CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007244
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 PKHD-type hydroxylase TPA1 
Protein Synonyms/Alias
 Termination and polyadenylation protein 1 
Gene Name
 TPA1 
Gene Synonyms/Alias
 YER049W 
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
17GEKERNSKQISLEEDacetylation[1]
44KTFQDGLKKEIEDSQubiquitination[2]
142AGKLSGSKTDMSINTubiquitination[2]
317AKTDNTPKESMTSVIacetylation[1]
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
 Part of a messenger ribonucleoprotein (mRNP) complex at the 3'-UTR of mRNAs. It associates specifically with components of the translation termination complex and is involved in both translation termination and in regulation of normal mRNA decay through translation termination-coupled poly(A) shortening. 
Sequence Annotation
 DOMAIN 141 247 Fe2OG dioxygenase.
 METAL 159 159 Iron (By similarity).
 METAL 161 161 Iron (By similarity).
 METAL 227 227 Iron (By similarity).
 BINDING 236 236 2-oxoglutarate (Potential).
 MOD_RES 607 607 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Vitamin C. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 644 AA 
Protein Sequence
MKRKTAEVKG EKERNSKQIS LEEDKIKGMF NPKIWDKTFQ DGLKKEIEDS QPYNWGTIHE 60
LVNDDLLRAV RKEIETEIHF TKKETDIYRV NQSGDLANLS GLDWDDLSRL PNLFKLRQIL 120
YSKQYRDFFG YVTKAGKLSG SKTDMSINTY TKGCHLLTHD DVIGSRRISF ILYLPDPDRK 180
WKSHYGGGLR LFPSILPNVP HSDPSAKLVP QFNQIAFFKV LPGFSFHDVE EVKVDKHRLS 240
IQGWYHIPQV GEEGYIPGEE EAWVRNNTST LAQIESNVLE DFEFPKDERN ILSFHEVKHF 300
EKMLKGDAGA KTDNTPKESM TSVISDSVKL SEAEFTYLSQ YISPEHLSSK GIEKLQKQFV 360
ENSSLQIESF LNDDKSELLK KVIKQKELEQ ECPYHSKDVK APWKTAIPPH KARYLYIDGK 420
EYRNFQTEAD ILEALNNNDL PNFQFTKDAI KIISDASGNS RENNFDAELA LIDLAVFHKS 480
TIFKKYLALL TSLCPVSEQI LIRRFRPGMD FTLATKCRFN ELLKSNPDII DAVLEGTLCL 540
TPSAGWESGE LGGYELYMMD DDEDNKQYLK EDVEDASVYR ADDSGDSVLI NDPPAWNTFN 600
LVLRDESVLE FVKYVSWSAK SSRWDVKMKW DVKSCDEDGQ EDEA 644 
Gene Ontology
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
 GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro.
 GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
 GO:0008143; F:poly(A) RNA binding; IDA:SGD.
 GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:SGD.
 GO:0006415; P:translational termination; IMP:SGD. 
Interpro
 IPR005123; Oxoglu/Fe-dep_dioxygenase.
 IPR019601; Oxoglutarate/Fe-dep_Oase_C.
 IPR006620; Pro_4_hyd_alph. 
Pfam
 PF13640; 2OG-FeII_Oxy_3
 PF10637; Ofd1_CTDD 
SMART
 SM00702; P4Hc 
PROSITE
 PS51471; FE2OG_OXY 
PRINTS