DPH1_HUMAN
ID DPH1_HUMAN Reviewed; 443 AA.
AC Q9BZG8; D3DTI3; Q16439; Q4VBA2; Q9BTW7; Q9UCY0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 {ECO:0000305};
DE EC=2.5.1.108 {ECO:0000250|UniProtKB:Q5NCQ5};
DE AltName: Full=Diphthamide biosynthesis protein 1 {ECO:0000305};
DE AltName: Full=Diphtheria toxin resistance protein 1 {ECO:0000305};
DE AltName: Full=Ovarian cancer-associated gene 1 protein {ECO:0000305};
DE AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1 {ECO:0000305};
GN Name=DPH1 {ECO:0000303|PubMed:26220823};
GN Synonyms=DPH2L {ECO:0000303|PubMed:8603384}, DPH2L1,
GN OVCA1 {ECO:0000303|PubMed:8616839};
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=8603384; DOI=10.1016/0304-3835(96)04169-9;
RA Phillips N.J., Zeigler M.R., Deaven L.L.;
RT "A cDNA from the ovarian cancer critical region of deletion on chromosome
RT 17p13.3.";
RL Cancer Lett. 102:85-90(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP ARG-226.
RX PubMed=8616839;
RA Schultz D.C., Vanderveer L., Berman D.B., Hamilton T.C., Wong A.J.,
RA Godwin A.K.;
RT "Identification of two candidate tumor suppressor genes on chromosome
RT 17p13.3.";
RL Cancer Res. 56:1997-2002(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANTS BREAST AND
RP OVARIAN CANCER VAL-7; ASP-34; VAL-335 AND ARG-389, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=10519411;
RA Bruening W., Prowse A.H., Schultz D.C., Holgado-Madruga M., Wong A.,
RA Godwin A.K.;
RT "Expression of OVCA1, a candidate tumor suppressor, is reduced in tumors
RT and inhibits growth of ovarian cancer cells.";
RL Cancer Res. 59:4973-4983(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 8-443 (ISOFORM 1).
RC TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-443 (ISOFORMS 1/2/3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INTERACTION WITH RBM8A.
RX PubMed=11013075; DOI=10.1006/geno.2000.6315;
RA Salicioni A.M., Xi M., Vanderveer L.A., Balsara B., Testa J.R.,
RA Dunbrack R.L. Jr., Godwin A.K.;
RT "Identification and structural analysis of human RBM8A and RBM8B: two
RT highly conserved RNA-binding motif proteins that interact with OVCA1, a
RT candidate tumor suppressor.";
RL Genomics 69:54-62(2000).
RN [9]
RP INVOLVEMENT IN DEDSSH, AND VARIANT DEDSSH PRO-234.
RX PubMed=25558065; DOI=10.1016/j.celrep.2014.12.015;
RA Alazami A.M., Patel N., Shamseldin H.E., Anazi S., Al-Dosari M.S.,
RA Alzahrani F., Hijazi H., Alshammari M., Aldahmesh M.A., Salih M.A.,
RA Faqeih E., Alhashem A., Bashiri F.A., Al-Owain M., Kentab A.Y., Sogaty S.,
RA Al Tala S., Temsah M.H., Tulbah M., Aljelaify R.F., Alshahwan S.A.,
RA Seidahmed M.Z., Alhadid A.A., Aldhalaan H., Alqallaf F., Kurdi W.,
RA Alfadhel M., Babay Z., Alsogheer M., Kaya N., Al-Hassnan Z.N.,
RA Abdel-Salam G.M., Al-Sannaa N., Al Mutairi F., El Khashab H.Y., Bohlega S.,
RA Jia X., Nguyen H.C., Hammami R., Adly N., Mohamed J.Y., Abdulwahab F.,
RA Ibrahim N., Naim E.A., Al-Younes B., Meyer B.F., Hashem M., Shaheen R.,
RA Xiong Y., Abouelhoda M., Aldeeri A.A., Monies D.M., Alkuraya F.S.;
RT "Accelerating novel candidate gene discovery in neurogenetic disorders via
RT whole-exome sequencing of prescreened multiplex consanguineous families.";
RL Cell Rep. 10:148-161(2015).
RN [10]
RP INVOLVEMENT IN DEDSSH, AND VARIANT DEDSSH LYS-6.
RX PubMed=26220823; DOI=10.1002/humu.22843;
RA Loucks C.M., Parboosingh J.S., Shaheen R., Bernier F.P., McLeod D.R.,
RA Seidahmed M.Z., Puffenberger E.G., Ober C., Hegele R.A., Boycott K.M.,
RA Alkuraya F.S., Innes A.M.;
RT "Matching two independent cohorts validates DPH1 as a gene responsible for
RT autosomal recessive intellectual disability with short stature,
RT craniofacial, and ectodermal anomalies.";
RL Hum. Mutat. 36:1015-1019(2015).
RN [11]
RP VARIANT DEDSSH PRO-164.
RX PubMed=29362492; DOI=10.1038/s10038-017-0399-2;
RA Nakajima J., Oana S., Sakaguchi T., Nakashima M., Numabe H., Kawashima H.,
RA Matsumoto N., Miyake N.;
RT "Novel compound heterozygous DPH1 mutations in a patient with the unique
RT clinical features of airway obstruction and external genital
RT abnormalities.";
RL J. Hum. Genet. 63:529-532(2018).
RN [12]
RP CHARACTERIZATION OF VARIANTS DEDSSH LYS-6; CYS-112; PRO-125 AND PRO-164,
RP VARIANTS DEDSSH CYS-112 AND PRO-125, AND FUNCTION.
RX PubMed=30877278; DOI=10.1038/s41431-019-0374-9;
RA Urreizti R., Mayer K., Evrony G.D., Said E., Castilla-Vallmanya L.,
RA Cody N.A.L., Plasencia G., Gelb B.D., Grinberg D., Brinkmann U., Webb B.D.,
RA Balcells S.;
RT "DPH1 syndrome: two novel variants and structural and functional analyses
RT of seven missense variants identified in syndromic patients.";
RL Eur. J. Hum. Genet. 28:64-75(2020).
CC -!- FUNCTION: Catalyzes the first step of diphthamide biosynthesis, a post-
CC translational modification of histidine which occurs in elongation
CC factor 2 (PubMed:30877278). DPH1 and DPH2 transfer a 3-amino-3-
CC carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a
CC histidine residue, the reaction is assisted by a reduction system
CC comprising DPH3 and a NADH-dependent reductase (By similarity). Acts as
CC a tumor suppressor (PubMed:10519411). {ECO:0000250|UniProtKB:P40487,
CC ECO:0000269|PubMed:10519411, ECO:0000269|PubMed:30877278}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[translation elongation factor 2] + S-adenosyl-L-
CC methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation
CC elongation factor 2] + H(+) + S-methyl-5'-thioadenosine;
CC Xref=Rhea:RHEA:36783, Rhea:RHEA-COMP:9748, Rhea:RHEA-COMP:9749,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:73995; EC=2.5.1.108;
CC Evidence={ECO:0000250|UniProtKB:Q5NCQ5};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P40487};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:P40487};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Component of the 2-(3-amino-3-carboxypropyl)histidine synthase
CC complex composed of DPH1, DPH2, DPH3 and a NADH-dependent reductase (By
CC similarity). Interacts with DPH2 (By similarity). Interacts with RBM8A
CC (PubMed:11013075). {ECO:0000250|UniProtKB:P40487,
CC ECO:0000250|UniProtKB:Q5NCQ5, ECO:0000269|PubMed:11013075}.
CC -!- INTERACTION:
CC Q9BZG8; Q12800: TFCP2; NbExp=3; IntAct=EBI-10303200, EBI-717422;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10519411}. Cytoplasm
CC {ECO:0000269|PubMed:10519411}. Note=Punctate, primarily perinuclear
CC localization. {ECO:0000269|PubMed:10519411}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BZG8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZG8-2; Sequence=VSP_028852;
CC Name=3;
CC IsoId=Q9BZG8-3; Sequence=VSP_028851;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver,
CC skeletal muscle, kidney, pancreas, spleen, thymus, mammary gland,
CC colon, small intestine, testis and ovary. Reduced expression in primary
CC breast and ovarian tumors. {ECO:0000269|PubMed:10519411,
CC ECO:0000269|PubMed:8616839}.
CC -!- DISEASE: Developmental delay with short stature, dysmorphic facial
CC features, and sparse hair (DEDSSH) [MIM:616901]: An autosomal recessive
CC syndrome characterized by intellectual disability, short stature, and
CC craniofacial and ectodermal anomalies including scaphocephaly with or
CC without craniosynostosis, prominent forehead, sparse eyebrows and hair,
CC hypoplastic toenails and, in some cases, dental anomalies.
CC {ECO:0000269|PubMed:25558065, ECO:0000269|PubMed:26220823,
CC ECO:0000269|PubMed:29362492, ECO:0000269|PubMed:30877278}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
CC {ECO:0000305}.
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DR EMBL; S81752; AAB36297.1; -; mRNA.
DR EMBL; U34880; AAD10198.1; -; mRNA.
DR EMBL; AF321876; AAK13428.1; -; mRNA.
DR EMBL; AC099684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90567.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90569.1; -; Genomic_DNA.
DR EMBL; BC003099; AAH03099.2; -; mRNA.
DR EMBL; BC096088; AAH96088.1; -; mRNA.
DR EMBL; BT019878; AAV38681.1; -; mRNA.
DR RefSeq; NP_001333505.1; NM_001346576.1. [Q9BZG8-3]
DR RefSeq; NP_001374.3; NM_001383.4.
DR AlphaFoldDB; Q9BZG8; -.
DR SMR; Q9BZG8; -.
DR BioGRID; 108135; 59.
DR IntAct; Q9BZG8; 19.
DR STRING; 9606.ENSP00000263083; -.
DR iPTMnet; Q9BZG8; -.
DR PhosphoSitePlus; Q9BZG8; -.
DR BioMuta; DPH1; -.
DR DMDM; 269849559; -.
DR EPD; Q9BZG8; -.
DR jPOST; Q9BZG8; -.
DR MassIVE; Q9BZG8; -.
DR MaxQB; Q9BZG8; -.
DR PaxDb; Q9BZG8; -.
DR PeptideAtlas; Q9BZG8; -.
DR PRIDE; Q9BZG8; -.
DR ProteomicsDB; 79843; -. [Q9BZG8-1]
DR ProteomicsDB; 79844; -. [Q9BZG8-2]
DR ProteomicsDB; 79845; -. [Q9BZG8-3]
DR Antibodypedia; 22821; 216 antibodies from 25 providers.
DR DNASU; 1801; -.
DR Ensembl; ENST00000570477.6; ENSP00000458726.1; ENSG00000108963.19. [Q9BZG8-2]
DR Ensembl; ENST00000674200.2; ENSP00000501368.1; ENSG00000108963.19. [Q9BZG8-1]
DR GeneID; 1801; -.
DR KEGG; hsa:1801; -.
DR UCSC; uc002fts.4; human. [Q9BZG8-1]
DR CTD; 1801; -.
DR DisGeNET; 1801; -.
DR GeneCards; DPH1; -.
DR HGNC; HGNC:3003; DPH1.
DR HPA; ENSG00000108963; Low tissue specificity.
DR MalaCards; DPH1; -.
DR MIM; 603527; gene.
DR MIM; 616901; phenotype.
DR neXtProt; NX_Q9BZG8; -.
DR OpenTargets; ENSG00000108963; -.
DR Orphanet; 459061; Craniofacial dysplasia-short stature-ectodermal anomalies-intellectual disability syndrome.
DR PharmGKB; PA27461; -.
DR VEuPathDB; HostDB:ENSG00000108963; -.
DR eggNOG; KOG2648; Eukaryota.
DR GeneTree; ENSGT00940000153694; -.
DR HOGENOM; CLU_037146_1_1_1; -.
DR InParanoid; Q9BZG8; -.
DR OrthoDB; 750182at2759; -.
DR PhylomeDB; Q9BZG8; -.
DR TreeFam; TF105746; -.
DR PathwayCommons; Q9BZG8; -.
DR Reactome; R-HSA-5358493; Synthesis of diphthamide-EEF2.
DR SignaLink; Q9BZG8; -.
DR UniPathway; UPA00559; -.
DR BioGRID-ORCS; 1801; 265 hits in 1090 CRISPR screens.
DR ChiTaRS; DPH1; human.
DR GeneWiki; DPH1; -.
DR GenomeRNAi; 1801; -.
DR Pharos; Q9BZG8; Tbio.
DR PRO; PR:Q9BZG8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BZG8; protein.
DR Bgee; ENSG00000108963; Expressed in pituitary gland and 95 other tissues.
DR ExpressionAtlas; Q9BZG8; baseline and differential.
DR Genevisible; Q9BZG8; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR Gene3D; 3.40.50.11840; -; 1.
DR Gene3D; 3.40.50.11850; -; 1.
DR Gene3D; 3.40.50.11860; -; 1.
DR InterPro; IPR016435; DPH1/DPH2.
DR InterPro; IPR042263; DPH1/DPH2_1.
DR InterPro; IPR042264; DPH1/DPH2_2.
DR InterPro; IPR042265; DPH1/DPH2_3.
DR PANTHER; PTHR10762; PTHR10762; 1.
DR Pfam; PF01866; Diphthamide_syn; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR TIGRFAMs; TIGR00322; diphth2_R; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant; Dwarfism;
KW Ectodermal dysplasia; Hypotrichosis; Intellectual disability; Iron;
KW Iron-sulfur; Metal-binding; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Tumor suppressor.
FT CHAIN 1..443
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT subunit 1"
FT /id="PRO_0000307882"
FT REGION 396..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
FT BINDING 219
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
FT BINDING 347
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
FT VAR_SEQ 1..140
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028851"
FT VAR_SEQ 1..80
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8603384"
FT /id="VSP_028852"
FT VARIANT 6
FT /note="M -> K (in DEDSSH; normal diphthamide modification
FT of elongation factor 2; dbSNP:rs757167361)"
FT /evidence="ECO:0000269|PubMed:26220823,
FT ECO:0000269|PubMed:30877278"
FT /id="VAR_076412"
FT VARIANT 7
FT /note="A -> V (in breast and ovarian cancer;
FT dbSNP:rs778705666)"
FT /evidence="ECO:0000269|PubMed:10519411"
FT /id="VAR_036702"
FT VARIANT 34
FT /note="A -> D (in breast and ovarian cancer)"
FT /evidence="ECO:0000269|PubMed:10519411"
FT /id="VAR_036703"
FT VARIANT 51
FT /note="I -> M (in dbSNP:rs8070453)"
FT /id="VAR_059255"
FT VARIANT 112
FT /note="Y -> C (in DEDSSH; impairs diphthamide modification
FT of elongation factor 2; dbSNP:rs772969956)"
FT /evidence="ECO:0000269|PubMed:30877278"
FT /id="VAR_086296"
FT VARIANT 125
FT /note="L -> P (in DEDSSH; impairs diphthamide modification
FT of elongation factor 2; dbSNP:rs200530055)"
FT /evidence="ECO:0000269|PubMed:30877278"
FT /id="VAR_086297"
FT VARIANT 164
FT /note="L -> P (in DEDSSH; impairs diphthamide modification
FT of elongation factor 2)"
FT /evidence="ECO:0000269|PubMed:29362492,
FT ECO:0000269|PubMed:30877278"
FT /id="VAR_086298"
FT VARIANT 226
FT /note="K -> R (in dbSNP:rs1131600)"
FT /evidence="ECO:0000269|PubMed:8616839"
FT /id="VAR_055706"
FT VARIANT 234
FT /note="L -> P (in DEDSSH; impairs diphthamide modification
FT of elongation factor 2.; dbSNP:rs730882250)"
FT /evidence="ECO:0000269|PubMed:25558065"
FT /id="VAR_076413"
FT VARIANT 335
FT /note="L -> V (in breast and ovarian cancer; requires 2
FT nucleotide substitutions; dbSNP:rs35394823)"
FT /evidence="ECO:0000269|PubMed:10519411"
FT /id="VAR_036704"
FT VARIANT 389
FT /note="S -> R (in breast and ovarian cancer)"
FT /evidence="ECO:0000269|PubMed:10519411"
FT /id="VAR_036705"
FT CONFLICT 8
FT /note="A -> V (in Ref. 3; AAK13428)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="T -> I (in Ref. 6; AAH96088)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="F -> S (in Ref. 1; AAD10198/AAB36297)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 48805 MW; 6AF0FD0D8EE35E2D CRC64;
MRRQVMAALV VSGAAEQGGR DGPGRGRAPR GRVANQIPPE ILKNPQLQAA IRVLPSNYNF
EIPKTIWRIQ QAQAKKVALQ MPEGLLLFAC TIVDILERFT EAEVMVMGDV TYGACCVDDF
TARALGADFL VHYGHSCLIP MDTSAQDFRV LYVFVDIRID TTHLLDSLRL TFPPATALAL
VSTIQFVSTL QAAAQELKAE YRVSVPQCKP LSPGEILGCT SPRLSKEVEA VVYLGDGRFH
LESVMIANPN VPAYRYDPYS KVLSREHYDH QRMQAARQEA IATARSAKSW GLILGTLGRQ
GSPKILEHLE SRLRALGLSF VRLLLSEIFP SKLSLLPEVD VWVQVACPRL SIDWGTAFPK
PLLTPYEAAV ALRDISWQQP YPMDFYAGSS LGPWTVNHGQ DRRPHAPGRP ARGKVQEGSA
RPPSAVACED CSCRDEKVAP LAP
