Full text data of PSMC2
PSMC2
(MSS1)
[Confidence: high (present in two of the MS resources)]
26S protease regulatory subunit 7 (26S proteasome AAA-ATPase subunit RPT1; Proteasome 26S subunit ATPase 2; Protein MSS1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S protease regulatory subunit 7 (26S proteasome AAA-ATPase subunit RPT1; Proteasome 26S subunit ATPase 2; Protein MSS1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00021435
IPI00021435 Proteasome 26S ATPase subunit 2 The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00021435 Proteasome 26S ATPase subunit 2 The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P35998
ID PRS7_HUMAN Reviewed; 433 AA.
AC P35998; A4D0Q1; Q3LIA5; Q9UDI3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=26S protease regulatory subunit 7;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT1;
DE AltName: Full=Proteasome 26S subunit ATPase 2;
DE AltName: Full=Protein MSS1;
GN Name=PSMC2; Synonyms=MSS1;
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=1377363; DOI=10.1038/357700a0;
RA Shibuya H., Irie K., Ninomiya-Tsuji J., Goebl M., Taniguchi T.,
RA Matsumoto K.;
RT "New human gene encoding a positive modulator of HIV Tat-mediated
RT transactivation.";
RL Nature 357:700-702(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/S0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of
RT the genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-23; 139-158 AND 320-331.
RC TISSUE=Blood;
RX PubMed=8500623; DOI=10.1016/0014-5793(93)81356-5;
RA Dubiel W., Ferrell K., Rechsteiner M.;
RT "Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated
RT transactivation, as subunit 7 of the 26 S protease.";
RL FEBS Lett. 323:276-278(1993).
RN [7]
RP PROTEIN SEQUENCE OF 2-10.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 85-97; 101-110; 201-210; 269-284 AND 298-312, AND
RP MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP FUNCTION, AND INTERACTION WITH NDC80.
RX PubMed=9295362; DOI=10.1074/jbc.272.38.24081;
RA Chen Y., Sharp Z.D., Lee W.-H.;
RT "HEC binds to the seventh regulatory subunit of the 26 S proteasome
RT and modulates the proteolysis of mitotic cyclins.";
RL J. Biol. Chem. 272:24081-24087(1997).
RN [10]
RP INTERACTION WITH NDC80.
RX PubMed=10409732;
RA Zheng L., Chen Y., Lee W.-H.;
RT "Hec1p, an evolutionarily conserved coiled-coil protein, modulates
RT chromosome segregation through interaction with SMC proteins.";
RL Mol. Cell. Biol. 19:5417-5428(1999).
RN [11]
RP INTERACTION WITH SQSTM1.
RX PubMed=15340068; DOI=10.1128/MCB.24.18.8055-8068.2004;
RA Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R.,
RA Wooten M.W.;
RT "Sequestosome 1/p62 is a polyubiquitin chain binding protein involved
RT in ubiquitin proteasome degradation.";
RL Mol. Cell. Biol. 24:8055-8068(2004).
RN [12]
RP INTERACTION WITH PAAF1.
RX PubMed=15831487; DOI=10.1128/MCB.25.9.3842-3853.2005;
RA Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
RT "Proteasomal ATPase-associated factor 1 negatively regulates
RT proteasome activity by interacting with proteasomal ATPases.";
RL Mol. Cell. Biol. 25:3842-3853(2005).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116 AND LYS-422, 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 [15]
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 [16]
RP INTERACTION WITH TRIM5.
RX PubMed=22078707; DOI=10.1186/1742-4690-8-93;
RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
RA Luban J., Campbell E.M.;
RT "TRIM5alpha associates with proteasomal subunits in cells while in
RT complex with HIV-1 virions.";
RL Retrovirology 8:93-93(2011).
RN [17]
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).
CC -!- FUNCTION: The 26S protease is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the
CC 26S complex. In case of HIV-1 infection, positive modulator of
CC Tat-mediated transactivation.
CC -!- SUBUNIT: Interacts with NDC80 and SQSTM1. Interacts with PAAF1.
CC Interacts with HIV-1 Tat. Interacts with TRIM5.
CC -!- INTERACTION:
CC P62191:PSMC1; NbExp=4; IntAct=EBI-359710, EBI-357598;
CC P62195:PSMC5; NbExp=10; IntAct=EBI-359710, EBI-357745;
CC Q16401:PSMD5; NbExp=5; IntAct=EBI-359710, EBI-752143;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, P-body (By
CC similarity). Note=Colocalizes with TRIM5 in the cytoplasmic bodies
CC (By similarity).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR EMBL; D11094; BAA01868.1; -; mRNA.
DR EMBL; AB075520; BAE45763.1; -; mRNA.
DR EMBL; CH236947; EAL24412.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83332.1; -; Genomic_DNA.
DR EMBL; BC002589; AAH02589.1; -; mRNA.
DR PIR; S24353; S24353.
DR RefSeq; NP_001191382.1; NM_001204453.1.
DR RefSeq; NP_002794.1; NM_002803.3.
DR UniGene; Hs.437366; -.
DR ProteinModelPortal; P35998; -.
DR SMR; P35998; 45-422.
DR DIP; DIP-27554N; -.
DR IntAct; P35998; 30.
DR MINT; MINT-1163662; -.
DR STRING; 9606.ENSP00000292644; -.
DR PhosphoSite; P35998; -.
DR DMDM; 547930; -.
DR OGP; P35998; -.
DR REPRODUCTION-2DPAGE; IPI00021435; -.
DR REPRODUCTION-2DPAGE; P35998; -.
DR PaxDb; P35998; -.
DR PeptideAtlas; P35998; -.
DR PRIDE; P35998; -.
DR DNASU; 5701; -.
DR Ensembl; ENST00000292644; ENSP00000292644; ENSG00000161057.
DR Ensembl; ENST00000435765; ENSP00000391211; ENSG00000161057.
DR GeneID; 5701; -.
DR KEGG; hsa:5701; -.
DR UCSC; uc003vbs.3; human.
DR CTD; 5701; -.
DR GeneCards; GC07P102984; -.
DR HGNC; HGNC:9548; PSMC2.
DR HPA; HPA019238; -.
DR MIM; 154365; gene.
DR neXtProt; NX_P35998; -.
DR PharmGKB; PA33893; -.
DR eggNOG; COG1222; -.
DR HOGENOM; HOG000225143; -.
DR HOVERGEN; HBG000109; -.
DR InParanoid; P35998; -.
DR KO; K03061; -.
DR OMA; RDIRYDL; -.
DR OrthoDB; EOG7TF78Z; -.
DR PhylomeDB; P35998; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMC2; human.
DR GeneWiki; PSMC2; -.
DR GenomeRNAi; 5701; -.
DR NextBio; 22150; -.
DR PRO; PR:P35998; -.
DR ArrayExpress; P35998; -.
DR Bgee; P35998; -.
DR CleanEx; HS_PSMC2; -.
DR Genevestigator; P35998; -.
DR GO; GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR005937; 26S_Psome_P45.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Nucleotide-binding;
KW Nucleus; Proteasome; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 433 26S protease regulatory subunit 7.
FT /FTId=PRO_0000084709.
FT NP_BIND 216 223 ATP (Potential).
FT MOD_RES 116 116 N6-acetyllysine.
FT MOD_RES 422 422 N6-acetyllysine.
FT CONFLICT 15 15 D -> V (in Ref. 2; BAE45763).
SQ SEQUENCE 433 AA; 48634 MW; 85FD95F6DF7A3E84 CRC64;
MPDYLGADQR KTKEDEKDDK PIRALDEGDI ALLKTYGQST YSRQIKQVED DIQQLLKKIN
ELTGIKESDT GLAPPALWDL AADKQTLQSE QPLQVARCTK IINADSEDPK YIINVKQFAK
FVVDLSDQVA PTDIEEGMRV GVDRNKYQIH IPLPPKIDPT VTMMQVEEKP DVTYSDVGGC
KEQIEKLREV VETPLLHPER FVNLGIEPPK GVLLFGPPGT GKTLCARAVA NRTDACFIRV
IGSELVQKYV GEGARMVREL FEMARTKKAC LIFFDEIDAI GGARFDDGAG GDNEVQRTML
ELINQLDGFD PRGNIKVLMA TNRPDTLDPA LMRPGRLDRK IEFSLPDLEG RTHIFKIHAR
SMSVERDIRF ELLARLCPNS TGAEIRSVCT EAGMFAIRAR RKIATEKDFL EAVNKVIKSY
AKFSATPRYM TYN
//
ID PRS7_HUMAN Reviewed; 433 AA.
AC P35998; A4D0Q1; Q3LIA5; Q9UDI3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=26S protease regulatory subunit 7;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT1;
DE AltName: Full=Proteasome 26S subunit ATPase 2;
DE AltName: Full=Protein MSS1;
GN Name=PSMC2; Synonyms=MSS1;
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=1377363; DOI=10.1038/357700a0;
RA Shibuya H., Irie K., Ninomiya-Tsuji J., Goebl M., Taniguchi T.,
RA Matsumoto K.;
RT "New human gene encoding a positive modulator of HIV Tat-mediated
RT transactivation.";
RL Nature 357:700-702(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/S0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of
RT the genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-23; 139-158 AND 320-331.
RC TISSUE=Blood;
RX PubMed=8500623; DOI=10.1016/0014-5793(93)81356-5;
RA Dubiel W., Ferrell K., Rechsteiner M.;
RT "Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated
RT transactivation, as subunit 7 of the 26 S protease.";
RL FEBS Lett. 323:276-278(1993).
RN [7]
RP PROTEIN SEQUENCE OF 2-10.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 85-97; 101-110; 201-210; 269-284 AND 298-312, AND
RP MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP FUNCTION, AND INTERACTION WITH NDC80.
RX PubMed=9295362; DOI=10.1074/jbc.272.38.24081;
RA Chen Y., Sharp Z.D., Lee W.-H.;
RT "HEC binds to the seventh regulatory subunit of the 26 S proteasome
RT and modulates the proteolysis of mitotic cyclins.";
RL J. Biol. Chem. 272:24081-24087(1997).
RN [10]
RP INTERACTION WITH NDC80.
RX PubMed=10409732;
RA Zheng L., Chen Y., Lee W.-H.;
RT "Hec1p, an evolutionarily conserved coiled-coil protein, modulates
RT chromosome segregation through interaction with SMC proteins.";
RL Mol. Cell. Biol. 19:5417-5428(1999).
RN [11]
RP INTERACTION WITH SQSTM1.
RX PubMed=15340068; DOI=10.1128/MCB.24.18.8055-8068.2004;
RA Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R.,
RA Wooten M.W.;
RT "Sequestosome 1/p62 is a polyubiquitin chain binding protein involved
RT in ubiquitin proteasome degradation.";
RL Mol. Cell. Biol. 24:8055-8068(2004).
RN [12]
RP INTERACTION WITH PAAF1.
RX PubMed=15831487; DOI=10.1128/MCB.25.9.3842-3853.2005;
RA Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
RT "Proteasomal ATPase-associated factor 1 negatively regulates
RT proteasome activity by interacting with proteasomal ATPases.";
RL Mol. Cell. Biol. 25:3842-3853(2005).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116 AND LYS-422, 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 [15]
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 [16]
RP INTERACTION WITH TRIM5.
RX PubMed=22078707; DOI=10.1186/1742-4690-8-93;
RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
RA Luban J., Campbell E.M.;
RT "TRIM5alpha associates with proteasomal subunits in cells while in
RT complex with HIV-1 virions.";
RL Retrovirology 8:93-93(2011).
RN [17]
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).
CC -!- FUNCTION: The 26S protease is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the
CC 26S complex. In case of HIV-1 infection, positive modulator of
CC Tat-mediated transactivation.
CC -!- SUBUNIT: Interacts with NDC80 and SQSTM1. Interacts with PAAF1.
CC Interacts with HIV-1 Tat. Interacts with TRIM5.
CC -!- INTERACTION:
CC P62191:PSMC1; NbExp=4; IntAct=EBI-359710, EBI-357598;
CC P62195:PSMC5; NbExp=10; IntAct=EBI-359710, EBI-357745;
CC Q16401:PSMD5; NbExp=5; IntAct=EBI-359710, EBI-752143;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, P-body (By
CC similarity). Note=Colocalizes with TRIM5 in the cytoplasmic bodies
CC (By similarity).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR EMBL; D11094; BAA01868.1; -; mRNA.
DR EMBL; AB075520; BAE45763.1; -; mRNA.
DR EMBL; CH236947; EAL24412.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83332.1; -; Genomic_DNA.
DR EMBL; BC002589; AAH02589.1; -; mRNA.
DR PIR; S24353; S24353.
DR RefSeq; NP_001191382.1; NM_001204453.1.
DR RefSeq; NP_002794.1; NM_002803.3.
DR UniGene; Hs.437366; -.
DR ProteinModelPortal; P35998; -.
DR SMR; P35998; 45-422.
DR DIP; DIP-27554N; -.
DR IntAct; P35998; 30.
DR MINT; MINT-1163662; -.
DR STRING; 9606.ENSP00000292644; -.
DR PhosphoSite; P35998; -.
DR DMDM; 547930; -.
DR OGP; P35998; -.
DR REPRODUCTION-2DPAGE; IPI00021435; -.
DR REPRODUCTION-2DPAGE; P35998; -.
DR PaxDb; P35998; -.
DR PeptideAtlas; P35998; -.
DR PRIDE; P35998; -.
DR DNASU; 5701; -.
DR Ensembl; ENST00000292644; ENSP00000292644; ENSG00000161057.
DR Ensembl; ENST00000435765; ENSP00000391211; ENSG00000161057.
DR GeneID; 5701; -.
DR KEGG; hsa:5701; -.
DR UCSC; uc003vbs.3; human.
DR CTD; 5701; -.
DR GeneCards; GC07P102984; -.
DR HGNC; HGNC:9548; PSMC2.
DR HPA; HPA019238; -.
DR MIM; 154365; gene.
DR neXtProt; NX_P35998; -.
DR PharmGKB; PA33893; -.
DR eggNOG; COG1222; -.
DR HOGENOM; HOG000225143; -.
DR HOVERGEN; HBG000109; -.
DR InParanoid; P35998; -.
DR KO; K03061; -.
DR OMA; RDIRYDL; -.
DR OrthoDB; EOG7TF78Z; -.
DR PhylomeDB; P35998; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMC2; human.
DR GeneWiki; PSMC2; -.
DR GenomeRNAi; 5701; -.
DR NextBio; 22150; -.
DR PRO; PR:P35998; -.
DR ArrayExpress; P35998; -.
DR Bgee; P35998; -.
DR CleanEx; HS_PSMC2; -.
DR Genevestigator; P35998; -.
DR GO; GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR005937; 26S_Psome_P45.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Nucleotide-binding;
KW Nucleus; Proteasome; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 433 26S protease regulatory subunit 7.
FT /FTId=PRO_0000084709.
FT NP_BIND 216 223 ATP (Potential).
FT MOD_RES 116 116 N6-acetyllysine.
FT MOD_RES 422 422 N6-acetyllysine.
FT CONFLICT 15 15 D -> V (in Ref. 2; BAE45763).
SQ SEQUENCE 433 AA; 48634 MW; 85FD95F6DF7A3E84 CRC64;
MPDYLGADQR KTKEDEKDDK PIRALDEGDI ALLKTYGQST YSRQIKQVED DIQQLLKKIN
ELTGIKESDT GLAPPALWDL AADKQTLQSE QPLQVARCTK IINADSEDPK YIINVKQFAK
FVVDLSDQVA PTDIEEGMRV GVDRNKYQIH IPLPPKIDPT VTMMQVEEKP DVTYSDVGGC
KEQIEKLREV VETPLLHPER FVNLGIEPPK GVLLFGPPGT GKTLCARAVA NRTDACFIRV
IGSELVQKYV GEGARMVREL FEMARTKKAC LIFFDEIDAI GGARFDDGAG GDNEVQRTML
ELINQLDGFD PRGNIKVLMA TNRPDTLDPA LMRPGRLDRK IEFSLPDLEG RTHIFKIHAR
SMSVERDIRF ELLARLCPNS TGAEIRSVCT EAGMFAIRAR RKIATEKDFL EAVNKVIKSY
AKFSATPRYM TYN
//
MIM
154365
*RECORD*
*FIELD* NO
154365
*FIELD* TI
*154365 PROTEASOME 26S SUBUNIT, ATPase, 2; PSMC2
;;MAMMALIAN SUPPRESSOR OF sgv-1 OF YEAST; MSS1;;
read morePROTEASE 26S, SUBUNIT 7; S7
*FIELD* TX
DESCRIPTION
The 26S proteasome (see PSMC1; 602706) is a multisubunit protease
complex composed of a 20S core component and two 19S regulatory
complexes. PSMC2 is 1 of 6 putative ATPases contained within the
regulatory complex. PSMC2 was first identified as a possible cellular
factor that cooperates with the human immunodeficiency virus-1 (HIV-1)
protein Tat, a potent activator of virus gene expression.
CLONING
By transcomplementation of a yeast sgv1-deficient mutant, Shibuya et al.
(1992) isolated a human cDNA from a novel gene, MSS1. The MSS1 protein
was found to share 42% sequence identity with the human TBP1 protein
(PSMC3; 186852), which binds Tat in vitro and suppresses Tat-mediated
transactivation in vivo (Nelbock et al., 1990). Shibuya et al. (1992)
found that the levels of HIV activation by Tat correlated with
endogenous levels of MSS1 mRNA. Furthermore, they provided evidence that
expression of MSS1 enhances the Tat-mediated transactivation. The 1.5-kb
MSS1 cDNA encodes a protein of 433 amino acids.
To characterize components of the 26S proteasome, Dubiel et al. (1993)
performed peptide sequence analysis on subunit 7 (S7). They determined
that S7 is identical to MSS1. By SDS-PAGE, S7 has a molecular mass of 49
kD.
By Western blot analysis of rat tissues, Yanagi et al. (2000) found that
the level of PSMC2 expression varied among tissues but was ubiquitous.
This was in contrast to the expression pattern of the 30-kD component of
the proteasome 20S core, which showed similar levels of expression in
all tissues. Immunolocalization of proteasome subunits in HeLa and HepG2
cells showed proteasome localization within nuclei, while
immunolocalization of PSMC2 gave homogeneous staining of both cytoplasm
and nucleoplasm. By glycerol gradient sedimentation, Yanagi et al.
(2000) found PSMC2 purified from rat liver nuclear extracts associated
with the proteasome and with protein complexes of lighter density, and
it also existed as a monomer. They also found that several basal
transcription factors for RNA polymerase II, including TATA box-binding
protein (TBP; 600075), and the general transcription factors IIB (GFT2B;
189963), IIH (see GTF2H1; 189972), and IIF (see GTF2F1; 189968)
coimmunoprecipitated with PSMC2 from rat liver lysosomes, suggesting
dual functionality of PSMC2.
MAPPING
Tanahashi et al. (1998) mapped the PSMC2 gene to 7q22.1-q22.3 by
fluorescence in situ hybridization.
*FIELD* RF
1. Dubiel, W.; Ferrell, K.; Rechsteiner, M.: Peptide sequencing identifies
MSS1, a modulator of HIV Tat-mediated transactivation, as subunit
7 of the 26 S protease. FEBS Lett. 323: 276-278, 1993.
2. Nelbock, P.; Dillon, P. J.; Perkins, A.; Rosen, C. A.: A cDNA
for a protein that interacts with the human immunodeficiency virus
Tat activator. Science 248: 1650-1653, 1990.
3. Shibuya, H.; Irie, K.; Ninomiya-Tsuji, J.; Goebl, M.; Taniguchi,
T.; Matsumoto, K.: New human gene encoding a positive modulator of
HIV Tat-mediated transactivation. Nature 357: 700-702, 1992.
4. Tanahashi, N.; Suzuki, M.; Fujiwara, T.; Takahashi, E.; Shimbara,
N.; Chung, C. H.; Tanaka, K.: Chromosomal localization and immunological
analysis of a family of human 26S proteasomal ATPases. Biochem. Biophys.
Res. Commun. 243: 229-232, 1998.
5. Yanagi, S.; Shimbara, N.; Tamura, T.: Tissue and cell distribution
of a mammalian proteasomal ATPase, MSS1, and its complex formation
with the basal transcription factors. Biochem. Biophys. Res. Commun. 279:
568-573, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 8/12/2002
Rebekah S. Rasooly - updated: 6/10/1998
*FIELD* CD
Victor A. McKusick: 7/7/1992
*FIELD* ED
carol: 12/26/2007
mgross: 8/12/2002
psherman: 6/10/1998
mark: 2/13/1997
terry: 2/11/1997
carol: 10/19/1992
carol: 8/25/1992
carol: 7/7/1992
*RECORD*
*FIELD* NO
154365
*FIELD* TI
*154365 PROTEASOME 26S SUBUNIT, ATPase, 2; PSMC2
;;MAMMALIAN SUPPRESSOR OF sgv-1 OF YEAST; MSS1;;
read morePROTEASE 26S, SUBUNIT 7; S7
*FIELD* TX
DESCRIPTION
The 26S proteasome (see PSMC1; 602706) is a multisubunit protease
complex composed of a 20S core component and two 19S regulatory
complexes. PSMC2 is 1 of 6 putative ATPases contained within the
regulatory complex. PSMC2 was first identified as a possible cellular
factor that cooperates with the human immunodeficiency virus-1 (HIV-1)
protein Tat, a potent activator of virus gene expression.
CLONING
By transcomplementation of a yeast sgv1-deficient mutant, Shibuya et al.
(1992) isolated a human cDNA from a novel gene, MSS1. The MSS1 protein
was found to share 42% sequence identity with the human TBP1 protein
(PSMC3; 186852), which binds Tat in vitro and suppresses Tat-mediated
transactivation in vivo (Nelbock et al., 1990). Shibuya et al. (1992)
found that the levels of HIV activation by Tat correlated with
endogenous levels of MSS1 mRNA. Furthermore, they provided evidence that
expression of MSS1 enhances the Tat-mediated transactivation. The 1.5-kb
MSS1 cDNA encodes a protein of 433 amino acids.
To characterize components of the 26S proteasome, Dubiel et al. (1993)
performed peptide sequence analysis on subunit 7 (S7). They determined
that S7 is identical to MSS1. By SDS-PAGE, S7 has a molecular mass of 49
kD.
By Western blot analysis of rat tissues, Yanagi et al. (2000) found that
the level of PSMC2 expression varied among tissues but was ubiquitous.
This was in contrast to the expression pattern of the 30-kD component of
the proteasome 20S core, which showed similar levels of expression in
all tissues. Immunolocalization of proteasome subunits in HeLa and HepG2
cells showed proteasome localization within nuclei, while
immunolocalization of PSMC2 gave homogeneous staining of both cytoplasm
and nucleoplasm. By glycerol gradient sedimentation, Yanagi et al.
(2000) found PSMC2 purified from rat liver nuclear extracts associated
with the proteasome and with protein complexes of lighter density, and
it also existed as a monomer. They also found that several basal
transcription factors for RNA polymerase II, including TATA box-binding
protein (TBP; 600075), and the general transcription factors IIB (GFT2B;
189963), IIH (see GTF2H1; 189972), and IIF (see GTF2F1; 189968)
coimmunoprecipitated with PSMC2 from rat liver lysosomes, suggesting
dual functionality of PSMC2.
MAPPING
Tanahashi et al. (1998) mapped the PSMC2 gene to 7q22.1-q22.3 by
fluorescence in situ hybridization.
*FIELD* RF
1. Dubiel, W.; Ferrell, K.; Rechsteiner, M.: Peptide sequencing identifies
MSS1, a modulator of HIV Tat-mediated transactivation, as subunit
7 of the 26 S protease. FEBS Lett. 323: 276-278, 1993.
2. Nelbock, P.; Dillon, P. J.; Perkins, A.; Rosen, C. A.: A cDNA
for a protein that interacts with the human immunodeficiency virus
Tat activator. Science 248: 1650-1653, 1990.
3. Shibuya, H.; Irie, K.; Ninomiya-Tsuji, J.; Goebl, M.; Taniguchi,
T.; Matsumoto, K.: New human gene encoding a positive modulator of
HIV Tat-mediated transactivation. Nature 357: 700-702, 1992.
4. Tanahashi, N.; Suzuki, M.; Fujiwara, T.; Takahashi, E.; Shimbara,
N.; Chung, C. H.; Tanaka, K.: Chromosomal localization and immunological
analysis of a family of human 26S proteasomal ATPases. Biochem. Biophys.
Res. Commun. 243: 229-232, 1998.
5. Yanagi, S.; Shimbara, N.; Tamura, T.: Tissue and cell distribution
of a mammalian proteasomal ATPase, MSS1, and its complex formation
with the basal transcription factors. Biochem. Biophys. Res. Commun. 279:
568-573, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 8/12/2002
Rebekah S. Rasooly - updated: 6/10/1998
*FIELD* CD
Victor A. McKusick: 7/7/1992
*FIELD* ED
carol: 12/26/2007
mgross: 8/12/2002
psherman: 6/10/1998
mark: 2/13/1997
terry: 2/11/1997
carol: 10/19/1992
carol: 8/25/1992
carol: 7/7/1992