ID   DJC13_HUMAN             Reviewed;        2243 AA.
AC   O75165; Q3L0T1; Q6PI82; Q6UJ77; Q6ZSW1; Q6ZUT5; Q86XG3; Q96DC1;
AC   Q9BWK9;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 4.
DT   15-DEC-2009, entry version 72.
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], AND VARIANT ALA-1463.
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].
RC   TISSUE=Brain;
RX   MEDLINE=98403880; 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 MRNA] OF 1-747 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 617-2243.
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   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1843, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1701, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18187866; DOI=10.2116/analsci.24.161;
RA   Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
RT   "Automated phosphoproteome analysis for cultured cancer cells by two-
RT   dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
RL   Anal. Sci. 24:161-166(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2151, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [10]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [11]
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., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH43583.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 748;
CC       Sequence=BAC86835.1; Type=Erroneous termination; Positions=1651; Note=Translated as Glu;
CC       Sequence=BAC86835.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR   EMBL; AY779857; AAV41096.1; -; mRNA.
DR   EMBL; AB014578; BAA31653.2; ALT_INIT; mRNA.
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   IPI; IPI00307259; -.
DR   PIR; T00361; T00361.
DR   RefSeq; NP_056083.3; -.
DR   UniGene; Hs.12707; -.
DR   PhosphoSite; O75165; -.
DR   PRIDE; O75165; -.
DR   Ensembl; ENST00000260818; ENSP00000260818; ENSG00000138246; Homo sapiens.
DR   GeneID; 23317; -.
DR   KEGG; hsa:23317; -.
DR   CTD; 23317; -.
DR   GeneCards; GC03P133665; -.
DR   HGNC; HGNC:30343; DNAJC13.
DR   PharmGKB; PA134947358; -.
DR   HOVERGEN; O75165; -.
DR   InParanoid; O75165; -.
DR   ArrayExpress; O75165; -.
DR   Bgee; O75165; -.
DR   CleanEx; HS_DNAJC13; -.
DR   Genevestigator; O75165; -.
DR   GermOnline; ENSG00000138246; Homo sapiens.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR015609; Hsp40/DnaJ_Rel.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   PANTHER; PTHR11821; Hsp40/DnaJ_Rel; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   SMART; SM00271; DnaJ; 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; Phosphoprotein;
KW   Polymorphism.
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   MOD_RES    1701   1701       Phosphothreonine.
FT   MOD_RES    1843   1843       Phosphoserine.
FT   MOD_RES    2151   2151       Phosphoserine.
FT   VARIANT    1463   1463       S -> A (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. 3; BAA31653).
FT   CONFLICT    562    562       N -> D (in Ref. 4; AAH43583).
FT   CONFLICT   1097   1097       I -> T (in Ref. 5; BAC86133).
FT   CONFLICT   1148   1148       T -> I (in Ref. 5; BAC86835).
FT   CONFLICT   1227   1227       Q -> H (in Ref. 3; BAA31653).
FT   CONFLICT   1230   1230       T -> A (in Ref. 5; BAC86835).
FT   CONFLICT   1269   1269       D -> N (in Ref. 5; BAC86133).
FT   CONFLICT   2041   2041       L -> P (in Ref. 5; BAC86835).
FT   CONFLICT   2091   2091       T -> A (in Ref. 5; BAC86835).
SQ   SEQUENCE   2243 AA;  254431 MW;  5EF0378B6E5FF807 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 TRSSKPSDMS 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
//