Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DnaJ homolog subfamily B member 6

Gene

DNAJB6

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

Functioni

Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Isoform B but not isoform A inhibits huntingtin aggregation. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity.4 Publications

GO - Molecular functioni

  • ATPase activator activity Source: UniProtKB
  • chaperone binding Source: UniProtKB
  • DNA binding Source: Ensembl
  • heat shock protein binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiREACT_264487. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily B member 6
Alternative name(s):
HHDJ1
Heat shock protein J2
Short name:
HSJ-2
MRJ
MSJ-1
Gene namesi
Name:DNAJB6
Synonyms:HSJ2, MRJ, MSJ1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:14888. DNAJB6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • Z disc Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Limb-girdle muscular dystrophy 1E (LGMD1E)2 Publications

The disease is caused by mutations affecting the gene represented in this entry. There is evidence that LGMD1E is caused by dysfunction of isoform B (PubMed:22366786).

Disease descriptionAn autosomal dominant myopathy characterized by adult onset of proximal muscle weakness, beginning in the hip girdle region and later progressing to the shoulder girdle region.

See also OMIM:603511
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891F → I in LGMD1E; the mutation results in inefficient inhibition of protein aggregation by isoform B. 1 Publication
VAR_067833
Natural varianti93 – 931F → L in LGMD1E; the mutation results in inefficient inhibition of protein aggregation by isoform B. 2 Publications
VAR_067834
Natural varianti96 – 961P → R in LGMD1E. 1 Publication
VAR_067835

Keywords - Diseasei

Disease mutation, Limb-girdle muscular dystrophy

Organism-specific databases

MIMi603511. phenotype.
Orphaneti34516. Autosomal dominant limb-girdle muscular dystrophy type 1D.
PharmGKBiPA27418.

Polymorphism and mutation databases

BioMutaiDNAJB6.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 326325DnaJ homolog subfamily B member 6PRO_0000071025Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei277 – 2771Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75190.
PaxDbiO75190.
PRIDEiO75190.

PTM databases

PhosphoSiteiO75190.

Expressioni

Tissue specificityi

Widely expressed. Highest levels in testis and brain, and lower levels in heart, spleen, intestine, ovary, placenta, lung, kidney, pancreas, thymus, prostate, skeletal muscle, liver and leukocytes. In testis, expressed in germ cells in the earlier stages of differentiation pathway as well as in spermatids. In brain, expressed at a higher level in hippocampus and thalamus and a lower level in amygdala, substantia nigra, corpus callosum and caudate nucleus.4 Publications

Gene expression databases

BgeeiO75190.
CleanExiHS_DNAJB6.
ExpressionAtlasiO75190. baseline and differential.
GenevisibleiO75190. HS.

Organism-specific databases

HPAiCAB004670.
HPA024258.
HPA058593.

Interactioni

Subunit structurei

Homooligomer. Interacts with BAG3, HSPB8 and STUB1. Interacts with ALKBH1 (By similarity). Interacts with HSP70, KRT18 and PTTG. Isoform B interacts with histone deacetylases HDAC4, HDAC6, and SIRT2, HDAC activity is required for antiaggregation.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRMS1Q9HCU92EBI-1053164,EBI-714781
DYSFO759232EBI-1053164,EBI-2799016
KRT18P057836EBI-1053164,EBI-297888
MLF1P583402EBI-1053164,EBI-721328
MLF2Q157733EBI-1053164,EBI-1051875
SGCGQ133262EBI-1053164,EBI-5357343

Protein-protein interaction databases

BioGridi115360. 37 interactions.
IntActiO75190. 42 interactions.
MINTiMINT-4713234.
STRINGi9606.ENSP00000262177.

Structurei

3D structure databases

ProteinModelPortaliO75190.
SMRiO75190. Positions 1-105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 6968JPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 146145Interaction with HSP70Add
BLAST
Regioni119 – 242124Interaction with KRT18Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi83 – 17290Gly/Phe-richAdd
BLAST
Compositional biasi155 – 19440Ser-richAdd
BLAST

Domaini

The antiaggregation activity of isoform B resides in the serine-rich region and the C-terminus.

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0484.
GeneTreeiENSGT00760000118947.
HOVERGENiHBG066998.
InParanoidiO75190.
KOiK09512.
OMAiNPFEFGF.
PhylomeDBiO75190.
TreeFamiTF105142.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: O75190-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVDYYEVLGV QRHASPEDIK KAYRKLALKW HPDKNPENKE EAERKFKQVA
60 70 80 90 100
EAYEVLSDAK KRDIYDKYGK EGLNGGGGGG SHFDSPFEFG FTFRNPDDVF
110 120 130 140 150
REFFGGRDPF SFDFFEDPFE DFFGNRRGPR GSRSRGTGSF FSAFSGFPSF
160 170 180 190 200
GSGFSSFDTG FTSFGSLGHG GLTSFSSTSF GGSGMGNFKS ISTSTKMVNG
210 220 230 240 250
RKITTKRIVE NGQERVEVEE DGQLKSLTIN GVADDDALAE ERMRRGQNAL
260 270 280 290 300
PAQPAGLRPP KPPRPASLLR HAPHCLSEEE GEQDRPRAPG PWDPLASAAG
310 320
LKEGGKRKKQ KQREESKKKK STKGNH
Length:326
Mass (Da):36,087
Last modified:October 18, 2001 - v2
Checksum:iECF1628BF7A524F3
GO
Isoform B (identifier: O75190-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     232-241: VADDDALAEE → KEQLLRLDNK
     242-326: Missing.

Show »
Length:241
Mass (Da):26,900
Checksum:iCD5A49CAB66C2E16
GO
Isoform C (identifier: O75190-3) [UniParc]FASTAAdd to basket

Also known as: a

The sequence of this isoform differs from the canonical sequence as follows:
     301-326: LKEGGKRKKQKQREESKKKKSTKGNH → VQREAAVEQAQSETSLGARGQRGHK

Note: No experimental confirmation available.
Show »
Length:325
Mass (Da):35,714
Checksum:i01F47DA9A87EBC74
GO
Isoform D (identifier: O75190-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDA → MPHPRILKRP

Note: No experimental confirmation available.
Show »
Length:277
Mass (Da):30,369
Checksum:i97C70A8C1DF2CACC
GO

Sequence cautioni

The sequence AAD16010.1 differs from that shown. Reason: Frameshift at position 197. Curated
The sequence BAD93096.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti128 – 1281G → S in BAD97321 (Ref. 9) Curated
Sequence conflicti303 – 3031E → G in BAF85714 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891F → I in LGMD1E; the mutation results in inefficient inhibition of protein aggregation by isoform B. 1 Publication
VAR_067833
Natural varianti93 – 931F → L in LGMD1E; the mutation results in inefficient inhibition of protein aggregation by isoform B. 2 Publications
VAR_067834
Natural varianti96 – 961P → R in LGMD1E. 1 Publication
VAR_067835

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5959MVDYY…VLSDA → MPHPRILKRP in isoform D. CuratedVSP_053894Add
BLAST
Alternative sequencei232 – 24110VADDDALAEE → KEQLLRLDNK in isoform B. 10 PublicationsVSP_001289
Alternative sequencei242 – 32685Missing in isoform B. 10 PublicationsVSP_001290Add
BLAST
Alternative sequencei301 – 32626LKEGG…TKGNH → VQREAAVEQAQSETSLGARG QRGHK in isoform C. 4 PublicationsVSP_026180Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF080569 mRNA. Translation: AAD16010.1. Frameshift.
AB015798 mRNA. Translation: BAA88769.1.
AB015799 mRNA. Translation: BAA88770.1.
AF060703 mRNA. Translation: AAF21257.1.
AB014888 mRNA. Translation: BAA32209.1.
AF075601 mRNA. Translation: AAD43194.1.
CR533498 mRNA. Translation: CAG38529.1.
AB209859 mRNA. Translation: BAD93096.1. Different initiation.
AK223601 mRNA. Translation: BAD97321.1.
AK291953 mRNA. Translation: BAF84642.1.
AK293025 mRNA. Translation: BAF85714.1.
AK297796 mRNA. Translation: BAG60135.1.
AL136707 mRNA. Translation: CAB66642.1.
AC006372 Genomic DNA. No translation available.
AC079306 Genomic DNA. Translation: AAS07392.1.
AC079306 Genomic DNA. Translation: AAS07393.1.
CH236954 Genomic DNA. Translation: EAL23923.1.
CH236954 Genomic DNA. Translation: EAL23924.1.
CH471149 Genomic DNA. Translation: EAX04570.1.
BC000177 mRNA. Translation: AAH00177.1.
BC002446 mRNA. Translation: AAH02446.1.
CCDSiCCDS47755.1. [O75190-2]
CCDS5946.1. [O75190-1]
RefSeqiNP_005485.1. NM_005494.2. [O75190-2]
NP_490647.1. NM_058246.3. [O75190-1]
UniGeneiHs.188591.
Hs.490745.

Genome annotation databases

EnsembliENST00000262177; ENSP00000262177; ENSG00000105993.
ENST00000429029; ENSP00000397556; ENSG00000105993. [O75190-2]
GeneIDi10049.
KEGGihsa:10049.
UCSCiuc003wnj.3. human. [O75190-2]
uc003wnk.3. human. [O75190-1]
uc003wnl.3. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF080569 mRNA. Translation: AAD16010.1. Frameshift.
AB015798 mRNA. Translation: BAA88769.1.
AB015799 mRNA. Translation: BAA88770.1.
AF060703 mRNA. Translation: AAF21257.1.
AB014888 mRNA. Translation: BAA32209.1.
AF075601 mRNA. Translation: AAD43194.1.
CR533498 mRNA. Translation: CAG38529.1.
AB209859 mRNA. Translation: BAD93096.1. Different initiation.
AK223601 mRNA. Translation: BAD97321.1.
AK291953 mRNA. Translation: BAF84642.1.
AK293025 mRNA. Translation: BAF85714.1.
AK297796 mRNA. Translation: BAG60135.1.
AL136707 mRNA. Translation: CAB66642.1.
AC006372 Genomic DNA. No translation available.
AC079306 Genomic DNA. Translation: AAS07392.1.
AC079306 Genomic DNA. Translation: AAS07393.1.
CH236954 Genomic DNA. Translation: EAL23923.1.
CH236954 Genomic DNA. Translation: EAL23924.1.
CH471149 Genomic DNA. Translation: EAX04570.1.
BC000177 mRNA. Translation: AAH00177.1.
BC002446 mRNA. Translation: AAH02446.1.
CCDSiCCDS47755.1. [O75190-2]
CCDS5946.1. [O75190-1]
RefSeqiNP_005485.1. NM_005494.2. [O75190-2]
NP_490647.1. NM_058246.3. [O75190-1]
UniGeneiHs.188591.
Hs.490745.

3D structure databases

ProteinModelPortaliO75190.
SMRiO75190. Positions 1-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115360. 37 interactions.
IntActiO75190. 42 interactions.
MINTiMINT-4713234.
STRINGi9606.ENSP00000262177.

PTM databases

PhosphoSiteiO75190.

Polymorphism and mutation databases

BioMutaiDNAJB6.

Proteomic databases

MaxQBiO75190.
PaxDbiO75190.
PRIDEiO75190.

Protocols and materials databases

DNASUi10049.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262177; ENSP00000262177; ENSG00000105993.
ENST00000429029; ENSP00000397556; ENSG00000105993. [O75190-2]
GeneIDi10049.
KEGGihsa:10049.
UCSCiuc003wnj.3. human. [O75190-2]
uc003wnk.3. human. [O75190-1]
uc003wnl.3. human.

Organism-specific databases

CTDi10049.
GeneCardsiGC07P157128.
GeneReviewsiDNAJB6.
HGNCiHGNC:14888. DNAJB6.
HPAiCAB004670.
HPA024258.
HPA058593.
MIMi603511. phenotype.
611332. gene.
neXtProtiNX_O75190.
Orphaneti34516. Autosomal dominant limb-girdle muscular dystrophy type 1D.
PharmGKBiPA27418.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0484.
GeneTreeiENSGT00760000118947.
HOVERGENiHBG066998.
InParanoidiO75190.
KOiK09512.
OMAiNPFEFGF.
PhylomeDBiO75190.
TreeFamiTF105142.

Enzyme and pathway databases

ReactomeiREACT_264487. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

ChiTaRSiDNAJB6. human.
GeneWikiiDNAJB6.
GenomeRNAii10049.
NextBioi35464742.
PROiO75190.
SOURCEiSearch...

Gene expression databases

BgeeiO75190.
CleanExiHS_DNAJB6.
ExpressionAtlasiO75190. baseline and differential.
GenevisibleiO75190. HS.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells."
    Pei L.
    J. Biol. Chem. 274:3151-3158(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), INTERACTION WITH PTTG, TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently."
    Chuang J.-Z., Zhou H., Zhu M., Li S.-H., Li X.-J., Sung C.-H.
    J. Biol. Chem. 277:19831-19838(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, TISSUE SPECIFICITY.
  3. "Characterization of two isoforms of a human DnaJ homologue, HSJ2."
    Hanai R., Mashima K.
    Mol. Biol. Rep. 30:149-153(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
  4. Zhang J.S., Nelson M., Wang L., Smith D.I.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
    Tissue: Pancreas.
  5. "Cloning, tissue expression, and chromosomal assignment of human MRJ gene for a member of the DNAJ protein family."
    Seki N., Hattori A., Hayashi A., Kozuma S., Miyajima N., Saito T.
    J. Hum. Genet. 44:185-189(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), TISSUE SPECIFICITY.
    Tissue: Testis.
  6. "HSJ2, a novel human homologue of the bacterial heat-shock protein DnaJ."
    Zhang W., Wan T., Yuan Z., Cao X.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
  7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
  8. "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] (ISOFORMS A; B AND C).
    Tissue: Uterus.
  9. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
    Tissue: Aortic endothelium and Kidney.
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Tissue: Fetal kidney.
  11. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  14. "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 A AND B).
    Tissue: Placenta and Skin.
  15. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12; 48-60; 71-101; 208-242 AND 271-287, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  16. "Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein."
    Izawa I., Nishizawa M., Ohtakara K., Ohtsuka K., Inada H., Inagaki M.
    J. Biol. Chem. 275:34521-34527(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSP70 AND KRT18, SUBCELLULAR LOCATION.
  17. "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-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation."
    Hageman J., Rujano M.A., van Waarde M.A., Kakkar V., Dirks R.P., Govorukhina N., Oosterveld-Hut H.M., Lubsen N.H., Kampinga H.H.
    Mol. Cell 37:355-369(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS SUPPRESSOR OF PROTEIN AGGREGATION.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: FUNCTION IN INHIBITION OF HUNTINGTIN AGGREGATION, SUBUNIT, INTERACTION WITH BAG3; HSPB8 AND STUB1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANTS LGMD1E ILE-89 AND LEU-93, CHARACTERIZATION OF VARIANTS LGMD1E ILE-89 AND LEU-93.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Exome sequencing reveals DNAJB6 mutations in dominantly-inherited myopathy."
    Harms M.B., Sommerville R.B., Allred P., Bell S., Ma D., Cooper P., Lopate G., Pestronk A., Weihl C.C., Baloh R.H.
    Ann. Neurol. 71:407-416(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LGMD1E LEU-93 AND ARG-96.

Entry informationi

Entry nameiDNJB6_HUMAN
AccessioniPrimary (citable) accession number: O75190
Secondary accession number(s): A4D232
, A8K7D8, A8KAG0, B4DN73, E9PCZ2, O95806, Q53EN8, Q59EF2, Q6FIC8, Q75MA2, Q9UIK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: October 18, 2001
Last modified: July 22, 2015
This is version 151 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.