CPLM-012198

Genbank Nucleotide ID

Nascent polypeptide-associated complex subunit alpha

Protein Synonyms/Alias

NAC-alpha; Alpha-NAC; Hom s 2

Homo sapiens (Human)

Position	Peptide	Type	References
100	RVTIRKSKNILFVIT	ubiquitination	[1, 2, 3, 4]
108	NILFVITKPDVYKSP	acetylation	[5]
108	NILFVITKPDVYKSP	ubiquitination	[1, 2, 3, 4]
113	ITKPDVYKSPASDTY	ubiquitination	[2, 4]
127	YIVFGEAKIEDLSQQ	ubiquitination	[2, 4]
142	AQLAAAEKFKVQGEA	acetylation	[5, 6]
142	AQLAAAEKFKVQGEA	ubiquitination	[1, 2, 3, 4, 7, 8]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[5] 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]
[6] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[7] 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]
[8] 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]

Functional Description

Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters.

DOMAIN 70 135 NAC-A/B.
DOMAIN 176 213 UBA.
REGION 69 80 Required for DNA-binding (By similarity).
MOD_RES 43 43 Phosphoserine; by ILK1.
MOD_RES 142 142 N6-acetyllysine.
MOD_RES 159 159 Phosphothreonine; by GSK3-beta (By
MOD_RES 161 161 Phosphothreonine.
MOD_RES 166 166 Phosphoserine.
MOD_RES 186 186 Phosphoserine.
MOD_RES 191 191 Phosphoserine.
MOD_RES 203 203 Phosphoserine.

3D-structure; Acetylation; Allergen; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Host-virus interaction; Nucleus; Phosphoprotein; Protein transport; Reference proteome; Transcription; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005854; C:nascent polypeptide-associated complex; TAS:ProtInc.
GO:0005634; C:nucleus; ISS:BHF-UCL.
GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO:0017025; F:TBP-class protein binding; ISS:BHF-UCL.
GO:0003713; F:transcription coactivator activity; ISS:BHF-UCL.
GO:0003231; P:cardiac ventricle development; ISS:BHF-UCL.
GO:0061384; P:heart trabecula morphogenesis; ISS:BHF-UCL.
GO:0010664; P:negative regulation of striated muscle cell apoptotic process; ISS:BHF-UCL.
GO:1901227; P:negative regulation of transcription from RNA polymerase II promoter involved in heart development; ISS:BHF-UCL.
GO:2000138; P:positive regulation of cell proliferation involved in heart morphogenesis; ISS:BHF-UCL.
GO:0048633; P:positive regulation of skeletal muscle tissue growth; ISS:BHF-UCL.
GO:1901228; P:positive regulation of transcription from RNA polymerase II promoter involved in heart development; ISS:BHF-UCL.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO:0048742; P:regulation of skeletal muscle fiber development; ISS:BHF-UCL.
GO:0043403; P:skeletal muscle tissue regeneration; ISS:BHF-UCL.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0006412; P:translation; TAS:ProtInc.
GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.

IPR016641; EGD2/NACA.
IPR002715; Nas_poly-pep-assoc_cplx_dom.

PS51151; NAC_AB
PS50030; UBA