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Q8IXB1

- DJC10_HUMAN

UniProt

Q8IXB1 - DJC10_HUMAN

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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

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 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ8IXB1.
ExpressionAtlasiQ8IXB1. baseline and differential.
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.
GeneTreeiENSGT00730000110455.
HOVERGENiHBG057048.
InParanoidiQ8IXB1.
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

        10         20         30         40         50
MGVWLNKDDY IRDLKRIILC FLIVYMAILV GTDQDFYSLL GVSKTASSRE
60 70 80 90 100
IRQAFKKLAL KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG
110 120 130 140 150
EKGLEDNQGG QYESWNYYRY DFGIYDDDPE IITLERREFD AAVNSGELWF
160 170 180 190 200
VNFYSPGCSH CHDLAPTWRD FAKEVDGLLR IGAVNCGDDR MLCRMKGVNS
210 220 230 240 250
YPSLFIFRSG MAPVKYHGDR SKESLVSFAM QHVRSTVTEL WTGNFVNSIQ
260 270 280 290 300
TAFAAGIGWL ITFCSKGGDC LTSQTRLRLS GMLDGLVNVG WMDCATQDNL
310 320 330 340 350
CKSLDITTST TAYFPPGATL NNKEKNSILF LNSLDAKEIY LEVIHNLPDF
360 370 380 390 400
ELLSANTLED RLAHHRWLLF FHFGKNENSN DPELKKLKTL LKNDHIQVGR
410 420 430 440 450
FDCSSAPDIC SNLYVFQPSL AVFKGQGTKE YEIHHGKKIL YDILAFAKES
460 470 480 490 500
VNSHVTTLGP QNFPANDKEP WLVDFFAPWC PPCRALLPEL RRASNLLYGQ
510 520 530 540 550
LKFGTLDCTV HEGLCNMYNI QAYPTTVVFN QSNIHEYEGH HSAEQILEFI
560 570 580 590 600
EDLMNPSVVS LTPTTFNELV TQRKHNEVWM VDFYSPWCHP CQVLMPEWKR
610 620 630 640 650
MARTLTGLIN VGSIDCQQYH SFCAQENVQR YPEIRFFPPK SNKAYHYHSY
660 670 680 690 700
NGWNRDAYSL RIWGLGFLPQ VSTDLTPQTF SEKVLQGKNH WVIDFYAPWC
710 720 730 740 750
GPCQNFAPEF ELLARMIKGK VKAGKVDCQA YAQTCQKAGI RAYPTVKFYF
760 770 780 790
YERAKRNFQE EQINTRDAKA IAALISEKLE TLRNQGKRNK DEL
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.Curated
The sequence BAC11281.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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]
CCDS74613.1. [Q8IXB1-2]
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]
ENST00000616986; ENSP00000479930; ENSG00000077232. [Q8IXB1-2]
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:
EMBLi
GenBanki
DDBJi
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 ]
CCDS74613.1. [Q8IXB1-2 ]
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 ]
ENST00000616986 ; ENSP00000479930 ; ENSG00000077232 . [Q8IXB1-2 ]
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.
GeneTreei ENSGT00730000110455.
HOVERGENi HBG057048.
InParanoidi Q8IXB1.
KOi K09530.
OMAi YPSLFIF.
OrthoDBi EOG7RZ5QH.
PhylomeDBi Q8IXB1.
TreeFami TF105169.

Miscellaneous databases

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

Gene expression databases

Bgeei Q8IXB1.
ExpressionAtlasi Q8IXB1. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 114 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