O75190 (DNJB6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DnaJ homolog subfamily B member 6

Alternative name(s):
HHDJ1
Heat shock protein J2
Short name=HSJ-2
MRJ
MSJ-1

Gene names

Name:	DNAJB6
Synonyms:	HSJ2, MRJ, MSJ1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	326 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2 Ref.16 Ref.19 Ref.22
Subunit structure	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. Ref.1 Ref.16 Ref.22
Subcellular location	Cytoplasm › perinuclear region. Nucleus. Cytoplasm › myofibril › sarcomere › Z line Ref.16 Ref.22.
Tissue specificity	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. Ref.1 Ref.2 Ref.5 Ref.22
Domain	The antiaggregation activity of isoform B resides in the serine-rich region and the C-terminus.
Involvement in disease	Limb-girdle muscular dystrophy 1E (LGMD1E) [MIM:603511]: An 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. Note: 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 (Ref.22). Ref.22 Ref.23
Sequence similarities	Contains 1 J domain.
Sequence caution	The sequence AAD16010.1 differs from that shown. Reason: Frameshift at position 197. The sequence BAD93096.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Limb-girdle muscular dystrophy
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intermediate filament organization Inferred from direct assay Ref.16. Source: UniProtKB negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay Ref.2. Source: UniProtKB protein folding Inferred from direct assay Ref.2. Source: UniProtKB response to unfolded protein Non-traceable author statement. Source: UniProtKB
Cellular_component	Z disc Inferred from direct assay Ref.22. Source: UniProtKB nucleus Inferred from direct assay Ref.16. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay Ref.16. Source: UniProtKB
Molecular_function	ATPase activator activity Inferred from direct assay Ref.2. Source: UniProtKB chaperone binding Inferred from direct assay Ref.2. Source: UniProtKB heat shock protein binding Inferred from direct assay Ref.16. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRMS1	Q9HCU9	2	EBI-1053164,EBI-714781
DYSF	O75923	2	EBI-1053164,EBI-2799016
KRT18	P05783	6	EBI-1053164,EBI-297888
SGCG	Q13326	2	EBI-1053164,EBI-5357343

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: O75190-1)

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.

Isoform B (identifier: O75190-2)

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

Isoform C (identifier: O75190-3)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.15
	Chain	2 – 326	325	DnaJ homolog subfamily B member 6		PRO_0000071025
Regions
	Domain	2 – 69	68	J
	Region	2 – 146	145	Interaction with HSP70
	Region	119 – 242	124	Interaction with KRT18
	Compositional bias	83 – 172	90	Gly/Phe-rich
	Compositional bias	155 – 194	40	Ser-rich
Amino acid modifications
	Modified residue	277	1	Phosphoserine Ref.17 Ref.21
Natural variations
	Alternative sequence	232 – 241	10	VADDDALAEE → KEQLLRLDNK in isoform B.		VSP_001289
	Alternative sequence	242 – 326	85	Missing in isoform B.		VSP_001290
	Alternative sequence	301 – 326	26	LKEGG…TKGNH → VQREAAVEQAQSETSLGARG QRGHK in isoform C.		VSP_026180
	Natural variant	89	1	F → I in LGMD1E; the mutation results in inefficient inhibition of protein aggregation by isoform B. Ref.22		VAR_067833
	Natural variant	93	1	F → L in LGMD1E; the mutation results in inefficient inhibition of protein aggregation by isoform B. Ref.22 Ref.23		VAR_067834
	Natural variant	96	1	P → R in LGMD1E. Ref.23		VAR_067835
Experimental info
	Sequence conflict	128	1	G → S in BAD97321. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified October 18, 2001. Version 2. Checksum: ECF1628BF7A524F3	FASTA	326	36,087
	10 20 30 40 50 60 MVDYYEVLGV QRHASPEDIK KAYRKLALKW HPDKNPENKE EAERKFKQVA EAYEVLSDAK 70 80 90 100 110 120 KRDIYDKYGK EGLNGGGGGG SHFDSPFEFG FTFRNPDDVF REFFGGRDPF SFDFFEDPFE 130 140 150 160 170 180 DFFGNRRGPR GSRSRGTGSF FSAFSGFPSF GSGFSSFDTG FTSFGSLGHG GLTSFSSTSF 190 200 210 220 230 240 GGSGMGNFKS ISTSTKMVNG RKITTKRIVE NGQERVEVEE DGQLKSLTIN GVADDDALAE 250 260 270 280 290 300 ERMRRGQNAL PAQPAGLRPP KPPRPASLLR HAPHCLSEEE GEQDRPRAPG PWDPLASAAG 310 320 LKEGGKRKKQ KQREESKKKK STKGNH
	Isoform B [UniParc]. Checksum: CD5A49CAB66C2E16	FASTA	241	26,900
	10 20 30 40 50 60 MVDYYEVLGV QRHASPEDIK KAYRKLALKW HPDKNPENKE EAERKFKQVA EAYEVLSDAK 70 80 90 100 110 120 KRDIYDKYGK EGLNGGGGGG SHFDSPFEFG FTFRNPDDVF REFFGGRDPF SFDFFEDPFE 130 140 150 160 170 180 DFFGNRRGPR GSRSRGTGSF FSAFSGFPSF GSGFSSFDTG FTSFGSLGHG GLTSFSSTSF 190 200 210 220 230 240 GGSGMGNFKS ISTSTKMVNG RKITTKRIVE NGQERVEVEE DGQLKSLTIN GKEQLLRLDN K
	Isoform C (a) [UniParc]. Checksum: 01F47DA9A87EBC74	FASTA	325	35,714
	10 20 30 40 50 60 MVDYYEVLGV QRHASPEDIK KAYRKLALKW HPDKNPENKE EAERKFKQVA EAYEVLSDAK 70 80 90 100 110 120 KRDIYDKYGK EGLNGGGGGG SHFDSPFEFG FTFRNPDDVF REFFGGRDPF SFDFFEDPFE 130 140 150 160 170 180 DFFGNRRGPR GSRSRGTGSF FSAFSGFPSF GSGFSSFDTG FTSFGSLGHG GLTSFSSTSF 190 200 210 220 230 240 GGSGMGNFKS ISTSTKMVNG RKITTKRIVE NGQERVEVEE DGQLKSLTIN GVADDDALAE 250 260 270 280 290 300 ERMRRGQNAL PAQPAGLRPP KPPRPASLLR HAPHCLSEEE GEQDRPRAPG PWDPLASAAG 310 320 VQREAAVEQA QSETSLGARG QRGHK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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] (ISOFORM B).
[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]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, LACK OF N-TERMINAL ACETYLATION, 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
[22]	"Mutations affecting the cytoplasmic functions of the co-chaperone DNAJB6 cause limb-girdle muscular dystrophy." Sarparanta J., Jonson P.H., Golzio C., Sandell S., Luque H., Screen M., McDonald K., Stajich J.M., Mahjneh I., Vihola A., Raheem O., Penttila S., Lehtinen S., Huovinen S., Palmio J., Tasca G., Ricci E., Hackman P. , Hauser M., Katsanis N., Udd B. Nat. Genet. 44:450-455(2012) [PubMed] [Europe PMC] [Abstract] 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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. AL136707 mRNA. Translation: CAB66642.1. 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.
IPI	IPI00024523. IPI00098523. IPI00556073.
RefSeq	NP_005485.1. NM_005494.2. NP_490647.1. NM_058246.3.
UniGene	Hs.188591. Hs.730749.
3D structure databases
ProteinModelPortal	O75190.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75190. 23 interactions.
MINT	MINT-4713234.
PTM databases
PhosphoSite	O75190.
Proteomic databases
PaxDb	O75190.
PRIDE	O75190.
Protocols and materials databases
DNASU	10049.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262177; ENSP00000262177; ENSG00000105993. ENST00000429029; ENSP00000397556; ENSG00000105993.
GeneID	10049.
KEGG	hsa:10049.
UCSC	uc003wnj.3. human. uc003wnk.3. human.
Organism-specific databases
CTD	10049.
GeneCards	GC07P157128.
HGNC	HGNC:14888. DNAJB6.
HPA	CAB004670. HPA024258.
MIM	603511. phenotype. 611332. gene.
neXtProt	NX_O75190.
Orphanet	34516. Autosomal dominant limb-girdle muscular dystrophy type 1D.
PharmGKB	PA27418.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0484.
HOVERGEN	HBG066998.
InParanoid	O75190.
KO	K09512.
OMA	MRRGQNA.
PhylomeDB	O75190.
Gene expression databases
ArrayExpress	O75190.
Bgee	O75190.
CleanEx	HS_DNAJB6.
Genevestigator	O75190.
GermOnline	ENSG00000105993. Homo sapiens.
Family and domain databases
Gene3D	1.10.287.110. 1 hit.
InterPro	IPR001623. DnaJ_domain. IPR018253. DnaJ_domain_CS. [Graphical view]
Pfam	PF00226. DnaJ. 1 hit. [Graphical view]
PRINTS	PR00625. JDOMAIN.
SMART	SM00271. DnaJ. 1 hit. [Graphical view]
SUPFAM	SSF46565. DnaJ_N. 1 hit.
PROSITE	PS00636. DNAJ_1. 1 hit. PS50076. DNAJ_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DNAJB6. human.
GenomeRNAi	10049.
NextBio	37959.
SOURCE	Search...

Entry information

Entry name

DNJB6_HUMAN

Accession

Primary (citable) accession number: O75190
Secondary accession number(s): A4D232 , A8K7D8, O95806, Q53EN8, Q59EF2, Q6FIC8, Q75MA2, Q9UIK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	October 18, 2001
Last modified:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.