Full text data of RPL27
RPL27
[Confidence: low (only semi-automatic identification from reviews)]
60S ribosomal protein L27
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L27
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P61353
ID RL27_HUMAN Reviewed; 136 AA.
AC P61353; P08526; Q4G0A9;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=60S ribosomal protein L27;
GN Name=RPL27;
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].
RC TISSUE=Kidney;
RX PubMed=8148381; DOI=10.1016/0167-4781(94)90295-X;
RA Gallagher R.A., McClean P.M., Malik A.N.;
RT "Cloning and nucleotide sequence of a full length cDNA encoding
RT ribosomal protein L27 from human fetal kidney.";
RL Biochim. Biophys. Acta 1217:329-332(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative
RT analysis of 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bhat K.S.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, Brain, Eye, and Skin;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-93, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- SIMILARITY: Belongs to the ribosomal protein L27e family.
CC -!- SIMILARITY: Contains 1 KOW domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L19527; AAA19815.1; -; mRNA.
DR EMBL; AB061851; BAB79492.1; -; Genomic_DNA.
DR EMBL; L05094; AAC15857.1; -; mRNA.
DR EMBL; BC001700; AAH01700.1; -; mRNA.
DR EMBL; BC002588; AAH02588.1; -; mRNA.
DR EMBL; BC007273; AAH07273.1; -; mRNA.
DR EMBL; BC010026; AAH10026.1; -; mRNA.
DR EMBL; BC098560; AAH98560.1; -; mRNA.
DR PIR; S43505; S43505.
DR RefSeq; NP_000979.1; NM_000988.3.
DR UniGene; Hs.514196; -.
DR UniGene; Hs.660076; -.
DR PDB; 3J3B; EM; 5.00 A; Z=1-136.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P61353; -.
DR SMR; P61353; 2-136.
DR IntAct; P61353; 14.
DR MINT; MINT-1145695; -.
DR STRING; 9606.ENSP00000253788; -.
DR PhosphoSite; P61353; -.
DR DMDM; 47117772; -.
DR SWISS-2DPAGE; P61353; -.
DR PaxDb; P61353; -.
DR PRIDE; P61353; -.
DR DNASU; 6155; -.
DR Ensembl; ENST00000253788; ENSP00000253788; ENSG00000131469.
DR Ensembl; ENST00000589037; ENSP00000467587; ENSG00000131469.
DR Ensembl; ENST00000589913; ENSP00000464813; ENSG00000131469.
DR GeneID; 6155; -.
DR KEGG; hsa:6155; -.
DR UCSC; uc002icj.3; human.
DR CTD; 6155; -.
DR GeneCards; GC17P041150; -.
DR HGNC; HGNC:10328; RPL27.
DR HPA; HPA002649; -.
DR MIM; 607526; gene.
DR neXtProt; NX_P61353; -.
DR PharmGKB; PA34707; -.
DR eggNOG; COG2163; -.
DR HOGENOM; HOG000210138; -.
DR HOVERGEN; HBG050005; -.
DR InParanoid; P61353; -.
DR KO; K02901; -.
DR OMA; KIYKPGK; -.
DR OrthoDB; EOG7J181Z; -.
DR PhylomeDB; P61353; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; RPL27; human.
DR GeneWiki; RPL27; -.
DR GenomeRNAi; 6155; -.
DR NextBio; 23903; -.
DR PRO; PR:P61353; -.
DR ArrayExpress; P61353; -.
DR Bgee; P61353; -.
DR CleanEx; HS_RPL27; -.
DR Genevestigator; P61353; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR001141; Ribosomal_L27e.
DR InterPro; IPR018262; Ribosomal_L27e_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like.
DR PANTHER; PTHR10497; PTHR10497; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF01777; Ribosomal_L27e; 1.
DR ProDom; PD009396; Ribosomal_L27e; 1.
DR SMART; SM00739; KOW; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR PROSITE; PS01107; RIBOSOMAL_L27E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 136 60S ribosomal protein L27.
FT /FTId=PRO_0000126077.
FT DOMAIN 5 40 KOW.
FT MOD_RES 27 27 N6-acetyllysine.
FT MOD_RES 93 93 N6-acetyllysine.
SQ SEQUENCE 136 AA; 15798 MW; 73F4151495029A32 CRC64;
MGKFMKPGKV VLVLAGRYSG RKAVIVKNID DGTSDRPYSH ALVAGIDRYP RKVTAAMGKK
KIAKRSKIKS FVKVYNYNHL MPTRYSVDIP LDKTVVNKDV FRDPALKRKA RREAKVKFEE
RYKTGKNKWF FQKLRF
//
ID RL27_HUMAN Reviewed; 136 AA.
AC P61353; P08526; Q4G0A9;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=60S ribosomal protein L27;
GN Name=RPL27;
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].
RC TISSUE=Kidney;
RX PubMed=8148381; DOI=10.1016/0167-4781(94)90295-X;
RA Gallagher R.A., McClean P.M., Malik A.N.;
RT "Cloning and nucleotide sequence of a full length cDNA encoding
RT ribosomal protein L27 from human fetal kidney.";
RL Biochim. Biophys. Acta 1217:329-332(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative
RT analysis of 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bhat K.S.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, Brain, Eye, and Skin;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-93, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- SIMILARITY: Belongs to the ribosomal protein L27e family.
CC -!- SIMILARITY: Contains 1 KOW domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L19527; AAA19815.1; -; mRNA.
DR EMBL; AB061851; BAB79492.1; -; Genomic_DNA.
DR EMBL; L05094; AAC15857.1; -; mRNA.
DR EMBL; BC001700; AAH01700.1; -; mRNA.
DR EMBL; BC002588; AAH02588.1; -; mRNA.
DR EMBL; BC007273; AAH07273.1; -; mRNA.
DR EMBL; BC010026; AAH10026.1; -; mRNA.
DR EMBL; BC098560; AAH98560.1; -; mRNA.
DR PIR; S43505; S43505.
DR RefSeq; NP_000979.1; NM_000988.3.
DR UniGene; Hs.514196; -.
DR UniGene; Hs.660076; -.
DR PDB; 3J3B; EM; 5.00 A; Z=1-136.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P61353; -.
DR SMR; P61353; 2-136.
DR IntAct; P61353; 14.
DR MINT; MINT-1145695; -.
DR STRING; 9606.ENSP00000253788; -.
DR PhosphoSite; P61353; -.
DR DMDM; 47117772; -.
DR SWISS-2DPAGE; P61353; -.
DR PaxDb; P61353; -.
DR PRIDE; P61353; -.
DR DNASU; 6155; -.
DR Ensembl; ENST00000253788; ENSP00000253788; ENSG00000131469.
DR Ensembl; ENST00000589037; ENSP00000467587; ENSG00000131469.
DR Ensembl; ENST00000589913; ENSP00000464813; ENSG00000131469.
DR GeneID; 6155; -.
DR KEGG; hsa:6155; -.
DR UCSC; uc002icj.3; human.
DR CTD; 6155; -.
DR GeneCards; GC17P041150; -.
DR HGNC; HGNC:10328; RPL27.
DR HPA; HPA002649; -.
DR MIM; 607526; gene.
DR neXtProt; NX_P61353; -.
DR PharmGKB; PA34707; -.
DR eggNOG; COG2163; -.
DR HOGENOM; HOG000210138; -.
DR HOVERGEN; HBG050005; -.
DR InParanoid; P61353; -.
DR KO; K02901; -.
DR OMA; KIYKPGK; -.
DR OrthoDB; EOG7J181Z; -.
DR PhylomeDB; P61353; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; RPL27; human.
DR GeneWiki; RPL27; -.
DR GenomeRNAi; 6155; -.
DR NextBio; 23903; -.
DR PRO; PR:P61353; -.
DR ArrayExpress; P61353; -.
DR Bgee; P61353; -.
DR CleanEx; HS_RPL27; -.
DR Genevestigator; P61353; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR001141; Ribosomal_L27e.
DR InterPro; IPR018262; Ribosomal_L27e_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like.
DR PANTHER; PTHR10497; PTHR10497; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF01777; Ribosomal_L27e; 1.
DR ProDom; PD009396; Ribosomal_L27e; 1.
DR SMART; SM00739; KOW; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR PROSITE; PS01107; RIBOSOMAL_L27E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 136 60S ribosomal protein L27.
FT /FTId=PRO_0000126077.
FT DOMAIN 5 40 KOW.
FT MOD_RES 27 27 N6-acetyllysine.
FT MOD_RES 93 93 N6-acetyllysine.
SQ SEQUENCE 136 AA; 15798 MW; 73F4151495029A32 CRC64;
MGKFMKPGKV VLVLAGRYSG RKAVIVKNID DGTSDRPYSH ALVAGIDRYP RKVTAAMGKK
KIAKRSKIKS FVKVYNYNHL MPTRYSVDIP LDKTVVNKDV FRDPALKRKA RREAKVKFEE
RYKTGKNKWF FQKLRF
//
MIM
607526
*RECORD*
*FIELD* NO
607526
*FIELD* TI
*607526 RIBOSOMAL PROTEIN L27; RPL27
*FIELD* TX
CLONING
By differential screening of fetal and adult kidney mRNA, Gallagher et
read moreal. (1994) cloned RPL27 as 1 of several transcripts showing high
expression during fetal development. The deduced 135-amino acid protein
has a calculated molecular mass of about 18 kD. RPL27 shares 100% amino
acid identity with rat and chicken Rpl27, although there are several
silent base pair changes at the DNA level. Northern blot analysis
revealed expression of a 1.0-kb transcript or 2 transcripts of 1.0 and
1.25 kb in fetal kidney. The 1.0-kb transcript was present at lower
levels in adult kidney. RPL27 expression was also detected in several
other fetal tissues, including muscle, liver, lung, heart, and brain.
The 1.0-kb transcript was present in adult muscle at lower levels than
in fetal muscle. Gallagher et al. (1994) determined that RPL27 was
downregulated 20-fold in adult kidney compared with fetal kidney.
GENE FUNCTION
Using RT-PCR, Sim et al. (2010) found that a subset of genes encoding
proteins of the large ribosomal subunit was differentially expressed in
nasopharyngeal carcinoma (see 607107) cell lines compared with a normal
nasopharyngeal epithelial cell line. RPL27 was 1 of 3 genes
significantly downregulated in the carcinoma cell lines.
MAPPING
By Southern blot analysis, Gallagher et al. (1994) determined that there
are multiple RPL27 copies in the genome. The International Radiation
Hybrid Mapping Consortium mapped the RPL27 gene to chromosome 17 (TMAP
RH26918).
*FIELD* RF
1. Gallagher, R. A.; McClean, P. M.; Malik, A. N.: Cloning and nucleotide
sequence of a full length cDNA encoding ribosomal protein L27 from
human fetal kidney. Biochim. Biophys. Acta 1217: 329-332, 1994.
2. Sim, E. U. H.; Ang, C. H.; Ng, C. C.; Lee, C. W.; Narayanan, K.
: Differential expression of a subset of ribosomal protein genes in
cell lines derived from human nasopharyngeal epithelium. J. Hum.
Genet. 55: 118-120, 2010.
*FIELD* CN
Patricia A. Hartz - updated: 3/22/2010
*FIELD* CD
Patricia A. Hartz: 1/29/2003
*FIELD* ED
mgross: 03/23/2010
mgross: 3/22/2010
mgross: 1/29/2003
*RECORD*
*FIELD* NO
607526
*FIELD* TI
*607526 RIBOSOMAL PROTEIN L27; RPL27
*FIELD* TX
CLONING
By differential screening of fetal and adult kidney mRNA, Gallagher et
read moreal. (1994) cloned RPL27 as 1 of several transcripts showing high
expression during fetal development. The deduced 135-amino acid protein
has a calculated molecular mass of about 18 kD. RPL27 shares 100% amino
acid identity with rat and chicken Rpl27, although there are several
silent base pair changes at the DNA level. Northern blot analysis
revealed expression of a 1.0-kb transcript or 2 transcripts of 1.0 and
1.25 kb in fetal kidney. The 1.0-kb transcript was present at lower
levels in adult kidney. RPL27 expression was also detected in several
other fetal tissues, including muscle, liver, lung, heart, and brain.
The 1.0-kb transcript was present in adult muscle at lower levels than
in fetal muscle. Gallagher et al. (1994) determined that RPL27 was
downregulated 20-fold in adult kidney compared with fetal kidney.
GENE FUNCTION
Using RT-PCR, Sim et al. (2010) found that a subset of genes encoding
proteins of the large ribosomal subunit was differentially expressed in
nasopharyngeal carcinoma (see 607107) cell lines compared with a normal
nasopharyngeal epithelial cell line. RPL27 was 1 of 3 genes
significantly downregulated in the carcinoma cell lines.
MAPPING
By Southern blot analysis, Gallagher et al. (1994) determined that there
are multiple RPL27 copies in the genome. The International Radiation
Hybrid Mapping Consortium mapped the RPL27 gene to chromosome 17 (TMAP
RH26918).
*FIELD* RF
1. Gallagher, R. A.; McClean, P. M.; Malik, A. N.: Cloning and nucleotide
sequence of a full length cDNA encoding ribosomal protein L27 from
human fetal kidney. Biochim. Biophys. Acta 1217: 329-332, 1994.
2. Sim, E. U. H.; Ang, C. H.; Ng, C. C.; Lee, C. W.; Narayanan, K.
: Differential expression of a subset of ribosomal protein genes in
cell lines derived from human nasopharyngeal epithelium. J. Hum.
Genet. 55: 118-120, 2010.
*FIELD* CN
Patricia A. Hartz - updated: 3/22/2010
*FIELD* CD
Patricia A. Hartz: 1/29/2003
*FIELD* ED
mgross: 03/23/2010
mgross: 3/22/2010
mgross: 1/29/2003