UniProt Accession

 DNJA1_HUMAN; P31689; Q5T7Q0; Q86TL9 

Genbank Protein ID

 D13388; L08069; AY186741; BT007292; AK289623; CH471071; CH471071; BC008182 

Genbank Nucleotide ID

 BAA02656.1; AAC37517.1; AAO31694.1; AAP35956.1; BAF82312.1; EAW58525.1; EAW58526.1; AAH08182.1 

Protein Name

 DnaJ homolog subfamily A member 1 

Protein Synonyms/Alias

 DnaJ protein homolog 2; HSDJ; Heat shock 40 kDa protein 4; Heat shock protein J2; HSJ-2; Human DnaJ protein 2; hDj-2 

Gene Name

 DNAJA1 

Gene Synonyms/Alias

 DNAJ2; HDJ2; HSJ2; HSPF4 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
3	*****MVKETTYYDV	ubiquitination	[1]
14	YYDVLGVKPNATQEE	ubiquitination	[1, 2, 3, 4, 5, 6]
23	NATQEELKKAYRKLA	acetylation	[7]
23	NATQEELKKAYRKLA	ubiquitination	[3, 4, 5]
28	ELKKAYRKLALKYHP	ubiquitination	[5]
32	AYRKLALKYHPDKNP	acetylation	[8]
32	AYRKLALKYHPDKNP	ubiquitination	[1, 2, 3, 4, 5, 6, 9]
37	ALKYHPDKNPNEGEK	ubiquitination	[1, 2, 3, 4, 5, 6, 9]
44	KNPNEGEKFKQISQA	acetylation	[6, 8, 10]
44	KNPNEGEKFKQISQA	ubiquitination	[3, 4, 6, 9]
46	PNEGEKFKQISQAYE	ubiquitination	[1, 2, 3, 4, 5, 6, 9]
59	YEVLSDAKKRELYDK	ubiquitination	[2, 3, 4, 5, 6, 9, 11]
60	EVLSDAKKRELYDKG	ubiquitination	[3, 5, 6]
66	KKRELYDKGGEQAIK	acetylation	[7, 8]
66	KKRELYDKGGEQAIK	ubiquitination	[3, 4, 5, 6, 9]
73	KGGEQAIKEGGAGGG	ubiquitination	[5]
105	MQRERRGKNVVHQLS	ubiquitination	[2, 3, 4, 6, 9, 12]
125	LYNGATRKLALQKNV	ubiquitination	[9]
130	TRKLALQKNVICDKC	ubiquitination	[6, 9]
136	QKNVICDKCEGRGGK	acetylation	[6]
136	QKNVICDKCEGRGGK	ubiquitination	[1, 4, 6, 9, 12]
143	KCEGRGGKKGAVECC	ubiquitination	[9]
144	CEGRGGKKGAVECCP	ubiquitination	[3, 4, 6, 9, 11, 12]
206	RKIVREKKILEVHID	ubiquitination	[9]
214	ILEVHIDKGMKDGQK	ubiquitination	[9]
217	VHIDKGMKDGQKITF	ubiquitination	[9]
246	IIIVLDQKDHAVFTR	ubiquitination	[9]
296	SHPGQIVKHGDIKCV	ubiquitination	[1, 2, 9, 13]
301	IVKHGDIKCVLNEGM	ubiquitination	[9]
338	NGFLSPDKLSLLEKL	ubiquitination	[1, 2, 3, 5, 9, 12, 13]
344	DKLSLLEKLLPERKE	ubiquitination	[1, 2, 3, 5, 9, 14]
350	EKLLPERKEVEETDE	ubiquitination	[3, 5, 9, 11]

Reference

 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [9] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [10] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [11] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [12] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [13] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [14] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865] 

Functional Description

 Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria. 

Sequence Annotation

 DOMAIN 6 68 J.
 REPEAT 134 141 CXXCXGXG motif.
 REPEAT 150 157 CXXCXGXG motif.
 REPEAT 177 184 CXXCXGXG motif.
 REPEAT 193 200 CXXCXGXG motif.
 ZN_FING 121 205 CR-type.
 METAL 134 134 Zinc 1 (By similarity).
 METAL 137 137 Zinc 1 (By similarity).
 METAL 150 150 Zinc 2 (By similarity).
 METAL 153 153 Zinc 2 (By similarity).
 METAL 177 177 Zinc 2 (By similarity).
 METAL 180 180 Zinc 2 (By similarity).
 METAL 193 193 Zinc 1 (By similarity).
 METAL 196 196 Zinc 1 (By similarity).
 MOD_RES 66 66 N6-acetyllysine.
 MOD_RES 83 83 Phosphoserine.
 MOD_RES 335 335 Phosphoserine.
 MOD_RES 381 381 Phosphotyrosine.
 MOD_RES 394 394 Cysteine methyl ester (Probable).
 LIPID 394 394 S-farnesyl cysteine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Chaperone; Complete proteome; Lipoprotein; Membrane; Metal-binding; Methylation; Phosphoprotein; Prenylation; Reference proteome; Repeat; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 397 AA 

Protein Sequence

Gene Ontology

 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:MGI.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0030521; P:androgen receptor signaling pathway; IEA:Compara.
 GO:0042769; P:DNA damage response, detection of DNA damage; IEA:Compara.
 GO:0006457; P:protein folding; TAS:ProtInc.
 GO:0009408; P:response to heat; IEA:InterPro.
 GO:0006986; P:response to unfolded protein; TAS:ProtInc.
 GO:0030317; P:sperm motility; IEA:Compara.
 GO:0007283; P:spermatogenesis; IEA:Compara. 

Interpro

 IPR012724; DnaJ.
 IPR002939; DnaJ_C.
 IPR001623; DnaJ_domain.
 IPR018253; DnaJ_domain_CS.
 IPR008971; HSP40/DnaJ_pept-bd.
 IPR001305; HSP_DnaJ_Cys-rich_dom. 

Pfam

 PF00226; DnaJ
 PF01556; DnaJ_C
 PF00684; DnaJ_CXXCXGXG 

SMART

 SM00271; DnaJ 

PROSITE

 PS00636; DNAJ_1
 PS50076; DNAJ_2
 PS51188; ZF_CR 

PRINTS

 PR00625; JDOMAIN.