UniProt Accession

 RS27A_HUMAN; P62979; P02248; P02249; P02250; P14798; P62988; Q29120; Q6LBL4; Q6LDU5; Q8WYN8; Q91887; Q91888; Q9BQ77; Q9BWD6; Q9BX98; Q9UEF2; Q9UEG1; Q9UEK8; Q9UPK7 

Genbank Protein ID

 X63237; S79522; AC012358; BC001392; BC066293; AB062071; M10939; AB007163 

Genbank Nucleotide ID

 CAA44911.1; AAB21188.1; AAH01392.1; AAH66293.1; BAB79490.1; AAA36788.1; BAA25826.1 

Protein Name

 Ubiquitin-40S ribosomal protein S27a 

Protein Synonyms/Alias

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

Gene Name

 RPS27A 

Gene Synonyms/Alias

 UBA80; UBCEP1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MQIFVKTLTGKTI	acetylation	[1, 2, 3]
6	**MQIFVKTLTGKTI	ubiquitination	[4, 5, 6, 7, 8]
11	FVKTLTGKTITLEVE	acetylation	[1]
11	FVKTLTGKTITLEVE	ubiquitination	[4, 5, 6, 7, 8]
27	SDTIENVKAKIQDKE	acetylation	[1]
27	SDTIENVKAKIQDKE	ubiquitination	[4, 5, 6, 7, 8]
29	TIENVKAKIQDKEGI	acetylation	[1]
29	TIENVKAKIQDKEGI	ubiquitination	[4, 5, 6, 7, 8]
33	VKAKIQDKEGIPPDQ	acetylation	[1]
33	VKAKIQDKEGIPPDQ	ubiquitination	[4, 5, 6, 7, 8]
48	QRLIFAGKQLEDGRT	acetylation	[1, 2]
48	QRLIFAGKQLEDGRT	ubiquitination	[4, 5, 6, 7, 8]
63	LSDYNIQKESTLHLV	acetylation	[1]
63	LSDYNIQKESTLHLV	ubiquitination	[4, 5, 6, 7, 8]
104	KVKLAVLKYYKVDEN	acetylation	[2, 9]
104	KVKLAVLKYYKVDEN	ubiquitination	[5, 6, 10, 11]
107	LAVLKYYKVDENGKI	acetylation	[2, 9, 12, 13]
107	LAVLKYYKVDENGKI	ubiquitination	[4, 5, 6, 8, 10, 11, 13]
113	YKVDENGKISRLRRE	acetylation	[2, 12, 13]
113	YKVDENGKISRLRRE	ubiquitination	[4, 5, 6, 7, 8, 10, 11, 13, 14, 15, 16]
143	FDRHYCGKCCLTYCF	acetylation	[13]
143	FDRHYCGKCCLTYCF	ubiquitination	[6, 7, 10, 11, 13]
152	CLTYCFNKPEDK***	acetylation	[2, 9, 13, 17]
152	CLTYCFNKPEDK***	ubiquitination	[6, 7, 10, 11, 13]
156	CFNKPEDK*******	ubiquitination	[13]

Reference

 [1] N-epsilon-acetylation of porcine mature erythrocytes ubiquitin.
 Zhu DX, Xu LX, Zhu NZ, Briand G, Han KK.
 Int J Biochem. 1985;17(6):719-21. [PMID: 2993057]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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]
 [13] 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]
 [14] Proteomic snapshot of the EGF-induced ubiquitin network.
 Argenzio E, Bange T, Oldrini B, Bianchi F, Peesari R, Mari S, Di Fiore PP, Mann M, Polo S.
 Mol Syst Biol. 2011 Jan 18;7:462. [PMID: 21245847]
 [15] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [16] 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]
 [17] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224] 

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. 

Sequence Annotation

 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 (By similarity).
 MOD_RES 104 104 N6-acetyllysine.
 MOD_RES 113 113 N6-acetyllysine.
 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)  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 156 AA 

Protein Sequence

Gene Ontology

 GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
 GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
 GO:0010008; C:endosome membrane; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
 GO:0000187; P:activation of MAPK activity; TAS:Reactome.
 GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
 GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
 GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
 GO:0016044; P:cellular membrane organization; TAS:Reactome.
 GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
 GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
 GO:0006281; P:DNA repair; TAS:Reactome.
 GO:0046788; P:egress of virus within host cell; TAS:Reactome.
 GO:0016197; P:endosomal transport; TAS:Reactome.
 GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
 GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0034220; P:ion transmembrane transport; TAS:Reactome.
 GO:0007254; P:JNK cascade; TAS:Reactome.
 GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
 GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
 GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
 GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
 GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
 GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0007220; P:Notch receptor processing; TAS:Reactome.
 GO:0007219; P:Notch signaling pathway; TAS:Reactome.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
 GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; TAS:Reactome.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
 GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
 GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0000209; P:protein polyubiquitination; TAS:Reactome.
 GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
 GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
 GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
 GO:0034166; P:toll-like receptor 10 signaling pathway; TAS:Reactome.
 GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome.
 GO:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome.
 GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
 GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome.
 GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
 GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
 GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
 GO:0006414; P:translational elongation; TAS:Reactome.
 GO:0006413; P:translational initiation; TAS:Reactome.
 GO:0006415; P:translational termination; TAS:Reactome.
 GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
 GO:0019082; P:viral protein processing; TAS:Reactome.
 GO:0019083; P:viral transcription; TAS:Reactome.
 GO:0019068; P:virion assembly; TAS:Reactome. 

Interpro

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

Pfam

 PF01599; Ribosomal_S27
 PF00240; ubiquitin 

SMART

 SM00213; UBQ 

PROSITE

 PS00299; UBIQUITIN_1
 PS50053; UBIQUITIN_2 

PRINTS

 PR00348; UBIQUITIN.