the SKI family. {ECO:0000305}.
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EMBL; X15218; CAA33288.1; -; mRNA.
EMBL; AL590822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS39.1; -.
PIR; S06053; TVHUSK.
RefSeq; NP_003027.1; NM_003036.3.
UniGene; Hs.656507; -.
PDB; 1MR1; X-ray; 2.85 A; C/D=219-313.
PDB; 1SBX; X-ray; 1.65 A; A=91-192.
PDBsum; 1MR1; -.
PDBsum; 1SBX; -.
ProteinModelPortal; P12755; -.
SMR; P12755; -.
BioGrid; 112388; 121.
CORUM; P12755; -.
DIP; DIP-31514N; -.
IntAct; P12755; 17.
MINT; MINT-269973; -.
STRING; 9606.ENSP00000367797; -.
iPTMnet; P12755; -.
PhosphoSitePlus; P12755; -.
BioMuta; SKI; -.
DMDM; 134517; -.
EPD; P12755; -.
MaxQB; P12755; -.
PaxDb; P12755; -.
PeptideAtlas; P12755; -.
PRIDE; P12755; -.
Ensembl; ENST00000378536; ENSP00000367797; ENSG00000157933.
GeneID; 6497; -.
KEGG; hsa:6497; -.
UCSC; uc001aja.5; human.
CTD; 6497; -.
DisGeNET; 6497; -.
EuPathDB; HostDB:ENSG00000157933.9; -.
GeneCards; SKI; -.
GeneReviews; SKI; -.
HGNC; HGNC:10896; SKI.
HPA; CAB010449; -.
HPA; HPA066567; -.
MalaCards; SKI; -.
MIM; 164780; gene.
MIM; 182212; phenotype.
neXtProt; NX_P12755; -.
OpenTargets; ENSG00000157933; -.
Orphanet; 1606; 1p36 deletion syndrome.
Orphanet; 2462; Shprintzen-Goldberg syndrome.
PharmGKB; PA35796; -.
eggNOG; ENOG410IFDK; Eukaryota.
eggNOG; ENOG410Y8AU; LUCA.
GeneTree; ENSGT00530000063040; -.
HOGENOM; HOG000039989; -.
HOVERGEN; HBG006599; -.
InParanoid; P12755; -.
OMA; EQLWPRP; -.
OrthoDB; EOG091G0O02; -.
PhylomeDB; P12755; -.
TreeFam; TF324133; -.
Reactome; R-HSA-201451; Signaling by BMP.
Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
SignaLink; P12755; -.
SIGNOR; P12755; -.
ChiTaRS; SKI; human.
EvolutionaryTrace; P12755; -.
GeneWiki; SKI_protein; -.
GenomeRNAi; 6497; -.
PRO; PR:P12755; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000157933; -.
CleanEx; HS_SKI; -.
Genevisible; P12755; HS.
GO; GO:0005813; C:centrosome; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; ISS:BHF-UCL.
GO; GO:0017053; C:transcriptional repressor complex; ISS:BHF-UCL.
GO; GO:0046811; F:histone deacetylase inhibitor activity; ISS:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; IPI:UniProtKB.
GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0009948; P:anterior/posterior axis specification; ISS:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; TAS:Reactome.
GO; GO:0060349; P:bone morphogenesis; ISS:BHF-UCL.
GO; GO:0043010; P:camera-type eye development; ISS:BHF-UCL.
GO; GO:0048593; P:camera-type eye morphogenesis; ISS:BHF-UCL.
GO; GO:0048870; P:cell motility; NAS:BHF-UCL.
GO; GO:0008283; P:cell proliferation; NAS:BHF-UCL.
GO; GO:0030326; P:embryonic limb morphogenesis; ISS:BHF-UCL.
GO; GO:0060325; P:face morphogenesis; ISS:BHF-UCL.
GO; GO:0002089; P:lens morphogenesis in camera-type eye; ISS:BHF-UCL.
GO; GO:0022011; P:myelination in peripheral nervous system; ISS:BHF-UCL.
GO; GO:0014902; P:myotube differentiation; IDA:UniProtKB.
GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:BHF-UCL.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:UniProtKB.
GO; GO:0010626; P:negative regulation of Schwann cell proliferation; IGI:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
GO; GO:0001843; P:neural tube closure; ISS:BHF-UCL.
GO; GO:0048666; P:neuron development; IBA:GO_Central.
GO; GO:0043585; P:nose morphogenesis; ISS:BHF-UCL.
GO; GO:0021772; P:olfactory bulb development; ISS:BHF-UCL.
GO; GO:0060021; P:palate development; ISS:BHF-UCL.
GO; GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; NAS:BHF-UCL.
GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
GO; GO:0060041; P:retina development in camera-type eye; ISS:BHF-UCL.
GO; GO:0048741; P:skeletal muscle fiber development; ISS:BHF-UCL.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:UniProtKB.
GO; GO:0035019; P:somatic stem cell population maintenance; ISS:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; NAS:BHF-UCL.
Gene3D; 3.10.260.20; -; 1.
Gene3D; 3.10.390.10; -; 1.
InterPro; IPR014890; c-SKI_SMAD4-bd_dom.
InterPro; IPR009061; DNA-bd_dom_put_sf.
InterPro; IPR010919; SAND-like_dom_sf.
InterPro; IPR028760; Ski.
InterPro; IPR003380; SKI/SNO/DAC.
InterPro; IPR037000; Ski_DNA-bd_sf.
InterPro; IPR023216; Tscrpt_reg_SKI_SnoN.
PANTHER; PTHR10005; PTHR10005; 1.
PANTHER; PTHR10005:SF15; PTHR10005:SF15; 1.
Pfam; PF08782; c-SKI_SMAD_bind; 1.
Pfam; PF02437; Ski_Sno; 1.
SMART; SM01046; c-SKI_SMAD_bind; 1.
SUPFAM; SSF46955; SSF46955; 1.
SUPFAM; SSF63763; SSF63763; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Craniosynostosis;
Disease mutation; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 728 Ski oncogene.
/FTId=PRO_0000129382.
COILED 536 710 {ECO:0000255}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 480 480 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 720 720 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 21 21 L -> R (in SGS; dbSNP:rs869312902).
{ECO:0000269|PubMed:23023332}.
/FTId=VAR_071170.
VARIANT 28 28 S -> T (in SGS).
{ECO:0000269|PubMed:24736733}.
/FTId=VAR_071659.
VARIANT 31 31 S -> L (in SGS).
{ECO:0000269|PubMed:23103230,
ECO:0000269|PubMed:24736733}.
/FTId=VAR_071171.
VARIANT 32 32 L -> P (in SGS).
{ECO:0000269|PubMed:23103230}.
/FTId=VAR_071172.
VARIANT 32 32 L -> V (in SGS; dbSNP:rs387907304).
{ECO:0000269|PubMed:23023332,
ECO:0000269|PubMed:23103230,
ECO:0000269|PubMed:24736733}.
/FTId=VAR_071173.
VARIANT 34 34 G -> A (in SGS).
{ECO:0000269|PubMed:24736733}.
/FTId=VAR_071660.
VARIANT 34 34 G -> C (in SGS; dbSNP:rs387907306).
{ECO:0000269|PubMed:23023332,
ECO:0000269|PubMed:23103230}.
/FTId=VAR_071174.
VARIANT 34 34 G -> D (in SGS; dbSNP:rs387907305).
{ECO:0000269|PubMed:23023332,
ECO:0000269|PubMed:24736733}.
/FTId=VAR_071175.
VARIANT 34 34 G -> S (in SGS; dbSNP:rs387907306).
{ECO:0000269|PubMed:23023332,
ECO:0000269|PubMed:23103230,
ECO:0000269|PubMed:24736733}.
/FTId=VAR_071176.
VARIANT 34 34 G -> V (in SGS; dbSNP:rs387907305).
{ECO:0000269|PubMed:23103230,
ECO:0000269|PubMed:24736733}.
/FTId=VAR_071177.
VARIANT 35 35 P -> Q (in SGS; dbSNP:rs397514589).
{ECO:0000269|PubMed:23103230}.
/FTId=VAR_071178.
VARIANT 35 35 P -> S (in SGS; dbSNP:rs397514590).
{ECO:0000269|PubMed:23023332,
ECO:0000269|PubMed:23103230,
ECO:0000269|PubMed:24357594,
ECO:0000269|PubMed:24736733}.
/FTId=VAR_071179.
VARIANT 94 97 Missing (in SGS).
{ECO:0000269|PubMed:23103230}.
/FTId=VAR_071180.
VARIANT 95 97 Missing (in SGS).
{ECO:0000269|PubMed:23023332,
ECO:0000269|PubMed:23103230}.
/FTId=VAR_071181.
VARIANT 116 116 G -> E (in SGS; dbSNP:rs387907303).
{ECO:0000269|PubMed:23023332,
ECO:0000269|PubMed:24357594}.
/FTId=VAR_071182.
VARIANT 117 117 G -> R (in SGS; dbSNP:rs869312901).
{ECO:0000269|PubMed:23023332}.
/FTId=VAR_071183.
STRAND 101 105 {ECO:0000244|PDB:1SBX}.
STRAND 108 115 {ECO:0000244|PDB:1SBX}.
STRAND 118 122 {ECO:0000244|PDB:1SBX}.
HELIX 123 127 {ECO:0000244|PDB:1SBX}.
TURN 128 133 {ECO:0000244|PDB:1SBX}.
HELIX 136 145 {ECO:0000244|PDB:1SBX}.
HELIX 155 163 {ECO:0000244|PDB:1SBX}.
STRAND 175 178 {ECO:0000244|PDB:1SBX}.
HELIX 179 190 {ECO:0000244|PDB:1SBX}.
STRAND 219 222 {ECO:0000244|PDB:1MR1}.
STRAND 228 232 {ECO:0000244|PDB:1MR1}.
HELIX 234 236 {ECO:0000244|PDB:1MR1}.
STRAND 245 247 {ECO:0000244|PDB:1MR1}.
TURN 248 250 {ECO:0000244|PDB:1MR1}.
HELIX 256 259 {ECO:0000244|PDB:1MR1}.
STRAND 269 275 {ECO:0000244|PDB:1MR1}.
HELIX 278 280 {ECO:0000244|PDB:1MR1}.
HELIX 281 284 {ECO:0000244|PDB:1MR1}.
HELIX 296 310 {ECO:0000244|PDB:1MR1}.
SEQUENCE 728 AA; 80005 MW; 9B78C4840A28C2DA CRC64;
MEAAAGGRGC FQPHPGLQKT LEQFHLSSMS SLGGPAAFSA RWAQEAYKKE SAKEAGAAAV
PAPVPAATEP PPVLHLPAIQ PPPPVLPGPF FMPSDRSTER CETVLEGETI SCFVVGGEKR
LCLPQILNSV LRDFSLQQIN AVCDELHIYC SRCTADQLEI LKVMGILPFS APSCGLITKT
DAERLCNALL YGGAYPPPCK KELAASLALG LELSERSVRV YHECFGKCKG LLVPELYSSP
SAACIQCLDC RLMYPPHKFV VHSHKALENR TCHWGFDSAN WRAYILLSQD YTGKEEQARL
GRCLDDVKEK FDYGNKYKRR VPRVSSEPPA SIRPKTDDTS SQSPAPSEKD KPSSWLRTLA
GSSNKSLGCV HPRQRLSAFR PWSPAVSASE KELSPHLPAL IRDSFYSYKS FETAVAPNVA
LAPPAQQKVV SSPPCAAAVS RAPEPLATCT QPRKRKLTVD TPGAPETLAP VAAPEEDKDS
EAEVEVESRE EFTSSLSSLS SPSFTSSSSA KDLGSPGARA LPSAVPDAAA PADAPSGLEA
ELEHLRQALE GGLDTKEAKE KFLHEVVKMR VKQEEKLSAA LQAKRSLHQE LEFLRVAKKE
KLREATEAKR NLRKEIERLR AENEKKMKEA NESRLRLKRE LEQARQARVC DKGCEAGRLR
AKYSAQIEDL QVKLQHAEAD REQLRADLLR EREAREHLEK VVKELQEQLW PRARPEAAGS
EGAAELEP


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