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Q99615 (DNJC7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Cytoplasmcytoskeleton. 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

vifP125043EBI-357552,EBI-779991From 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 494493DnaJ homolog subfamily C member 7
PRO_0000071058

Regions

Repeat28 – 6134TPR 1
Repeat62 – 9534TPR 2
Repeat96 – 12934TPR 3
Repeat142 – 17534TPR 4
Repeat177 – 20933TPR 5
Repeat210 – 24334TPR 6
Repeat256 – 28934TPR 7
Repeat294 – 32734TPR 8
Repeat328 – 36134TPR 9
Domain381 – 45171J

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.15

Natural variations

Alternative sequence1 – 5656Missing in isoform 2.
VSP_044279

Experimental info

Mutagenesis1011R → 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
Mutagenesis3331R → 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
Mutagenesis4091H → A: Predominantly nuclear localization. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-101 and A-333. Ref.9 Ref.10
Sequence conflict3751K → R in BX647209. Ref.1

Sequences

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

Last modified April 13, 2004. Version 2.
Checksum: 81C60CF71BFE951D

FASTA49456,441
        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 

« Hide

Isoform 2 [UniParc].

Checksum: C1C5BF7A49DF56B0
Show »

FASTA43850,097

References

« Hide '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. 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 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. expand/collapse author list , 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. 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 (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, IDENTIFICATION BY 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].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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.
CCDSCCDS45677.1. [Q99615-1]
CCDS45678.1. [Q99615-2]
RefSeqNP_001138238.1. NM_001144766.2. [Q99615-2]
NP_003306.3. NM_003315.3. [Q99615-1]
UniGeneHs.500156.

3D structure databases

ProteinModelPortalQ99615.
SMRQ99615. Positions 27-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113117. 31 interactions.
IntActQ99615. 9 interactions.
MINTMINT-1143801.
STRING9606.ENSP00000406463.

PTM databases

PhosphoSiteQ99615.

Polymorphism databases

DMDM46397879.

Proteomic databases

MaxQBQ99615.
PaxDbQ99615.
PeptideAtlasQ99615.
PRIDEQ99615.

Protocols and materials databases

DNASU7266.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316603; ENSP00000313311; ENSG00000168259. [Q99615-2]
ENST00000426588; ENSP00000394327; ENSG00000168259. [Q99615-2]
ENST00000457167; ENSP00000406463; ENSG00000168259. [Q99615-1]
ENST00000572436; ENSP00000460089; ENSG00000262684. [Q99615-1]
ENST00000577172; ENSP00000461130; ENSG00000262684. [Q99615-2]
GeneID7266.
KEGGhsa:7266.
UCSCuc002hyo.3. human. [Q99615-1]

Organism-specific databases

CTD7266.
GeneCardsGC17M040128.
HGNCHGNC:12392. DNAJC7.
HPAHPA023015.
MIM601964. gene.
neXtProtNX_Q99615.
PharmGKBPA27424.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000210360.
HOVERGENHBG051376.
InParanoidQ99615.
KOK09527.
OMACFQRVLE.
PhylomeDBQ99615.
TreeFamTF105166.

Gene expression databases

ArrayExpressQ99615.
BgeeQ99615.
CleanExHS_DNAJC7.
GenevestigatorQ99615.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
1.25.40.10. 3 hits.
InterProIPR001623. DnaJ_domain.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF00226. DnaJ. 1 hit.
PF00515. TPR_1. 5 hits.
PF07719. TPR_2. 1 hit.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
SM00028. TPR. 7 hits.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
PROSITEPS50076. DNAJ_2. 1 hit.
PS50005. TPR. 8 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNAJC7. human.
GeneWikiDNAJC7.
GenomeRNAi7266.
NextBio28407.
PMAP-CutDBQ99615.
PROQ99615.
SOURCESearch...

Entry information

Entry nameDNJC7_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 138 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 chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM