CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000711
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peptidyl-prolyl cis-trans isomerase H 
Protein Synonyms/Alias
 PPIase H; Rotamase H; Small nuclear ribonucleoprotein particle-specific cyclophilin H; CypH; U-snRNP-associated cyclophilin SnuCyp-20; USA-CYP 
Gene Name
 PPIH 
Gene Synonyms/Alias
 CYP20; CYPH 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
28GQEVGRMKIELFADVubiquitination[1]
38LFADVVPKTAENFRQacetylation[2]
38LFADVVPKTAENFRQubiquitination[1]
53FCTGEFRKDGVPIGYubiquitination[1]
61DGVPIGYKGSTFHRVubiquitination[1, 3, 4]
70STFHRVIKDFMIQGGubiquitination[1, 5]
101PFADENFKLRHSAPGubiquitination[1, 3, 4, 5, 6, 7, 8, 9]
137KCDWLDGKHVVFGKIubiquitination[1]
143GKHVVFGKIIDGLLVubiquitination[1]
153DGLLVMRKIENVPTGubiquitination[5]
164VPTGPNNKPKLPVVIubiquitination[1, 5]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [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] 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]
 [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] 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]
 [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] 
Functional Description
 PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone. 
Sequence Annotation
 DOMAIN 14 176 PPIase cyclophilin-type.  
Keyword
 3D-structure; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Isomerase; mRNA processing; mRNA splicing; Nucleus; Reference proteome; Rotamase; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 177 AA 
Protein Sequence
MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGE FRKDGVPIGY 60
KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN 120
GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIENVPTG PNNKPKLPVV ISQCGEM 177 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:BHF-UCL.
 GO:0016607; C:nuclear speck; IDA:BHF-UCL.
 GO:0005681; C:spliceosomal complex; IC:BHF-UCL.
 GO:0071001; C:U4/U6 snRNP; IDA:BHF-UCL.
 GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:BHF-UCL.
 GO:0016018; F:cyclosporin A binding; TAS:ProtInc.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:BHF-UCL.
 GO:0043021; F:ribonucleoprotein complex binding; IDA:BHF-UCL.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:BHF-UCL.
 GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
 GO:0006461; P:protein complex assembly; TAS:ProtInc.
 GO:0006457; P:protein folding; TAS:ProtInc. 
Interpro
 IPR002130; Cyclophilin-like_PPIase_dom.
 IPR024936; Cyclophilin-type_PPIase.
 IPR020892; Cyclophilin-type_PPIase_CS. 
Pfam
 PF00160; Pro_isomerase 
SMART
  
PROSITE
 PS00170; CSA_PPIASE_1
 PS50072; CSA_PPIASE_2 
PRINTS
 PR00153; CSAPPISMRASE.