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Q8IXB1

- DJC10_HUMAN

UniProt

Q8IXB1 - DJC10_HUMAN

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Protein
DnaJ homolog subfamily C member 10
Gene
DNAJC10, ERDJ5, UNQ495/PRO1012
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. Hsp70 protein binding Source: UniProtKB
  4. chaperone binding Source: UniProtKB
  5. disulfide oxidoreductase activity 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
Complete GO annotation...

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  2. cell redox homeostasis Source: InterPro
  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 Publications

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

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 – 3232 Reviewed prediction
Add
BLAST
Chaini33 – 793761DnaJ homolog subfamily C member 10
PRO_0000281483Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi158 ↔ 161Redox-active
Disulfide bondi480 ↔ 483Redox-active
Glycosylationi530 – 5301N-linked (GlcNAc...) Reviewed prediction
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).2 Publications

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ8IXB1.
SMRiQ8IXB1. Positions 34-782.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 10066J
Add
BLAST
Domaini130 – 232103Thioredoxin 1
Add
BLAST
Domaini454 – 553100Thioredoxin 2
Add
BLAST
Domaini557 – 662106Thioredoxin 3
Add
BLAST
Domaini671 – 778108Thioredoxin 4
Add
BLAST

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi790 – 7934Prevents secretion from ER Reviewed prediction

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.
Contains 4 thioredoxin domains.

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.

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.
VSP_024011Add
BLAST
Alternative sequencei330 – 3323FLN → LLH in isoform 3.
VSP_054434
Alternative sequencei333 – 793461Missing in isoform 3.
VSP_054435Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51L → S in AAM09527. 1 Publication
Sequence conflicti5 – 51L → S in BAB55304. 1 Publication
Sequence conflicti213 – 2131P → A in AAN73271. 1 Publication
Sequence conflicti356 – 3594NTLE → KRVK in AAN73271. 1 Publication
Sequence conflicti446 – 4461F → S in BAB55121. 1 Publication
Sequence conflicti565 – 5651T → A in CAD89982. 1 Publication
Sequence conflicti633 – 6331E → K in CAB70858. 1 Publication
Sequence conflicti755 – 7551K → N in BAB55304. 1 Publication
Sequence conflicti771 – 7711I → T in CAD89982. 1 Publication

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.
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...

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 .
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

« 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: September 3, 2014
This is version 111 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

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