DJC13_HUMAN
ID DJC13_HUMAN Reviewed; 2243 AA.
AC O75165; Q3L0T1; Q6PI82; Q6UJ77; Q6ZSW1; Q6ZUT5; Q86XG3; Q96DC1; Q9BWK9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 5.
DT 03-AUG-2022, entry version 176.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT 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., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., 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., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., 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 project:
RT 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 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18256511; DOI=10.1247/csf.07045;
RA Fujibayashi A., Taguchi T., Misaki R., Ohtani M., Dohmae N., Takio K.,
RA Yamada M., Gu J., Yamakami M., Fukuda M., Waguri S., Uchiyama Y.,
RA Yoshimori T., Sekiguchi K.;
RT "Human RME-8 is involved in membrane trafficking through early endosomes.";
RL Cell Struct. Funct. 33:35-50(2008).
RN [9]
RP FUNCTION.
RX PubMed=18307993; DOI=10.1016/j.febslet.2008.02.042;
RA Girard M., McPherson P.S.;
RT "RME-8 regulates trafficking of the epidermal growth factor receptor.";
RL FEBS Lett. 582:961-966(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
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).
RN [11]
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., Buerckstuemmer T.,
RA 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 [12]
RP POSSIBLE INVOLVEMENT IN PARK, VARIANT PARK SER-855, VARIANTS GLN-264;
RP ILE-1082 AND LEU-2115, AND CHARACTERIZATION OF VARIANT PARK SER-855.
RX PubMed=24218364; DOI=10.1093/hmg/ddt570;
RA Vilarino-Guell C., Rajput A., Milnerwood A.J., Shah B., Szu-Tu C.,
RA Trinh J., Yu I., Encarnacion M., Munsie L.N., Tapia L., Gustavsson E.K.,
RA Chou P., Tatarnikov I., Evans D.M., Pishotta F.T., Volta M.,
RA Beccano-Kelly D., Thompson C., Lin M.K., Sherman H.E., Han H.J.,
RA Guenther B.L., Wasserman W.W., Bernard V., Ross C.J., Appel-Cresswell S.,
RA Stoessl A.J., Robinson C.A., Dickson D.W., Ross O.A., Wszolek Z.K.,
RA Aasly J.O., Wu R.M., Hentati F., Gibson R.A., McPherson P.S., Girard M.,
RA Rajput M., Rajput A.H., Farrer M.J.;
RT "DNAJC13 mutations in Parkinson disease.";
RL Hum. Mol. Genet. 23:1794-1801(2014).
RN [13]
RP FUNCTION, INTERACTION WITH WASHC2C, AND SUBCELLULAR LOCATION.
RX PubMed=24643499; DOI=10.1242/jcs.144659;
RA Freeman C.L., Hesketh G., Seaman M.N.;
RT "RME-8 coordinates the activity of the WASH complex with the function of
RT the retromer SNX dimer to control endosomal tubulation.";
RL J. Cell Sci. 127:2053-2070(2014).
RN [14]
RP POSSIBLE INVOLVEMENT IN PARK, VARIANTS SER-556; ALA-674; LYS-903; PHE-997;
RP SER-1135; GLY-1291; HIS-1516; GLN-1740; SER-2057 AND TRP-2170, AND VARIANTS
RP PARK LEU-722; SER-855; GLN-1266 AND MET-1895.
RX PubMed=25393719; DOI=10.1002/mds.26064;
RA Gustavsson E.K., Trinh J., Guella I., Vilarino-Gueell C.,
RA Appel-Cresswell S., Stoessl A.J., Tsui J.K., McKeown M., Rajput A.,
RA Rajput A.H., Aasly J.O., Farrer M.J.;
RT "DNAJC13 genetic variants in parkinsonism.";
RL Mov. Disord. 30:273-278(2015).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP DISCUSSION ON POSSIBLE INVOLVEMENT IN PARK.
RX PubMed=27270108; DOI=10.1038/ng.3589;
RA Deng H.X., Shi Y., Yang Y., Ahmeti K.B., Miller N., Huang C., Cheng L.,
RA Zhai H., Deng S., Nuytemans K., Corbett N.J., Kim M.J., Deng H., Tang B.,
RA Yang Z., Xu Y., Chan P., Huang B., Gao X.P., Song Z., Liu Z., Fecto F.,
RA Siddique N., Foroud T., Jankovic J., Ghetti B., Nicholson D.A., Krainc D.,
RA Melen O., Vance J.M., Pericak-Vance M.A., Ma Y.C., Rajput A.H.,
RA Siddique T.;
RT "Identification of TMEM230 mutations in familial Parkinson's disease.";
RL Nat. Genet. 48:733-739(2016).
CC -!- FUNCTION: Involved in membrane trafficking through early endosomes,
CC such as the early endosome to recycling endosome transport implicated
CC in the recycling of transferrin and the early endosome to late endosome
CC transport implicated in degradation of EGF and EGFR (PubMed:18256511,
CC PubMed:18307993). Involved in the regulation of endosomal membrane
CC tubulation and regulates th dynamics of SNX1 on the endosomal membrane;
CC via association with WASHC2 may link the WASH complex to the retromer
CC SNX-BAR subcomplex (PubMed:24643499). {ECO:0000269|PubMed:18256511,
CC ECO:0000269|PubMed:18307993, ECO:0000269|PubMed:24643499}.
CC -!- SUBUNIT: Interacts with WASHC2C; mediates the association with the WASH
CC complex (PubMed:24643499). {ECO:0000269|PubMed:24643499}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:18256511}.
CC Early endosome membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18256511}. Endosome membrane
CC {ECO:0000269|PubMed:24643499}.
CC -!- DISEASE: Parkinson disease (PARK) [MIM:168600]: A complex
CC neurodegenerative disorder characterized by bradykinesia, resting
CC tremor, muscular rigidity and postural instability. Additional features
CC are characteristic postural abnormalities, dysautonomia, dystonic
CC cramps, and dementia. The pathology of Parkinson disease involves the
CC loss of dopaminergic neurons in the substantia nigra and the presence
CC of Lewy bodies (intraneuronal accumulations of aggregated proteins), in
CC surviving neurons in various areas of the brain. The disease is
CC progressive and usually manifests after the age of 50 years, although
CC early-onset cases (before 50 years) are known. The majority of the
CC cases are sporadic suggesting a multifactorial etiology based on
CC environmental and genetic factors. However, some patients present with
CC a positive family history for the disease. Familial forms of the
CC disease usually begin at earlier ages and are associated with atypical
CC clinical features. {ECO:0000269|PubMed:24218364,
CC ECO:0000269|PubMed:25393719}. Note=The gene represented in this entry
CC may be involved in disease pathogenesis. Genetic variants in DNAJC13
CC (PubMed:24218364, PubMed:25393719) and TMEM230 (PubMed:27270108) have
CC been found in the same large multigenerational family with adult-onset
CC Parkinson disease. The pathological role of each gene and therefore the
CC exact molecular basis of the disease is unclear.
CC {ECO:0000305|PubMed:27270108}.
CC -!- CAUTION: In human, WASHC2 has undergone evolutionary duplication giving
CC rise to highly homologous family members. A WASHC2C construct with
CC WASHC2A-specific sequence insertions (of 2 aa and 21 aa length
CC resulting in a construct length of 1341 aa similar to WASHC2A length)
CC has been used to demonstrate the interaction with WASHC2
CC (PubMed:24643499). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH43583.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAA31653.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC86133.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC86835.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC86835.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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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 CCDS; CCDS33857.1; -.
DR PIR; T00361; T00361.
DR RefSeq; NP_056083.3; NM_015268.3.
DR AlphaFoldDB; O75165; -.
DR SMR; O75165; -.
DR BioGRID; 116908; 119.
DR IntAct; O75165; 50.
DR MINT; O75165; -.
DR STRING; 9606.ENSP00000260818; -.
DR iPTMnet; O75165; -.
DR MetOSite; O75165; -.
DR PhosphoSitePlus; O75165; -.
DR SwissPalm; O75165; -.
DR BioMuta; DNAJC13; -.
DR EPD; O75165; -.
DR jPOST; O75165; -.
DR MassIVE; O75165; -.
DR MaxQB; O75165; -.
DR PaxDb; O75165; -.
DR PeptideAtlas; O75165; -.
DR PRIDE; O75165; -.
DR ProteomicsDB; 49830; -.
DR Antibodypedia; 51566; 47 antibodies from 19 providers.
DR Ensembl; ENST00000260818.11; ENSP00000260818.6; ENSG00000138246.17.
DR GeneID; 23317; -.
DR KEGG; hsa:23317; -.
DR MANE-Select; ENST00000260818.11; ENSP00000260818.6; NM_015268.4; NP_056083.3.
DR UCSC; uc003eor.4; human.
DR CTD; 23317; -.
DR DisGeNET; 23317; -.
DR GeneCards; DNAJC13; -.
DR HGNC; HGNC:30343; DNAJC13.
DR HPA; ENSG00000138246; Low tissue specificity.
DR MalaCards; DNAJC13; -.
DR MIM; 168600; phenotype.
DR MIM; 614334; gene.
DR neXtProt; NX_O75165; -.
DR OpenTargets; ENSG00000138246; -.
DR Orphanet; 411602; Hereditary late-onset Parkinson disease.
DR PharmGKB; PA134947358; -.
DR VEuPathDB; HostDB:ENSG00000138246; -.
DR eggNOG; KOG1789; Eukaryota.
DR GeneTree; ENSGT00390000017582; -.
DR HOGENOM; CLU_001238_1_0_1; -.
DR InParanoid; O75165; -.
DR OMA; EITNQWL; -.
DR PhylomeDB; O75165; -.
DR TreeFam; TF105172; -.
DR PathwayCommons; O75165; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; O75165; -.
DR BioGRID-ORCS; 23317; 78 hits in 1074 CRISPR screens.
DR ChiTaRS; DNAJC13; human.
DR GeneWiki; DNAJC13; -.
DR GenomeRNAi; 23317; -.
DR Pharos; O75165; Tbio.
DR PRO; PR:O75165; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O75165; protein.
DR Bgee; ENSG00000138246; Expressed in calcaneal tendon and 207 other tissues.
DR ExpressionAtlas; O75165; baseline and differential.
DR Genevisible; O75165; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:2000641; P:regulation of early endosome to late endosome transport; IMP:UniProtKB.
DR GO; GO:1902954; P:regulation of early endosome to recycling endosome transport; IMP:UniProtKB.
DR CDD; cd06257; DnaJ; 1.
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; IPR044978; GRV2/DNAJC13.
DR InterPro; IPR045802; GRV2/DNAJC13_N.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR InterPro; IPR025640; GYF_2.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR36983; PTHR36983; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF14237; GYF_2; 1.
DR Pfam; PF19432; RME-8_N; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
DR SUPFAM; SSF55277; SSF55277; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Disease variant; Endosome; Membrane;
KW Neurodegeneration; Parkinson disease; Parkinsonism; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..2243
FT /note="DnaJ homolog subfamily C member 13"
FT /id="PRO_0000071072"
FT DOMAIN 1301..1366
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 1..453
FT /note="Involved in membrane association"
FT /evidence="ECO:0000269|PubMed:18256511"
FT MOD_RES 84
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 264
FT /note="E -> Q"
FT /evidence="ECO:0000269|PubMed:24218364"
FT /id="VAR_073784"
FT VARIANT 556
FT /note="L -> S (in dbSNP:rs749000301)"
FT /evidence="ECO:0000269|PubMed:25393719"
FT /id="VAR_076716"
FT VARIANT 674
FT /note="D -> A (in dbSNP:rs199541720)"
FT /evidence="ECO:0000269|PubMed:25393719"
FT /id="VAR_076717"
FT VARIANT 722
FT /note="V -> L (in PARK; unknown pathological significance;
FT dbSNP:rs146930051)"
FT /evidence="ECO:0000269|PubMed:25393719"
FT /id="VAR_076718"
FT VARIANT 855
FT /note="N -> S (in PARK; unknown pathological significance;
FT affects regulation of endosomal membrane trafficking as
FT indicated by accumulation of transferrin in endosomal
FT compartments; dbSNP:rs387907571)"
FT /evidence="ECO:0000269|PubMed:24218364,
FT ECO:0000269|PubMed:25393719"
FT /id="VAR_073785"
FT VARIANT 903
FT /note="R -> K (in dbSNP:rs141952333)"
FT /evidence="ECO:0000269|PubMed:25393719"
FT /id="VAR_076719"
FT VARIANT 997
FT /note="L -> F (in dbSNP:rs752189478)"
FT /evidence="ECO:0000269|PubMed:25393719"
FT /id="VAR_076720"
FT VARIANT 1082
FT /note="T -> I (in dbSNP:rs202127368)"
FT /evidence="ECO:0000269|PubMed:24218364"
FT /id="VAR_073786"
FT VARIANT 1135
FT /note="N -> S (in dbSNP:rs751747947)"
FT /evidence="ECO:0000269|PubMed:25393719"
FT /id="VAR_076721"
FT VARIANT 1266
FT /note="R -> Q (in PARK; sporadic case; unknown pathological
FT significance; dbSNP:rs766013346)"
FT /evidence="ECO:0000269|PubMed:25393719"
FT /id="VAR_076722"
FT VARIANT 1291
FT /note="E -> G (in dbSNP:rs61748101)"
FT /evidence="ECO:0000269|PubMed:25393719"
FT /id="VAR_076723"
FT VARIANT 1463
FT /note="A -> S (in dbSNP:rs3762672)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9734811"
FT /id="VAR_047458"
FT VARIANT 1487
FT /note="F -> C (in dbSNP:rs4405917)"
FT /id="VAR_047459"
FT VARIANT 1515
FT /note="P -> S (in dbSNP:rs55825559)"
FT /id="VAR_061144"
FT VARIANT 1516
FT /note="R -> H (in dbSNP:rs139620588)"
FT /evidence="ECO:0000269|PubMed:25393719"
FT /id="VAR_076724"
FT VARIANT 1740
FT /note="E -> Q (in dbSNP:rs142160751)"
FT /evidence="ECO:0000269|PubMed:25393719"
FT /id="VAR_076725"
FT VARIANT 1895
FT /note="T -> M (in PARK; unknown pathological significance;
FT dbSNP:rs145242123)"
FT /evidence="ECO:0000269|PubMed:25393719"
FT /id="VAR_076726"
FT VARIANT 1995
FT /note="V -> I (in dbSNP:rs10935014)"
FT /id="VAR_047460"
FT VARIANT 2057
FT /note="A -> S (in dbSNP:rs138693725)"
FT /evidence="ECO:0000269|PubMed:25393719"
FT /id="VAR_076727"
FT VARIANT 2115
FT /note="R -> L (in dbSNP:rs770715465)"
FT /evidence="ECO:0000269|PubMed:24218364"
FT /id="VAR_073787"
FT VARIANT 2170
FT /note="L -> W (in dbSNP:rs140537885)"
FT /evidence="ECO:0000269|PubMed:25393719"
FT /id="VAR_076728"
FT CONFLICT 476
FT /note="D -> E (in Ref. 2; BAA31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="N -> D (in Ref. 5; AAH43583)"
FT /evidence="ECO:0000305"
FT CONFLICT 1097
FT /note="I -> T (in Ref. 6; BAC86133)"
FT /evidence="ECO:0000305"
FT CONFLICT 1148
FT /note="T -> I (in Ref. 6; BAC86835)"
FT /evidence="ECO:0000305"
FT CONFLICT 1227
FT /note="Q -> H (in Ref. 2; BAA31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 1230
FT /note="T -> A (in Ref. 6; BAC86835)"
FT /evidence="ECO:0000305"
FT CONFLICT 1269
FT /note="D -> N (in Ref. 6; BAC86133)"
FT /evidence="ECO:0000305"
FT CONFLICT 2041
FT /note="L -> P (in Ref. 6; BAC86835)"
FT /evidence="ECO:0000305"
FT CONFLICT 2091
FT /note="T -> A (in Ref. 6; BAC86835)"
FT /evidence="ECO:0000305"
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
