CPLM-004512

Genbank Nucleotide ID

Y-box-binding protein 3

Protein Synonyms/Alias

Cold shock domain-containing protein A; DNA-binding protein A; Single-strand DNA-binding protein NF-GMB

Homo sapiens (Human)

Position	Peptide	Type	References
84	AGSEDAEKKVLATKV	ubiquitination	[1, 2, 3]
90	EKKVLATKVLGTVKW	ubiquitination	[4, 5, 6, 7, 8]
96	TKVLGTVKWFNVRNG	ubiquitination	[4, 5, 6, 7]
113	FINRNDTKEDVFVHQ	acetylation	[9]
113	FINRNDTKEDVFVHQ	ubiquitination	[1, 4, 5, 6]
124	FVHQTAIKKNNPRKY	ubiquitination	[1, 2, 4, 5, 6, 10, 11]
125	VHQTAIKKNNPRKYL	ubiquitination	[1, 2, 4, 6]
150	FDVVEGEKGAEAANV	ubiquitination	[1]
268	AGEIGEMKDGVPEGA	ubiquitination	[1, 6]
311	AVGEAEDKENQQATS	acetylation	[12]
311	AVGEAEDKENQQATS	ubiquitination	[3, 8]
353	SQDGKEAKAGEAPTE	ubiquitination	[1, 2, 3]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[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] 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]
[8] 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]
[9] 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]
[10] 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]
[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]
[12] 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]

Functional Description

Binds to the GM-CSF promoter. Seems to act as a repressor. Binds also to full length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression (By similarity).

DOMAIN 93 157 CSD.
MOD_RES 2 2 N-acetylserine.
MOD_RES 134 134 Phosphoserine.
MOD_RES 201 201 Phosphoserine.
MOD_RES 203 203 Phosphoserine.
MOD_RES 204 204 Phosphoserine.
MOD_RES 287 287 Phosphotyrosine (By similarity).
MOD_RES 324 324 Phosphoserine.

Acetylation; Alternative splicing; Complete proteome; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005634; C:nucleus; ISS:BHF-UCL.
GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
GO:0005844; C:polysome; IEA:Compara.
GO:0005923; C:tight junction; ISS:BHF-UCL.
GO:0003690; F:double-stranded DNA binding; TAS:ProtInc.
GO:0003730; F:mRNA 3'-UTR binding; ISS:BHF-UCL.
GO:0017048; F:Rho GTPase binding; ISS:BHF-UCL.
GO:0003700; F:sequence-specific DNA binding transcription factor activity; NAS:ProtInc.
GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO:0070935; P:3'-UTR-mediated mRNA stabilization; IC:BHF-UCL.
GO:0071474; P:cellular hyperosmotic response; IMP:BHF-UCL.
GO:0071356; P:cellular response to tumor necrosis factor; IMP:BHF-UCL.
GO:0009566; P:fertilization; IEA:Compara.
GO:0001701; P:in utero embryonic development; IEA:Compara.
GO:0008584; P:male gonad development; IEA:Compara.
GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
GO:0060547; P:negative regulation of necrotic cell death; IMP:BHF-UCL.
GO:0048642; P:negative regulation of skeletal muscle tissue development; IEA:Compara.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO:2000767; P:positive regulation of cytoplasmic translation; ISS:BHF-UCL.
GO:0046622; P:positive regulation of organ growth; IEA:Compara.
GO:0009409; P:response to cold; TAS:ProtInc.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR019844; Cold-shock_CS.
IPR011129; Cold_shock_prot.
IPR002059; CSP_DNA-bd.
IPR012340; NA-bd_OB-fold.