RBCC Red Blood Cell Collection

ART4 (DO, DOK1) [Confidence: high (a blood group or CD marker)]
Ecto-ADP-ribosyltransferase 4; 2.4.2.31 (ADP-ribosyltransferase C2 and C3 toxin-like 4; ARTC4; Dombrock blood group carrier molecule; Mono(ADP-ribosyl)transferase 4; NAD(P)(+)--arginine ADP-ribosyltransferase 4; CD297; Flags: Precursor)

hRBCD IPI00004065
IPI00004065 Ecto-ADP-ribosyltransferase 4 precursor Ecto-ADP-ribosyltransferase 4 precursor membrane n/a n/a 3 2 2 2 1 n/a n/a n/a 3 4 1 2 n/a 4 2 n/a 2 1 Integral membrane protein n/a found at its expected molecular weight found at molecular weight

BGMUT dombrock
942 dombrock DO DO 185C,378T,624C,793G 185T>C; 378C>T; 624T>C; 793A>G F62S; Y126Y; L208L; N265D exons 1 to 3 in cDNA Do(a-b-), Hy-, Gy(a-) rare 17655578 ABL75286 Westhoff et al. Transfusion 2007 47:1356-1362 molecular modeling indicates that F62S change in the DOB protein disrupts an aromatic side chain interaction; no cell surface expression in transfected HEK 293T cells was observed. Blumenfeld OO, curator 2007-07-31 15:41:52.190 NA

UniProt Q93070
ID NAR4_HUMAN Reviewed; 314 AA.
AC Q93070; Q9BZ50; Q9BZ51; Q9HB06;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-AUG-2002, sequence version 2.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Ecto-ADP-ribosyltransferase 4;
DE EC=2.4.2.31;
DE AltName: Full=ADP-ribosyltransferase C2 and C3 toxin-like 4;
DE Short=ARTC4;
DE AltName: Full=Dombrock blood group carrier molecule;
DE AltName: Full=Mono(ADP-ribosyl)transferase 4;
DE AltName: Full=NAD(P)(+)--arginine ADP-ribosyltransferase 4;
DE AltName: CD_antigen=CD297;
DE Flags: Precursor;
GN Name=ART4; Synonyms=DO, DOK1;
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], AND VARIANT DO(B).
RX PubMed=11001920;
RA Gubin A.N., Njoroge J.M., Wojda U., Pack S.D., Rios M., Reid M.E.,
RA Miller J.L.;
RT "Identification of the Dombrock blood group glycoprotein as a
RT polymorphic member of the ADP-ribosyltransferase gene family.";
RL Blood 96:2621-2627(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS DO(B); JO(A); HY1 AND
RP HY2.
RX PubMed=11896313; DOI=10.1046/j.1537-2995.2002.00004.x;
RA Rios M., Hue-Roye K., Oyen R., Miller J., Reid M.E.;
RT "Insights into the Holley- and Joseph- phenotypes.";
RL Transfusion 42:52-58(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-108; ILE-117;
RP GLU-135; MET-189; ASP-265 AND VAL-300.
RG SeattleSNPs variation discovery resource;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-314.
RX PubMed=9119374; DOI=10.1006/geno.1996.4520;
RA Koch-Nolte F., Haag F., Braren R., Kuehl M., Hoovers J.,
RA Balasubramanian S., Bazan J.F., Thiele H.-G.;
RT "Two novel human members of an emerging mammalian gene family related
RT to mono-ADP-ribosylating bacterial toxins.";
RL Genomics 39:370-376(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-284, AND VARIANT DO(B).
RX PubMed=11520417; DOI=10.1046/j.1423-0410.2001.00052.x;
RA Wu G.-G., Jin S.-Z., Deng Z.-H., Zhao T.-M.;
RT "Polymerase chain reaction with sequence-specific primers-based
RT genotyping of the human Dombrock blood group DO1 and DO2 alleles and
RT the DO gene frequencies in Chinese blood donors.";
RL Vox Sang. 81:49-51(2001).
RN [7]
RP NOMENCLATURE.
RX PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
RA Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
RT "Toward a unified nomenclature for mammalian ADP-
RT ribosyltransferases.";
RL Trends Biochem. Sci. 35:208-219(2010).
CC -!- CATALYTIC ACTIVITY: NAD(+) + protein-L-arginine = nicotinamide +
CC N(omega)-(ADP-D-ribosyl)-protein-L-arginine.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Expressed in spleen and T-cells.
CC -!- POLYMORPHISM: DO is responsible for the Dombrock blood group
CC system. The molecular basis of the Do(a)/Do(b) blood group antigen
CC is a single variation in position 265; Asn-265 corresponds to
CC Do(a) and Asp-265 to Do(b). It is also responsible for the
CC antigens Gregory [Gy(a)], Holley [Hy] and Joseph [Jo(a)].
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase
CC family.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
CC mutation database;
CC URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system;=dombrock";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/do/";
CC -----------------------------------------------------------------------
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DR EMBL; AF290204; AAG17845.1; -; mRNA.
DR EMBL; AF382213; AAM21462.1; -; Genomic_DNA.
DR EMBL; AF382211; AAM21462.1; JOINED; Genomic_DNA.
DR EMBL; AF382212; AAM21462.1; JOINED; Genomic_DNA.
DR EMBL; AF382216; AAM21464.1; -; Genomic_DNA.
DR EMBL; AF382214; AAM21464.1; JOINED; Genomic_DNA.
DR EMBL; AF382215; AAM21464.1; JOINED; Genomic_DNA.
DR EMBL; AF382219; AAM21465.1; -; Genomic_DNA.
DR EMBL; AF382217; AAM21465.1; JOINED; Genomic_DNA.
DR EMBL; AF382218; AAM21465.1; JOINED; Genomic_DNA.
DR EMBL; AF382222; AAM21466.1; -; Genomic_DNA.
DR EMBL; AF382220; AAM21466.1; JOINED; Genomic_DNA.
DR EMBL; AF382221; AAM21466.1; JOINED; Genomic_DNA.
DR EMBL; AF382225; AAM21467.1; -; Genomic_DNA.
DR EMBL; AF382223; AAM21467.1; JOINED; Genomic_DNA.
DR EMBL; AF382224; AAM21467.1; JOINED; Genomic_DNA.
DR EMBL; AY899803; AAW65375.1; -; Genomic_DNA.
DR EMBL; BC074727; AAH74727.1; -; mRNA.
DR EMBL; X95826; CAA65095.1; -; Genomic_DNA.
DR EMBL; AF340233; AAK11274.1; -; Genomic_DNA.
DR EMBL; AF340234; AAK11275.1; -; Genomic_DNA.
DR RefSeq; NP_066549.2; NM_021071.2.
DR UniGene; Hs.591158; -.
DR UniGene; Hs.655792; -.
DR UniGene; Hs.668803; -.
DR ProteinModelPortal; Q93070; -.
DR SMR; Q93070; 55-256.
DR PhosphoSite; Q93070; -.
DR DMDM; 22261809; -.
DR PaxDb; Q93070; -.
DR PRIDE; Q93070; -.
DR Ensembl; ENST00000228936; ENSP00000228936; ENSG00000111339.
DR GeneID; 420; -.
DR KEGG; hsa:420; -.
DR UCSC; uc001rcl.1; human.
DR CTD; 420; -.
DR GeneCards; GC12M014982; -.
DR H-InvDB; HIX0036719; -.
DR HGNC; HGNC:726; ART4.
DR HPA; HPA040879; -.
DR MIM; 110600; gene+phenotype.
DR neXtProt; NX_Q93070; -.
DR PharmGKB; PA142672580; -.
DR eggNOG; NOG44842; -.
DR HOGENOM; HOG000273888; -.
DR HOVERGEN; HBG004464; -.
DR InParanoid; Q93070; -.
DR KO; K06717; -.
DR OrthoDB; EOG7D85WV; -.
DR GeneWiki; ART4; -.
DR GenomeRNAi; 420; -.
DR NextBio; 1775; -.
DR PRO; PR:Q93070; -.
DR ArrayExpress; Q93070; -.
DR Bgee; Q93070; -.
DR CleanEx; HS_ART4; -.
DR CleanEx; HS_DOK1; -.
DR Genevestigator; Q93070; -.
DR GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003956; F:NAD(P)+-protein-arginine ADP-ribosyltransferase activity; NAS:UniProtKB.
DR GO; GO:0006525; P:arginine metabolic process; NAS:UniProtKB.
DR GO; GO:0006471; P:protein ADP-ribosylation; NAS:UniProtKB.
DR InterPro; IPR000768; ART.
DR PANTHER; PTHR10339; PTHR10339; 1.
DR Pfam; PF01129; ART; 1.
DR PRINTS; PR00970; RIBTRNSFRASE.
DR PROSITE; PS01291; ART; 1.
PE 2: Evidence at transcript level;
KW Blood group antigen; Cell membrane; Complete proteome; Disulfide bond;
KW Glycoprotein; Glycosyltransferase; GPI-anchor; Lipoprotein; Membrane;
KW NAD; NADP; Polymorphism; Reference proteome; Signal; Transferase.
FT SIGNAL 1 46 Potential.
FT CHAIN 47 285 Ecto-ADP-ribosyltransferase 4.
FT /FTId=PRO_0000019329.
FT PROPEP 286 314 Removed in mature form (Potential).
FT /FTId=PRO_0000019330.
FT ACT_SITE 251 251 By similarity.
FT BINDING 126 126 NAD (By similarity).
FT BINDING 206 206 NAD (By similarity).
FT BINDING 240 240 NAD (By similarity).
FT LIPID 285 285 GPI-anchor amidated alanine (Potential).
FT CARBOHYD 114 114 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 178 178 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 222 222 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 257 257 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 274 274 N-linked (GlcNAc...) (Potential).
FT DISULFID 69 280 By similarity.
FT DISULFID 182 231 By similarity.
FT VARIANT 108 108 G -> V (in Hy1 and Hy2;
FT dbSNP:rs28362797).
FT /FTId=VAR_013707.
FT VARIANT 117 117 T -> I (in Jo(a); dbSNP:rs28362798).
FT /FTId=VAR_013708.
FT VARIANT 135 135 D -> E (in dbSNP:rs28362799).
FT /FTId=VAR_022266.
FT VARIANT 189 189 T -> M (in dbSNP:rs28362800).
FT /FTId=VAR_022267.
FT VARIANT 265 265 N -> D (in Do(b), Hy1 and Hy2;
FT dbSNP:rs11276).
FT /FTId=VAR_013709.
FT VARIANT 300 300 L -> V (in Hy1; dbSNP:rs3088190).
FT /FTId=VAR_013710.
FT CONFLICT 48 48 E -> Q (in Ref. 5; CAA65095).
FT CONFLICT 116 116 T -> S (in Ref. 5; CAA65095).
SQ SEQUENCE 314 AA; 35878 MW; 174913890C9D158F CRC64;
MGPLINRCKK ILLPTTVPPA TMRIWLLGGL LPFLLLLSGL QRPTEGSEVA IKIDFDFAPG
SFDDQYQGCS KQVMEKLTQG DYFTKDIEAQ KNYFRMWQKA HLAWLNQGKV LPQNMTTTHA
VAILFYTLNS NVHSDFTRAM ASVARTPQQY ERSFHFKYLH YYLTSAIQLL RKDSIMENGT
LCYEVHYRTK DVHFNAYTGA TIRFGQFLST SLLKEEAQEF GNQTLFTIFT CLGAPVQYFS
LKKEVLIPPY ELFKVINMSY HPRGNWLQLR STGNLSTYNC QLLKASSKKC IPDPIAIASL
SFLTSVIIFS KSRV
//

MIM 110600
*RECORD*
*FIELD* NO
110600
*FIELD* TI
+110600 ADP-RIBOSYLTRANSFERASE 4; ART4
BLOOD GROUP--DOMBROCK SYSTEM, INCLUDED; DO, INCLUDED;;
read moreDOMBROCK BLOOD GROUP, INCLUDED;;
DOK1, INCLUDED;;
DOMBROCK-NULL PHENOTYPE, INCLUDED
*FIELD* TX

CLONING

Mono-ADP-ribosylation is a posttranslational protein modification that
involves the transfer of the ADP-ribose moiety from NAD+ to a specific
amino acid in the target protein. This modification helps regulate
cellular metabolism in prokaryotes and is the mechanism by which some
bacterial toxins function. The rodent T-cell alloantigen RT6 has
structural homology to prokaryotic ADP-ribosylation proteins and
possesses mono-ADP-ribosyltransferase enzyme activity. By searching an
EST database with the deduced protein sequences of ART1 (601625) and
ART2P (see ART1), both of which are homologous to RT6, Koch-Nolte et al.
(1997) identified human cDNAs encoding ART3 (603086) and ART4. They
isolated the corresponding genes from P1 and PAC1 genomic clones by PCR
using EST-derived primers. Southern blot analysis demonstrated that
human ART4 is a single-copy gene which has homologs in other primates
and in mouse. Northern blot analysis detected prominent ART4 transcripts
of 1.4 kb, 2.4 kb, and 5.5 kb only in spleen, or T-cell, RNA. The
predicted ART3 and ART4 proteins contain structural motifs similar to
those in ADP-ribosylating toxins, and hydrophobic N-terminal and
C-terminal signal peptides characteristic of
glycosylphosphatidylinositol (GPI)-anchored cell membrane proteins;
unlike ART3, ART4 does not contain a repeated motif at the C terminus.
Koch-Nolte et al. (1997) reported that ART1 is the closest known family
member of ART4, with 39% amino acid sequence identity.

Gubin et al. (2000) provided the first molecular description of the
Dombrock blood group system. A candidate gene was identified by in
silico analyses of approximately 5,000 ESTs from terminally
differentiating human erythroid cells. Transfection experiments
demonstrated specific binding of anti-Dombrock and confirmed
glycosylphosphatidylinositol membrane attachment. Dombrock expression is
developmentally regulated during erythroid differentiation and occurs at
highest levels in fetal liver. Homology studies suggested that the
Dombrock molecule is a member of the adenosine 5-prime-diphosphate
(ADP)-ribosyltransferase ectoenzyme gene family. The ART4 gene encodes a
predicted 314-amino acid polypeptide containing an
arginine-glycine-aspartic acid (RGD) motif (DO*B allele product only),
commonly involved in cell-to-cell interactions involving integrin
binding and the GPI anchor motif. Gubin et al. (2000) stated that
although the identity of DO to ART4 had been established, enzymatic
activity has not been demonstrated in any cell type, including erythroid
cells.

POPULATION GENETICS

About 64% of northern Europeans are DO(a+) (Swanson et al., 1965).

GENE STRUCTURE

A comparison of the genomic and cDNA sequences of ART4 by Koch-Nolte et
al. (1997) revealed a conserved exon/intron structure, with an unusually
large exon encoding the mature protein.

The ART4 gene contains 3 exons spanning 14 kb (Gubin et al., 2000).

MAPPING

Lewis et al. (1983) reported evidence of linkage of DO and PGD (172200)
on chromosome 1, but data presented by Mohr et al. (1985) appeared to
negate this assignment of DO. In a linkage study of 832 families from
the Copenhagen region, Eiberg and Mohr (1996) found a strong indication
of tight linkage of DO with 2 flanking DNA polymorphisms, D12S358 and
D12S364. They thus assigned the DO locus to 12p13.2-p12.1.

By PCR screening of human/rodent somatic cell hybrids and by in situ
hybridization, Koch-Nolte et al. (1997) mapped the ART4 gene to
12p13.1-p12.2.

MOLECULAR GENETICS

Genotypic comparisons performed by Gubin et al. (2000) suggested that
Do(a) versus Do(b) antigenicity results from a single amino acid
substitution within an encoded RGD motif of the DO molecule; see
110600.0001.

The antithetical Dombrock antigens Do(a)/Do(b) also carry 3
high-incidence antigens: Gregory, Gy(a); Holley, Hy; and Joseph, Jo(a)
(Lucien et al., 2002). The Holley polymorphisms derive from a DO*B
background. The rare Dombrock-null phenotype, in which the RBCs lack all
5 antigens, may arise from a single nucleotide mutation in the acceptor
splice site of intron 1, causing the skipping of exon 2 (110600.0002)
(Rios et al., 2001) or from the absence of GPI-anchored proteins on RBCs
from patients with paroxysmal nocturnal hemoglobinemia (PNH; 300818). In
all cases, negative and null phenotypes can develop anti-Dombrock
antibodies that may cause severe hemolytic transfusion reactions
(Halverson et al., 1994; Strupp et al., 1998).

Rios et al. (2002) studied 2 probands in whom RBCs with the
Dombrock-null phenotype lacked all antigens in the Dombrock blood group
system. Sequence analysis of DNA from 1 proband with the Dombrock null
phenotype revealed a T-to-C mutation (110600.0004) with outsplicing of
exon 2. The second proband was homozygous for a 442C-T mutation
(110600.0005) in exon 2.

Lucien et al. (2002) identified an 8-bp deletion (110600.0003) in the
ART4 gene in a woman with the DO-null phenotype.

Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).

Telen (1996) reviewed erythrocyte blood group antigens that represent
polymorphisms of functionally important molecules.

HISTORY

The Dombrock blood group was named for a transfused patient, Mrs.
Dombrock, in whom anti-Do(a) was detected.

*FIELD* AV
.0001
DOMBROCK BLOOD GROUP
ART4, ASN265ASP

Gubin et al. (2000) studied 8 blood donors of defined serology, i.e., 4
Do(a+b-) and 4 Do(a-b+), and determined the sequence of the coding
region of DO. Three SNP sites were identified. While 2 SNPs did not
alter the predicted amino acid primary structure, the third predicted a
mutation in the protein sequence, asn265 to asp (N265D). This SNP fell
within an RGD adhesion motif of the molecule.

.0002
DOMBROCK-NULL PHENOTYPE
ART4, IVS1AS, A-G, -2

Rios et al. (2001) identified an A-to-G mutation in the 3-prime splice
site of intron 1 of the ART4 gene in 3 probands with the Dombrock-null
phenotype.

.0003
DOMBROCK-NULL PHENOTYPE
ART4, 8-BP DEL, NT343

Lucien et al. (2002) identified a novel alteration of the blood group
DO*A allele in a female DO-null donor from Reunion Island with
allo-anti-DO3 in her serum; her parents were consanguineous. The only
deviation from the wildtype DO*A allele sequence was an 8-bp
(nucleotides 343-350) deletion within exon 2. This short deletion
generated a premature stop codon and encoded a truncated protein lacking
the predicted functional motif of the ADP-ribosyltransferase enzyme and
the glycosylphosphatidylinositol anchor motif essential for RBC membrane
attachment. An allele-specific PCR to detect the DO(del8) deletion was
developed.

.0004
DOMBROCK-NULL PHENOTYPE
ART4, IVS1DS, T-C, +2

Rios et al. (2002) described the Dombrock null phenotype in a proband
with a T-to-C substitution in the donor splice site of the ART4 gene,
resulting in outsplicing of exon 2.

.0005
DOMBROCK-NULL PHENOTYPE
ART4, GLN148TER

In a proband with the Dombrock-null phenotype, Rios et al. (2002) found
homozygosity for a 442C-T mutation in exon 2 of the ART4 gene, resulting
in a premature stop codon, gln148 to ter (Q148X).

*FIELD* SA
Bailly et al. (2001); Lewis et al. (1978); Molthan et al. (1973);
Polesky and Swanson (1966); Williams and Crawford (1966)
*FIELD* RF
1. Bailly, P.; Lucien, N.; Celton, J. L.; Le Pennec, P. Y.; Cartron,
J. P.: A short deletion within the blood group Dombrock locus causing
a Do(null) phenotype. (Abstract) Transfusion Clinique et Biologique 8:
167s only, 2001.

2. Eiberg, H.; Mohr, J.: Dombrock blood group (DO): assignment to
chromosome 12p. Hum. Genet. 98: 518-521, 1996.

3. Gubin, A. N.; Njoroge, J. M.; Wojda, U.; Pack, S. D.; Rios, M.;
Reid, M. E.; Miller, J. L.: Identification of the Dombrock blood
group glycoprotein as a polymorphic member of the ADP-ribosyltransferase
gene family. Blood 96: 2621-2627, 2000.

4. Halverson, G.; Shanahan, E.; Santiago, I.; Mabile, R.; Thurrell,
T.; Strupp, A. M.; Wolf, C. F. W.; Spruell, P.; Moulds, M. K.: The
first reported case of anti-Dob causing an acute hemolytic transfusion
reaction. Vox Sang. 66: 206-209, 1994.

5. Koch-Nolte, F.; Haag, F.; Braren, R.; Kuhl, M.; Hoovers, J.; Balasubramanian,
S.; Bazan, F.; Thiele, H.-G.: Two novel human members of an emerging
mammalian gene family related to mono-ADP-ribosylating bacterial toxins. Genomics 39:
370-376, 1997. Note: Erratum: Genomics 55: 130 only, 1999.

6. Lewis, M.; Kaita, H.; Giblett, E. R.; Anderson, J. E.: Genetic
linkage analysis of the Dombrock (Do) blood group locus. Cytogenet.
Cell Genet. 22: 313-318, 1978.

7. Lewis, M.; Kaita, H.; Philipps, S.; Giblett, E. R.; Anderson, J.
E.: Genetic linkage data for the Dombrock blood group locus relative
to chromosome 1 and chromosome 4 loci. Ann. Hum. Genet. 47: 49-53,
1983.

8. Lucien, N.; Celton, J.-L.; Le Pennec, P.-Y.; Cartron, J.-P.; Bailly,
P.: Short deletion within the blood group Dombrock locus causing
a Do(null) phenotype. Blood 100: 1063-1064, 2002.

9. Mohr, J.; Eiberg, H.; Nielsen, L. S.: Various linkage relationships
of the Dombrock blood group system. (Abstract) Cytogenet. Cell Genet. 40:
701 only, 1985.

10. Molthan, L.; Crawford, M. N.; Tippett, P.: Enlargement of the
Dombrock blood group system: the finding of anti-Do(b). Vox Sang. 24:
382-384, 1973.

11. Polesky, H. F.; Swanson, J. L.: Studies on distribution of the
blood group antigen Do(a) (Dombrock) and the characteristics of anti-Do(a). Transfusion 6:
268-270, 1966.

12. Rios, M.; Hue-Roye, K.; Lee, A. H.; Chiofolo, J. T.; Miller, J.
L.; Reid, M. E.: DNA analysis for the Dombrock polymorphism. Transfusion 41:
1143-1146, 2001.

13. Rios, M.; Hue-Roye, K.; Storry, J. R.; Lee, T.; Miller, J. L.;
Reid, M. E.: Molecular basis of the Dombrock null phenotype. Transfusion 41:
1405-1407, 2001.

14. Rios, M.; Storry, J. R.; Hue-Roye, K.; Chung, A.; Reid, M. E.
: Two new molecular bases for the Dombrock null phenotype. Brit.
J. Haemat. 117: 765-767, 2002.

15. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World
Distribution. New York: Oxford Univ. Press (pub.) 1988.

16. Strupp, A.; Cash, K.; Uehlinger, J.: Difficulties in identifying
antibodies in the Dombrock blood group system in multiply alloimmunized
patients. Transfusion 38: 1022-1025, 1998.

17. Swanson, J. L.; Polesky, H. F.; Tippett, P.; Sanger, R.: A 'new'
blood group antigen, Do(a). Nature 206: 313 only, 1965.

18. Telen, M. J.: Erythrocyte blood group antigens: polymorphisms
of functionally important molecules. Semin. Hemat. 33: 302-314,
1996.

19. Williams, C. H.; Crawford, M. N.: The third example of anti-Do. Transfusion 6:
310 only, 1966.

*FIELD* CN
Victor A. McKusick - updated: 12/22/2005
Victor A. McKusick - updated: 4/11/2003
Victor A. McKusick - updated: 3/4/2003
Victor A. McKusick - updated: 1/9/2001
Victor A. McKusick - updated: 4/25/1998

*FIELD* CD
Victor A. McKusick: 6/4/1986

*FIELD* ED
carol: 07/27/2012
mgross: 7/1/2010
carol: 12/23/2005
terry: 12/22/2005
carol: 3/17/2004
terry: 7/31/2003
carol: 4/11/2003
tkritzer: 4/11/2003
carol: 4/11/2003
carol: 4/10/2003
cwells: 3/7/2003
terry: 3/4/2003
carol: 5/25/2001
mcapotos: 1/22/2001
mcapotos: 1/16/2001
terry: 1/9/2001
carol: 5/1/1998
terry: 4/25/1998
jamie: 1/15/1997
terry: 1/10/1997
mimadm: 2/11/1994
supermim: 3/16/1992
carol: 2/28/1992
carol: 2/26/1992
supermim: 3/20/1990
ddp: 10/26/1989