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Protein

DnaJ homolog subfamily C member 24

Gene

Dnajc24

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The iron-bound form is redox-active and can function as electron carrier (By similarity). Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2).By similarity2 Publications

Pathwayi: peptidyl-diphthamide biosynthesis

This protein is involved in the pathway peptidyl-diphthamide biosynthesis, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway peptidyl-diphthamide biosynthesis and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri140 – 19556DPH-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00559.

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily C member 24
Alternative name(s):
CSL-type zinc finger-containing protein 3
Diphthamide biosynthesis protein 4
J domain protein DjC7
Gene namesi
Name:Dnajc24
Synonyms:Dph4, Zcsl3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1919522. Dnajc24.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

High embryonic lethality at 14.5 dpc. As early as 10.5 dpc, embryos are smaller than their wild-type littermates. Embryos that survive long enough to initiate digit formation show one or more additional preaxial digits.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196DnaJ homolog subfamily C member 24PRO_0000082623Add
BLAST

Proteomic databases

EPDiQ91ZF0.
MaxQBiQ91ZF0.
PaxDbiQ91ZF0.
PRIDEiQ91ZF0.

PTM databases

PhosphoSiteiQ91ZF0.

Expressioni

Tissue specificityi

Detected in heart, brain, spleen, lung, liver, kidney and testis.1 Publication

Gene expression databases

BgeeiQ91ZF0.

Interactioni

Subunit structurei

Monomer and homooligomer. Iron binding promotes oligomerization (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099615.

Structurei

Secondary structure

1
196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi52 – 554Combined sources
Helixi59 – 624Combined sources
Helixi71 – 8010Combined sources
Beta strandi83 – 853Combined sources
Helixi96 – 11621Combined sources
Beta strandi117 – 1204Combined sources
Helixi121 – 1288Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJZNMR-A49-129[»]
ProteinModelPortaliQ91ZF0.
SMRiQ91ZF0. Positions 48-194.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91ZF0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 12972JPROSITE-ProRule annotationAdd
BLAST

Domaini

The DPH-type zinc finger can also bind iron ions instead of the expected zinc ions.By similarity

Sequence similaritiesi

Belongs to the DPH4 family.Curated
Contains 1 DPH-type zinc finger.PROSITE-ProRule annotation
Contains 1 J domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri140 – 19556DPH-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0715. Eukaryota.
COG0484. LUCA.
HOGENOMiHOG000189813.
HOVERGENiHBG066253.
InParanoidiQ91ZF0.
KOiK17867.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR007872. Znf_DHP.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF05207. zf-CSL. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
PS51074. ZF_DPH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91ZF0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
LTLCGARGRH QQGQPRWGGR LPVDAACPPS CGCFRVIREG SLLGQRTLMA
60 70 80 90 100
LEQTLKKDWY SILGADPSAN MSDLKQKYQK LILLYHPDKQ SADVPAGTME
110 120 130 140 150
ECMQKFIEID QAWKILGNEE TKKKYDLQRH EDELRNVGPV DAQVRLEEMS
160 170 180 190
WNQGDESFFL SCRCGGKYTV SKDEAQEATL ISCDACSLIV ELLHQS
Length:196
Mass (Da):22,080
Last modified:October 3, 2012 - v3
Checksum:iC95BA763ADE5390A
GO

Sequence cautioni

The sequence AAK21968.1 differs from that shown.A nucleotide mismatch versus the mouse genome results in the formation of an upstream ATG start codon.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501S → F in AAK21968 (PubMed:11595173).Curated
Sequence conflicti194 – 1941H → Q in AAK21968 (PubMed:11595173).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY028460 mRNA. Translation: AAK21968.1. Sequence problems.
AK006521 mRNA. Translation: BAB24631.1.
AL590380 Genomic DNA. No translation available.
AL928773 Genomic DNA. No translation available.
BX649381 Genomic DNA. No translation available.
BC030072 mRNA. Translation: AAH30072.1.
BC091774 mRNA. Translation: AAH91774.1.
RefSeqiNP_081268.1. NM_026992.3.
UniGeneiMm.25661.

Genome annotation databases

GeneIDi99349.
KEGGimmu:99349.
UCSCiuc008llf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY028460 mRNA. Translation: AAK21968.1. Sequence problems.
AK006521 mRNA. Translation: BAB24631.1.
AL590380 Genomic DNA. No translation available.
AL928773 Genomic DNA. No translation available.
BX649381 Genomic DNA. No translation available.
BC030072 mRNA. Translation: AAH30072.1.
BC091774 mRNA. Translation: AAH91774.1.
RefSeqiNP_081268.1. NM_026992.3.
UniGeneiMm.25661.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJZNMR-A49-129[»]
ProteinModelPortaliQ91ZF0.
SMRiQ91ZF0. Positions 48-194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099615.

PTM databases

PhosphoSiteiQ91ZF0.

Proteomic databases

EPDiQ91ZF0.
MaxQBiQ91ZF0.
PaxDbiQ91ZF0.
PRIDEiQ91ZF0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi99349.
KEGGimmu:99349.
UCSCiuc008llf.2. mouse.

Organism-specific databases

CTDi120526.
MGIiMGI:1919522. Dnajc24.

Phylogenomic databases

eggNOGiKOG0715. Eukaryota.
COG0484. LUCA.
HOGENOMiHOG000189813.
HOVERGENiHBG066253.
InParanoidiQ91ZF0.
KOiK17867.

Enzyme and pathway databases

UniPathwayiUPA00559.

Miscellaneous databases

EvolutionaryTraceiQ91ZF0.
PROiQ91ZF0.
SOURCEiSearch...

Gene expression databases

BgeeiQ91ZF0.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR007872. Znf_DHP.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF05207. zf-CSL. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
PS51074. ZF_DPH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a new soluble murine J-domain protein that stimulates BiP, Hsc70 and DnaK ATPase activity with different efficiencies."
    Kroczynska B., Blond S.Y.
    Gene 273:267-274(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  3. "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].
    Strain: C57BL/6J and FVB/N.
    Tissue: Mammary tumor and Thymus.
  4. "Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development."
    Webb T.R., Cross S.H., McKie L., Edgar R., Vizor L., Harrison J., Peters J., Jackson I.J.
    J. Cell Sci. 121:3140-3145(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DIPHTHAMIDE BIOSYNTHESIS, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.
  6. "Solution structure of J-domain of mouse DNAJ-like protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 49-129.

Entry informationi

Entry nameiDJC24_MOUSE
AccessioniPrimary (citable) accession number: Q91ZF0
Secondary accession number(s): Q9D9S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: October 3, 2012
Last modified: June 8, 2016
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.