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Database: UniProt
Entry: O00238
LinkDB: O00238
Original site: O00238 
ID   BMR1B_HUMAN             Reviewed;         502 AA.
AC   O00238; B2R953; B4DSV1; P78366;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   19-MAR-2014, entry version 151.
DE   RecName: Full=Bone morphogenetic protein receptor type-1B;
DE            Short=BMP type-1B receptor;
DE            Short=BMPR-1B;
DE            EC=2.7.11.30;
DE   AltName: CD_antigen=CDw293;
DE   Flags: Precursor;
GN   Name=BMPR1B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=9178898; DOI=10.1038/sj.onc.1200964;
RA   Ide H., Katoh M., Sasaki H., Yoshida T., Aoki K., Nawa Y., Osada Y.,
RA   Sugimura T., Terada M.;
RT   "Cloning of human bone morphogenetic protein type IB receptor (BMPR-
RT   IB) and its expression in prostate cancer in comparison with other
RT   BMPRs.";
RL   Oncogene 14:1377-1382(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Ovary;
RX   PubMed=10051328; DOI=10.1007/s003359900990;
RA   Astroem A.-K., Jin D.F., Imamura T., Roijer E., Rosenzweig B.,
RA   Miyazono K., ten Dijke P., Stenman G.;
RT   "Chromosomal localization of three human genes encoding bone
RT   morphogenetic protein receptors.";
RL   Mamm. Genome 10:299-302(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Uterus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=PNS;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   VARIANTS BDA2 LYS-200 AND TRP-486.
RX   PubMed=14523231; DOI=10.1073/pnas.2133476100;
RA   Lehmann K., Seemann P., Stricker S., Sammar M., Meyer B., Suering K.,
RA   Majewski F., Tinschert S., Grzeschik K.-H., Mueller D., Knaus P.,
RA   Nuernberg P., Mundlos S.;
RT   "Mutations in bone morphogenetic protein receptor 1B cause
RT   brachydactyly type A2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12277-12282(2003).
RN   [8]
RP   INVOLVEMENT IN AMDGA.
RX   PubMed=15805157; DOI=10.1136/jmg.2004.023564;
RA   Demirhan O., Tuerkmen S., Schwabe G.C., Soyupak S., Akguel E.,
RA   Tastemir D., Karahan D., Mundlos S., Lehmann K.;
RT   "A homozygous BMPR1B mutation causes a new subtype of acromesomelic
RT   chondrodysplasia with genital anomalies.";
RL   J. Med. Genet. 42:314-317(2005).
RN   [9]
RP   VARIANT BRACHYDACTYLY TYPE C/BDA2 GLN-486.
RX   PubMed=16957682; DOI=10.1038/sj.ejhg.5201708;
RA   Lehmann K., Seemann P., Boergermann J., Morin G., Reif S., Knaus P.,
RA   Mundlos S.;
RT   "A novel R486Q mutation in BMPR1B resulting in either a brachydactyly
RT   type C/symphalangism-like phenotype or brachydactyly type A2.";
RL   Eur. J. Hum. Genet. 14:1248-1254(2006).
RN   [10]
RP   VARIANTS [LARGE SCALE ANALYSIS] HIS-31; TRP-149; HIS-224; ASN-297 AND
RP   GLN-371.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA   Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA   O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA   Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA   Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA   Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA   Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA   West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA   Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA   DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA   Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA   Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: On ligand binding, forms a receptor complex consisting
CC       of two type II and two type I transmembrane serine/threonine
CC       kinases. Type II receptors phosphorylate and activate type I
CC       receptors which autophosphorylate, then bind and activate SMAD
CC       transcriptional regulators. Receptor for BMP7/OP-1 and GDF5.
CC   -!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
CC       protein] phosphate.
CC   -!- COFACTOR: Magnesium or manganese (By similarity).
CC   -!- INTERACTION:
CC       P12643:BMP2; NbExp=3; IntAct=EBI-7527193, EBI-1029262;
CC       P43026:GDF5; NbExp=6; IntAct=EBI-7527193, EBI-8571476;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O00238-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O00238-2; Sequence=VSP_045100;
CC   -!- DISEASE: Acromesomelic chondrodysplasia, with genital anomalies
CC       (AMDGA) [MIM:609441]: A form of chondrodysplasia. Acromesomelic
CC       chondrodysplasias are rare hereditary skeletal disorders
CC       characterized by short stature, very short limbs and hand/foot
CC       malformations. The severity of limb abnormalities increases from
CC       proximal to distal with profoundly affected hands and feet showing
CC       brachydactyly and/or rudimentary fingers (knob-like fingers).
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Brachydactyly A2 (BDA2) [MIM:112600]: A form of
CC       brachydactyly. Brachydactyly defines a group of inherited
CC       malformations characterized by shortening of the digits due to
CC       abnormal development of the phalanges and/or the metacarpals. In
CC       brachydactyly type A2 shortening of the middle phalanges is
CC       confined to the index finger and the second toe, all other digits
CC       being more or less normal. Because of a rhomboid or triangular
CC       shape of the affected middle phalanx, the end of the second finger
CC       usually deviates radially. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC   -!- SIMILARITY: Contains 1 GS domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/books/NBK1116/?term=BMPR1B[genesymbol]";
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DR   EMBL; D89675; BAA19765.1; -; mRNA.
DR   EMBL; U89326; AAC28131.1; -; mRNA.
DR   EMBL; AK299930; BAG61763.1; -; mRNA.
DR   EMBL; AK313642; BAG36400.1; -; mRNA.
DR   EMBL; AC004061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC093634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC105395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471057; EAX06060.1; -; Genomic_DNA.
DR   EMBL; BC047773; AAH47773.1; -; mRNA.
DR   EMBL; BC069796; AAH69796.1; -; mRNA.
DR   EMBL; BC069803; AAH69803.1; -; mRNA.
DR   RefSeq; NP_001194.1; NM_001203.2.
DR   RefSeq; NP_001243721.1; NM_001256792.1.
DR   RefSeq; NP_001243722.1; NM_001256793.1.
DR   RefSeq; NP_001243723.1; NM_001256794.1.
DR   RefSeq; XP_005263237.1; XM_005263180.1.
DR   RefSeq; XP_005263238.1; XM_005263181.1.
DR   UniGene; Hs.598475; -.
DR   PDB; 3MDY; X-ray; 2.05 A; A/C=168-502.
DR   PDBsum; 3MDY; -.
DR   ProteinModelPortal; O00238; -.
DR   SMR; O00238; 29-113, 174-500.
DR   BioGrid; 107126; 67.
DR   IntAct; O00238; 3.
DR   MINT; MINT-1340235; -.
DR   STRING; 9606.ENSP00000264568; -.
DR   BindingDB; O00238; -.
DR   ChEMBL; CHEMBL5476; -.
DR   GuidetoPHARMACOLOGY; 1789; -.
DR   PhosphoSite; O00238; -.
DR   PaxDb; O00238; -.
DR   PRIDE; O00238; -.
DR   DNASU; 658; -.
DR   Ensembl; ENST00000264568; ENSP00000264568; ENSG00000138696. [O00238-1]
DR   Ensembl; ENST00000394931; ENSP00000378389; ENSG00000138696. [O00238-1]
DR   Ensembl; ENST00000440890; ENSP00000401907; ENSG00000138696. [O00238-2]
DR   Ensembl; ENST00000509540; ENSP00000421671; ENSG00000138696. [O00238-1]
DR   Ensembl; ENST00000512312; ENSP00000425444; ENSG00000138696. [O00238-1]
DR   Ensembl; ENST00000515059; ENSP00000426617; ENSG00000138696. [O00238-1]
DR   GeneID; 658; -.
DR   KEGG; hsa:658; -.
DR   UCSC; uc003htm.4; human. [O00238-1]
DR   CTD; 658; -.
DR   GeneCards; GC04P095679; -.
DR   HGNC; HGNC:1077; BMPR1B.
DR   HPA; CAB009634; -.
DR   HPA; HPA046821; -.
DR   MIM; 112600; phenotype.
DR   MIM; 603248; gene.
DR   MIM; 609441; phenotype.
DR   neXtProt; NX_O00238; -.
DR   Orphanet; 93396; Brachydactyly type A2.
DR   Orphanet; 93384; Brachydactyly type C.
DR   PharmGKB; PA25387; -.
DR   eggNOG; COG0515; -.
DR   HOGENOM; HOG000230587; -.
DR   HOVERGEN; HBG054502; -.
DR   InParanoid; O00238; -.
DR   KO; K13578; -.
DR   OMA; LRCKCHH; -.
DR   OrthoDB; EOG7Q8CN3; -.
DR   PhylomeDB; O00238; -.
DR   TreeFam; TF314724; -.
DR   BRENDA; 2.7.10.2; 2681.
DR   Reactome; REACT_111102; Signal Transduction.
DR   SignaLink; O00238; -.
DR   ChiTaRS; BMPR1B; human.
DR   EvolutionaryTrace; O00238; -.
DR   GeneWiki; BMPR1B; -.
DR   GenomeRNAi; 658; -.
DR   NextBio; 2676; -.
DR   PRO; PR:O00238; -.
DR   ArrayExpress; O00238; -.
DR   Bgee; O00238; -.
DR   CleanEx; HS_BMPR1B; -.
DR   Genevestigator; O00238; -.
DR   GO; GO:0005887; C:integral component of plasma membrane; IC:UniProtKB.
DR   GO; GO:0043235; C:receptor complex; TAS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:HGNC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004702; F:receptor signaling protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0046332; F:SMAD binding; IDA:HGNC.
DR   GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IEA:Ensembl.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IMP:UniProtKB.
DR   GO; GO:0030509; P:BMP signaling pathway; NAS:UniProtKB.
DR   GO; GO:0001502; P:cartilage condensation; NAS:UniProtKB.
DR   GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR   GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:GOC.
DR   GO; GO:0035108; P:limb morphogenesis; IMP:UniProtKB.
DR   GO; GO:0001550; P:ovarian cumulus expansion; ISS:UniProtKB.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL.
DR   GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
DR   GO; GO:0023014; P:signal transduction by phosphorylation; IEA:GOC.
DR   InterPro; IPR000472; Activin_rcpt.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR003605; TGF_beta_rcpt_GS.
DR   InterPro; IPR000333; TGFB_receptor.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   SMART; SM00467; GS; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51256; GS; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Chondrogenesis;
KW   Complete proteome; Disease mutation; Disulfide bond; Dwarfism; Kinase;
KW   Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW   Polymorphism; Receptor; Reference proteome;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     13       Potential.
FT   CHAIN        14    502       Bone morphogenetic protein receptor type-
FT                                1B.
FT                                /FTId=PRO_0000024412.
FT   TOPO_DOM     14    126       Extracellular (Potential).
FT   TRANSMEM    127    148       Helical; (Potential).
FT   TOPO_DOM    149    502       Cytoplasmic (Potential).
FT   DOMAIN      174    203       GS.
FT   DOMAIN      204    494       Protein kinase.
FT   NP_BIND     210    218       ATP (By similarity).
FT   ACT_SITE    332    332       Proton acceptor (By similarity).
FT   BINDING     231    231       ATP (By similarity).
FT   DISULFID     32     53       By similarity.
FT   DISULFID     34     38       By similarity.
FT   DISULFID     47     71       By similarity.
FT   DISULFID     81     95       By similarity.
FT   DISULFID     96    102       By similarity.
FT   VAR_SEQ       1      1       M -> MGWLEELNWQLHIFLLILLSMHTRANFLDNM (in
FT                                isoform 2).
FT                                /FTId=VSP_045100.
FT   VARIANT      31     31       R -> H (in a gastric adenocarcinoma
FT                                sample; somatic mutation).
FT                                /FTId=VAR_041401.
FT   VARIANT     149    149       R -> W (in dbSNP:rs34231464).
FT                                /FTId=VAR_041402.
FT   VARIANT     200    200       I -> K (in BDA2; dbSNP:rs28939703).
FT                                /FTId=VAR_023819.
FT   VARIANT     224    224       R -> H (in dbSNP:rs35973133).
FT                                /FTId=VAR_041403.
FT   VARIANT     297    297       D -> N (in a metastatic melanoma sample;
FT                                somatic mutation).
FT                                /FTId=VAR_041404.
FT   VARIANT     371    371       R -> Q (in dbSNP:rs34970181).
FT                                /FTId=VAR_041405.
FT   VARIANT     486    486       R -> Q (in brachydactyly type C and BDA2;
FT                                with also additional features of
FT                                symphalangism-1).
FT                                /FTId=VAR_037967.
FT   VARIANT     486    486       R -> W (in BDA2; dbSNP:rs28939704).
FT                                /FTId=VAR_023820.
FT   HELIX       176    186
FT   STRAND      190    192
FT   HELIX       194    197
FT   HELIX       200    203
FT   STRAND      205    213
FT   STRAND      216    223
FT   STRAND      226    234
FT   HELIX       235    237
FT   HELIX       238    248
FT   STRAND      261    268
FT   HELIX       270    272
FT   STRAND      274    279
FT   HELIX       287    293
FT   HELIX       298    316
FT   STRAND      337    340
FT   STRAND      346    348
FT   HELIX       375    377
FT   HELIX       380    383
FT   HELIX       393    411
FT   TURN        426    430
FT   HELIX       437    444
FT   HELIX       455    459
FT   HELIX       461    473
FT   HELIX       478    480
FT   HELIX       484    496
FT   TURN        497    499
SQ   SEQUENCE   502 AA;  56930 MW;  B283D9BF45535C79 CRC64;
     MLLRSAGKLN VGTKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED
     DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKNRDFVD
     GPIHHRALLI SVTVCSLLLV LIILFCYFRY KRQETRPRYS IGLEQDETYI PPGESLRDLI
     EQSQSSGSGS GLPLLVQRTI AKQIQMVKQI GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS
     WFRETEIYQT VLMRHENILG FIAADIKGTG SWTQLYLITD YHENGSLYDY LKSTTLDAKS
     MLKLAYSSVS GLCHLHTEIF STQGKPAIAH RDLKSKNILV KKNGTCCIAD LGLAVKFISD
     TNEVDIPPNT RVGTKRYMPP EVLDESLNRN HFQSYIMADM YSFGLILWEV ARRCVSGGIV
     EEYQLPYHDL VPSDPSYEDM REIVCIKKLR PSFPNRWSSD ECLRQMGKLM TECWAHNPAS
     RLTALRVKKT LAKMSESQDI KL
//
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