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Protein

DnaJ homolog subfamily A member 2

Gene

Dnaja2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Co-chaperone of Hsc70.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi143 – 1431Zinc 1By similarity
Metal bindingi146 – 1461Zinc 1By similarity
Metal bindingi159 – 1591Zinc 2By similarity
Metal bindingi162 – 1621Zinc 2By similarity
Metal bindingi186 – 1861Zinc 2By similarity
Metal bindingi189 – 1891Zinc 2By similarity
Metal bindingi202 – 2021Zinc 1By similarity
Metal bindingi205 – 2051Zinc 1By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri130 – 21485CR-typeAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily A member 2
Alternative name(s):
mDj3
Gene namesi
Name:Dnaja2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1931882. Dnaja2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409DnaJ homolog subfamily A member 2PRO_0000071012Add
BLAST
Propeptidei410 – 4123Removed in mature formBy similarityPRO_0000396758

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391N6-acetyllysineCombined sources
Modified residuei78 – 781PhosphoserineBy similarity
Modified residuei123 – 1231PhosphoserineBy similarity
Modified residuei152 – 1521N6-acetyllysineCombined sources
Modified residuei391 – 3911PhosphotyrosineBy similarity
Modified residuei394 – 3941PhosphoserineBy similarity
Modified residuei395 – 3951PhosphoserineBy similarity
Modified residuei409 – 4091Cysteine methyl esterBy similarity
Lipidationi409 – 4091S-farnesyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

EPDiQ9QYJ0.
MaxQBiQ9QYJ0.
PaxDbiQ9QYJ0.
PeptideAtlasiQ9QYJ0.
PRIDEiQ9QYJ0.

PTM databases

iPTMnetiQ9QYJ0.
PhosphoSiteiQ9QYJ0.
SwissPalmiQ9QYJ0.

Expressioni

Gene expression databases

BgeeiQ9QYJ0.
CleanExiMM_DNAJA2.
GenevisibleiQ9QYJ0. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207986. 3 interactions.
IntActiQ9QYJ0. 7 interactions.
MINTiMINT-1857712.
STRINGi10090.ENSMUSP00000034138.

Structurei

3D structure databases

ProteinModelPortaliQ9QYJ0.
SMRiQ9QYJ0. Positions 4-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 7063JAdd
BLAST
Repeati143 – 1508CXXCXGXG motif
Repeati159 – 1668CXXCXGXG motif
Repeati186 – 1938CXXCXGXG motif
Repeati202 – 2098CXXCXGXG motif

Sequence similaritiesi

Contains 1 CR-type zinc finger.Curated
Contains 1 J domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri130 – 21485CR-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0712. Eukaryota.
COG0484. LUCA.
GeneTreeiENSGT00490000043321.
HOGENOMiHOG000226718.
HOVERGENiHBG066727.
InParanoidiQ9QYJ0.
KOiK09503.
OMAiAGMDDIF.
OrthoDBiEOG7XM2XK.
PhylomeDBiQ9QYJ0.
TreeFamiTF105141.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPiMF_01152. DnaJ.
InterProiIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QYJ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANVADTKLY DILGVPPGAS ENELKKAYRK LAKEYHPDKN PNAGDKFKEI
60 70 80 90 100
SFAYEVLSNP EKRELYDRYG EQGLREGSGG GGGMDDIFSH IFGGGLFGFM
110 120 130 140 150
GNQSRSRNGR RRGEDMMHPL KVSLEDLYNG KTTKLQLSKN VLCSACSGQG
160 170 180 190 200
GKSGAVQKCS ACRGRGVRIM IRQLAPGMVQ QMQSVCSDCN GEGEVINEKD
210 220 230 240 250
RCKKCEGKKV IKEVKILEVH VDKGMKHGQR ITFTGEADQA PGVEPGDIVL
260 270 280 290 300
LLQEKEHEVF QRDGNDLHMT YKIGLVEALC GFQFTFKHLD ARQIVVKYPP
310 320 330 340 350
GKVIEPGCVR VVRGEGMPQY RNPFEKGDLY IKFDVQFPEN NWINPDKLSE
360 370 380 390 400
LEDLLPSRPE VPNVIGETEE VELQEFDSTR GSGGGQRREA YNDSSDEESS
410
SHHGPGVQCA HQ
Length:412
Mass (Da):45,746
Last modified:May 1, 2000 - v1
Checksum:i98130EC0925CB42E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028853 mRNA. Translation: BAA88301.1.
AK077672 mRNA. Translation: BAC36946.1.
AK083208 mRNA. Translation: BAC38809.1.
BC003420 mRNA. Translation: AAH03420.1.
CCDSiCCDS22500.1.
RefSeqiNP_062768.1. NM_019794.4.
UniGeneiMm.475573.

Genome annotation databases

EnsembliENSMUST00000034138; ENSMUSP00000034138; ENSMUSG00000031701.
GeneIDi56445.
KEGGimmu:56445.
UCSCiuc009mqa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028853 mRNA. Translation: BAA88301.1.
AK077672 mRNA. Translation: BAC36946.1.
AK083208 mRNA. Translation: BAC38809.1.
BC003420 mRNA. Translation: AAH03420.1.
CCDSiCCDS22500.1.
RefSeqiNP_062768.1. NM_019794.4.
UniGeneiMm.475573.

3D structure databases

ProteinModelPortaliQ9QYJ0.
SMRiQ9QYJ0. Positions 4-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207986. 3 interactions.
IntActiQ9QYJ0. 7 interactions.
MINTiMINT-1857712.
STRINGi10090.ENSMUSP00000034138.

PTM databases

iPTMnetiQ9QYJ0.
PhosphoSiteiQ9QYJ0.
SwissPalmiQ9QYJ0.

Proteomic databases

EPDiQ9QYJ0.
MaxQBiQ9QYJ0.
PaxDbiQ9QYJ0.
PeptideAtlasiQ9QYJ0.
PRIDEiQ9QYJ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034138; ENSMUSP00000034138; ENSMUSG00000031701.
GeneIDi56445.
KEGGimmu:56445.
UCSCiuc009mqa.1. mouse.

Organism-specific databases

CTDi10294.
MGIiMGI:1931882. Dnaja2.

Phylogenomic databases

eggNOGiKOG0712. Eukaryota.
COG0484. LUCA.
GeneTreeiENSGT00490000043321.
HOGENOMiHOG000226718.
HOVERGENiHBG066727.
InParanoidiQ9QYJ0.
KOiK09503.
OMAiAGMDDIF.
OrthoDBiEOG7XM2XK.
PhylomeDBiQ9QYJ0.
TreeFamiTF105141.

Miscellaneous databases

ChiTaRSiDnaja2. mouse.
PROiQ9QYJ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QYJ0.
CleanExiMM_DNAJA2.
GenevisibleiQ9QYJ0. MM.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPiMF_01152. DnaJ.
InterProiIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature."
    Ohtsuka K., Hata M.
    Cell Stress Chaperones 5:98-112(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  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: Hippocampus.
  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].
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 140-152; 231-255 AND 273-287, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39 AND LYS-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiDNJA2_MOUSE
AccessioniPrimary (citable) accession number: Q9QYJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.