CPLM-009640

Genbank Nucleotide ID

Ubiquitin-40S ribosomal protein S27a

Protein Synonyms/Alias

Ubiquitin carboxyl extension protein 80; Ubiquitin; 40S ribosomal protein S27a

Mus musculus (Mouse)

Position	Peptide	Type	References
6	**MQIFVKTLTGKTI	ubiquitination	[1]
11	FVKTLTGKTITLEVE	ubiquitination	[1]
27	SDTIENVKAKIQDKE	ubiquitination	[1]
29	TIENVKAKIQDKEGI	ubiquitination	[1, 2]
33	VKAKIQDKEGIPPDQ	ubiquitination	[1, 2]
48	QRLIFAGKQLEDGRT	ubiquitination	[1, 2]
63	LSDYNIQKESTLHLV	ubiquitination	[1, 2]
104	KVKLAVLKYYKVDEN	acetylation	[3, 4, 5]
107	LAVLKYYKVDENGKI	acetylation	[6, 7, 8]
107	LAVLKYYKVDENGKI	ubiquitination	[1]
113	YKVDENGKISRLRRE	acetylation	[7]
113	YKVDENGKISRLRRE	ubiquitination	[1]
143	FDRHYCGKCCLTYCF	acetylation	[3]
152	CLTYCFNKPEDK***	acetylation	[3, 5, 6, 7, 8, 9, 10]
152	CLTYCFNKPEDK***	ubiquitination	[1]

[1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[2] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144]
[3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[4] 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]
[5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
[6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
[7] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[8] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
[9] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
[10] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]

Functional Description

Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.

DOMAIN 1 76 Ubiquitin-like.
ZN_FING 121 144 C4-type.
BINDING 54 54 Activating enzyme.
BINDING 72 72 Activating enzyme.
MOD_RES 57 57 Phosphoserine.
MOD_RES 104 104 N6-acetyllysine (By similarity).
MOD_RES 113 113 N6-acetyllysine (By similarity).
CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys)

Acetylation; Complete proteome; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation; Zinc; Zinc-finger.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0022627; C:cytosolic small ribosomal subunit; IEA:Compara.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0003735; F:structural constituent of ribosome; IEA:Compara.
GO:0006412; P:translation; IEA:InterPro.

IPR002906; Ribosomal_S27a.
IPR000626; Ubiquitin.
IPR019954; Ubiquitin_CS.
IPR019956; Ubiquitin_subgr.
IPR019955; Ubiquitin_supergroup.

PF01599; Ribosomal_S27
PF00240; ubiquitin

PS00299; UBIQUITIN_1
PS50053; UBIQUITIN_2