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DNAJC7

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

DNAJC7

Identifiers

Aliases

DNAJC7, DJ11, DJC7, TPR2, TTC2, DnaJ heat shock protein family (Hsp40) member C7

External IDs

OMIM:601964;MGI:1928373;HomoloGene:68306;GeneCards:DNAJC7;OMA:DNAJC7 - orthologs

Gene location (Human)

Chr.	Chromosome 17 (human)^[1]

Band	17q21.2	Start	41,976,421bp^[1]
Band	17q21.2	End	42,021,376bp^[1]

Gene location (Mouse)

Chr.	Chromosome 11 (mouse)^[2]

Band	11 D\|11 63.47 cM	Start	100,473,644bp^[2]
Band	11 D\|11 63.47 cM	End	100,511,014bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

nucleus accumbens

caudate nucleus

right frontal lobe

anterior pituitary

monocyte

mucosa of transverse colon

apex of heart

cingulate gyrus

Brodmann area 9

anterior cingulate cortex

Top expressed in

tail of embryo

neural layer of retina

ventricular zone

genital tubercle

superior frontal gyrus

thymus

ganglionic eminence

cerebellar cortex

primary visual cortex

trigeminal ganglion

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	protein binding heat shock protein binding ATPase activator activity
Cellular component	cytoplasm extracellular exosome cytoskeleton membrane nucleus nucleoplasm cytosol
Biological process	regulation of cellular response to heat protein folding positive regulation of ATP-dependent activity chaperone cofactor-dependent protein refolding
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


7266


56354

Ensembl


ENSG00000168259


ENSMUSG00000014195

UniProt


Q99615


Q9QYI3

RefSeq (mRNA)


NM_001144766 NM_003315


NM_019795 NM_001378962 NM_001378963

RefSeq (protein)


NP_001138238 NP_003306


NP_062769 NP_001365891 NP_001365892

Location (UCSC)

Chr 17: 41.98 – 42.02 Mb

Chr 11: 100.47 – 100.51 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

DnaJ homolog subfamily C member 7 is aprotein that in humans is encoded by theDNAJC7gene.^[5]^[6]^[7]

Interactions

[edit]

DNAJC7 has been shown tointeract withRAD9A.^[8]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000168259 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000014195 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^Murthy AE, Bernards A, Church D, Wasmuth J, Gusella JF (Nov 1996). "Identification and characterization of two novel tetratricopeptide repeat-containing genes".DNA Cell Biol.15 (9):727–35.doi:10.1089/dna.1996.15.727.PMID 8836031.
^Ohtsuka K, Hata M (Jan 2001)."Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature".Cell Stress Chaperones.5 (2):98–112.doi:10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2 (inactive 12 July 2025).PMC 312896.PMID 11147971.{{cite journal}}: CS1 maint: DOI inactive as of July 2025 (link)
^"Entrez Gene: DNAJC7 DnaJ (Hsp40) homolog, subfamily C, member 7".
^Xiang SL, Kumano T, Iwasaki SI, Sun X, Yoshioka K, Yamamoto KC (2001)."The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9".Biochem. Biophys. Res. Commun.287 (4):932–40.doi:10.1006/bbrc.2001.5685.hdl:2297/1794.PMID 11573955.S2CID 20694221.

Hartley JL, Temple GF, Brasch MA (2001)."DNA Cloning Using In Vitro Site-Specific Recombination".Genome Res.10 (11):1788–95.doi:10.1101/gr.143000.PMC 310948.PMID 11076863.
Wiemann S, Weil B, Wellenreuther R, et al. (2001)."Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs".Genome Res.11 (3):422–35.doi:10.1101/gr.GR1547R.PMC 311072.PMID 11230166.
Xiang SL, Kumano T, Iwasaki SI, et al. (2001)."The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9".Biochem. Biophys. Res. Commun.287 (4):932–40.doi:10.1006/bbrc.2001.5685.hdl:2297/1794.PMID 11573955.S2CID 20694221.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003)."Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences".Proc. Natl. Acad. Sci. U.S.A.99 (26):16899–903.Bibcode:2002PNAS...9916899M.doi:10.1073/pnas.242603899.PMC 139241.PMID 12477932.
Brychzy A, Rein T, Winklhofer KF, et al. (2003)."Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system".EMBO J.22 (14):3613–23.doi:10.1093/emboj/cdg362.PMC 165632.PMID 12853476.
Gerhard DS, Wagner L, Feingold EA, et al. (2004)."The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)".Genome Res.14 (10B):2121–7.doi:10.1101/gr.2596504.PMC 528928.PMID 15489334.
Wiemann S, Arlt D, Huber W, et al. (2004)."From ORFeome to Biology: A Functional Genomics Pipeline".Genome Res.14 (10B):2136–44.doi:10.1101/gr.2576704.PMC 528930.PMID 15489336.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells".Nat. Biotechnol.23 (1):94–101.doi:10.1038/nbt1046.PMID 15592455.S2CID 7200157.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network".Nature.437 (7062):1173–8.Bibcode:2005Natur.437.1173R.doi:10.1038/nature04209.PMID 16189514.S2CID 4427026.
Mehrle A, Rosenfelder H, Schupp I, et al. (2006)."The LIFEdb database in 2006".Nucleic Acids Res.34 (Database issue): D415–8.doi:10.1093/nar/gkj139.PMC 1347501.PMID 16381901.

Posttranslational modification

Chaperones/
protein folding

Heat shock proteins/ Chaperonins	Hsp10/GroES Hsp27 Hsp47 HSP60/GroEL Hsp40/DnaJ A1 A2 A3 B1 B2 B11 B4 B6 B9 C1 C3 C5 C6 C7 C10 C11 C13 C14 C19 Hsp70 1A 1B 1L 2 4 4L 5 6 7 8 9 12A 14 Hsp90 α₁ α₂ β ER TRAP1
Other	Alpha crystallin Clusterin Survival of motor neuron SMN1 SMN2

Protein targeting

Ubiquitin
(ubiquitylation)

E1Ubiquitin-activating enzyme
- UBA1
- UBA2
- UBA3
- UBA5
- UBA6
- UBA7
- ATG7
- NAE1
- SAE1

E2Ubiquitin-conjugating enzyme
- A
- B
- C
- D1
- D2
- D3
- E1
- E2
- E3
- G1
- G2
- H
- I
- J1
- J2
- K
- L1
- L2
- L3
- L4
- L6
- M
- N
- O
- Q1
- Q2
- R1 (CDC34)
- R2
- S
- V1
- V2
- Z

E3Ubiquitin ligase
- VHL
- Cullin
- CBL
- MDM2
- FANCL
- UBR1

Ubiquitin-like proteins
(UBL)

SUMO protein (SUMOylation)	E1 SUMO-activating enzyme SAE1 SAE2 E2 SUMO-conjugating enzyme UBC9 E3 SUMO ligase PIAS1 PIAS2 PIAS3 PIAS4
Other	ISG15 URM1 UFM1 NEDD8 (neddylation) FAT10 ATG8 ATG12 FUB1 MUB UBL5 Prokaryotic ubiquitin-like protein

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