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Q8IXB1 (DJC10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DNAJC10
Synonyms:ERDJ5
ORF Names:UNQ495/PRO1012
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length793 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.10 Ref.11 Ref.13

Subunit structure

Interacts with EDEM1 By similarity. Interacts with HSPA5 (via its J domain). Ref.1 Ref.13

Subcellular location

Endoplasmic reticulum lumen Ref.1 Ref.13.

Induction

By endoplasmic reticulum stress.

Domain

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 similarities

Contains 1 J domain.

Contains 4 thioredoxin domains.

Sequence caution

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.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRedox-active center
Repeat
Signal
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.10. Source: UniProtKB

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from direct assay Ref.11. Source: UniProtKB

negative regulation of protein phosphorylation

Inferred from direct assay Ref.11. Source: UniProtKB

positive regulation of ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein folding in endoplasmic reticulum

Inferred from direct assay Ref.13. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from direct assay Ref.11. Source: UniProtKB

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.1. Source: UniProtKB

endoplasmic reticulum chaperone complex

Inferred from direct assay Ref.10. Source: UniProtKB

endoplasmic reticulum lumen

Inferred from direct assay Ref.13. Source: UniProtKB

   Molecular_functionATPase activator activity

Inferred from sequence or structural similarity. Source: UniProtKB

ATPase binding

Inferred from physical interaction Ref.1. Source: UniProtKB

Hsp70 protein binding

Inferred from physical interaction Ref.13. Source: UniProtKB

chaperone binding

Inferred from direct assay Ref.1. Source: UniProtKB

disulfide oxidoreductase activity

Inferred from sequence or structural similarity. Source: UniProtKB

misfolded protein binding

Inferred from direct assay Ref.10. Source: UniProtKB

oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 19706418PubMed 19815549. Source: UniProtKB

protein disulfide oxidoreductase activity

Inferred from direct assay Ref.13. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IXB1-1)

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.
Isoform 2 (identifier: Q8IXB1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     284-329: Missing.
Isoform 3 (identifier: Q8IXB1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     330-332: FLN → LLH
     333-793: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 793761DnaJ homolog subfamily C member 10
PRO_0000281483

Regions

Domain35 – 10066J
Domain130 – 232103Thioredoxin 1
Domain454 – 553100Thioredoxin 2
Domain557 – 662106Thioredoxin 3
Domain671 – 778108Thioredoxin 4
Region235 – 350116Trxb 1
Region348 – 463116Trxb 2
Motif790 – 7934Prevents secretion from ER Potential

Amino acid modifications

Glycosylation5301N-linked (GlcNAc...) Potential
Disulfide bond158 ↔ 161Redox-active
Disulfide bond480 ↔ 483Redox-active
Disulfide bond588 ↔ 591Redox-active
Disulfide bond700 ↔ 703Redox-active

Natural variations

Alternative sequence284 – 32946Missing in isoform 2.
VSP_024011
Alternative sequence330 – 3323FLN → LLH in isoform 3.
VSP_054434
Alternative sequence333 – 793461Missing in isoform 3.
VSP_054435
Natural variant761D → N. Ref.2 Ref.8
Corresponds to variant rs6729801 [ dbSNP | Ensembl ].
VAR_031247
Natural variant3471L → I.
Corresponds to variant rs13414223 [ dbSNP | Ensembl ].
VAR_048912
Natural variant4141Y → C.
Corresponds to variant rs11681366 [ dbSNP | Ensembl ].
VAR_031248
Natural variant6461H → Q. Ref.3 Ref.7 Ref.8
Corresponds to variant rs288334 [ dbSNP | Ensembl ].
VAR_031249

Experimental info

Mutagenesis631H → Q: Prevents interaction with HSPA5, leading to prolonged interaction with substrate proteins. Ref.13
Mutagenesis1611C → A: Abolishes disulfide reductase activity; when associated with A-483; A-591 and A-703. Ref.13
Mutagenesis4831C → A: Abolishes disulfide reductase activity; when associated with A-161; A-591 and A-703. Ref.13
Mutagenesis5911C → A: Abolishes disulfide reductase activity; when associated with A-161; A-483 and A-703. Ref.13
Mutagenesis7031C → A: Abolishes disulfide reductase activity; when associated with A-161; A-483 and A-591. Ref.13
Sequence conflict51L → S in AAM09527. Ref.2
Sequence conflict51L → S in BAB55304. Ref.4
Sequence conflict2131P → A in AAN73271. Ref.1
Sequence conflict356 – 3594NTLE → KRVK in AAN73271. Ref.1
Sequence conflict4461F → S in BAB55121. Ref.4
Sequence conflict5651T → A in CAD89982. Ref.8
Sequence conflict6331E → K in CAB70858. Ref.8
Sequence conflict7551K → N in BAB55304. Ref.4
Sequence conflict7711I → T in CAD89982. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: BD39B64325432D5D

FASTA79391,080
        10         20         30         40         50         60 
MGVWLNKDDY IRDLKRIILC FLIVYMAILV GTDQDFYSLL GVSKTASSRE IRQAFKKLAL 

        70         80         90        100        110        120 
KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWNYYRY 

       130        140        150        160        170        180 
DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRD FAKEVDGLLR 

       190        200        210        220        230        240 
IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAPVKYHGDR SKESLVSFAM QHVRSTVTEL 

       250        260        270        280        290        300 
WTGNFVNSIQ TAFAAGIGWL ITFCSKGGDC LTSQTRLRLS GMLDGLVNVG WMDCATQDNL 

       310        320        330        340        350        360 
CKSLDITTST TAYFPPGATL NNKEKNSILF LNSLDAKEIY LEVIHNLPDF ELLSANTLED 

       370        380        390        400        410        420 
RLAHHRWLLF FHFGKNENSN DPELKKLKTL LKNDHIQVGR FDCSSAPDIC SNLYVFQPSL 

       430        440        450        460        470        480 
AVFKGQGTKE YEIHHGKKIL YDILAFAKES VNSHVTTLGP QNFPANDKEP WLVDFFAPWC 

       490        500        510        520        530        540 
PPCRALLPEL RRASNLLYGQ LKFGTLDCTV HEGLCNMYNI QAYPTTVVFN QSNIHEYEGH 

       550        560        570        580        590        600 
HSAEQILEFI EDLMNPSVVS LTPTTFNELV TQRKHNEVWM VDFYSPWCHP CQVLMPEWKR 

       610        620        630        640        650        660 
MARTLTGLIN VGSIDCQQYH SFCAQENVQR YPEIRFFPPK SNKAYHYHSY NGWNRDAYSL 

       670        680        690        700        710        720 
RIWGLGFLPQ VSTDLTPQTF SEKVLQGKNH WVIDFYAPWC GPCQNFAPEF ELLARMIKGK 

       730        740        750        760        770        780 
VKAGKVDCQA YAQTCQKAGI RAYPTVKFYF YERAKRNFQE EQINTRDAKA IAALISEKLE 

       790 
TLRNQGKRNK DEL 

« Hide

Isoform 2 [UniParc].

Checksum: D9F26A53E1B35455
Show »

FASTA74786,136
Isoform 3 [UniParc].

Checksum: 256FEF2695B28BE7
Show »

FASTA33237,682

References

« Hide 'large scale' references
[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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS33345.1. [Q8IXB1-1]
PIRT46333.
RefSeqNP_001258510.1. NM_001271581.1. [Q8IXB1-2]
NP_061854.1. NM_018981.2. [Q8IXB1-1]
UniGeneHs.516632.
Hs.744512.

3D structure databases

ProteinModelPortalQ8IXB1.
SMRQ8IXB1. Positions 34-782.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119947. 23 interactions.
DIPDIP-48947N.
IntActQ8IXB1. 10 interactions.
MINTMINT-1451539.

PTM databases

PhosphoSiteQ8IXB1.

Polymorphism databases

DMDM142981524.

Proteomic databases

MaxQBQ8IXB1.
PaxDbQ8IXB1.
PRIDEQ8IXB1.

Protocols and materials databases

DNASU54431.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264065; ENSP00000264065; ENSG00000077232. [Q8IXB1-1]
ENST00000537515; ENSP00000441560; ENSG00000077232.
GeneID54431.
KEGGhsa:54431.
UCSCuc002uow.2. human. [Q8IXB1-1]
uc002uoz.2. human. [Q8IXB1-2]

Organism-specific databases

CTD54431.
GeneCardsGC02P183580.
HGNCHGNC:24637. DNAJC10.
HPAHPA031111.
MIM607987. gene.
neXtProtNX_Q8IXB1.
PharmGKBPA134917195.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0526.
HOVERGENHBG057048.
KOK09530.
OMAYPSLFIF.
OrthoDBEOG7RZ5QH.
PhylomeDBQ8IXB1.
TreeFamTF105169.

Gene expression databases

ArrayExpressQ8IXB1.
BgeeQ8IXB1.
GenevestigatorQ8IXB1.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
3.40.30.10. 5 hits.
InterProIPR001623. DnaJ_domain.
IPR021170. DnaJ_homolog_subfam-C.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00226. DnaJ. 1 hit.
PF00085. Thioredoxin. 4 hits.
[Graphical view]
PIRSFPIRSF037293. DnaJ_homolog_subfam-C. 1 hit.
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
SSF52833. SSF52833. 6 hits.
PROSITEPS50076. DNAJ_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDNAJC10.
GenomeRNAi54431.
NextBio56629.
PROQ8IXB1.
SOURCESearch...

Entry information

Entry nameDJC10_HUMAN
AccessionPrimary (citable) accession number: Q8IXB1
Secondary accession number(s): Q17RJ6 expand/collapse secondary AC list , Q3B7W8, Q4ZG06, Q53QT7, Q6UWZ6, Q86T61, Q8NC82, Q8TD87, Q96K38, Q96K44, Q96K54, Q9NSY6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM