UniProt Accession

 UN45A_HUMAN; Q9H3U1; A8K6F7; Q7L3Y6; Q9H3U8; Q9NSE8; Q9NSE9 

Genbank Protein ID

 AB014729; AB014736; AL357537; AL357538; AK291622; AK125721; CH471101; BC006214; BC010995; BC037992; BC045635 

Genbank Nucleotide ID

 BAB20266.1; BAB20273.1; CAB93428.1; CAB93429.1; BAF84311.1; BAG54239.1; EAX02127.1; AAH06214.1; AAH10995.2; AAH37992.1; AAH45635.1 

Protein Name

 Protein unc-45 homolog A 

Protein Synonyms/Alias

 Unc-45A; GCUNC-45; Smooth muscle cell-associated protein 1; SMAP-1 

Gene Name

 UNC45A 

Gene Synonyms/Alias

 SMAP1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
70	NRAACHLKLEDYDKA	acetylation	[1, 2, 3]
87	EASKAIEKDGGDVKA	acetylation	[4]
126	VSLEPKNKVFQEALR	ubiquitination	[5]
142	IGGQIQEKVRYMSST	ubiquitination	[6]
170	PEEKGTEKKQKASQN	ubiquitination	[6]
171	EEKGTEKKQKASQNL	ubiquitination	[6]
190	REDAGAEKIFRSNGV	ubiquitination	[7, 8]
279	VKKGFRGKEGAIIVD	ubiquitination	[4, 6]
321	NALTLLIKAVPRKSL	acetylation	[3]
321	NALTLLIKAVPRKSL	ubiquitination	[6, 9, 10]
329	AVPRKSLKDPNNSLT	ubiquitination	[7, 8]
383	SKLFDDLKCDAEREN	ubiquitination	[6]
411	EGQGLAGKLRAIQTV	ubiquitination	[6, 7, 8]
483	ANGVSLLKDLYKCSE	acetylation	[1]
483	ANGVSLLKDLYKCSE	ubiquitination	[6, 7, 8]
487	SLLKDLYKCSEKDSI	ubiquitination	[4]
516	GGTDFSMKQFAEGST	ubiquitination	[6, 11]
525	FAEGSTLKLAKQCRK	ubiquitination	[6]
614	PKMVELAKYAKQHVP	ubiquitination	[4, 6]
617	VELAKYAKQHVPEQH	ubiquitination	[6]
707	GTDVGQTKAAQALAK	ubiquitination	[4, 6, 7, 8, 9, 10]
806	MCNLAMSKEVQDLFE	ubiquitination	[6]
930	AAAACLDKAVEYGLI	ubiquitination	[6]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [9] 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]
 [10] 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]
 [11] 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] 

Functional Description

 Acts as co-chaperone for HSP90. Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell. May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen (By similarity). 

Sequence Annotation

 REPEAT 21 54 TPR 1.
 REPEAT 58 91 TPR 2.
 REPEAT 92 125 TPR 3.
 MOD_RES 15 15 Phosphothreonine.
 MOD_RES 70 70 N6-acetyllysine.
 MOD_RES 483 483 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Chaperone; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Myogenesis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; TPR repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 944 AA 

Protein Sequence

Gene Ontology

 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0061077; P:chaperone-mediated protein folding; IEA:Compara.
 GO:0007517; P:muscle organ development; IEA:UniProtKB-KW. 

Interpro

 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR013105; TPR_2.
 IPR019734; TPR_repeat.
 IPR024660; UNC-45/Ring3. 

Pfam

 PF07719; TPR_2
 PF11701; UNC45-central 

SMART

 SM00028; TPR 

PROSITE

 PS50005; TPR
 PS50293; TPR_REGION 

PRINTS