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Protein

DnaJ homolog subfamily C member 17

Gene

DNAJC17

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily C member 17
Gene namesi
Name:DNAJC17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:25556. DNAJC17.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671965.

Polymorphism and mutation databases

BioMutaiDNAJC17.
DMDMi74761740.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304DnaJ homolog subfamily C member 17PRO_0000247118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei112 – 1121Phosphoserine5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NVM6.
PaxDbiQ9NVM6.
PeptideAtlasiQ9NVM6.
PRIDEiQ9NVM6.

PTM databases

PhosphoSiteiQ9NVM6.

Expressioni

Gene expression databases

BgeeiQ9NVM6.
CleanExiHS_DNAJC17.
ExpressionAtlasiQ9NVM6. baseline and differential.
GenevisibleiQ9NVM6. HS.

Organism-specific databases

HPAiHPA040914.
HPA041187.

Interactioni

Protein-protein interaction databases

BioGridi120489. 1 interaction.
MINTiMINT-4650891.
STRINGi9606.ENSP00000220496.

Structurei

Secondary structure

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi172 – 1765Combined sources
Helixi191 – 1999Combined sources
Beta strandi204 – 22219Combined sources
Helixi224 – 2329Combined sources
Beta strandi238 – 2414Combined sources
Beta strandi243 – 2453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9ONMR-A168-254[»]
ProteinModelPortaliQ9NVM6.
SMRiQ9NVM6. Positions 13-74, 170-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NVM6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 7666JPROSITE-ProRule annotationAdd
BLAST
Domaini178 – 24972RRMAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi111 – 1177Poly-Glu

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2214.
GeneTreeiENSGT00550000074688.
HOGENOMiHOG000239711.
HOVERGENiHBG062744.
InParanoidiQ9NVM6.
KOiK09537.
OMAiDSAQHRI.
OrthoDBiEOG7RRF89.
PhylomeDBiQ9NVM6.
TreeFamiTF321770.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR012677. Nucleotide-bd_a/b_plait.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NVM6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVTKELLQM DLYALLGIEE KAADKEVKKA YRQKALSCHP DKNPDNPRAA
60 70 80 90 100
ELFHQLSQAL EVLTDAAARA AYDKVRKAKK QAAERTQKLD EKRKKVKLDL
110 120 130 140 150
EARERQAQAQ ESEEEEESRS TRTLEQEIER LREEGSRQLE EQQRLIREQI
160 170 180 190 200
RQERDQRLRG KAENTEGQGT PKLKLKWKCK KEDESKGGYS KDVLLRLLQK
210 220 230 240 250
YGEVLNLVLS SKKPGTAVVE FATVKAAELA VQNEVGLVDN PLKISWLEGQ
260 270 280 290 300
PQDAVGRSHS GLSKGSVLSE RDYESLVMMR MRQAAERQQL IARMQQEDQE

GPPT
Length:304
Mass (Da):34,687
Last modified:October 1, 2000 - v1
Checksum:i98A1BA8ABFF4120E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001496 mRNA. Translation: BAA91724.1.
BC000048 mRNA. Translation: AAH00048.1.
CCDSiCCDS10065.1.
RefSeqiNP_060633.1. NM_018163.2.
UniGeneiHs.511069.

Genome annotation databases

EnsembliENST00000220496; ENSP00000220496; ENSG00000104129.
GeneIDi55192.
KEGGihsa:55192.
UCSCiuc001zms.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001496 mRNA. Translation: BAA91724.1.
BC000048 mRNA. Translation: AAH00048.1.
CCDSiCCDS10065.1.
RefSeqiNP_060633.1. NM_018163.2.
UniGeneiHs.511069.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9ONMR-A168-254[»]
ProteinModelPortaliQ9NVM6.
SMRiQ9NVM6. Positions 13-74, 170-258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120489. 1 interaction.
MINTiMINT-4650891.
STRINGi9606.ENSP00000220496.

PTM databases

PhosphoSiteiQ9NVM6.

Polymorphism and mutation databases

BioMutaiDNAJC17.
DMDMi74761740.

Proteomic databases

MaxQBiQ9NVM6.
PaxDbiQ9NVM6.
PeptideAtlasiQ9NVM6.
PRIDEiQ9NVM6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000220496; ENSP00000220496; ENSG00000104129.
GeneIDi55192.
KEGGihsa:55192.
UCSCiuc001zms.2. human.

Organism-specific databases

CTDi55192.
GeneCardsiGC15M041060.
HGNCiHGNC:25556. DNAJC17.
HPAiHPA040914.
HPA041187.
neXtProtiNX_Q9NVM6.
PharmGKBiPA142671965.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2214.
GeneTreeiENSGT00550000074688.
HOGENOMiHOG000239711.
HOVERGENiHBG062744.
InParanoidiQ9NVM6.
KOiK09537.
OMAiDSAQHRI.
OrthoDBiEOG7RRF89.
PhylomeDBiQ9NVM6.
TreeFamiTF321770.

Miscellaneous databases

ChiTaRSiDNAJC17. human.
EvolutionaryTraceiQ9NVM6.
GenomeRNAii55192.
NextBioi59047.
PROiQ9NVM6.

Gene expression databases

BgeeiQ9NVM6.
CleanExiHS_DNAJC17.
ExpressionAtlasiQ9NVM6. baseline and differential.
GenevisibleiQ9NVM6. HS.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR012677. Nucleotide-bd_a/b_plait.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Solution structure of RNA binding domain in hypothetical protein FLJ10634."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 162-258.

Entry informationi

Entry nameiDJC17_HUMAN
AccessioniPrimary (citable) accession number: Q9NVM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.