CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010987
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 5'-3' exoribonuclease 2 
Protein Synonyms/Alias
 Ribonucleic acid-trafficking protein 1; p116 
Gene Name
 RAT1 
Gene Synonyms/Alias
 HKE1; TAP1; YOR048C 
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
484DKNNELMKDISKEEIacetylation[1]
497EIDDAVSKANKTNFNacetylation[1]
500DAVSKANKTNFNLAEacetylation[1]
522NKKHRLEKDNEEEEIacetylation[1]
531NEEEEIAKDSKKVKTacetylation[1]
900WNFGNDLKQNIVPVGacetylation[1]
900WNFGNDLKQNIVPVGubiquitination[2]
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] 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, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Possesses 5'->3' exoribonuclease activity. Required for the processing of nuclear mRNA, rRNA and small nucleolar RNA (snoRNA) precursors. May promote termination of transcription by RNA polymerase II via the recruitment of 3'-end processing factors to the poly(A) site and by the degradation of nascent RNA downstream of the poly(A) site. 
Sequence Annotation
 REPEAT 955 958 1-1.
 REPEAT 961 964 2-1.
 REPEAT 972 975 2-2.
 REPEAT 975 978 3-1.
 REPEAT 984 986 3-2.
 REPEAT 996 999 1-2.
 REGION 492 529 Required for retention in the nucleus.
 REGION 955 999 2 X 4 AA repeats of S-R-Y-D, N-N-N-Y, Y-
 MOD_RES 574 574 Phosphoserine.  
Keyword
 Coiled coil; Complete proteome; Direct protein sequencing; Exonuclease; Hydrolase; mRNA processing; Nuclease; Nucleus; Phosphoprotein; Reference proteome; Repeat; rRNA processing; Transcription; Transcription regulation; Transcription termination. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1006 AA 
Protein Sequence
MGVPSFFRWL SRKYPKIISP VLEEQPQIVD GVILPLDYSA SNPNGELDNL YLDMNGIVHP 60
CSHPENKPPP ETEDEMLLAV FEYTNRVLNM ARPRKVLVMA VDGVAPRAKM NQQRARRFRS 120
ARDAQIENEA REEIMRQREE VGEIIDDAVR NKKTWDSNAI TPGTPFMDKL AAALRYWTAF 180
KLATDPGWKN LQVIISDATV PGEGEHKIMN FIRSQRADPE YNPNTTHCIY GLDADLIFLG 240
LATHEPHFKI LREDVFAQDN RKRNNLKDTI NMTEEEKQFL QKQNSEQPFL WLHINVLREY 300
LSAELWVPGL PFTFDLERAI DDWVFMCFFC GNDFLPHLPC LDVRENSIDI LLDIWKVVLP 360
KLKTYMTCDG VLNLPSVETL LQHLGSREGD IFKTRHIQEA RKKEAFERRK AQKNMSKGQD 420
RHPTVATEQL QMYDTQGNLA KGSWNLTTSD MVRLKKELML ANEGNEEAIA KVKQQSDKNN 480
ELMKDISKEE IDDAVSKANK TNFNLAEVMK QKIINKKHRL EKDNEEEEIA KDSKKVKTEK 540
AESECDLDAE IKDEIVADVN DRENSETTEV SRDSPVHSTV NVSEGPKNGV FDTDEFVKLF 600
EPGYHERYYT AKFHVTPQDI EQLRKDMVKC YIEGVAWVLM YYYQGCASWN WFYPYHYAPL 660
ATDFHGFSHL EIKFEEGTPF LPYEQLMSVL PAASGHALPK IFRSLMSEPD SEIIDFYPEE 720
FPIDMNGKKM SWQGIALLPF IDQDRLLTAV RAQYPLLSDA ERARNIRGEP VLLISNKNAN 780
YERFSKKLYS KENNNNNVVV KFQHFKSGLS GIVSKDVEGF ELNGKIVCPI QGGSLPNLST 840
TLILKMSYRL IPLPSRNKSI ILNGFIPSEP VLTAYDLDSI MYKYNNQNYS RRWNFGNDLK 900
QNIVPVGPKG ITQYKPRTGG YRAFFYFAEL SRNNVQPAHN YGRNSYNSQP GFNNSRYDGG 960
NNNYRQNSNY RNNNYSGNRN SGQYSGNSYS RNNKQSRYDN SRANRR 1006 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0004534; F:5'-3' exoribonuclease activity; IDA:SGD.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006364; P:rRNA processing; IMP:SGD.
 GO:0030847; P:termination of RNA polymerase II transcription, exosome-dependent; IMP:SGD.
 GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IMP:SGD. 
Interpro
 IPR027073; 5_3_exoribonuclease.
 IPR017151; 5_3_exoribonuclease_2.
 IPR004859; Put_53exo. 
Pfam
 PF03159; XRN_N 
SMART
  
PROSITE
  
PRINTS