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UniProtKB/Swiss-Prot entry Q9NVM6


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DJC17_HUMAN
Primary accession number Q9NVM6
Secondary accession numbers None
Integrated into Swiss-Prot on July 25, 2006
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 62)
Name and origin of the protein
Protein name DnaJ homolog subfamily C member 17
Synonyms None
Gene name
Name: DNAJC17
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[5]
STRUCTURE BY NMR OF 162-258.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RNA binding domain in hypothetical protein FLJ10634.";
Submitted (JUN-2006) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK001496; BAA91724.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000048; AAH00048.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_060633.1; -.
UniGene Hs.511069
3D structure databases
PDB
2D9O; NMR; -; A=162-258.[ExPASy / RCSB / EBI]
PDBsum 2D9O; -.
ModBase Q9NVM6.
PTM databases
PhosphoSite Q9NVM6; -.
Organism-specific databases
HGNC HGNC:25556; DNAJC17.
GenAtlas DNAJC17.
PharmGKB PA142671965; -.
GeneCards Q9NVM6.
Gene expression databases
ArrayExpress Q9NVM6; -.
CleanEx HS_DNAJC17; -.
GermOnline ENSG00000104129; Homo sapiens.
Ontologies
GO
GO:0031072; Molecular function: heat shock protein binding (inferred from electronic annotation from InterPro).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051082; Molecular function: unfolded protein binding (inferred from electronic annotation from InterPro).
GO:0006457; Biological process: protein folding (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001623; DnaJ_N.
IPR015609; Hsp40/DnaJ_Rel.
IPR003095; Hsp_DnaJ.
IPR000504; RRM_RNP1.
Graphical view of domain structure.
Gene3D G3DSA:1.10.287.110; DnaJ_N; 1.
PANTHER PTHR11821; Hsp40/DnaJ_Rel; 1.
Pfam PF00226; DnaJ; 1.
PF00076; RRM_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00625; DNAJPROTEIN.
SMART SM00271; DnaJ; 1.
SMART graphical view of domain structure.
PROSITE PS00636; DNAJ_1; FALSE_NEG.
PS50076; DNAJ_2; 1.
PS50102; RRM; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9NVM6.
Proteomic databases
PeptideAtlas Q9NVM6; -.
Genome annotation databases
Ensembl ENSG00000104129; Homo sapiens. [Contig view]
GeneID 55192; -.
KEGG hsa:55192; -.
Phylogenomic databases
HOGENOM Q9NVM6; -.
HOVERGEN Q9NVM6; -.
Other
NextBio 59047; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chaperone; Phosphoprotein; RNA-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   304  304     DnaJ homolog subfamily C member 17. PRO_0000247118
DOMAIN   11    76  66     J. 
DOMAIN   178   249  72     RRM. 
COMPBIAS   111   117  7     Poly-Glu. 
MOD_RES   112   112        Phosphoserine. 
STRAND   172   176  5      
HELIX   191   199  9      
STRAND   204   222  19      
HELIX   224   232  9      
STRAND   238   241  4      
STRAND   243   245  3      
Sequence information
Length: 304 AA [This is the length of the unprocessed precursor] Molecular weight: 34687 Da [This is the MW of the unprocessed precursor] CRC64: 98A1BA8ABFF4120E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVTKELLQM DLYALLGIEE KAADKEVKKA YRQKALSCHP DKNPDNPRAA ELFHQLSQAL 

        70         80         90        100        110        120 
EVLTDAAARA AYDKVRKAKK QAAERTQKLD EKRKKVKLDL EARERQAQAQ ESEEEEESRS 

       130        140        150        160        170        180 
TRTLEQEIER LREEGSRQLE EQQRLIREQI RQERDQRLRG KAENTEGQGT PKLKLKWKCK 

       190        200        210        220        230        240 
KEDESKGGYS KDVLLRLLQK YGEVLNLVLS SKKPGTAVVE FATVKAAELA VQNEVGLVDN 

       250        260        270        280        290        300 
PLKISWLEGQ PQDAVGRSHS GLSKGSVLSE RDYESLVMMR MRQAAERQQL IARMQQEDQE 


GPPT 

Q9NVM6 in FASTA format

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