Q99615 (DNJC7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DnaJ homolog subfamily C member 7

Alternative name(s):
Tetratricopeptide repeat protein 2
Short name=TPR repeat protein 2

Gene names

Name:	DNAJC7
Synonyms:	TPR2, TTC2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm By similarity. Ref.7 Ref.10
Subunit structure	Associates with complexes containing chaperones HSP70 and HSP90. Interacts with the GAP domain of NF1. Interacts with HSP90AA1. Interacts with HSPA1A/B; the interaction is enhanced by ATP. Interacts with HSP90AB1. Interacts with PGR. Interacts with RAD9A; the interaction is interrupted by UV and heat shock treatments. Interacts with HUS1 and RAD1. Interacts with NR1I3. The DNAJC7-NR1I3 complex may also include HSP90 By similarity. Interacts with HSPA8. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton. Note: Colocalizes with NR1I3 to microtubules By similarity. Ref.6 Ref.7
Sequence similarities	Contains 1 J domain. Contains 9 TPR repeats.
Sequence caution	The sequence AAB36872.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH33772.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Domain	Repeat TPR repeat
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chaperone cofactor-dependent protein refolding Inferred from direct assay Ref.7Ref.10. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay Ref.7. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular function	heat shock protein binding Inferred from physical interaction Ref.7. Source: UniProtKB unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 494	493	DnaJ homolog subfamily C member 7		PRO_0000071058
Regions
	Repeat	28 – 61	34	TPR 1
	Repeat	62 – 95	34	TPR 2
	Repeat	96 – 129	34	TPR 3
	Repeat	142 – 175	34	TPR 4
	Repeat	177 – 209	33	TPR 5
	Repeat	210 – 243	34	TPR 6
	Repeat	256 – 289	34	TPR 7
	Repeat	294 – 327	34	TPR 8
	Repeat	328 – 361	34	TPR 9
	Domain	381 – 451	71	J
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.3 Ref.11
	Modified residue	50	1	Phosphotyrosine Ref.9
Experimental info
	Mutagenesis	101	1	R → A: Impairs interaction with HSP90AA1 and HSPA1A/B. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-333 and A-409. Ref.7
	Mutagenesis	333	1	R → A: Impairs interaction with HSP90AA1 and HSPA1A/B. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-101 and A-409. Ref.7
	Mutagenesis	409	1	H → A: Predominantly nuclear localization. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-101 and A-333. Ref.6 Ref.7
	Sequence conflict	375	1	K → R in BX647209. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q99615 [UniParc]. Last modified April 13, 2004. Version 2. Checksum: 81C60CF71BFE951D	FASTA	494	56,441
	10 20 30 40 50 60 MAAAAECDVV MAATEPELLD DQEAKREAET FKEQGNAYYA KKDYNEAYNY YTKAIDMCPK 70 80 90 100 110 120 NASYYGNRAA TLMMLGRFRE ALGDAQQSVR LDDSFVRGHL REGKCHLSLG NAMAACRSFQ 130 140 150 160 170 180 RALELDHKNA QAQQEFKNAN AVMEYEKIAE TDFEKRDFRK VVFCMDRALE FAPACHRFKI 190 200 210 220 230 240 LKAECLAMLG RYPEAQSVAS DILRMDSTNA DALYVRGLCL YYEDCIEKAV QFFVQALRMA 250 260 270 280 290 300 PDHEKACIAC RNAKALKAKK EDGNKAFKEG NYKLAYELYT EALGIDPNNI KTNAKLYCNR 310 320 330 340 350 360 GTVNSKLRKL DDAIEDCTNA VKLDDTYIKA YLRRAQCYMD TEQYEEAVRD YEKVYQTEKT 370 380 390 400 410 420 KEHKQLLKNA QLELKKSKRK DYYKILGVDK NASEDEIKKA YRKRALMHHP DRHSGASAEV 430 440 450 460 470 480 QKEEEKKFKE VGEAFTILSD PKKKTRYDSG QDLDEEGMNM GDFDPNNIFK AFFGGPGGFS 490 FEASGPGNFF FQFG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Salivary gland.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung and Skin.
[3]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-26; 69-77; 80-90; 138-156; 192-238; 274-291 AND 430-442, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[4]	"Identification and characterization of two novel tetratricopeptide repeat-containing genes." Murthy A.E., Bernards A., Church D., Wasmuth J., Gusella J.F. DNA Cell Biol. 15:727-735(1996) [PubMed: 8836031] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-494.
[5]	"Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats." Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C. J. Biol. Chem. 274:34425-34432(1999) [PubMed: 10567422] [Abstract] Cited for: INTERACTION WITH HSPA8.
[6]	"The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9." Xiang S.L., Kumano T., Iwasaki S.I., Sun X., Yoshioka K., Yamamoto K.C. Biochem. Biophys. Res. Commun. 287:932-940(2001) [PubMed: 11573955] [Abstract] Cited for: INTERACTION WITH RAD9A; HUS1 AND RAD1, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-409.
[7]	"Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system." Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C., Obermann W.M. EMBO J. 22:3613-3623(2003) [PubMed: 12853476] [Abstract] Cited for: FUNCTION, INTERACTION WITH HSP90AA1 AND HSPA1A/B, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-101; ARG-333 AND HIS-409.
[8]	"Cytoplasmic accumulation of the nuclear receptor CAR by a tetratricopeptide repeat protein in HepG2 cells." Kobayashi K., Sueyoshi T., Inoue K., Moore R., Negishi M. Mol. Pharmacol. 64:1069-1075(2003) [PubMed: 14573755] [Abstract] Cited for: INTERACTION WITH NR1I3.
[9]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-50, MASS SPECTROMETRY.
[10]	"Role of the cochaperone Tpr2 in Hsp90 chaperoning." Moffatt N.S., Bruinsma E., Uhl C., Obermann W.M., Toft D. Biochemistry 47:8203-8213(2008) [PubMed: 18620420] [Abstract] Cited for: FUNCTION, INTERACTION WITH HSP90AB1; HSPA1A/B AND PGR.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX647209 mRNA. No translation available. BC011837 mRNA. Translation: AAH11837.2. BC033772 mRNA. Translation: AAH33772.1. Different initiation. U46571 mRNA. Translation: AAB36872.1. Different initiation.
IPI	IPI00329629.
RefSeq	NP_003306.3. NM_003315.3.
UniGene	Hs.500156.
3D structure databases
ProteinModelPortal	Q99615.
SMR	Q99615. Positions 24-449.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99615. 4 interactions.
MINT	MINT-1143801.
STRING	Q99615.
PTM databases
PhosphoSite	Q99615.
Polymorphism databases
DMDM	46397879.
Proteomic databases
PeptideAtlas	Q99615.
PRIDE	Q99615.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000457167; ENSP00000406463; ENSG00000168259.
GeneID	7266.
KEGG	hsa:7266.
Organism-specific databases
CTD	7266.
GeneCards	GC17M040128.
H-InvDB	HIX0013829.
HGNC	HGNC:12392. DNAJC7.
HPA	HPA023015.
MIM	601964. gene.
neXtProt	NX_Q99615.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00590000083090.
HOGENOM	HBG717809.
HOVERGEN	HBG051376.
InParanoid	Q99615.
OMA	REAESFK.
OrthoDB	EOG4W3SMS.
PhylomeDB	Q99615.
Gene expression databases
ArrayExpress	Q99615.
Bgee	Q99615.
CleanEx	HS_DNAJC7.
Genevestigator	Q99615.
GermOnline	ENSG00000168259. Homo sapiens.
Family and domain databases
InterPro	IPR001623. DnaJ_N. IPR023114. Elongated_TPR_rpt_dom. IPR003095. Hsp_DnaJ. IPR001440. TPR-1. IPR013026. TPR-contain. IPR011990. TPR-like_helical. IPR019734. TPR_repeat. [Graphical view]
Gene3D	G3DSA:1.10.287.110. DnaJ_N. 1 hit. G3DSA:1.10.150.160. Elongated_TPR_rpt_dom. 1 hit. G3DSA:1.25.40.10. TPR-like_helical. 3 hits.
KO	K09527.
Pfam	PF00226. DnaJ. 1 hit. PF00515. TPR_1. 4 hits. [Graphical view]
PRINTS	PR00625. JDOMAIN.
SMART	SM00271. DnaJ. 1 hit. SM00028. TPR. 7 hits. [Graphical view]
SUPFAM	SSF46565. DnaJ_N. 1 hit.
PROSITE	PS00636. DNAJ_1. False negative. PS50076. DNAJ_2. 1 hit. PS50005. TPR. 8 hits. PS50293. TPR_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	28407.
PMAP-CutDB	Q99615.
SOURCE	Search...

Entry information

Entry name

DNJC7_HUMAN

Accession

Primary (citable) accession number: Q99615

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	April 13, 2004
Last modified:	January 25, 2012
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.