CPLM-009629

Genbank Nucleotide ID

Peptidyl-prolyl cis-trans isomerase A

Protein Synonyms/Alias

PPIase A; Cyclophilin A; Cyclosporin A-binding protein; Rotamase A; Peptidyl-prolyl cis-trans isomerase A, N-terminally processed

Homo sapiens (Human)

Position	Peptide	Type	References
28	SFELFADKVPKTAEN	acetylation	[1]
28	SFELFADKVPKTAEN	ubiquitination	[2, 3, 4, 5, 6, 7]
31	LFADKVPKTAENFRA	ubiquitination	[4, 5, 6]
44	RALSTGEKGFGYKGS	acetylation	[1]
44	RALSTGEKGFGYKGS	ubiquitination	[4, 5, 6, 8]
49	GEKGFGYKGSCFHRI	acetylation	[1]
49	GEKGFGYKGSCFHRI	ubiquitination	[4, 6, 8]
76	RHNGTGGKSIYGEKF	acetylation	[1]
76	RHNGTGGKSIYGEKF	ubiquitination	[4, 5, 6, 7, 8, 9]
82	GKSIYGEKFEDENFI	acetylation	[1]
82	GKSIYGEKFEDENFI	ubiquitination	[3, 4, 5, 6, 7, 8, 9]
91	EDENFILKHTGPGIL	ubiquitination	[6, 10]
118	QFFICTAKTEWLDGK	acetylation	[1, 11]
118	QFFICTAKTEWLDGK	ubiquitination	[4, 6, 10]
125	KTEWLDGKHVVFGKV	acetylation	[1, 11, 12, 13, 14, 15, 16]
125	KTEWLDGKHVVFGKV	ubiquitination	[3, 4, 5, 6, 7, 8, 10, 16, 17]
131	GKHVVFGKVKEGMNI	acetylation	[1, 15, 16]
131	GKHVVFGKVKEGMNI	ubiquitination	[3, 4, 5, 6, 7, 8]
133	HVVFGKVKEGMNIVE	ubiquitination	[4, 5, 6, 8, 10, 16]
155	RNGKTSKKITIADCG	acetylation	[16]
155	RNGKTSKKITIADCG	ubiquitination	[6, 8, 10, 16]

[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] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
Meierhofer D, Wang X, Huang L, Kaiser P.
J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
[3] 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]
[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] 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]
[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] 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]
[8] 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]
[9] 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]
[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] 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]
[12] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
[13] Proteome-wide prediction of acetylation substrates.
Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
[14] 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]
[15] 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]
[16] 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]
[17] 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]

Functional Description

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

DOMAIN 7 163 PPIase cyclophilin-type.
MOD_RES 1 1 N-acetylmethionine.
MOD_RES 2 2 N-acetylvaline; partial; in Peptidyl-
MOD_RES 21 21 Phosphoserine (By similarity).
MOD_RES 28 28 N6-acetyllysine; alternate.
MOD_RES 44 44 N6-acetyllysine.
MOD_RES 76 76 N6-acetyllysine.
MOD_RES 82 82 N6-acetyllysine.
MOD_RES 93 93 Phosphothreonine.
MOD_RES 125 125 N6-acetyllysine.
MOD_RES 131 131 N6-acetyllysine.
CARBOHYD 108 108 N-linked (GlcNAc...) (Potential).
CROSSLNK 28 28 Glycyl lysine isopeptide (Lys-Gly)

3D-structure; Acetylation; Complete proteome; Cyclosporin; Cytoplasm; Direct protein sequencing; Glycoprotein; Host-virus interaction; Isomerase; Isopeptide bond; Phosphoprotein; Reference proteome; Rotamase; Secreted; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; IDA:UniProtKB.
GO:0005576; C:extracellular region; TAS:Reactome.
GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0042277; F:peptide binding; IEA:UniProtKB-KW.
GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
GO:0051082; F:unfolded protein binding; TAS:UniProtKB.
GO:0046790; F:virion binding; NAS:UniProtKB.
GO:0030260; P:entry into host cell; TAS:Reactome.
GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
GO:0050900; P:leukocyte migration; TAS:Reactome.
GO:0034389; P:lipid particle organization; IMP:UniProtKB.
GO:0030168; P:platelet activation; TAS:Reactome.
GO:0002576; P:platelet degranulation; TAS:Reactome.
GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
GO:0006457; P:protein folding; TAS:UniProtKB.
GO:0006278; P:RNA-dependent DNA replication; TAS:Reactome.
GO:0019061; P:uncoating of virus; TAS:Reactome.
GO:0019076; P:viral release from host cell; TAS:UniProtKB.

IPR002130; Cyclophilin-like_PPIase_dom.
IPR024936; Cyclophilin-type_PPIase.
IPR020892; Cyclophilin-type_PPIase_CS.

PF00160; Pro_isomerase

PS00170; CSA_PPIASE_1
PS50072; CSA_PPIASE_2

PR00153; CSAPPISMRASE.