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Q8IXB1

- DJC10_HUMAN

UniProt

Q8IXB1 - DJC10_HUMAN

Protein

DnaJ homolog subfamily C member 10

Gene

DNAJC10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, but to facilitate the release of DNAJC10 from its substrate. Promotes apoptotic signaling pathway in response to endoplasmic reticulum stress.4 Publications

    GO - Molecular functioni

    1. ATPase activator activity Source: UniProtKB
    2. ATPase binding Source: UniProtKB
    3. chaperone binding Source: UniProtKB
    4. disulfide oxidoreductase activity Source: UniProtKB
    5. Hsp70 protein binding Source: UniProtKB
    6. misfolded protein binding Source: UniProtKB
    7. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. protein disulfide oxidoreductase activity Source: UniProtKB

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
    3. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
    4. negative regulation of protein phosphorylation Source: UniProtKB
    5. positive regulation of ATPase activity Source: UniProtKB
    6. protein folding in endoplasmic reticulum Source: UniProtKB
    7. response to endoplasmic reticulum stress Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DnaJ homolog subfamily C member 10 (EC:1.8.4.-)
    Alternative name(s):
    Endoplasmic reticulum DNA J domain-containing protein 5
    Short name:
    ER-resident protein ERdj5
    Short name:
    ERdj5
    Macrothioredoxin
    Short name:
    MTHr
    Gene namesi
    Name:DNAJC10
    Synonyms:ERDJ5
    ORF Names:UNQ495/PRO1012
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:24637. DNAJC10.

    Subcellular locationi

    Endoplasmic reticulum lumen 2 PublicationsPROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum chaperone complex Source: UniProtKB
    3. endoplasmic reticulum lumen Source: UniProtKB
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi63 – 631H → Q: Prevents interaction with HSPA5, leading to prolonged interaction with substrate proteins. 1 Publication
    Mutagenesisi161 – 1611C → A: Abolishes disulfide reductase activity; when associated with A-483; A-591 and A-703. 1 Publication
    Mutagenesisi483 – 4831C → A: Abolishes disulfide reductase activity; when associated with A-161; A-591 and A-703. 1 Publication
    Mutagenesisi591 – 5911C → A: Abolishes disulfide reductase activity; when associated with A-161; A-483 and A-703. 1 Publication
    Mutagenesisi703 – 7031C → A: Abolishes disulfide reductase activity; when associated with A-161; A-483 and A-591. 1 Publication

    Organism-specific databases

    PharmGKBiPA134917195.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Sequence AnalysisAdd
    BLAST
    Chaini33 – 793761DnaJ homolog subfamily C member 10PRO_0000281483Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi158 ↔ 161Redox-active
    Disulfide bondi480 ↔ 483Redox-active
    Glycosylationi530 – 5301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi588 ↔ 591Redox-active
    Disulfide bondi700 ↔ 703Redox-active

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ8IXB1.
    PaxDbiQ8IXB1.
    PRIDEiQ8IXB1.

    PTM databases

    PhosphoSiteiQ8IXB1.

    Expressioni

    Inductioni

    By endoplasmic reticulum stress.

    Gene expression databases

    ArrayExpressiQ8IXB1.
    BgeeiQ8IXB1.
    GenevestigatoriQ8IXB1.

    Organism-specific databases

    HPAiHPA031111.

    Interactioni

    Subunit structurei

    Interacts with EDEM1 By similarity. Interacts with HSPA5 (via its J domain).By similarity2 Publications

    Protein-protein interaction databases

    BioGridi119947. 20 interactions.
    DIPiDIP-48947N.
    IntActiQ8IXB1. 10 interactions.
    MINTiMINT-1451539.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IXB1.
    SMRiQ8IXB1. Positions 34-782.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 10066JPROSITE-ProRule annotationAdd
    BLAST
    Domaini130 – 232103Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini454 – 553100Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini557 – 662106Thioredoxin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini671 – 778108Thioredoxin 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni235 – 350116Trxb 1Add
    BLAST
    Regioni348 – 463116Trxb 2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi790 – 7934Prevents secretion from ERPROSITE-ProRule annotation

    Domaini

    The thioredoxin-like regions Trxb 1 and 2 lack a redox-active CXXC motif.By similarity
    Thioredoxin domains 3 and 4 are the primary reductase domains.By similarity

    Sequence similaritiesi

    Contains 1 J domain.PROSITE-ProRule annotation
    Contains 4 thioredoxin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG0526.
    HOVERGENiHBG057048.
    KOiK09530.
    OMAiYPSLFIF.
    OrthoDBiEOG7RZ5QH.
    PhylomeDBiQ8IXB1.
    TreeFamiTF105169.

    Family and domain databases

    Gene3Di1.10.287.110. 1 hit.
    3.40.30.10. 5 hits.
    InterProiIPR001623. DnaJ_domain.
    IPR021170. DnaJ_homolog_subfam-C.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00226. DnaJ. 1 hit.
    PF00085. Thioredoxin. 4 hits.
    [Graphical view]
    PIRSFiPIRSF037293. DnaJ_homolog_subfam-C. 1 hit.
    PRINTSiPR00625. JDOMAIN.
    SMARTiSM00271. DnaJ. 1 hit.
    [Graphical view]
    SUPFAMiSSF46565. SSF46565. 1 hit.
    SSF52833. SSF52833. 6 hits.
    PROSITEiPS50076. DNAJ_2. 1 hit.
    PS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IXB1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGVWLNKDDY IRDLKRIILC FLIVYMAILV GTDQDFYSLL GVSKTASSRE    50
    IRQAFKKLAL KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG 100
    EKGLEDNQGG QYESWNYYRY DFGIYDDDPE IITLERREFD AAVNSGELWF 150
    VNFYSPGCSH CHDLAPTWRD FAKEVDGLLR IGAVNCGDDR MLCRMKGVNS 200
    YPSLFIFRSG MAPVKYHGDR SKESLVSFAM QHVRSTVTEL WTGNFVNSIQ 250
    TAFAAGIGWL ITFCSKGGDC LTSQTRLRLS GMLDGLVNVG WMDCATQDNL 300
    CKSLDITTST TAYFPPGATL NNKEKNSILF LNSLDAKEIY LEVIHNLPDF 350
    ELLSANTLED RLAHHRWLLF FHFGKNENSN DPELKKLKTL LKNDHIQVGR 400
    FDCSSAPDIC SNLYVFQPSL AVFKGQGTKE YEIHHGKKIL YDILAFAKES 450
    VNSHVTTLGP QNFPANDKEP WLVDFFAPWC PPCRALLPEL RRASNLLYGQ 500
    LKFGTLDCTV HEGLCNMYNI QAYPTTVVFN QSNIHEYEGH HSAEQILEFI 550
    EDLMNPSVVS LTPTTFNELV TQRKHNEVWM VDFYSPWCHP CQVLMPEWKR 600
    MARTLTGLIN VGSIDCQQYH SFCAQENVQR YPEIRFFPPK SNKAYHYHSY 650
    NGWNRDAYSL RIWGLGFLPQ VSTDLTPQTF SEKVLQGKNH WVIDFYAPWC 700
    GPCQNFAPEF ELLARMIKGK VKAGKVDCQA YAQTCQKAGI RAYPTVKFYF 750
    YERAKRNFQE EQINTRDAKA IAALISEKLE TLRNQGKRNK DEL 793
    Length:793
    Mass (Da):91,080
    Last modified:April 3, 2007 - v2
    Checksum:iBD39B64325432D5D
    GO
    Isoform 2 (identifier: Q8IXB1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         284-329: Missing.

    Show »
    Length:747
    Mass (Da):86,136
    Checksum:iD9F26A53E1B35455
    GO
    Isoform 3 (identifier: Q8IXB1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         330-332: FLN → LLH
         333-793: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:332
    Mass (Da):37,682
    Checksum:i256FEF2695B28BE7
    GO

    Sequence cautioni

    The sequence BAB55121.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC11281.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51L → S in AAM09527. (PubMed:14587667)Curated
    Sequence conflicti5 – 51L → S in BAB55304. (PubMed:14702039)Curated
    Sequence conflicti213 – 2131P → A in AAN73271. (PubMed:12411443)Curated
    Sequence conflicti356 – 3594NTLE → KRVK in AAN73271. (PubMed:12411443)Curated
    Sequence conflicti446 – 4461F → S in BAB55121. (PubMed:14702039)Curated
    Sequence conflicti565 – 5651T → A in CAD89982. (PubMed:17974005)Curated
    Sequence conflicti633 – 6331E → K in CAB70858. (PubMed:17974005)Curated
    Sequence conflicti755 – 7551K → N in BAB55304. (PubMed:14702039)Curated
    Sequence conflicti771 – 7711I → T in CAD89982. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti76 – 761D → N.2 Publications
    Corresponds to variant rs6729801 [ dbSNP | Ensembl ].
    VAR_031247
    Natural varianti347 – 3471L → I.
    Corresponds to variant rs13414223 [ dbSNP | Ensembl ].
    VAR_048912
    Natural varianti414 – 4141Y → C.
    Corresponds to variant rs11681366 [ dbSNP | Ensembl ].
    VAR_031248
    Natural varianti646 – 6461H → Q.3 Publications
    Corresponds to variant rs288334 [ dbSNP | Ensembl ].
    VAR_031249

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei284 – 32946Missing in isoform 2. 2 PublicationsVSP_024011Add
    BLAST
    Alternative sequencei330 – 3323FLN → LLH in isoform 3. 1 PublicationVSP_054434
    Alternative sequencei333 – 793461Missing in isoform 3. 1 PublicationVSP_054435Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038503 mRNA. Translation: AAN73271.1.
    AF490904 mRNA. Translation: AAM09527.1.
    AY358577 mRNA. Translation: AAQ88940.1.
    AK027450 mRNA. Translation: BAB55121.1. Different initiation.
    AK027647 mRNA. Translation: BAB55263.1.
    AK027696 mRNA. Translation: BAB55304.1.
    AC073951 Genomic DNA. Translation: AAX88931.1.
    AC105396 Genomic DNA. Translation: AAY24240.1.
    CH471058 Genomic DNA. Translation: EAX10960.1.
    CH471058 Genomic DNA. Translation: EAX10963.1.
    BC107425 mRNA. Translation: AAI07426.1.
    BC117299 mRNA. Translation: AAI17300.1.
    BC126168 mRNA. Translation: AAI26169.1.
    AL137648 mRNA. Translation: CAB70858.1.
    AL832646 mRNA. Translation: CAD89982.1.
    AK074905 mRNA. Translation: BAC11281.1. Different initiation.
    CCDSiCCDS33345.1. [Q8IXB1-1]
    PIRiT46333.
    RefSeqiNP_001258510.1. NM_001271581.1. [Q8IXB1-2]
    NP_061854.1. NM_018981.2. [Q8IXB1-1]
    UniGeneiHs.516632.
    Hs.744512.

    Genome annotation databases

    EnsembliENST00000264065; ENSP00000264065; ENSG00000077232. [Q8IXB1-1]
    ENST00000537515; ENSP00000441560; ENSG00000077232. [Q8IXB1-3]
    GeneIDi54431.
    KEGGihsa:54431.
    UCSCiuc002uow.2. human. [Q8IXB1-1]
    uc002uoz.2. human. [Q8IXB1-2]

    Polymorphism databases

    DMDMi142981524.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038503 mRNA. Translation: AAN73271.1 .
    AF490904 mRNA. Translation: AAM09527.1 .
    AY358577 mRNA. Translation: AAQ88940.1 .
    AK027450 mRNA. Translation: BAB55121.1 . Different initiation.
    AK027647 mRNA. Translation: BAB55263.1 .
    AK027696 mRNA. Translation: BAB55304.1 .
    AC073951 Genomic DNA. Translation: AAX88931.1 .
    AC105396 Genomic DNA. Translation: AAY24240.1 .
    CH471058 Genomic DNA. Translation: EAX10960.1 .
    CH471058 Genomic DNA. Translation: EAX10963.1 .
    BC107425 mRNA. Translation: AAI07426.1 .
    BC117299 mRNA. Translation: AAI17300.1 .
    BC126168 mRNA. Translation: AAI26169.1 .
    AL137648 mRNA. Translation: CAB70858.1 .
    AL832646 mRNA. Translation: CAD89982.1 .
    AK074905 mRNA. Translation: BAC11281.1 . Different initiation.
    CCDSi CCDS33345.1. [Q8IXB1-1 ]
    PIRi T46333.
    RefSeqi NP_001258510.1. NM_001271581.1. [Q8IXB1-2 ]
    NP_061854.1. NM_018981.2. [Q8IXB1-1 ]
    UniGenei Hs.516632.
    Hs.744512.

    3D structure databases

    ProteinModelPortali Q8IXB1.
    SMRi Q8IXB1. Positions 34-782.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119947. 20 interactions.
    DIPi DIP-48947N.
    IntActi Q8IXB1. 10 interactions.
    MINTi MINT-1451539.

    PTM databases

    PhosphoSitei Q8IXB1.

    Polymorphism databases

    DMDMi 142981524.

    Proteomic databases

    MaxQBi Q8IXB1.
    PaxDbi Q8IXB1.
    PRIDEi Q8IXB1.

    Protocols and materials databases

    DNASUi 54431.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264065 ; ENSP00000264065 ; ENSG00000077232 . [Q8IXB1-1 ]
    ENST00000537515 ; ENSP00000441560 ; ENSG00000077232 . [Q8IXB1-3 ]
    GeneIDi 54431.
    KEGGi hsa:54431.
    UCSCi uc002uow.2. human. [Q8IXB1-1 ]
    uc002uoz.2. human. [Q8IXB1-2 ]

    Organism-specific databases

    CTDi 54431.
    GeneCardsi GC02P183580.
    HGNCi HGNC:24637. DNAJC10.
    HPAi HPA031111.
    MIMi 607987. gene.
    neXtProti NX_Q8IXB1.
    PharmGKBi PA134917195.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0526.
    HOVERGENi HBG057048.
    KOi K09530.
    OMAi YPSLFIF.
    OrthoDBi EOG7RZ5QH.
    PhylomeDBi Q8IXB1.
    TreeFami TF105169.

    Miscellaneous databases

    GeneWikii DNAJC10.
    GenomeRNAii 54431.
    NextBioi 56629.
    PROi Q8IXB1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IXB1.
    Bgeei Q8IXB1.
    Genevestigatori Q8IXB1.

    Family and domain databases

    Gene3Di 1.10.287.110. 1 hit.
    3.40.30.10. 5 hits.
    InterProi IPR001623. DnaJ_domain.
    IPR021170. DnaJ_homolog_subfam-C.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00226. DnaJ. 1 hit.
    PF00085. Thioredoxin. 4 hits.
    [Graphical view ]
    PIRSFi PIRSF037293. DnaJ_homolog_subfam-C. 1 hit.
    PRINTSi PR00625. JDOMAIN.
    SMARTi SM00271. DnaJ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46565. SSF46565. 1 hit.
    SSF52833. SSF52833. 6 hits.
    PROSITEi PS50076. DNAJ_2. 1 hit.
    PS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress."
      Cunnea P.M., Miranda-Vizuete A., Bertoli G., Simmen T., Damdimopoulos A.E., Hermann S., Leinonen S., Huikko M.P., Gustafsson J.-A., Sitia R., Spyrou G.
      J. Biol. Chem. 278:1059-1066(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSPA5.
    2. "Cloning and identification of a novel cDNA which encodes a putative protein with a DnaJ domain and a thioredoxin active motif, human macrothioredoxin."
      Gu S.-H., Chen J.-Z., Ying K., Wang S., Jin W., Qian J., Zhao E.-P., Xie Y., Mao Y.-M.
      Biochem. Genet. 41:245-253(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ASN-76.
      Tissue: Fetal brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLN-646.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT GLN-646.
      Tissue: Colon and Placenta.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-793 (ISOFORM 1), VARIANTS ASN-76 AND GLN-646.
      Tissue: Spinal cord and Testis.
    9. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 414-793.
      Tissue: Teratocarcinoma.
    10. "ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C."
      Dong M., Bridges J.P., Apsley K., Xu Y., Weaver T.E.
      Mol. Biol. Cell 19:2620-2630(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "ERdj5 sensitizes neuroblastoma cells to endoplasmic reticulum stress-induced apoptosis."
      Thomas C.G., Spyrou G.
      J. Biol. Chem. 284:6282-6290(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor."
      Oka O.B., Pringle M.A., Schopp I.M., Braakman I., Bulleid N.J.
      Mol. Cell 50:793-804(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSPA5, MUTAGENESIS OF HIS-63; CYS-161; CYS-483; CYS-591 AND CYS-703.

    Entry informationi

    Entry nameiDJC10_HUMAN
    AccessioniPrimary (citable) accession number: Q8IXB1
    Secondary accession number(s): Q17RJ6
    , Q3B7W8, Q4ZG06, Q53QT7, Q6UWZ6, Q86T61, Q8NC82, Q8TD87, Q96K38, Q96K44, Q96K54, Q9NSY6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3