Full text data of HSPE1
HSPE1
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
10 kDa heat shock protein, mitochondrial; Hsp10 (10 kDa chaperonin; Chaperonin 10; CPN10; Early-pregnancy factor; EPF)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
10 kDa heat shock protein, mitochondrial; Hsp10 (10 kDa chaperonin; Chaperonin 10; CPN10; Early-pregnancy factor; EPF)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P61604
ID CH10_HUMAN Reviewed; 102 AA.
AC P61604; O95421; Q04984; Q53X54; Q9UDH0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=10 kDa heat shock protein, mitochondrial;
DE Short=Hsp10;
DE AltName: Full=10 kDa chaperonin;
DE AltName: Full=Chaperonin 10;
DE Short=CPN10;
DE AltName: Full=Early-pregnancy factor;
DE Short=EPF;
GN Name=HSPE1;
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].
RX PubMed=7914093; DOI=10.1016/0167-4781(94)90211-9;
RA Monzini N., Legname G., Marcucci F., Gromo G., Modena D.;
RT "Identification and cloning of human chaperonin 10 homologue.";
RL Biochim. Biophys. Acta 1218:478-480(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7916212; DOI=10.1016/0167-4781(94)90268-2;
RA Chen J.J., McNealy D.J., Dalal S., Androphy E.J.;
RT "Isolation, sequence analysis and characterization of a cDNA encoding
RT human chaperonin 10.";
RL Biochim. Biophys. Acta 1219:189-190(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12483302; DOI=10.1007/s00439-002-0837-9;
RA Hansen J.J., Bross P., Westergaard M., Nielsen M.N., Eiberg H.,
RA Boerglum A.D., Mogensen J., Kristiansen K., Bolund L., Gregersen N.;
RT "Genomic structure of the human mitochondrial chaperonin genes: HSP60
RT and HSP10 are localised head to head on chromosome 2 separated by a
RT bidirectional promoter.";
RL Hum. Genet. 112:71-77(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
RX PubMed=10763410; DOI=10.1023/A:1024488422990;
RA Summers K.M., Fletcher B.H., Macaranas D.D., Somodevilla-Torres M.J.,
RA Murphy R.M., Osborne M.J., Spurr N.K., Cassady A.I., Cavanagh A.C.;
RT "Mapping and characterization of the eukaryotic early pregnancy
RT factor/chaperonin 10 gene family.";
RL Somat. Cell Mol. Genet. 24:315-326(1998).
RN [10]
RP PROTEIN SEQUENCE OF 2-15; 41-54; 57-66 AND 81-92, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 8-19; 28-54 AND 70-102, AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=7912672; DOI=10.1111/j.1432-1033.1994.tb18897.x;
RA Cavanagh A.C., Morton H.;
RT "The purification of early-pregnancy factor to homogeneity from human
RT platelets and identification as chaperonin 10.";
RL Eur. J. Biochem. 222:551-560(1994).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-86 AND LYS-99, AND
RP MASS 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP MALONYLATION AT LYS-40; LYS-54 AND LYS-56.
RX PubMed=21908771; DOI=10.1074/mcp.M111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
RA He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
RA Dai J., Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
CC -!- FUNCTION: Eukaryotic CPN10 homolog which is essential for
CC mitochondrial protein biogenesis, together with CPN60. Binds to
CC CPN60 in the presence of Mg-ATP and suppresses the ATPase activity
CC of the latter.
CC -!- SUBUNIT: Homohexamer.
CC -!- INTERACTION:
CC P49789:FHIT; NbExp=4; IntAct=EBI-711483, EBI-741760;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- INDUCTION: By stress.
CC -!- MASS SPECTROMETRY: Mass=10843.5; Mass_error=0.2;
CC Method=Electrospray; Range=2-102; Source=PubMed:7912672;
CC -!- SIMILARITY: Belongs to the GroES chaperonin family.
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DR EMBL; X75821; CAA53455.1; -; mRNA.
DR EMBL; U07550; AAA50953.1; -; mRNA.
DR EMBL; AJ250915; CAB75425.1; -; Genomic_DNA.
DR EMBL; AK312104; BAG35040.1; -; mRNA.
DR EMBL; CR407688; CAG28616.1; -; mRNA.
DR EMBL; AC020550; AAX93146.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70163.1; -; Genomic_DNA.
DR EMBL; BC023518; AAH23518.1; -; mRNA.
DR EMBL; AH007060; AAC95387.1; -; Genomic_DNA.
DR PIR; S47532; S47532.
DR RefSeq; NP_002148.1; NM_002157.2.
DR UniGene; Hs.1197; -.
DR ProteinModelPortal; P61604; -.
DR SMR; P61604; 11-98.
DR IntAct; P61604; 25.
DR MINT; MINT-1373857; -.
DR STRING; 9606.ENSP00000233893; -.
DR PhosphoSite; P61604; -.
DR DMDM; 47606335; -.
DR UCD-2DPAGE; P61604; -.
DR PaxDb; P61604; -.
DR PeptideAtlas; P61604; -.
DR PRIDE; P61604; -.
DR DNASU; 3336; -.
DR Ensembl; ENST00000233893; ENSP00000233893; ENSG00000115541.
DR GeneID; 3336; -.
DR KEGG; hsa:3336; -.
DR UCSC; uc002uul.3; human.
DR CTD; 3336; -.
DR GeneCards; GC02P198328; -.
DR HGNC; HGNC:5269; HSPE1.
DR HPA; CAB017366; -.
DR MIM; 600141; gene.
DR neXtProt; NX_P61604; -.
DR PharmGKB; PA29535; -.
DR eggNOG; COG0234; -.
DR HOGENOM; HOG000133897; -.
DR HOVERGEN; HBG000385; -.
DR InParanoid; P61604; -.
DR KO; K04078; -.
DR OMA; LYIPDTG; -.
DR OrthoDB; EOG71CFPD; -.
DR PhylomeDB; P61604; -.
DR GeneWiki; GroES; -.
DR GenomeRNAi; 3336; -.
DR NextBio; 13204; -.
DR PRO; PR:P61604; -.
DR ArrayExpress; P61604; -.
DR Bgee; P61604; -.
DR CleanEx; HS_HSPE1; -.
DR Genevestigator; P61604; -.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; NAS:UniProtKB.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR Gene3D; 2.30.33.40; -; 1.
DR InterPro; IPR020818; Chaperonin_Cpn10.
DR InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR InterPro; IPR011032; GroES-like.
DR PANTHER; PTHR10772; PTHR10772; 1.
DR Pfam; PF00166; Cpn10; 1.
DR PRINTS; PR00297; CHAPERONIN10.
DR SMART; SM00883; Cpn10; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR PROSITE; PS00681; CHAPERONINS_CPN10; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Complete proteome; Direct protein sequencing;
KW Mitochondrion; Phosphoprotein; Reference proteome; Stress response.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 102 10 kDa heat shock protein, mitochondrial.
FT /FTId=PRO_0000174917.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 8 8 N6-acetyllysine (By similarity).
FT MOD_RES 40 40 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 40 40 N6-malonyllysine; alternate.
FT MOD_RES 54 54 N6-malonyllysine.
FT MOD_RES 56 56 N6-acetyllysine; alternate.
FT MOD_RES 56 56 N6-malonyllysine; alternate.
FT MOD_RES 66 66 N6-acetyllysine (By similarity).
FT MOD_RES 70 70 N6-acetyllysine (By similarity).
FT MOD_RES 79 79 Phosphothreonine.
FT MOD_RES 80 80 N6-acetyllysine (By similarity).
FT MOD_RES 86 86 N6-acetyllysine.
FT MOD_RES 99 99 N6-acetyllysine.
SQ SEQUENCE 102 AA; 10932 MW; 1F3192C81F6EDB78 CRC64;
MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGSKGKGGEI
QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY VD
//
ID CH10_HUMAN Reviewed; 102 AA.
AC P61604; O95421; Q04984; Q53X54; Q9UDH0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=10 kDa heat shock protein, mitochondrial;
DE Short=Hsp10;
DE AltName: Full=10 kDa chaperonin;
DE AltName: Full=Chaperonin 10;
DE Short=CPN10;
DE AltName: Full=Early-pregnancy factor;
DE Short=EPF;
GN Name=HSPE1;
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].
RX PubMed=7914093; DOI=10.1016/0167-4781(94)90211-9;
RA Monzini N., Legname G., Marcucci F., Gromo G., Modena D.;
RT "Identification and cloning of human chaperonin 10 homologue.";
RL Biochim. Biophys. Acta 1218:478-480(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7916212; DOI=10.1016/0167-4781(94)90268-2;
RA Chen J.J., McNealy D.J., Dalal S., Androphy E.J.;
RT "Isolation, sequence analysis and characterization of a cDNA encoding
RT human chaperonin 10.";
RL Biochim. Biophys. Acta 1219:189-190(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12483302; DOI=10.1007/s00439-002-0837-9;
RA Hansen J.J., Bross P., Westergaard M., Nielsen M.N., Eiberg H.,
RA Boerglum A.D., Mogensen J., Kristiansen K., Bolund L., Gregersen N.;
RT "Genomic structure of the human mitochondrial chaperonin genes: HSP60
RT and HSP10 are localised head to head on chromosome 2 separated by a
RT bidirectional promoter.";
RL Hum. Genet. 112:71-77(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
RX PubMed=10763410; DOI=10.1023/A:1024488422990;
RA Summers K.M., Fletcher B.H., Macaranas D.D., Somodevilla-Torres M.J.,
RA Murphy R.M., Osborne M.J., Spurr N.K., Cassady A.I., Cavanagh A.C.;
RT "Mapping and characterization of the eukaryotic early pregnancy
RT factor/chaperonin 10 gene family.";
RL Somat. Cell Mol. Genet. 24:315-326(1998).
RN [10]
RP PROTEIN SEQUENCE OF 2-15; 41-54; 57-66 AND 81-92, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 8-19; 28-54 AND 70-102, AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=7912672; DOI=10.1111/j.1432-1033.1994.tb18897.x;
RA Cavanagh A.C., Morton H.;
RT "The purification of early-pregnancy factor to homogeneity from human
RT platelets and identification as chaperonin 10.";
RL Eur. J. Biochem. 222:551-560(1994).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-86 AND LYS-99, AND
RP MASS 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP MALONYLATION AT LYS-40; LYS-54 AND LYS-56.
RX PubMed=21908771; DOI=10.1074/mcp.M111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
RA He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
RA Dai J., Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
CC -!- FUNCTION: Eukaryotic CPN10 homolog which is essential for
CC mitochondrial protein biogenesis, together with CPN60. Binds to
CC CPN60 in the presence of Mg-ATP and suppresses the ATPase activity
CC of the latter.
CC -!- SUBUNIT: Homohexamer.
CC -!- INTERACTION:
CC P49789:FHIT; NbExp=4; IntAct=EBI-711483, EBI-741760;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- INDUCTION: By stress.
CC -!- MASS SPECTROMETRY: Mass=10843.5; Mass_error=0.2;
CC Method=Electrospray; Range=2-102; Source=PubMed:7912672;
CC -!- SIMILARITY: Belongs to the GroES chaperonin family.
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; X75821; CAA53455.1; -; mRNA.
DR EMBL; U07550; AAA50953.1; -; mRNA.
DR EMBL; AJ250915; CAB75425.1; -; Genomic_DNA.
DR EMBL; AK312104; BAG35040.1; -; mRNA.
DR EMBL; CR407688; CAG28616.1; -; mRNA.
DR EMBL; AC020550; AAX93146.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70163.1; -; Genomic_DNA.
DR EMBL; BC023518; AAH23518.1; -; mRNA.
DR EMBL; AH007060; AAC95387.1; -; Genomic_DNA.
DR PIR; S47532; S47532.
DR RefSeq; NP_002148.1; NM_002157.2.
DR UniGene; Hs.1197; -.
DR ProteinModelPortal; P61604; -.
DR SMR; P61604; 11-98.
DR IntAct; P61604; 25.
DR MINT; MINT-1373857; -.
DR STRING; 9606.ENSP00000233893; -.
DR PhosphoSite; P61604; -.
DR DMDM; 47606335; -.
DR UCD-2DPAGE; P61604; -.
DR PaxDb; P61604; -.
DR PeptideAtlas; P61604; -.
DR PRIDE; P61604; -.
DR DNASU; 3336; -.
DR Ensembl; ENST00000233893; ENSP00000233893; ENSG00000115541.
DR GeneID; 3336; -.
DR KEGG; hsa:3336; -.
DR UCSC; uc002uul.3; human.
DR CTD; 3336; -.
DR GeneCards; GC02P198328; -.
DR HGNC; HGNC:5269; HSPE1.
DR HPA; CAB017366; -.
DR MIM; 600141; gene.
DR neXtProt; NX_P61604; -.
DR PharmGKB; PA29535; -.
DR eggNOG; COG0234; -.
DR HOGENOM; HOG000133897; -.
DR HOVERGEN; HBG000385; -.
DR InParanoid; P61604; -.
DR KO; K04078; -.
DR OMA; LYIPDTG; -.
DR OrthoDB; EOG71CFPD; -.
DR PhylomeDB; P61604; -.
DR GeneWiki; GroES; -.
DR GenomeRNAi; 3336; -.
DR NextBio; 13204; -.
DR PRO; PR:P61604; -.
DR ArrayExpress; P61604; -.
DR Bgee; P61604; -.
DR CleanEx; HS_HSPE1; -.
DR Genevestigator; P61604; -.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; NAS:UniProtKB.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR Gene3D; 2.30.33.40; -; 1.
DR InterPro; IPR020818; Chaperonin_Cpn10.
DR InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR InterPro; IPR011032; GroES-like.
DR PANTHER; PTHR10772; PTHR10772; 1.
DR Pfam; PF00166; Cpn10; 1.
DR PRINTS; PR00297; CHAPERONIN10.
DR SMART; SM00883; Cpn10; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR PROSITE; PS00681; CHAPERONINS_CPN10; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Complete proteome; Direct protein sequencing;
KW Mitochondrion; Phosphoprotein; Reference proteome; Stress response.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 102 10 kDa heat shock protein, mitochondrial.
FT /FTId=PRO_0000174917.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 8 8 N6-acetyllysine (By similarity).
FT MOD_RES 40 40 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 40 40 N6-malonyllysine; alternate.
FT MOD_RES 54 54 N6-malonyllysine.
FT MOD_RES 56 56 N6-acetyllysine; alternate.
FT MOD_RES 56 56 N6-malonyllysine; alternate.
FT MOD_RES 66 66 N6-acetyllysine (By similarity).
FT MOD_RES 70 70 N6-acetyllysine (By similarity).
FT MOD_RES 79 79 Phosphothreonine.
FT MOD_RES 80 80 N6-acetyllysine (By similarity).
FT MOD_RES 86 86 N6-acetyllysine.
FT MOD_RES 99 99 N6-acetyllysine.
SQ SEQUENCE 102 AA; 10932 MW; 1F3192C81F6EDB78 CRC64;
MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGSKGKGGEI
QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY VD
//
MIM
600141
*RECORD*
*FIELD* NO
600141
*FIELD* TI
*600141 HEAT-SHOCK 10-KD PROTEIN; HSPE1
;;CHAPERONIN 10 HOMOLOG;;
cpn10 HOMOLOG;;
GroES HOMOLOG; GroES;;
read moreHSP10
*FIELD* TX
DESCRIPTION
Chaperonins are ubiquitous, indispensable proteins that facilitate
protein folding in an ATP-dependent manner (Todd et al., 1994),
enhancing the yield of properly folded substrate protein under
conditions where spontaneous folding does not occur. Chaperonins are
typified by the E. coli heat-shock proteins GroEL (cpn60; 118190) and
GroES (cpn10). GroES is a heptameric ring of identical 10.4-kD subunits
that binds to each end of GroEL to form a symmetric, functional
heterodimer.
CLONING
Monzini et al. (1994) found complete identity of human and bovine
chaperonin 10 cDNA.
See reviews by Zeilstra-Ryalls et al. (1991) and Georgopoulos and Welch
(1993).
Hansen et al. (2003) presented the full sequence of the HSP60 (GroEL)
and HSP10 genes.
GENE FUNCTION
Using a luciferase-reporter assay, Hansen et al. (2003) demonstrated
that the region between the HSP10 and HSP60 (118190) genes functions as
a bidirectional promoter. The transcriptional activity of the promoter
fragment in the HSP60 direction is approximately twice that in the HSP10
direction under normal growth conditions; upon heat shock, promoter
activity in either direction increased by a factor of approximately 12.
Tokuriki and Tawfik (2009) examined the ability of the E. coli
GroEL/GroES chaperonins to buffer destabilizing and adaptive mutations.
Mutational drifts performed in vitro with 4 different enzymes indicated
the GroEL/GroES overexpression doubled the number of accumulating
mutations, and promoted the folding of enzyme variants carrying
mutations in the protein core and/or mutations with higher destabilizing
effects. The divergence of modified enzymatic specificity occurred much
faster under GroEL/GroES overexpression, in terms of the number of
adapted variants (greater than or equal to 2-fold) and their improved
specificity and activity (greater than or equal to 10-fold). Tokuriki
and Tawfik (2009) concluded that protein stability is a major constraint
in protein evolution, and that buffering mechanisms such as chaperonins
are key in alleviating this constraint.
GENE STRUCTURE
Hansen et al. (2003) found that the HSP10 gene consists of 4 exons. The
authors demonstrated that the 2 genes are linked head to head. The first
exon of HSP60 is noncoding, and the first exon of HSP10 ends with the
start codon.
MAPPING
By radiation hybrid analysis, Hansen et al. (2003) mapped the
mitochondrial chaperonin HSP60 (HSPD1; 118190) and its co-chaperonin
HSP10 (heat-shock protein 10) between markers AFMA121YH1 and WI-10756 on
chromosome 2. This localization and the position of 2 homologous
fragments in the human genome assembly were consistent with the
cytogenetic location 2q33.1.
*FIELD* RF
1. Georgopoulos, C.; Welch, W. J.: Role of the major heat shock proteins
as molecular chaperones. Annu. Rev. Cell Biol. 9: 601-634, 1993.
2. Hansen, J. J.; Bross, P.; Westergaard, M.; Nielsen, M. N.; Eiberg,
H.; Borglum, A. D.; Mogensen, J.; Kristiansen, K.; Bolund, L.; Gregersen,
N.: Genomic structure of the human mitochondrial chaperonin genes:
HSP60 and HSP10 are localised head to head on chromosome 2 separated
by a bidirectional promoter. Hum. Genet. 112: 71-77, 2003. Note:
Erratum: Hum. Genet. 112: 436 only, 2003.
3. Monzini, N.; Legname, G.; Marcucci, F.; Gromo, G.; Modena, D.:
Identification and cloning of human chaperonin 10 homologue. Biochim.
Biophys. Acta 1218: 478-480, 1994.
4. Todd, M. J.; Viitanen, P. V.; Lorimer, G. H.: Dynamics of the
chaperonin ATPase cycle: implications for facilitated protein folding. Science 265:
659-666, 1994.
5. Tokuriki, N.; Tawfik, D. S.: Chaperonin overexpression promotes
genetic variation and enzyme evolution. Nature 450: 668-673, 2009.
6. Zeilstra-Ryalls, J.; Fayet, O.; Georgopoulos, C.: The universally
conserved GroE (Hsp60) chaperonins. Annu. Rev. Microbiol. 45: 301-325,
1991.
*FIELD* CN
Ada Hamosh - updated: 6/16/2009
Victor A. McKusick - updated: 12/30/2002
Victor A. McKusick - updated: 5/17/2002
*FIELD* CD
Victor A. McKusick: 10/6/1994
*FIELD* ED
alopez: 06/17/2009
alopez: 6/17/2009
terry: 6/16/2009
terry: 3/16/2005
carol: 1/8/2003
tkritzer: 1/3/2003
terry: 12/30/2002
alopez: 5/24/2002
terry: 5/17/2002
carol: 10/12/1994
carol: 10/11/1994
carol: 10/7/1994
carol: 10/6/1994
*RECORD*
*FIELD* NO
600141
*FIELD* TI
*600141 HEAT-SHOCK 10-KD PROTEIN; HSPE1
;;CHAPERONIN 10 HOMOLOG;;
cpn10 HOMOLOG;;
GroES HOMOLOG; GroES;;
read moreHSP10
*FIELD* TX
DESCRIPTION
Chaperonins are ubiquitous, indispensable proteins that facilitate
protein folding in an ATP-dependent manner (Todd et al., 1994),
enhancing the yield of properly folded substrate protein under
conditions where spontaneous folding does not occur. Chaperonins are
typified by the E. coli heat-shock proteins GroEL (cpn60; 118190) and
GroES (cpn10). GroES is a heptameric ring of identical 10.4-kD subunits
that binds to each end of GroEL to form a symmetric, functional
heterodimer.
CLONING
Monzini et al. (1994) found complete identity of human and bovine
chaperonin 10 cDNA.
See reviews by Zeilstra-Ryalls et al. (1991) and Georgopoulos and Welch
(1993).
Hansen et al. (2003) presented the full sequence of the HSP60 (GroEL)
and HSP10 genes.
GENE FUNCTION
Using a luciferase-reporter assay, Hansen et al. (2003) demonstrated
that the region between the HSP10 and HSP60 (118190) genes functions as
a bidirectional promoter. The transcriptional activity of the promoter
fragment in the HSP60 direction is approximately twice that in the HSP10
direction under normal growth conditions; upon heat shock, promoter
activity in either direction increased by a factor of approximately 12.
Tokuriki and Tawfik (2009) examined the ability of the E. coli
GroEL/GroES chaperonins to buffer destabilizing and adaptive mutations.
Mutational drifts performed in vitro with 4 different enzymes indicated
the GroEL/GroES overexpression doubled the number of accumulating
mutations, and promoted the folding of enzyme variants carrying
mutations in the protein core and/or mutations with higher destabilizing
effects. The divergence of modified enzymatic specificity occurred much
faster under GroEL/GroES overexpression, in terms of the number of
adapted variants (greater than or equal to 2-fold) and their improved
specificity and activity (greater than or equal to 10-fold). Tokuriki
and Tawfik (2009) concluded that protein stability is a major constraint
in protein evolution, and that buffering mechanisms such as chaperonins
are key in alleviating this constraint.
GENE STRUCTURE
Hansen et al. (2003) found that the HSP10 gene consists of 4 exons. The
authors demonstrated that the 2 genes are linked head to head. The first
exon of HSP60 is noncoding, and the first exon of HSP10 ends with the
start codon.
MAPPING
By radiation hybrid analysis, Hansen et al. (2003) mapped the
mitochondrial chaperonin HSP60 (HSPD1; 118190) and its co-chaperonin
HSP10 (heat-shock protein 10) between markers AFMA121YH1 and WI-10756 on
chromosome 2. This localization and the position of 2 homologous
fragments in the human genome assembly were consistent with the
cytogenetic location 2q33.1.
*FIELD* RF
1. Georgopoulos, C.; Welch, W. J.: Role of the major heat shock proteins
as molecular chaperones. Annu. Rev. Cell Biol. 9: 601-634, 1993.
2. Hansen, J. J.; Bross, P.; Westergaard, M.; Nielsen, M. N.; Eiberg,
H.; Borglum, A. D.; Mogensen, J.; Kristiansen, K.; Bolund, L.; Gregersen,
N.: Genomic structure of the human mitochondrial chaperonin genes:
HSP60 and HSP10 are localised head to head on chromosome 2 separated
by a bidirectional promoter. Hum. Genet. 112: 71-77, 2003. Note:
Erratum: Hum. Genet. 112: 436 only, 2003.
3. Monzini, N.; Legname, G.; Marcucci, F.; Gromo, G.; Modena, D.:
Identification and cloning of human chaperonin 10 homologue. Biochim.
Biophys. Acta 1218: 478-480, 1994.
4. Todd, M. J.; Viitanen, P. V.; Lorimer, G. H.: Dynamics of the
chaperonin ATPase cycle: implications for facilitated protein folding. Science 265:
659-666, 1994.
5. Tokuriki, N.; Tawfik, D. S.: Chaperonin overexpression promotes
genetic variation and enzyme evolution. Nature 450: 668-673, 2009.
6. Zeilstra-Ryalls, J.; Fayet, O.; Georgopoulos, C.: The universally
conserved GroE (Hsp60) chaperonins. Annu. Rev. Microbiol. 45: 301-325,
1991.
*FIELD* CN
Ada Hamosh - updated: 6/16/2009
Victor A. McKusick - updated: 12/30/2002
Victor A. McKusick - updated: 5/17/2002
*FIELD* CD
Victor A. McKusick: 10/6/1994
*FIELD* ED
alopez: 06/17/2009
alopez: 6/17/2009
terry: 6/16/2009
terry: 3/16/2005
carol: 1/8/2003
tkritzer: 1/3/2003
terry: 12/30/2002
alopez: 5/24/2002
terry: 5/17/2002
carol: 10/12/1994
carol: 10/11/1994
carol: 10/7/1994
carol: 10/6/1994