Full text data of DNAJC13
DNAJC13
(KIAA0678, RME8)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
DnaJ homolog subfamily C member 13 (Required for receptor-mediated endocytosis 8; RME-8)
DnaJ homolog subfamily C member 13 (Required for receptor-mediated endocytosis 8; RME-8)
UniProt
O75165
ID DJC13_HUMAN Reviewed; 2243 AA.
AC O75165; Q3L0T1; Q6PI82; Q6UJ77; Q6ZSW1; Q6ZUT5; Q86XG3; Q96DC1;
read moreAC Q9BWK9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 5.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=DnaJ homolog subfamily C member 13;
DE AltName: Full=Required for receptor-mediated endocytosis 8;
DE Short=RME-8;
GN Name=DNAJC13; Synonyms=KIAA0678, RME8;
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=16179350; DOI=10.1074/jbc.M505036200;
RA Girard M., Poupon V., Blondeau F., McPherson P.S.;
RT "The DnaJ-domain protein RME-8 functions in endosomal trafficking.";
RL J. Biol. Chem. 280:40135-40143(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-1463.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP SEQUENCE REVISION.
RC TISSUE=Aortic endothelium;
RA Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-736 AND 1819-2243.
RC TISSUE=Cervix, Placenta, and 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 617-2243, AND VARIANT
RP SER-1463.
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 672-1098.
RA Chang H.C., Hull M.J., Mellman I.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84, AND 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 [9]
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).
CC -!- SIMILARITY: Contains 1 J domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH43583.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC Sequence=BAA31653.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAC86133.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAC86835.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAC86835.1; Type=Erroneous termination; Positions=1651; Note=Translated as Glu;
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DR EMBL; AY779857; AAV41096.1; -; mRNA.
DR EMBL; AB014578; BAA31653.2; ALT_INIT; mRNA.
DR EMBL; AC020632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000164; AAH00164.2; -; mRNA.
DR EMBL; BC009630; AAH09630.1; -; mRNA.
DR EMBL; BC040638; AAH40638.1; -; mRNA.
DR EMBL; BC043583; AAH43583.1; ALT_SEQ; mRNA.
DR EMBL; AK125330; BAC86133.1; ALT_INIT; mRNA.
DR EMBL; AK127112; BAC86835.1; ALT_SEQ; mRNA.
DR EMBL; AY369172; AAQ57271.1; -; mRNA.
DR PIR; T00361; T00361.
DR RefSeq; NP_056083.3; NM_015268.3.
DR UniGene; Hs.12707; -.
DR ProteinModelPortal; O75165; -.
DR IntAct; O75165; 8.
DR MINT; MINT-6772191; -.
DR PhosphoSite; O75165; -.
DR PaxDb; O75165; -.
DR PRIDE; O75165; -.
DR Ensembl; ENST00000260818; ENSP00000260818; ENSG00000138246.
DR GeneID; 23317; -.
DR KEGG; hsa:23317; -.
DR UCSC; uc003eor.3; human.
DR CTD; 23317; -.
DR GeneCards; GC03P132136; -.
DR H-InvDB; HIX0003688; -.
DR HGNC; HGNC:30343; DNAJC13.
DR HPA; HPA036923; -.
DR MIM; 614334; gene.
DR neXtProt; NX_O75165; -.
DR PharmGKB; PA134947358; -.
DR eggNOG; NOG299042; -.
DR HOVERGEN; HBG081459; -.
DR InParanoid; O75165; -.
DR KO; K09533; -.
DR OMA; FEVKYEC; -.
DR OrthoDB; EOG7TBC15; -.
DR ChiTaRS; DNAJC13; human.
DR GeneWiki; DNAJC13; -.
DR GenomeRNAi; 23317; -.
DR NextBio; 45204; -.
DR PRO; PR:O75165; -.
DR ArrayExpress; O75165; -.
DR Bgee; O75165; -.
DR CleanEx; HS_DNAJC13; -.
DR Genevestigator; O75165; -.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR025640; DUF4339.
DR InterPro; IPR003169; GYF.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF14237; DUF4339; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF48371; SSF48371; 7.
DR SUPFAM; SSF55277; SSF55277; 1.
DR PROSITE; PS00636; DNAJ_1; FALSE_NEG.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Complete proteome; Polymorphism;
KW Reference proteome.
FT CHAIN 1 2243 DnaJ homolog subfamily C member 13.
FT /FTId=PRO_0000071072.
FT DOMAIN 1301 1366 J.
FT MOD_RES 84 84 N6-acetyllysine.
FT VARIANT 1463 1463 A -> S (in dbSNP:rs3762672).
FT /FTId=VAR_047458.
FT VARIANT 1487 1487 F -> C (in dbSNP:rs4405917).
FT /FTId=VAR_047459.
FT VARIANT 1515 1515 P -> S (in dbSNP:rs55825559).
FT /FTId=VAR_061144.
FT VARIANT 1995 1995 V -> I (in dbSNP:rs10935014).
FT /FTId=VAR_047460.
FT CONFLICT 476 476 D -> E (in Ref. 2; BAA31653).
FT CONFLICT 562 562 N -> D (in Ref. 5; AAH43583).
FT CONFLICT 1097 1097 I -> T (in Ref. 6; BAC86133).
FT CONFLICT 1148 1148 T -> I (in Ref. 6; BAC86835).
FT CONFLICT 1227 1227 Q -> H (in Ref. 2; BAA31653).
FT CONFLICT 1230 1230 T -> A (in Ref. 6; BAC86835).
FT CONFLICT 1269 1269 D -> N (in Ref. 6; BAC86133).
FT CONFLICT 2041 2041 L -> P (in Ref. 6; BAC86835).
FT CONFLICT 2091 2091 T -> A (in Ref. 6; BAC86835).
SQ SEQUENCE 2243 AA; 254415 MW; C6D292837DE1F170 CRC64;
MNIIRENKDL ACFYTTKHSW RGKYKRVFSV GTHAITTYNP NTLEVTNQWP YGDICSISPV
GKGQGTEFNL TFRKGSGKKS ETLKFSTEHR TELLTEALRF RTDFSEGKIT GRRYNCYKHH
WSDSRKPVIL EVTPGGFDQI NPATNRVLCS YDYRNIEGFV DLSDYQGGFC ILYGGFSRLH
LFASEQREEI IKSAIDHAGN YIGISLRIRK EPLEFEQYLN LRFGKYSTDE SITSLAEFVV
QKISPRHSEP VKRVLALTET CLVERDPATY NIATLKPLGE VFALVCDSEN PQLFTIEFIK
GQVRKYSSTE RDSLLASLLD GVRASGNRDV CVKMTPTHKG QRWGLLSMPV DEEVESLHLR
FLATPPNGNF ADAVFRFNAN ISYSGVLHAV TQDGLFSENK EKLINNAITA LLSQEGDVVA
SNAELESQFQ AVRRLVASKA GFLAFTQLPK FRERLGVKVV KALKRSNNGI IHAAVDMLCA
LMCPMHDDYD LRQEQLNKAS LLSSKKFLEN LLEKFNSHVD HGTGALVISS LLDFLTFALC
APYSETTEGQ QFDMLLEMVA SNGRTLFKLF QHPSMAIIKG AGLVMKAIIE EGDKEIATKM
QELALSEGAL PRHLHTAMFT ISSDQRMLTN RQLSRHLVGL WTADNATATN LLKRILPPGL
LAYLESSDLV PEKDADRMHV RDNVKIAMDQ YGKFNKVPEW QRLAGKAAKE VEKFAKEKVD
LVLMHWRDRM GIAQKENINQ KPVVLRKRRQ RIKIEANWDL FYYRFGQDHA RSNLIWNFKT
REELKDTLES EMRAFNIDRE LGSANVISWN HHEFEVKYEC LAEEIKIGDY YLRLLLEEDE
NEESGSIKRS YEFFNELYHR FLLTPKVNMK CLCLQALAIV YGRCHEEIGP FTDTRYIIGM
LERCTDKLER DRLILFLNKL ILNKKNVKDL MDSNGIRILV DLLTLAHLHV SRATVPLQSN
VIEAAPDMKR ESEKEWYFGN ADKERSGPYG FHEMQELWTK GMLNAKTRCW AQGMDGWRPL
QSIPQLKWCL LASGQAVLNE TDLATLILNM LITMCGYFPS RDQDNAIIRP LPKVKRLLSD
STCLPHIIQL LLTFDPILVE KVAILLYHIM QDNPQLPRLY LSGVFFFIMM YTGSNVLPVA
RFLKYTHTKQ AFKSEETKGQ DIFQRSILGH ILPEAMVCYL ENYEPEKFSE IFLGEFDTPE
AIWSSEMRRL MIEKIAAHLA DFTPRLQSNT RALYQYCPIP IINYPQLENE LFCNIYYLKQ
LCDTLRFPDW PIKDPVKLLK DTLDAWKKEV EKKPPMMSID DAYEVLNLPQ GQGPHDESKI
RKAYFRLAQK YHPDKNPEGR DMFEKVNKAY EFLCTKSAKI VDGPDPENII LILKTQSILF
NRHKEDLQPY KYAGYPMLIR TITMETSDDL LFSKESPLLP AATELAFHTV NCSALNAEEL
RRENGLEVLQ EAFSRCVAVL TRASKPSDMS VQVCGYISKC YSVAAQFEEC REKITEMPSI
IKDLCRVLYF GKSIPRVAAL GVECVSSFAV DFWLQTHLFQ AGILWYLLGF LFNYDYTLEE
SGIQKSEETN QQEVANSLAK LSVHALSRLG GYLAEEQATP ENPTIRKSLA GMLTPYVARK
LAVASVTEIL KMLNSNTESP YLIWNNSTRA ELLEFLESQQ ENMIKKGDCD KTYGSEFVYS
DHAKELIVGE IFVRVYNEVP TFQLEVPKAF AASLLDYIGS QAQYLHTFMA ITHAAKVESE
QHGDRLPRVE MALEALRNVI KYNPGSESEC IGHFKLIFSL LRVHGAGQVQ QLALEVVNIV
TSNQDCVNNI AESMVLSSLL ALLHSLPSSR QLVLETLYAL TSSTKIIKEA MAKGALIYLL
DMFCNSTHPQ VRAQTAELFA KMTADKLIGP KVRITLMKFL PSVFMDAMRD NPEAAVHIFE
GTHENPELIW NDNSRDKVST TVREMMLEHF KNQQDNPEAN WKLPEDFAVV FGEAEGELAV
GGVFLRIFIA QPAWVLRKPR EFLIALLEKL TELLEKNNPH GETLETLTMA TVCLFSAQPQ
LADQVPPLGH LPKVIQAMNH RNNAIPKSAI RVIHALSENE LCVRAMASLE TIGPLMNGMK
KRADTVGLAC EAINRMFQKE QSELVAQALK ADLVPYLLKL LEGIGLENLD SPAATKAQIV
KALKAMTRSL QYGEQVNEIL CRSSVWSAFK DQKHDLFISE SQTAGYLTGP GVAGYLTAGT
STSVMSNLPP PVDHEAGDLG YQT
//
ID DJC13_HUMAN Reviewed; 2243 AA.
AC O75165; Q3L0T1; Q6PI82; Q6UJ77; Q6ZSW1; Q6ZUT5; Q86XG3; Q96DC1;
read moreAC Q9BWK9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 5.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=DnaJ homolog subfamily C member 13;
DE AltName: Full=Required for receptor-mediated endocytosis 8;
DE Short=RME-8;
GN Name=DNAJC13; Synonyms=KIAA0678, RME8;
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=16179350; DOI=10.1074/jbc.M505036200;
RA Girard M., Poupon V., Blondeau F., McPherson P.S.;
RT "The DnaJ-domain protein RME-8 functions in endosomal trafficking.";
RL J. Biol. Chem. 280:40135-40143(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-1463.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP SEQUENCE REVISION.
RC TISSUE=Aortic endothelium;
RA Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-736 AND 1819-2243.
RC TISSUE=Cervix, Placenta, and 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 617-2243, AND VARIANT
RP SER-1463.
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 672-1098.
RA Chang H.C., Hull M.J., Mellman I.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84, AND 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 [9]
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).
CC -!- SIMILARITY: Contains 1 J domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH43583.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC Sequence=BAA31653.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAC86133.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAC86835.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAC86835.1; Type=Erroneous termination; Positions=1651; Note=Translated as Glu;
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DR EMBL; AY779857; AAV41096.1; -; mRNA.
DR EMBL; AB014578; BAA31653.2; ALT_INIT; mRNA.
DR EMBL; AC020632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000164; AAH00164.2; -; mRNA.
DR EMBL; BC009630; AAH09630.1; -; mRNA.
DR EMBL; BC040638; AAH40638.1; -; mRNA.
DR EMBL; BC043583; AAH43583.1; ALT_SEQ; mRNA.
DR EMBL; AK125330; BAC86133.1; ALT_INIT; mRNA.
DR EMBL; AK127112; BAC86835.1; ALT_SEQ; mRNA.
DR EMBL; AY369172; AAQ57271.1; -; mRNA.
DR PIR; T00361; T00361.
DR RefSeq; NP_056083.3; NM_015268.3.
DR UniGene; Hs.12707; -.
DR ProteinModelPortal; O75165; -.
DR IntAct; O75165; 8.
DR MINT; MINT-6772191; -.
DR PhosphoSite; O75165; -.
DR PaxDb; O75165; -.
DR PRIDE; O75165; -.
DR Ensembl; ENST00000260818; ENSP00000260818; ENSG00000138246.
DR GeneID; 23317; -.
DR KEGG; hsa:23317; -.
DR UCSC; uc003eor.3; human.
DR CTD; 23317; -.
DR GeneCards; GC03P132136; -.
DR H-InvDB; HIX0003688; -.
DR HGNC; HGNC:30343; DNAJC13.
DR HPA; HPA036923; -.
DR MIM; 614334; gene.
DR neXtProt; NX_O75165; -.
DR PharmGKB; PA134947358; -.
DR eggNOG; NOG299042; -.
DR HOVERGEN; HBG081459; -.
DR InParanoid; O75165; -.
DR KO; K09533; -.
DR OMA; FEVKYEC; -.
DR OrthoDB; EOG7TBC15; -.
DR ChiTaRS; DNAJC13; human.
DR GeneWiki; DNAJC13; -.
DR GenomeRNAi; 23317; -.
DR NextBio; 45204; -.
DR PRO; PR:O75165; -.
DR ArrayExpress; O75165; -.
DR Bgee; O75165; -.
DR CleanEx; HS_DNAJC13; -.
DR Genevestigator; O75165; -.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR025640; DUF4339.
DR InterPro; IPR003169; GYF.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF14237; DUF4339; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF48371; SSF48371; 7.
DR SUPFAM; SSF55277; SSF55277; 1.
DR PROSITE; PS00636; DNAJ_1; FALSE_NEG.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Complete proteome; Polymorphism;
KW Reference proteome.
FT CHAIN 1 2243 DnaJ homolog subfamily C member 13.
FT /FTId=PRO_0000071072.
FT DOMAIN 1301 1366 J.
FT MOD_RES 84 84 N6-acetyllysine.
FT VARIANT 1463 1463 A -> S (in dbSNP:rs3762672).
FT /FTId=VAR_047458.
FT VARIANT 1487 1487 F -> C (in dbSNP:rs4405917).
FT /FTId=VAR_047459.
FT VARIANT 1515 1515 P -> S (in dbSNP:rs55825559).
FT /FTId=VAR_061144.
FT VARIANT 1995 1995 V -> I (in dbSNP:rs10935014).
FT /FTId=VAR_047460.
FT CONFLICT 476 476 D -> E (in Ref. 2; BAA31653).
FT CONFLICT 562 562 N -> D (in Ref. 5; AAH43583).
FT CONFLICT 1097 1097 I -> T (in Ref. 6; BAC86133).
FT CONFLICT 1148 1148 T -> I (in Ref. 6; BAC86835).
FT CONFLICT 1227 1227 Q -> H (in Ref. 2; BAA31653).
FT CONFLICT 1230 1230 T -> A (in Ref. 6; BAC86835).
FT CONFLICT 1269 1269 D -> N (in Ref. 6; BAC86133).
FT CONFLICT 2041 2041 L -> P (in Ref. 6; BAC86835).
FT CONFLICT 2091 2091 T -> A (in Ref. 6; BAC86835).
SQ SEQUENCE 2243 AA; 254415 MW; C6D292837DE1F170 CRC64;
MNIIRENKDL ACFYTTKHSW RGKYKRVFSV GTHAITTYNP NTLEVTNQWP YGDICSISPV
GKGQGTEFNL TFRKGSGKKS ETLKFSTEHR TELLTEALRF RTDFSEGKIT GRRYNCYKHH
WSDSRKPVIL EVTPGGFDQI NPATNRVLCS YDYRNIEGFV DLSDYQGGFC ILYGGFSRLH
LFASEQREEI IKSAIDHAGN YIGISLRIRK EPLEFEQYLN LRFGKYSTDE SITSLAEFVV
QKISPRHSEP VKRVLALTET CLVERDPATY NIATLKPLGE VFALVCDSEN PQLFTIEFIK
GQVRKYSSTE RDSLLASLLD GVRASGNRDV CVKMTPTHKG QRWGLLSMPV DEEVESLHLR
FLATPPNGNF ADAVFRFNAN ISYSGVLHAV TQDGLFSENK EKLINNAITA LLSQEGDVVA
SNAELESQFQ AVRRLVASKA GFLAFTQLPK FRERLGVKVV KALKRSNNGI IHAAVDMLCA
LMCPMHDDYD LRQEQLNKAS LLSSKKFLEN LLEKFNSHVD HGTGALVISS LLDFLTFALC
APYSETTEGQ QFDMLLEMVA SNGRTLFKLF QHPSMAIIKG AGLVMKAIIE EGDKEIATKM
QELALSEGAL PRHLHTAMFT ISSDQRMLTN RQLSRHLVGL WTADNATATN LLKRILPPGL
LAYLESSDLV PEKDADRMHV RDNVKIAMDQ YGKFNKVPEW QRLAGKAAKE VEKFAKEKVD
LVLMHWRDRM GIAQKENINQ KPVVLRKRRQ RIKIEANWDL FYYRFGQDHA RSNLIWNFKT
REELKDTLES EMRAFNIDRE LGSANVISWN HHEFEVKYEC LAEEIKIGDY YLRLLLEEDE
NEESGSIKRS YEFFNELYHR FLLTPKVNMK CLCLQALAIV YGRCHEEIGP FTDTRYIIGM
LERCTDKLER DRLILFLNKL ILNKKNVKDL MDSNGIRILV DLLTLAHLHV SRATVPLQSN
VIEAAPDMKR ESEKEWYFGN ADKERSGPYG FHEMQELWTK GMLNAKTRCW AQGMDGWRPL
QSIPQLKWCL LASGQAVLNE TDLATLILNM LITMCGYFPS RDQDNAIIRP LPKVKRLLSD
STCLPHIIQL LLTFDPILVE KVAILLYHIM QDNPQLPRLY LSGVFFFIMM YTGSNVLPVA
RFLKYTHTKQ AFKSEETKGQ DIFQRSILGH ILPEAMVCYL ENYEPEKFSE IFLGEFDTPE
AIWSSEMRRL MIEKIAAHLA DFTPRLQSNT RALYQYCPIP IINYPQLENE LFCNIYYLKQ
LCDTLRFPDW PIKDPVKLLK DTLDAWKKEV EKKPPMMSID DAYEVLNLPQ GQGPHDESKI
RKAYFRLAQK YHPDKNPEGR DMFEKVNKAY EFLCTKSAKI VDGPDPENII LILKTQSILF
NRHKEDLQPY KYAGYPMLIR TITMETSDDL LFSKESPLLP AATELAFHTV NCSALNAEEL
RRENGLEVLQ EAFSRCVAVL TRASKPSDMS VQVCGYISKC YSVAAQFEEC REKITEMPSI
IKDLCRVLYF GKSIPRVAAL GVECVSSFAV DFWLQTHLFQ AGILWYLLGF LFNYDYTLEE
SGIQKSEETN QQEVANSLAK LSVHALSRLG GYLAEEQATP ENPTIRKSLA GMLTPYVARK
LAVASVTEIL KMLNSNTESP YLIWNNSTRA ELLEFLESQQ ENMIKKGDCD KTYGSEFVYS
DHAKELIVGE IFVRVYNEVP TFQLEVPKAF AASLLDYIGS QAQYLHTFMA ITHAAKVESE
QHGDRLPRVE MALEALRNVI KYNPGSESEC IGHFKLIFSL LRVHGAGQVQ QLALEVVNIV
TSNQDCVNNI AESMVLSSLL ALLHSLPSSR QLVLETLYAL TSSTKIIKEA MAKGALIYLL
DMFCNSTHPQ VRAQTAELFA KMTADKLIGP KVRITLMKFL PSVFMDAMRD NPEAAVHIFE
GTHENPELIW NDNSRDKVST TVREMMLEHF KNQQDNPEAN WKLPEDFAVV FGEAEGELAV
GGVFLRIFIA QPAWVLRKPR EFLIALLEKL TELLEKNNPH GETLETLTMA TVCLFSAQPQ
LADQVPPLGH LPKVIQAMNH RNNAIPKSAI RVIHALSENE LCVRAMASLE TIGPLMNGMK
KRADTVGLAC EAINRMFQKE QSELVAQALK ADLVPYLLKL LEGIGLENLD SPAATKAQIV
KALKAMTRSL QYGEQVNEIL CRSSVWSAFK DQKHDLFISE SQTAGYLTGP GVAGYLTAGT
STSVMSNLPP PVDHEAGDLG YQT
//
MIM
614334
*RECORD*
*FIELD* NO
614334
*FIELD* TI
*614334 DNAJ/HSP40 HOMOLOG, SUBFAMILY C, MEMBER 13; DNAJC13
;;RECEPTOR-MEDIATED ENDOCYTOSIS 8, C. ELEGANS, HOMOLOG OF; RME8;;
read moreKIAA0678
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Ishikawa et al. (1998) obtained a partial DNAJC13 clone, which
they designated KIAA0678. RT-PCR detected DNAJC13 expression in all
tissues examined, with highest expression in ovary and lowest expression
in pancreas and spleen.
By searching for genes in a region of chromosome 3 linked to adolescent
nephronophthisis (NPHP3; 604387) and Senior-Loken syndrome (SLSN3;
606995), Volz et al. (2002) identified KIAA0678. The deduced protein
contains a DnaJ homology domain and a conserved his-pro-asp (HPD) motif
that may be involved in regulation of HSP70 (see HSPA1A; 140550) ATPase
activity.
By searching a database for sequences similar to rat Rme8, Girard et al.
(2005) obtained the full-length sequence for human DNAJC13, which they
called RME8. The deduced 2,243-amino acid protein has a central DnaJ
domain flanked on either side by 2 IWN repeats. It also has 4 potential
clathrin heavy chain (CHC, or CLTC; 118955) interaction motifs. Confocal
immunofluorescence analysis of COS-7 cells and HeLa cells revealed that
endogenous RME8 distributed in a punctate pattern that accumulated in
the perinuclear region and overlapped with endosomal markers. Western
blot analysis of rat tissues and several cell lines, including HEK293
and HeLa cells, detected RME8 at an apparent molecular mass of 220 kD.
Fractionation of rat kidney and protein extraction experiments revealed
that Rme8 is an extrinsic membrane protein associated with microsomes.
GENE FUNCTION
Girard et al. (2005) showed that the isolated DnaJ domain of human RME8
bound rat kidney Hsc70 (HSPA8; 600816) in an ATP-dependent manner.
Knockdown of Rme8 in COS-7 cells disrupted endocytic trafficking of Egfr
(131550), Cimpr (IGF2R; 147280), and cathepsin D (CTSD; 116840).
GENE STRUCTURE
Girard et al. (2005) determined that the DNAJC13 gene contains 56 exons.
MAPPING
By radiation hybrid analysis, Ishikawa et al. (1998) mapped the DNAJC13
gene to chromosome 3. Volz et al. (2002) mapped the DNAJC13 gene to
chromosome 3q21-q22 by genomic sequence analysis. Girard et al. (2005)
mapped the DNAJC13 gene to chromosome 3q22.1 by genomic sequence
analysis.
MOLECULAR GENETICS
For discussion of a possible role of variation in the DNAJC13 gene in
Tourette syndrome/chronic tic disorder, see 137580.
*FIELD* RF
1. Girard, M.; Poupon, V.; Blondeau, F.; McPherson, P. S.: The DnaJ-domain
protein RME-8 functions in endosomal trafficking. J. Biol. Chem. 280:
40135-40143, 2005.
2. Ishikawa, K.; Nagase, T.; Suyama, M.; Miyajima, N.; Tanaka, A.;
Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the coding sequences
of unidentified human genes. X. The complete sequences of 100 new
cDNA clones from brain which can code for large proteins in vitro. DNA
Res. 5: 169-176, 1998.
3. Volz, A.; Melkaoui, R.; Hildebrandt, F.; Omran, H.: Candidate
gene analysis of KIAA0678 encoding a DnaJ-like protein for adolescent
nephronophthisis and Senior-Loken syndrome type 3. Cytogenet. Genome
Res. 97: 163-166, 2002.
*FIELD* CN
Cassandra L. Kniffin - updated: 3/27/2012
*FIELD* CD
Patricia A. Hartz: 11/8/2011
*FIELD* ED
carol: 03/27/2012
ckniffin: 3/8/2012
mgross: 11/8/2011
alopez: 11/8/2011
*RECORD*
*FIELD* NO
614334
*FIELD* TI
*614334 DNAJ/HSP40 HOMOLOG, SUBFAMILY C, MEMBER 13; DNAJC13
;;RECEPTOR-MEDIATED ENDOCYTOSIS 8, C. ELEGANS, HOMOLOG OF; RME8;;
read moreKIAA0678
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Ishikawa et al. (1998) obtained a partial DNAJC13 clone, which
they designated KIAA0678. RT-PCR detected DNAJC13 expression in all
tissues examined, with highest expression in ovary and lowest expression
in pancreas and spleen.
By searching for genes in a region of chromosome 3 linked to adolescent
nephronophthisis (NPHP3; 604387) and Senior-Loken syndrome (SLSN3;
606995), Volz et al. (2002) identified KIAA0678. The deduced protein
contains a DnaJ homology domain and a conserved his-pro-asp (HPD) motif
that may be involved in regulation of HSP70 (see HSPA1A; 140550) ATPase
activity.
By searching a database for sequences similar to rat Rme8, Girard et al.
(2005) obtained the full-length sequence for human DNAJC13, which they
called RME8. The deduced 2,243-amino acid protein has a central DnaJ
domain flanked on either side by 2 IWN repeats. It also has 4 potential
clathrin heavy chain (CHC, or CLTC; 118955) interaction motifs. Confocal
immunofluorescence analysis of COS-7 cells and HeLa cells revealed that
endogenous RME8 distributed in a punctate pattern that accumulated in
the perinuclear region and overlapped with endosomal markers. Western
blot analysis of rat tissues and several cell lines, including HEK293
and HeLa cells, detected RME8 at an apparent molecular mass of 220 kD.
Fractionation of rat kidney and protein extraction experiments revealed
that Rme8 is an extrinsic membrane protein associated with microsomes.
GENE FUNCTION
Girard et al. (2005) showed that the isolated DnaJ domain of human RME8
bound rat kidney Hsc70 (HSPA8; 600816) in an ATP-dependent manner.
Knockdown of Rme8 in COS-7 cells disrupted endocytic trafficking of Egfr
(131550), Cimpr (IGF2R; 147280), and cathepsin D (CTSD; 116840).
GENE STRUCTURE
Girard et al. (2005) determined that the DNAJC13 gene contains 56 exons.
MAPPING
By radiation hybrid analysis, Ishikawa et al. (1998) mapped the DNAJC13
gene to chromosome 3. Volz et al. (2002) mapped the DNAJC13 gene to
chromosome 3q21-q22 by genomic sequence analysis. Girard et al. (2005)
mapped the DNAJC13 gene to chromosome 3q22.1 by genomic sequence
analysis.
MOLECULAR GENETICS
For discussion of a possible role of variation in the DNAJC13 gene in
Tourette syndrome/chronic tic disorder, see 137580.
*FIELD* RF
1. Girard, M.; Poupon, V.; Blondeau, F.; McPherson, P. S.: The DnaJ-domain
protein RME-8 functions in endosomal trafficking. J. Biol. Chem. 280:
40135-40143, 2005.
2. Ishikawa, K.; Nagase, T.; Suyama, M.; Miyajima, N.; Tanaka, A.;
Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the coding sequences
of unidentified human genes. X. The complete sequences of 100 new
cDNA clones from brain which can code for large proteins in vitro. DNA
Res. 5: 169-176, 1998.
3. Volz, A.; Melkaoui, R.; Hildebrandt, F.; Omran, H.: Candidate
gene analysis of KIAA0678 encoding a DnaJ-like protein for adolescent
nephronophthisis and Senior-Loken syndrome type 3. Cytogenet. Genome
Res. 97: 163-166, 2002.
*FIELD* CN
Cassandra L. Kniffin - updated: 3/27/2012
*FIELD* CD
Patricia A. Hartz: 11/8/2011
*FIELD* ED
carol: 03/27/2012
ckniffin: 3/8/2012
mgross: 11/8/2011
alopez: 11/8/2011