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Q9DC23

- DJC10_MOUSE

UniProt

Q9DC23 - DJC10_MOUSE

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Protein

DnaJ homolog subfamily C member 10

Gene

Dnajc10

Organism
Mus musculus (Mouse)
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. misfolded protein binding Source: UniProtKB
  6. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: UniProtKB
  7. 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
Endoplasmic reticulum DnaJ-PDI fusion protein 1
J domain-containing protein disulfide isomerase-like protein
Short name:
J domain-containing PDI-like protein
Short name:
JPDI
Gene namesi
Name:Dnajc10
Synonyms:Erdj5, Jpdi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1914111. Dnajc10.

Subcellular locationi

Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum chaperone complex Source: UniProtKB
  3. endoplasmic reticulum lumen Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Mice are viable and healthy but show enhanced endoplasmic reticulum stress response in the salivary gland.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi158 – 1581C → A: Abolishes disulfide reductase activity; when associated with A-161; A-480; A-483; A-588; A-591; A-700 and A-703. 2 Publications
Mutagenesisi161 – 1611C → A: Abolishes disulfide reductase activity; when associated with A-158; A-480; A-483; A-588; A-591; A-700 and A-703. 2 Publications
Mutagenesisi480 – 4801C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-483; A-588; A-591; A-700 and A-703. 2 Publications
Mutagenesisi483 – 4831C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-588; A-591; A-700 and A-703. 2 Publications
Mutagenesisi588 – 5881C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-591; A-700 and A-703. 2 Publications
Mutagenesisi591 – 5911C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-700 and A-703. 2 Publications
Mutagenesisi700 – 7001C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-591 and A-703. 2 Publications
Mutagenesisi703 – 7031C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-591 and A-700. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence AnalysisAdd
BLAST
Chaini33 – 793761DnaJ homolog subfamily C member 10PRO_0000281484Add
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

MaxQBiQ9DC23.
PaxDbiQ9DC23.
PRIDEiQ9DC23.

PTM databases

PhosphoSiteiQ9DC23.

Expressioni

Tissue specificityi

Ubiquitous. Particularly abundant in secretory tissues. Ubiquitous in fetal tissues and tumor tissues. Higher expression in fetal tissues than in adult tissues. Expressed in testis, pancreas, fetal thymus and fetal kidney. High expression in heart, liver, kidney, and testis. Low expression in spleen and skeletal muscle.2 Publications

Gene expression databases

BgeeiQ9DC23.
CleanExiMM_DNAJC10.
ExpressionAtlasiQ9DC23. baseline and differential.
GenevestigatoriQ9DC23.

Interactioni

Subunit structurei

Interacts with HSPA5 (via its J domain). Interacts with EDEM1.3 Publications

Protein-protein interaction databases

BioGridi211769. 2 interactions.

Structurei

Secondary structure

1
793
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 405Combined sources
Helixi48 – 6215Combined sources
Helixi64 – 663Combined sources
Helixi73 – 8715Combined sources
Helixi90 – 9910Combined sources
Turni100 – 1034Combined sources
Helixi115 – 1206Combined sources
Beta strandi121 – 1233Combined sources
Turni124 – 1274Combined sources
Beta strandi131 – 1333Combined sources
Helixi136 – 14510Combined sources
Beta strandi149 – 1546Combined sources
Helixi159 – 17416Combined sources
Turni175 – 1784Combined sources
Beta strandi179 – 1857Combined sources
Turni186 – 1883Combined sources
Helixi190 – 1956Combined sources
Beta strandi200 – 2078Combined sources
Helixi222 – 23413Combined sources
Beta strandi237 – 2393Combined sources
Helixi242 – 25514Combined sources
Beta strandi258 – 2647Combined sources
Helixi273 – 28210Combined sources
Turni283 – 2864Combined sources
Beta strandi287 – 2937Combined sources
Turni294 – 2963Combined sources
Helixi298 – 3014Combined sources
Beta strandi311 – 3144Combined sources
Turni322 – 3243Combined sources
Helixi325 – 3273Combined sources
Beta strandi328 – 3314Combined sources
Helixi336 – 34611Combined sources
Helixi355 – 3628Combined sources
Beta strandi365 – 3728Combined sources
Helixi382 – 3865Combined sources
Helixi387 – 3915Combined sources
Helixi392 – 3943Combined sources
Beta strandi396 – 4027Combined sources
Helixi403 – 4053Combined sources
Helixi407 – 4126Combined sources
Beta strandi419 – 4268Combined sources
Beta strandi429 – 4335Combined sources
Helixi440 – 45112Combined sources
Beta strandi455 – 4573Combined sources
Turni460 – 4623Combined sources
Beta strandi471 – 4766Combined sources
Helixi481 – 49616Combined sources
Turni497 – 5004Combined sources
Beta strandi502 – 5076Combined sources
Turni508 – 5103Combined sources
Helixi512 – 5176Combined sources
Beta strandi522 – 5309Combined sources
Beta strandi533 – 5375Combined sources
Helixi543 – 55412Combined sources
Beta strandi557 – 5604Combined sources
Helixi563 – 5697Combined sources
Turni570 – 5723Combined sources
Beta strandi579 – 5846Combined sources
Helixi589 – 60517Combined sources
Turni606 – 6083Combined sources
Beta strandi609 – 6157Combined sources
Turni616 – 6194Combined sources
Helixi620 – 6256Combined sources
Beta strandi630 – 6378Combined sources
Beta strandi641 – 6433Combined sources
Helixi657 – 6659Combined sources
Beta strandi672 – 6743Combined sources
Helixi677 – 6837Combined sources
Turni684 – 6863Combined sources
Beta strandi691 – 6966Combined sources
Helixi701 – 71717Combined sources
Turni718 – 7203Combined sources
Beta strandi722 – 7276Combined sources
Turni728 – 7303Combined sources
Helixi732 – 7376Combined sources
Beta strandi742 – 75211Combined sources
Helixi753 – 7553Combined sources
Beta strandi757 – 7637Combined sources
Helixi768 – 78013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3APOX-ray2.40A33-793[»]
3APQX-ray1.84A/B34-242[»]
3APSX-ray1.90A/B668-789[»]
ProteinModelPortaliQ9DC23.
SMRiQ9DC23. Positions 34-782.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9DC23.

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 – 665109Thioredoxin 3PROSITE-ProRule annotationAdd
BLAST
Domaini671 – 776106Thioredoxin 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

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

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.
HOGENOMiHOG000231882.
HOVERGENiHBG057048.
InParanoidiQ9DC23.
KOiK09530.
OMAiYPSLFIF.
OrthoDBiEOG7RZ5QH.
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]

Sequencei

Sequence statusi: Complete.

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

Q9DC23-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVWLNKDDF IRDLKRISLC LLILYVVVVV GTDQNFYSLL GVSKTASSRE
60 70 80 90 100
IRQAFKKLAL KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG
110 120 130 140 150
EKGLEDNQGG QYESWSYYRY DFGIYDDDPE IITLERREFD AAVNSGELWF
160 170 180 190 200
VNFYSPGCSH CHDLAPTWRE FAKEVDGLLR IGAVNCGDDR MLCRMKGVNS
210 220 230 240 250
YPSLFIFRSG MAAVKYNGDR SKESLVAFAM QHVRSTVTEL STGNFVNAIE
260 270 280 290 300
TAFAAGVGWL ITFCSKGEDC LTSQTRLRLS GMLDGLVNVG WVDCDAQDSL
310 320 330 340 350
CKSLDTTAST TAYFPPGATL NDREKSSVLF LNSLDAKEIY MEIIHNLPDF
360 370 380 390 400
ELLSANQLED RLAHHRWLVF FHFGKNENAN DPELKKLKTL LKNEHIQVGR
410 420 430 440 450
FDCSSAPGIC SDLYVFQPCL AVFKGQGTKE YEIHHGKKIL YDILAFAKES
460 470 480 490 500
VNSHVTTLGP QNFPASDKEP WLVDFFAPWC PPCRALLPEL RKASTLLYGQ
510 520 530 540 550
LKVGTLDCTI HEGLCNMYNI QAYPTTVVFN QSSIHEYEGH HSAEQILEFI
560 570 580 590 600
EDLRNPSVVS LTPSTFNELV KQRKHDEVWM VDFYSPWCHP CQVLMPEWKR
610 620 630 640 650
MARTLTGLIN VGSVDCQQYH SFCTQENVQR YPEIRFYPQK SSKAYQYHSY
660 670 680 690 700
NGWNRDAYSL RSWGLGFLPQ ASIDLTPQTF NEKVLQGKTH WVVDFYAPWC
710 720 730 740 750
GPCQNFAPEF ELLARMIKGK VRAGKVDCQA YPQTCQKAGI KAYPSVKLYQ
760 770 780 790
YERAKKSIWE EQINSRDAKT IAALIYGKLE TLQSQVKRNK DEL
Length:793
Mass (Da):90,583
Last modified:July 27, 2011 - v2
Checksum:i00C88EF3F5497BE1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911D → H in BAB23413. (PubMed:16141072)Curated
Sequence conflicti310 – 3101T → A in AAQ14555. 1 PublicationCurated
Sequence conflicti324 – 3241E → G in AAH33461. (PubMed:19468303)Curated
Sequence conflicti433 – 4331I → T in AAH33461. (PubMed:19468303)Curated
Sequence conflicti538 – 5381E → G in AAQ14555. 1 PublicationCurated
Sequence conflicti651 – 6522NG → RP in AAQ14555. 1 PublicationCurated
Sequence conflicti654 – 6541N → NS in AAN73273. (PubMed:12411443)Curated
Sequence conflicti680 – 6801F → FR in AAN73273. (PubMed:12411443)Curated
Sequence conflicti767 – 7671D → M in AAQ14555. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF255459 mRNA. Translation: AAN73273.1.
AF314002 mRNA. Translation: AAQ14555.1.
AK004617 mRNA. Translation: BAB23413.1.
AL928587 Genomic DNA. Translation: CAM19646.1.
BC002207 mRNA. Translation: AAH02207.1.
BC033461 mRNA. Translation: AAH33461.1.
CCDSiCCDS38159.1.
RefSeqiNP_077143.2. NM_024181.2.
UniGeneiMm.21762.

Genome annotation databases

EnsembliENSMUST00000028392; ENSMUSP00000028392; ENSMUSG00000027006.
GeneIDi66861.
KEGGimmu:66861.
UCSCiuc008khj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF255459 mRNA. Translation: AAN73273.1 .
AF314002 mRNA. Translation: AAQ14555.1 .
AK004617 mRNA. Translation: BAB23413.1 .
AL928587 Genomic DNA. Translation: CAM19646.1 .
BC002207 mRNA. Translation: AAH02207.1 .
BC033461 mRNA. Translation: AAH33461.1 .
CCDSi CCDS38159.1.
RefSeqi NP_077143.2. NM_024181.2.
UniGenei Mm.21762.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3APO X-ray 2.40 A 33-793 [» ]
3APQ X-ray 1.84 A/B 34-242 [» ]
3APS X-ray 1.90 A/B 668-789 [» ]
ProteinModelPortali Q9DC23.
SMRi Q9DC23. Positions 34-782.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 211769. 2 interactions.

PTM databases

PhosphoSitei Q9DC23.

Proteomic databases

MaxQBi Q9DC23.
PaxDbi Q9DC23.
PRIDEi Q9DC23.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028392 ; ENSMUSP00000028392 ; ENSMUSG00000027006 .
GeneIDi 66861.
KEGGi mmu:66861.
UCSCi uc008khj.1. mouse.

Organism-specific databases

CTDi 54431.
MGIi MGI:1914111. Dnajc10.

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00730000110455.
HOGENOMi HOG000231882.
HOVERGENi HBG057048.
InParanoidi Q9DC23.
KOi K09530.
OMAi YPSLFIF.
OrthoDBi EOG7RZ5QH.
TreeFami TF105169.

Miscellaneous databases

EvolutionaryTracei Q9DC23.
NextBioi 322847.
PROi Q9DC23.
SOURCEi Search...

Gene expression databases

Bgeei Q9DC23.
CleanExi MM_DNAJC10.
ExpressionAtlasi Q9DC23. baseline and differential.
Genevestigatori Q9DC23.

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], FUNCTION, TISSUE SPECIFICITY.
  2. "ERDJPs, a novel family of ER chaperones."
    Simmen T., Mezghrani A., Bertoli G., Sitia R.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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].
    Strain: Czech II and FVB/N x C57BL/6J.
    Tissue: Mammary tumor.
  6. "JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs."
    Hosoda A., Kimata Y., Tsuru A., Kohno K.
    J. Biol. Chem. 278:2669-2676(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, INTERACTION WITH HSPA5.
  7. "ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER."
    Ushioda R., Hoseki J., Araki K., Jansen G., Thomas D.Y., Nagata K.
    Science 321:569-572(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EDEM1, MUTAGENESIS OF CYS-158; CYS-161; CYS-480; CYS-483; CYS-588; CYS-591; CYS-700 AND CYS-703.
  8. "Positive contribution of ERdj5/JPDI to endoplasmic reticulum protein quality control in the salivary gland."
    Hosoda A., Tokuda M., Akai R., Kohno K., Iwawaki T.
    Biochem. J. 425:117-125(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5."
    Hagiwara M., Maegawa K., Suzuki M., Ushioda R., Araki K., Matsumoto Y., Hoseki J., Nagata K., Inaba K.
    Mol. Cell 41:432-444(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 33-793, FUNCTION, INTERACTION WITH EDEM1, MUTAGENESIS OF CYS-158; CYS-161; CYS-480; CYS-483; CYS-588; CYS-591; CYS-700 AND CYS-703.

Entry informationi

Entry nameiDJC10_MOUSE
AccessioniPrimary (citable) accession number: Q9DC23
Secondary accession number(s): A2ASA2
, Q71S84, Q8CH78, Q8CIB0, Q99LV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3