CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006301
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 H/ACA ribonucleoprotein complex subunit 4 
Protein Synonyms/Alias
 Centromere-binding factor 5; Centromere/microtubule-binding protein CBF5; H/ACA snoRNP protein CBF5; Small nucleolar RNP protein CBF5; p64' 
Gene Name
 CBF5 
Gene Synonyms/Alias
 YLR175W; L9470.11 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
3*****MSKEDFVIKPacetylation[1]
9SKEDFVIKPEAAGASacetylation[1]
9SKEDFVIKPEAAGASubiquitination[2, 3]
31LLLKNFDKLLVRSGHacetylation[1]
31LLLKNFDKLLVRSGHubiquitination[3]
50PAGSSPLKRDLKSYIubiquitination[3]
80HEVVAWIKRILRCEKubiquitination[3]
87KRILRCEKTGHSGTLubiquitination[3]
114DRATRLVKSQQGAGKubiquitination[3]
121KSQQGAGKEYVCIVRubiquitination[3]
134VRLHDALKDEKDLGRacetylation[1]
137HDALKDEKDLGRSLEubiquitination[2]
161PPLISAVKRQLRVRTubiquitination[3]
180NLIEFDNKRNLGVFWacetylation[1]
180NLIEFDNKRNLGVFWubiquitination[3]
267ETLLVGYKRIVVKDSubiquitination[2, 3]
272GYKRIVVKDSAVNAVubiquitination[3]
384NTPEQWKKEYVPLDNubiquitination[3]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [3] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. May function as a pseudouridine synthase. Binds in vitro to centromeres and microtubules. It is a centromeric DNA-CBF3-binding factor which is involved in mitotic chromosome segregation. Essential for cell growth. 
Sequence Annotation
 DOMAIN 266 341 PUA.
 REPEAT 434 436 1.
 REPEAT 437 439 2.
 REPEAT 440 442 3.
 REPEAT 443 445 4.
 REPEAT 446 448 5.
 REPEAT 449 451 6.
 REPEAT 452 454 7.
 REPEAT 455 457 8.
 REPEAT 458 460 9.
 REPEAT 461 463 10.
 REGION 434 463 10 X 3 AA tandem repeats of K-K-[DE].
 ACT_SITE 95 95 Nucleophile (By similarity).
 MOD_RES 47 47 Phosphoserine.
 MOD_RES 378 378 Phosphothreonine.
 MOD_RES 399 399 Phosphoserine; by ATM or ATR.  
Keyword
 3D-structure; Cell cycle; Cell division; Centromere; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; DNA-binding; Isomerase; Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 483 AA 
Protein Sequence
MSKEDFVIKP EAAGASTDTS EWPLLLKNFD KLLVRSGHYT PIPAGSSPLK RDLKSYISSG 60
VINLDKPSNP SSHEVVAWIK RILRCEKTGH SGTLDPKVTG CLIVCIDRAT RLVKSQQGAG 120
KEYVCIVRLH DALKDEKDLG RSLENLTGAL FQRPPLISAV KRQLRVRTIY ESNLIEFDNK 180
RNLGVFWASC EAGTYMRTLC VHLGMLLGVG GHMQELRRVR SGALSENDNM VTLHDVMDAQ 240
WVYDNTRDES YLRSIIQPLE TLLVGYKRIV VKDSAVNAVC YGAKLMIPGL LRYEEGIELY 300
DEIVLITTKG EAIAVAIAQM STVDLASCDH GVVASVKRCI MERDLYPRRW GLGPVAQKKK 360
QMKADGKLDK YGRVNENTPE QWKKEYVPLD NAEQSTSSSQ ETKETEEEPK KAKEDSLIKE 420
VETEKEEVKE DDSKKEKKEK KDKKEKKEKK EKKDKKEKKE KKEKKRKSED GDSEEKKSKK 480
SKK 483 
Gene Ontology
 GO:0030686; C:90S preribosome; IDA:SGD.
 GO:0031429; C:box H/ACA snoRNP complex; IPI:SGD.
 GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0009982; F:pseudouridine synthase activity; IMP:SGD.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0000495; P:box H/ACA snoRNA 3'-end processing; IMP:SGD.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0031118; P:rRNA pseudouridine synthesis; IMP:SGD.
 GO:0031120; P:snRNA pseudouridine synthesis; IDA:SGD. 
Interpro
 IPR012960; Dyskerin-like.
 IPR002501; PsdUridine_synth.
 IPR020103; PsdUridine_synth_cat_dom.
 IPR002478; PUA.
 IPR015947; PUA-like_domain.
 IPR004802; tRNA_PsdUridine_synth_B_fam.
 IPR004521; Uncharacterised_CHP00451. 
Pfam
 PF08068; DKCLD
 PF01472; PUA
 PF01509; TruB_N 
SMART
 SM00359; PUA 
PROSITE
 PS50890; PUA 
PRINTS