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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.10 Ref.13
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.8 Ref.9 Ref.10 Ref.11 Ref.13
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton. Note: Colocalizes with NR1I3 to microtubules By similarity. Ref.9 Ref.10
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
Coding sequence diversity	Alternative splicing
Domain	Repeat TPR repeat
Molecular function	Chaperone
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chaperone cofactor-dependent protein refolding Inferred from direct assay Ref.10Ref.13. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.10. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
vif	P12504	3	EBI-357552,EBI-779991	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q99615-1)

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: Q99615-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	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.6
Natural variations
	Alternative sequence	1 – 56	56	Missing in isoform 2.		VSP_044279
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.10
	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.10
	Mutagenesis	409	1	H → A: Predominantly nuclear localization. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-101 and A-333. Ref.9 Ref.10
	Sequence conflict	375	1	K → R in BX647209. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [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
	Isoform 2 [UniParc]. Checksum: C1C5BF7A49DF56B0	FASTA	438	50,097
	10 20 30 40 50 60 MCPKNASYYG NRAATLMMLG RFREALGDAQ QSVRLDDSFV RGHLREGKCH LSLGNAMAAC 70 80 90 100 110 120 RSFQRALELD HKNAQAQQEF KNANAVMEYE KIAETDFEKR DFRKVVFCMD RALEFAPACH 130 140 150 160 170 180 RFKILKAECL AMLGRYPEAQ SVASDILRMD STNADALYVR GLCLYYEDCI EKAVQFFVQA 190 200 210 220 230 240 LRMAPDHEKA CIACRNAKAL KAKKEDGNKA FKEGNYKLAY ELYTEALGID PNNIKTNAKL 250 260 270 280 290 300 YCNRGTVNSK LRKLDDAIED CTNAVKLDDT YIKAYLRRAQ CYMDTEQYEE AVRDYEKVYQ 310 320 330 340 350 360 TEKTKEHKQL LKNAQLELKK SKRKDYYKIL GVDKNASEDE IKKAYRKRAL MHHPDRHSGA 370 380 390 400 410 420 SAEVQKEEEK KFKEVGEAFT ILSDPKKKTR YDSGQDLDEE GMNMGDFDPN NIFKAFFGGP 430 GGFSFEASGP GNFFFQFG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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 2). Tissue: Salivary gland.
[2]	"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] (ISOFORM 1). Tissue: Salivary gland.
[3]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1 AND 2). Tissue: Lung and Skin.
[6]	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 (ISOFORM 1), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-494 (ISOFORM 1).
[8]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HSPA8.
[9]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAD9A; HUS1 AND RAD1, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-409.
[10]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HSP90AA1 AND HSPA1A/B, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-101; ARG-333 AND HIS-409.
[11]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NR1I3.
[12]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HSP90AB1; HSPA1A/B AND PGR.
[14]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK298860 mRNA. Translation: BAG60982.1. BX647209 mRNA. No translation available. AC105024 Genomic DNA. No translation available. AC125257 Genomic DNA. No translation available. CH471152 Genomic DNA. Translation: EAW60788.1. BC003601 mRNA. Translation: AAH03601.1. BC011837 mRNA. Translation: AAH11837.2. BC033772 mRNA. Translation: AAH33772.1. Different initiation. U46571 mRNA. Translation: AAB36872.1. Different initiation.
IPI	IPI00329629.
RefSeq	NP_001138238.1. NM_001144766.2. NP_003306.3. NM_003315.3.
UniGene	Hs.500156.
3D structure databases
ProteinModelPortal	Q99615.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99615. 7 interactions.
MINT	MINT-1143801.
STRING	9606.ENSP00000406463.
PTM databases
PhosphoSite	Q99615.
Polymorphism databases
DMDM	46397879.
Proteomic databases
PaxDb	Q99615.
PeptideAtlas	Q99615.
PRIDE	Q99615.
Protocols and materials databases
DNASU	7266.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000316603; ENSP00000313311; ENSG00000168259. ENST00000426588; ENSP00000394327; ENSG00000168259. ENST00000457167; ENSP00000406463; ENSG00000168259. ENST00000572436; ENSP00000460089; ENSG00000262684. ENST00000577172; ENSP00000461130; ENSG00000262684.
GeneID	7266.
KEGG	hsa:7266.
UCSC	uc002hyo.3. human.
Organism-specific databases
CTD	7266.
GeneCards	GC17M040128.
HGNC	HGNC:12392. DNAJC7.
HPA	HPA023015.
MIM	601964. gene.
neXtProt	NX_Q99615.
PharmGKB	PA27424.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0457.
HOGENOM	HOG000210360.
HOVERGEN	HBG051376.
InParanoid	Q99615.
KO	K09527.
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
Gene3D	1.10.287.110. 1 hit. 1.25.40.10. 3 hits.
InterPro	IPR001623. DnaJ_domain. IPR001440. TPR-1. IPR013026. TPR-contain_dom. IPR011990. TPR-like_helical. IPR019734. TPR_repeat. [Graphical view]
Pfam	PF00226. DnaJ. 1 hit. PF00515. TPR_1. 6 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
ChiTaRS	DNAJC7. human.
GenomeRNAi	7266.
NextBio	28407.
PMAP-CutDB	Q99615.
SOURCE	Search...

Entry information

Entry name

DNJC7_HUMAN

Accession

Primary (citable) accession number: Q99615
Secondary accession number(s): Q7Z784

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	April 13, 2004
Last modified:	May 1, 2013
This is version 127 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.