Full text data of SRP19
SRP19
[Confidence: low (only semi-automatic identification from reviews)]
Signal recognition particle 19 kDa protein; SRP19
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Signal recognition particle 19 kDa protein; SRP19
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P09132
ID SRP19_HUMAN Reviewed; 144 AA.
AC P09132; B2R4E9; D6RCQ5; Q05D77; Q96FG6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Signal recognition particle 19 kDa protein;
DE Short=SRP19;
GN Name=SRP19;
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), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2460823; DOI=10.1093/nar/16.20.9431;
RA Lingelbach K., Zwieb C., Webb J.R., Marshallsaz C., Hoben P.,
RA Walter P., Dobberstein B.;
RT "Isolation and characterization of a cDNA clone encoding the 19 kDa
RT protein of signal recognition particle (SRP): expression and binding
RT to 7SL RNA.";
RL Nucleic Acids Res. 16:9431-9442(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Erythroblast;
RA Gubin A.N., Lee Y.T., Bouffard G.G., Miller J.L.;
RT "Gene expression in human erythroid precursor cells.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP THR-4.
RC TISSUE=Brain, 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-128.
RX PubMed=11641499; DOI=10.1126/science.1063839;
RA Wild K., Sinning I., Cusack S.;
RT "Crystal structure of an early protein-RNA assembly complex of the
RT signal recognition particle.";
RL Science 294:598-601(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 14-120 IN COMPLEX WITH SRP54
RP AND 7SL RNA.
RX PubMed=12244299; DOI=10.1038/nsb843;
RA Kuglstatter A., Oubridge C., Nagai K.;
RT "Induced structural changes of 7SL RNA during the assembly of human
RT signal recognition particle.";
RL Nat. Struct. Biol. 9:740-744(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 1-120 IN COMPLEX WITH 7SL
RP RNA.
RX PubMed=20179341; DOI=10.1107/S0907444910000879;
RA Wild K., Bange G., Bozkurt G., Segnitz B., Hendricks A., Sinning I.;
RT "Structural insights into the assembly of the human and archaeal
RT signal recognition particles.";
RL Acta Crystallogr. D 66:295-303(2010).
CC -!- FUNCTION: Signal-recognition-particle assembly, binds directly to
CC 7S RNA and mediates binding of the 54 kDa subunit of the SRP.
CC -!- SUBUNIT: Signal recognition particle consists of a 7S RNA molecule
CC of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54,
CC SRP19, SRP14 and SRP9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P09132-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09132-2; Sequence=VSP_042540;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P09132-3; Sequence=VSP_044524;
CC -!- SIMILARITY: Belongs to the SRP19 family.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Signal recognition particle
CC entry;
CC URL="http://en.wikipedia.org/wiki/Signal-recognition_particle";
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DR EMBL; X12791; CAA31280.1; -; mRNA.
DR EMBL; BU661702; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK311803; BAG34746.1; -; mRNA.
DR EMBL; AC008536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471086; EAW48999.1; -; Genomic_DNA.
DR EMBL; CH471086; EAW49000.1; -; Genomic_DNA.
DR EMBL; BC010947; AAH10947.1; -; mRNA.
DR EMBL; BC017830; AAH17830.1; -; mRNA.
DR PIR; S01700; S01700.
DR RefSeq; NP_001191122.1; NM_001204193.1.
DR RefSeq; NP_001191123.1; NM_001204194.1.
DR RefSeq; NP_001191125.1; NM_001204196.1.
DR RefSeq; NP_003126.1; NM_003135.2.
DR UniGene; Hs.637001; -.
DR PDB; 1JID; X-ray; 1.80 A; A=1-120.
DR PDB; 1MFQ; X-ray; 3.10 A; B=14-120.
DR PDB; 1RY1; EM; 12.00 A; B=14-120.
DR PDB; 2J37; EM; 8.00 A; B=14-120.
DR PDB; 3KTV; X-ray; 3.80 A; B/D=1-120.
DR PDBsum; 1JID; -.
DR PDBsum; 1MFQ; -.
DR PDBsum; 1RY1; -.
DR PDBsum; 2J37; -.
DR PDBsum; 3KTV; -.
DR DisProt; DP00570; -.
DR ProteinModelPortal; P09132; -.
DR SMR; P09132; 5-118.
DR IntAct; P09132; 6.
DR MINT; MINT-247583; -.
DR STRING; 9606.ENSP00000282999; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR PhosphoSite; P09132; -.
DR DMDM; 115502457; -.
DR PaxDb; P09132; -.
DR PRIDE; P09132; -.
DR Ensembl; ENST00000282999; ENSP00000282999; ENSG00000153037.
DR Ensembl; ENST00000505459; ENSP00000424870; ENSG00000153037.
DR Ensembl; ENST00000515463; ENSP00000425562; ENSG00000153037.
DR GeneID; 6728; -.
DR KEGG; hsa:6728; -.
DR UCSC; uc003kqc.3; human.
DR CTD; 6728; -.
DR GeneCards; GC05P112196; -.
DR HGNC; HGNC:11300; SRP19.
DR HPA; HPA029272; -.
DR MIM; 182175; gene.
DR neXtProt; NX_P09132; -.
DR PharmGKB; PA36124; -.
DR eggNOG; NOG265516; -.
DR HOGENOM; HOG000237221; -.
DR HOVERGEN; HBG059463; -.
DR InParanoid; P09132; -.
DR KO; K03105; -.
DR OMA; YVAEMIP; -.
DR OrthoDB; EOG72G199; -.
DR PhylomeDB; P09132; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; SRP19; human.
DR EvolutionaryTrace; P09132; -.
DR GenomeRNAi; 6728; -.
DR NextBio; 26244; -.
DR PRO; PR:P09132; -.
DR ArrayExpress; P09132; -.
DR Bgee; P09132; -.
DR CleanEx; HS_SRP19; -.
DR Genevestigator; P09132; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:UniProtKB.
DR GO; GO:0008312; F:7S RNA binding; IDA:UniProtKB.
DR GO; GO:0042493; P:response to drug; IDA:UniProtKB.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
DR Gene3D; 3.30.56.30; -; 1.
DR InterPro; IPR002778; Signal_recog_particle_SRP19.
DR PANTHER; PTHR17453; PTHR17453; 1.
DR Pfam; PF01922; SRP19; 1.
DR SUPFAM; SSF69695; SSF69695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Polymorphism;
KW Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 144 Signal recognition particle 19 kDa
FT protein.
FT /FTId=PRO_0000135197.
FT REGION 136 144 Basic region, potentially involved in
FT RNA-binding.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 15 144 FICIYPAYLNNKKTIAEGRRIPISKAVENPTATEIQDVCSA
FT VGLNVFLEKNKMYSREWNRDVQYRGRVRVQLKQEDGSLCLV
FT QFPSRKSVMLYAAEMIPKLKTRTQKTGGADQSLQQGEGSKK
FT GKGKKKK -> LLKILQLQRFKMYVQQLDLTYFLRKIKCTL
FT ENGIVMSNTEAESGSSSNRKMGASALYSSHHVSQ (in
FT isoform 3).
FT /FTId=VSP_044524.
FT VAR_SEQ 101 144 RKSVMLYAAEMIPKLKTRTQKTGGADQSLQQGEGSKKGKGK
FT KKK -> HYTLSLTSGS (in isoform 2).
FT /FTId=VSP_042540.
FT VARIANT 4 4 A -> T (in dbSNP:rs17855423).
FT /FTId=VAR_027800.
FT HELIX 12 14
FT STRAND 15 18
FT HELIX 20 23
FT TURN 29 32
FT TURN 37 39
FT STRAND 41 43
FT HELIX 46 55
FT STRAND 60 63
FT HELIX 76 78
FT STRAND 81 84
FT STRAND 93 95
FT HELIX 101 111
FT HELIX 112 114
FT HELIX 116 119
SQ SEQUENCE 144 AA; 16156 MW; E25F661972338CAE CRC64;
MACAAARSPA DQDRFICIYP AYLNNKKTIA EGRRIPISKA VENPTATEIQ DVCSAVGLNV
FLEKNKMYSR EWNRDVQYRG RVRVQLKQED GSLCLVQFPS RKSVMLYAAE MIPKLKTRTQ
KTGGADQSLQ QGEGSKKGKG KKKK
//
ID SRP19_HUMAN Reviewed; 144 AA.
AC P09132; B2R4E9; D6RCQ5; Q05D77; Q96FG6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Signal recognition particle 19 kDa protein;
DE Short=SRP19;
GN Name=SRP19;
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), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2460823; DOI=10.1093/nar/16.20.9431;
RA Lingelbach K., Zwieb C., Webb J.R., Marshallsaz C., Hoben P.,
RA Walter P., Dobberstein B.;
RT "Isolation and characterization of a cDNA clone encoding the 19 kDa
RT protein of signal recognition particle (SRP): expression and binding
RT to 7SL RNA.";
RL Nucleic Acids Res. 16:9431-9442(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Erythroblast;
RA Gubin A.N., Lee Y.T., Bouffard G.G., Miller J.L.;
RT "Gene expression in human erythroid precursor cells.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP THR-4.
RC TISSUE=Brain, 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-128.
RX PubMed=11641499; DOI=10.1126/science.1063839;
RA Wild K., Sinning I., Cusack S.;
RT "Crystal structure of an early protein-RNA assembly complex of the
RT signal recognition particle.";
RL Science 294:598-601(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 14-120 IN COMPLEX WITH SRP54
RP AND 7SL RNA.
RX PubMed=12244299; DOI=10.1038/nsb843;
RA Kuglstatter A., Oubridge C., Nagai K.;
RT "Induced structural changes of 7SL RNA during the assembly of human
RT signal recognition particle.";
RL Nat. Struct. Biol. 9:740-744(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 1-120 IN COMPLEX WITH 7SL
RP RNA.
RX PubMed=20179341; DOI=10.1107/S0907444910000879;
RA Wild K., Bange G., Bozkurt G., Segnitz B., Hendricks A., Sinning I.;
RT "Structural insights into the assembly of the human and archaeal
RT signal recognition particles.";
RL Acta Crystallogr. D 66:295-303(2010).
CC -!- FUNCTION: Signal-recognition-particle assembly, binds directly to
CC 7S RNA and mediates binding of the 54 kDa subunit of the SRP.
CC -!- SUBUNIT: Signal recognition particle consists of a 7S RNA molecule
CC of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54,
CC SRP19, SRP14 and SRP9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P09132-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09132-2; Sequence=VSP_042540;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P09132-3; Sequence=VSP_044524;
CC -!- SIMILARITY: Belongs to the SRP19 family.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Signal recognition particle
CC entry;
CC URL="http://en.wikipedia.org/wiki/Signal-recognition_particle";
CC -----------------------------------------------------------------------
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DR EMBL; X12791; CAA31280.1; -; mRNA.
DR EMBL; BU661702; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK311803; BAG34746.1; -; mRNA.
DR EMBL; AC008536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471086; EAW48999.1; -; Genomic_DNA.
DR EMBL; CH471086; EAW49000.1; -; Genomic_DNA.
DR EMBL; BC010947; AAH10947.1; -; mRNA.
DR EMBL; BC017830; AAH17830.1; -; mRNA.
DR PIR; S01700; S01700.
DR RefSeq; NP_001191122.1; NM_001204193.1.
DR RefSeq; NP_001191123.1; NM_001204194.1.
DR RefSeq; NP_001191125.1; NM_001204196.1.
DR RefSeq; NP_003126.1; NM_003135.2.
DR UniGene; Hs.637001; -.
DR PDB; 1JID; X-ray; 1.80 A; A=1-120.
DR PDB; 1MFQ; X-ray; 3.10 A; B=14-120.
DR PDB; 1RY1; EM; 12.00 A; B=14-120.
DR PDB; 2J37; EM; 8.00 A; B=14-120.
DR PDB; 3KTV; X-ray; 3.80 A; B/D=1-120.
DR PDBsum; 1JID; -.
DR PDBsum; 1MFQ; -.
DR PDBsum; 1RY1; -.
DR PDBsum; 2J37; -.
DR PDBsum; 3KTV; -.
DR DisProt; DP00570; -.
DR ProteinModelPortal; P09132; -.
DR SMR; P09132; 5-118.
DR IntAct; P09132; 6.
DR MINT; MINT-247583; -.
DR STRING; 9606.ENSP00000282999; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR PhosphoSite; P09132; -.
DR DMDM; 115502457; -.
DR PaxDb; P09132; -.
DR PRIDE; P09132; -.
DR Ensembl; ENST00000282999; ENSP00000282999; ENSG00000153037.
DR Ensembl; ENST00000505459; ENSP00000424870; ENSG00000153037.
DR Ensembl; ENST00000515463; ENSP00000425562; ENSG00000153037.
DR GeneID; 6728; -.
DR KEGG; hsa:6728; -.
DR UCSC; uc003kqc.3; human.
DR CTD; 6728; -.
DR GeneCards; GC05P112196; -.
DR HGNC; HGNC:11300; SRP19.
DR HPA; HPA029272; -.
DR MIM; 182175; gene.
DR neXtProt; NX_P09132; -.
DR PharmGKB; PA36124; -.
DR eggNOG; NOG265516; -.
DR HOGENOM; HOG000237221; -.
DR HOVERGEN; HBG059463; -.
DR InParanoid; P09132; -.
DR KO; K03105; -.
DR OMA; YVAEMIP; -.
DR OrthoDB; EOG72G199; -.
DR PhylomeDB; P09132; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; SRP19; human.
DR EvolutionaryTrace; P09132; -.
DR GenomeRNAi; 6728; -.
DR NextBio; 26244; -.
DR PRO; PR:P09132; -.
DR ArrayExpress; P09132; -.
DR Bgee; P09132; -.
DR CleanEx; HS_SRP19; -.
DR Genevestigator; P09132; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:UniProtKB.
DR GO; GO:0008312; F:7S RNA binding; IDA:UniProtKB.
DR GO; GO:0042493; P:response to drug; IDA:UniProtKB.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
DR Gene3D; 3.30.56.30; -; 1.
DR InterPro; IPR002778; Signal_recog_particle_SRP19.
DR PANTHER; PTHR17453; PTHR17453; 1.
DR Pfam; PF01922; SRP19; 1.
DR SUPFAM; SSF69695; SSF69695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Polymorphism;
KW Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 144 Signal recognition particle 19 kDa
FT protein.
FT /FTId=PRO_0000135197.
FT REGION 136 144 Basic region, potentially involved in
FT RNA-binding.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 15 144 FICIYPAYLNNKKTIAEGRRIPISKAVENPTATEIQDVCSA
FT VGLNVFLEKNKMYSREWNRDVQYRGRVRVQLKQEDGSLCLV
FT QFPSRKSVMLYAAEMIPKLKTRTQKTGGADQSLQQGEGSKK
FT GKGKKKK -> LLKILQLQRFKMYVQQLDLTYFLRKIKCTL
FT ENGIVMSNTEAESGSSSNRKMGASALYSSHHVSQ (in
FT isoform 3).
FT /FTId=VSP_044524.
FT VAR_SEQ 101 144 RKSVMLYAAEMIPKLKTRTQKTGGADQSLQQGEGSKKGKGK
FT KKK -> HYTLSLTSGS (in isoform 2).
FT /FTId=VSP_042540.
FT VARIANT 4 4 A -> T (in dbSNP:rs17855423).
FT /FTId=VAR_027800.
FT HELIX 12 14
FT STRAND 15 18
FT HELIX 20 23
FT TURN 29 32
FT TURN 37 39
FT STRAND 41 43
FT HELIX 46 55
FT STRAND 60 63
FT HELIX 76 78
FT STRAND 81 84
FT STRAND 93 95
FT HELIX 101 111
FT HELIX 112 114
FT HELIX 116 119
SQ SEQUENCE 144 AA; 16156 MW; E25F661972338CAE CRC64;
MACAAARSPA DQDRFICIYP AYLNNKKTIA EGRRIPISKA VENPTATEIQ DVCSAVGLNV
FLEKNKMYSR EWNRDVQYRG RVRVQLKQED GSLCLVQFPS RKSVMLYAAE MIPKLKTRTQ
KTGGADQSLQ QGEGSKKGKG KKKK
//
MIM
182175
*RECORD*
*FIELD* NO
182175
*FIELD* TI
*182175 SIGNAL RECOGNITION PARTICLE, 19-KD; SRP19
*FIELD* TX
CLONING
The signal recognition particle (SRP) is a ribonucleoprotein complex
read morethat mediates the targeting of proteins to the endoplasmic reticulum
(ER). The complex consists of a 7S (or 7SL) RNA and 6 different
proteins, SRP9 (600707), SRP14 (600708), SRP19, SRP54 (604857), SRP68
(604858), and SRP72 (602122). The proteins are bound to the 7S RNA as
monomers (SRP19 and SRP54) or heterodimers (SRP9/SRP14 and SRP68/SRP72).
SRP9 and SRP14 bind to the Alu domain of the SRP, whereas the other 4
proteins belong to the S domain. SRP has at least 3 distinct functions
that can be associated with the protein subunits: signal recognition,
translational arrest, and ER membrane targeting by interaction with the
docking protein.
For information on a signal recognition particle database, see Larsen et
al. (1998).
By screening a liver cDNA library with an anti-SRP19 probe, Lingelbach
et al. (1988) isolated a human SRP19 cDNA encoding a 144-amino acid
protein. Sequence analysis showed that SRP19 contains a very basic
C-terminal domain of 7 lysine residues interrupted by 2 glycine
residues. Northern blot analysis revealed expression of a 0.9 kb
transcript in HeLa cells. SDS-PAGE analysis showed that SRP19 is
expressed as a 19-kD protein, identical in size to canine SRP19.
Functional analysis determined that the SRP19 protein binds to 7SL RNA
in canine pancreas.
GENE STRUCTURE
Groden et al. (1991) determined that the SRP19 gene consists of 5 exons.
GENE FUNCTION
In 2 small nested deletions of 100 to 260 kb identified by Joslyn et al.
(1991) in patients with adenomatous polyposis coli (APC; 175100), Groden
et al. (1991) identified 3 genes in a span of about 100 kb on chromosome
5. One of these was DP1 (125265); a second was the gene that is mutant
in APC, called by them DP2.5 (611731). The third was a gene which was
found to have the same sequence as that of SRP19. Horii et al. (1993)
discussed the occurrence of alternative splicing not only within the APC
gene but also between the APC gene and the neighboring SRP19 gene.
BIOCHEMICAL FEATURES
Wild et al. (2001) reported the 1.8-angstrom resolution crystal
structure of human SRP19 in complex with its primary binding site on
helix 6 of SRP RNA, which consists of a stem-loop structure closed by an
unusual GGAG tetraloop. Protein-RNA interactions are mediated by the
specific recognition of a widened major groove and the tetraloop without
any direct protein-base contacts and include a complex network of highly
ordered water molecules. Wild et al. (2001) proposed a model of the
assembly of the SRP core comprising SRP19, SRP54, and SRP RNA based on
crystallographic and biochemical data.
Halic et al. (2004) presented the structure of a targeting complex
consisting of mammalian SRP bound to an active 80S ribosome carrying a
signal sequence. This structure, determined to 12-angstrom resolution by
cryoelectron microscopy, enabled Halic et al. (2004) to generate a
molecular model of SRP in its functional conformation. The model showed
how the S domain of SRP contacts the large ribosomal subunit at the
nascent chain exit site to bind the signal sequence, and that the Alu
domain reaches into the elongation factor-binding site of the ribosome,
explaining its elongation arrest activity.
MAPPING
The SRP19 gene maps to chromosome 5q21-q22, between the DP1 (125265) and
APC (611731) genes (Groden et al., 1991).
*FIELD* RF
1. Groden, J.; Thliveris, A.; Samowitz, W.; Carlson, M.; Gelbert,
L.; Albertsen, H.; Joslyn, G.; Stevens, J.; Spirio, L.; Robertson,
M.; Sargeant, L.; Krapcho, K.; Wolff, E.; Burt, R.; Hughes, J. P.;
Warrington, J.; McPherson, J.; Wasmuth, J.; Le Paslier, D.; Abderrahim,
H.; Cohen, D.; Leppert, M.; White, R.: Identification and characterization
of the familial adenomatous polyposis coli gene. Cell 66: 589-600,
1991.
2. Halic, M.; Becker, T.; Pool, M. R.; Spahn, C. M. T.; Grassucci,
R. A.; Frank, J.; Beckmann, R.: Structure of the signal recognition
particle interacting with the elongation-arrested ribosome. Nature 427:
808-814, 2004.
3. Horii, A.; Nakatsuru, S.; Ichii, S.; Nagase, H.; Nakamura, Y.:
Multiple forms of the APC gene transcripts and their tissue-specific
expression. Hum. Molec. Genet. 2: 283-287, 1993.
4. Joslyn, G.; Carlson, M.; Thliveris, A.; Albertsen, H.; Gelbert,
L.; Samowitz, W.; Groden, J.; Stevens, J.; Spirio, L.; Robertson,
M.; Sargeant, L.; Krapcho, K.; Wolff, E.; Burt, R.; Hughes, J. P.;
Warrington, J.; McPherson, J.; Wasmuth, J.; Le Paslier, D.; Abderrahim,
H.; Cohen, D.; Leppert, M.; White, R.: Identification of deletion
mutations and three new genes at the familial polyposis locus. Cell 66:
601-613, 1991.
5. Larsen, N.; Samuelsson, T.; Swieb, C.: The Signal Recognition
Particle Database (SRPDB). Nucleic Acids Res. 26: 177-178, 1998.
6. Lingelbach, K.; Zweib, C.; Webb, J.; Marshallsay, C.; Hoben, P.;
Walter, P.; Dobberstein, B.: Isolation and characterization of a
cDNA clone encoding the 19 kDa protein of signal recognition particle
(SRP): expression and binding to 7SL RNA. Nucleic Acids Res. 16:
9431-9442, 1988.
7. Wild, K.; Sinning, I.; Cusack, S.: Crystal structure of an early
protein-RNA assembly complex of the signal recognition particle. Science 294:
598-601, 2001.
*FIELD* CN
Ada Hamosh - updated: 3/8/2004
Ada Hamosh - updated: 10/23/2001
Paul J. Converse - updated: 4/20/2000
*FIELD* CD
Victor A. McKusick: 9/30/1991
*FIELD* ED
alopez: 07/03/2008
ckniffin: 2/5/2008
tkritzer: 3/9/2004
terry: 3/8/2004
carol: 10/23/2001
terry: 10/23/2001
carol: 4/21/2000
carol: 4/20/2000
terry: 6/1/1998
carol: 4/26/1993
supermim: 3/16/1992
carol: 9/30/1991
*RECORD*
*FIELD* NO
182175
*FIELD* TI
*182175 SIGNAL RECOGNITION PARTICLE, 19-KD; SRP19
*FIELD* TX
CLONING
The signal recognition particle (SRP) is a ribonucleoprotein complex
read morethat mediates the targeting of proteins to the endoplasmic reticulum
(ER). The complex consists of a 7S (or 7SL) RNA and 6 different
proteins, SRP9 (600707), SRP14 (600708), SRP19, SRP54 (604857), SRP68
(604858), and SRP72 (602122). The proteins are bound to the 7S RNA as
monomers (SRP19 and SRP54) or heterodimers (SRP9/SRP14 and SRP68/SRP72).
SRP9 and SRP14 bind to the Alu domain of the SRP, whereas the other 4
proteins belong to the S domain. SRP has at least 3 distinct functions
that can be associated with the protein subunits: signal recognition,
translational arrest, and ER membrane targeting by interaction with the
docking protein.
For information on a signal recognition particle database, see Larsen et
al. (1998).
By screening a liver cDNA library with an anti-SRP19 probe, Lingelbach
et al. (1988) isolated a human SRP19 cDNA encoding a 144-amino acid
protein. Sequence analysis showed that SRP19 contains a very basic
C-terminal domain of 7 lysine residues interrupted by 2 glycine
residues. Northern blot analysis revealed expression of a 0.9 kb
transcript in HeLa cells. SDS-PAGE analysis showed that SRP19 is
expressed as a 19-kD protein, identical in size to canine SRP19.
Functional analysis determined that the SRP19 protein binds to 7SL RNA
in canine pancreas.
GENE STRUCTURE
Groden et al. (1991) determined that the SRP19 gene consists of 5 exons.
GENE FUNCTION
In 2 small nested deletions of 100 to 260 kb identified by Joslyn et al.
(1991) in patients with adenomatous polyposis coli (APC; 175100), Groden
et al. (1991) identified 3 genes in a span of about 100 kb on chromosome
5. One of these was DP1 (125265); a second was the gene that is mutant
in APC, called by them DP2.5 (611731). The third was a gene which was
found to have the same sequence as that of SRP19. Horii et al. (1993)
discussed the occurrence of alternative splicing not only within the APC
gene but also between the APC gene and the neighboring SRP19 gene.
BIOCHEMICAL FEATURES
Wild et al. (2001) reported the 1.8-angstrom resolution crystal
structure of human SRP19 in complex with its primary binding site on
helix 6 of SRP RNA, which consists of a stem-loop structure closed by an
unusual GGAG tetraloop. Protein-RNA interactions are mediated by the
specific recognition of a widened major groove and the tetraloop without
any direct protein-base contacts and include a complex network of highly
ordered water molecules. Wild et al. (2001) proposed a model of the
assembly of the SRP core comprising SRP19, SRP54, and SRP RNA based on
crystallographic and biochemical data.
Halic et al. (2004) presented the structure of a targeting complex
consisting of mammalian SRP bound to an active 80S ribosome carrying a
signal sequence. This structure, determined to 12-angstrom resolution by
cryoelectron microscopy, enabled Halic et al. (2004) to generate a
molecular model of SRP in its functional conformation. The model showed
how the S domain of SRP contacts the large ribosomal subunit at the
nascent chain exit site to bind the signal sequence, and that the Alu
domain reaches into the elongation factor-binding site of the ribosome,
explaining its elongation arrest activity.
MAPPING
The SRP19 gene maps to chromosome 5q21-q22, between the DP1 (125265) and
APC (611731) genes (Groden et al., 1991).
*FIELD* RF
1. Groden, J.; Thliveris, A.; Samowitz, W.; Carlson, M.; Gelbert,
L.; Albertsen, H.; Joslyn, G.; Stevens, J.; Spirio, L.; Robertson,
M.; Sargeant, L.; Krapcho, K.; Wolff, E.; Burt, R.; Hughes, J. P.;
Warrington, J.; McPherson, J.; Wasmuth, J.; Le Paslier, D.; Abderrahim,
H.; Cohen, D.; Leppert, M.; White, R.: Identification and characterization
of the familial adenomatous polyposis coli gene. Cell 66: 589-600,
1991.
2. Halic, M.; Becker, T.; Pool, M. R.; Spahn, C. M. T.; Grassucci,
R. A.; Frank, J.; Beckmann, R.: Structure of the signal recognition
particle interacting with the elongation-arrested ribosome. Nature 427:
808-814, 2004.
3. Horii, A.; Nakatsuru, S.; Ichii, S.; Nagase, H.; Nakamura, Y.:
Multiple forms of the APC gene transcripts and their tissue-specific
expression. Hum. Molec. Genet. 2: 283-287, 1993.
4. Joslyn, G.; Carlson, M.; Thliveris, A.; Albertsen, H.; Gelbert,
L.; Samowitz, W.; Groden, J.; Stevens, J.; Spirio, L.; Robertson,
M.; Sargeant, L.; Krapcho, K.; Wolff, E.; Burt, R.; Hughes, J. P.;
Warrington, J.; McPherson, J.; Wasmuth, J.; Le Paslier, D.; Abderrahim,
H.; Cohen, D.; Leppert, M.; White, R.: Identification of deletion
mutations and three new genes at the familial polyposis locus. Cell 66:
601-613, 1991.
5. Larsen, N.; Samuelsson, T.; Swieb, C.: The Signal Recognition
Particle Database (SRPDB). Nucleic Acids Res. 26: 177-178, 1998.
6. Lingelbach, K.; Zweib, C.; Webb, J.; Marshallsay, C.; Hoben, P.;
Walter, P.; Dobberstein, B.: Isolation and characterization of a
cDNA clone encoding the 19 kDa protein of signal recognition particle
(SRP): expression and binding to 7SL RNA. Nucleic Acids Res. 16:
9431-9442, 1988.
7. Wild, K.; Sinning, I.; Cusack, S.: Crystal structure of an early
protein-RNA assembly complex of the signal recognition particle. Science 294:
598-601, 2001.
*FIELD* CN
Ada Hamosh - updated: 3/8/2004
Ada Hamosh - updated: 10/23/2001
Paul J. Converse - updated: 4/20/2000
*FIELD* CD
Victor A. McKusick: 9/30/1991
*FIELD* ED
alopez: 07/03/2008
ckniffin: 2/5/2008
tkritzer: 3/9/2004
terry: 3/8/2004
carol: 10/23/2001
terry: 10/23/2001
carol: 4/21/2000
carol: 4/20/2000
terry: 6/1/1998
carol: 4/26/1993
supermim: 3/16/1992
carol: 9/30/1991