CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004806
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase UBR1 
Protein Synonyms/Alias
 N-end-recognizing protein; N-recognin-1 
Gene Name
 UBR1 
Gene Synonyms/Alias
 PTR1; YGR184C; G7168 
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
1182HQARLLAKFNNQQTKacetylation[1]
1192NQQTKFMKEHESEFDubiquitination[2]
1679NTYVTQSKEIKLREEubiquitination[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
 Ubiquitin ligase protein which is a component of the N- end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. 
Sequence Annotation
 ZN_FING 121 194 UBR-type.
 ZN_FING 1220 1324 RING-type; atypical.
 REGION 1117 1219 Interaction with UBC2.
 MOD_RES 296 296 Phosphoserine.
 MOD_RES 300 300 Phosphoserine.
 MOD_RES 1938 1938 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Ligase; Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1950 AA 
Protein Sequence
MSVADDDLGS LQGHIRRTLR SIHNLPYFRY TRGPTERADM SRALKEFIYR YLYFVISNSG 60
ENLPTLFNAH PKQKLSNPEL TVFPDSLEDA VDIDKITSQQ TIPFYKIDES RIGDVHKHTG 120
RNCGRKFKIG EPLYRCHECG CDDTCVLCIH CFNPKDHVNH HVCTDICTEF TSGICDCGDE 180
EAWNSPLHCK AEEQENDISE DPATNADIKE EDVWNDSVNI ALVELVLAEV FDYFIDVFNQ 240
NIEPLPTIQK DITIKLREMT QQGKMYERAQ FLNDLKYEND YMFDGTTTAK TSPSNSPEAS 300
PSLAKIDPEN YTVIIYNDEY HNYSQATTAL RQGVPDNVHI DLLTSRIDGE GRAMLKCSQD 360
LSSVLGGFFA VQTNGLSATL TSWSEYLHQE TCKYIILWIT HCLNIPNSSF QTTFRNMMGK 420
TLCSEYLNAT ECRDMTPVVE KYFSNKFDKN DPYRYIDLSI LADGNQIPLG HHKILPESST 480
HSLSPLINDV ETPTSRTYSN TRLQHILYFD NRYWKRLRKD IQNVIIPTLA SSNLYKPIFC 540
QQVVEIFNHI TRSVAYMDRE PQLTAIRECV VQLFTCPTNA KNIFENQSFL DIVWSIIDIF 600
KEFCKVEGGV LIWQRVQKSN LTKSYSISFK QGLYTVETLL SKVHDPNIPL RPKEIISLLT 660
LCKLFNGAWK IKRKEGEHVL HEDQNFISYL EYTTSIYSII QTAEKVSEKS KDSIDSKLFL 720
NAIRIISSFL GNRSLTYKLI YDSHEVIKFS VSHERVAFMN PLQTMLSFLI EKVSLKDAYE 780
ALEDCSDFLK ISDFSLRSVV LCSQIDVGFW VRNGMSVLHQ ASYYKNNPEL GSYSRDIHLN 840
QLAILWERDD IPRIIYNILD RWELLDWFTG EVDYQHTVYE DKISFIIQQF IAFIYQILTE 900
RQYFKTFSSL KDRRMDQIKN SIIYNLYMKP LSYSKLLRSV PDYLTEDTTE FDEALEEVSV 960
FVEPKGLADN GVFKLKASLY AKVDPLKLLN LENEFESSAT IIKSHLAKDK DEIAKVVLIP 1020
QVSIKQLDKD ALNLGAFTRN TVFAKVVYKL LQVCLDMEDS TFLNELLHLV HGIFRDDELI 1080
NGKDSIPEAY LSKPICNLLL SIANAKSDVF SESIVRKADY LLEKMIMKKP NELFESLIAS 1140
FGNQYVNDYK DKKLRQGVNL QETEKERKRR LAKKHQARLL AKFNNQQTKF MKEHESEFDE 1200
QDNDVDMVGE KVYESEDFTC ALCQDSSSTD FFVIPAYHDH SPIFRPGNIF NPNEFMPMWD 1260
GFYNDDEKQA YIDDDVLEAL KENGSCGSRK VFVSCNHHIH HNCFKRYVQK KRFSSNAFIC 1320
PLCQTFSNCT LPLCQTSKAN TGLSLDMFLE SELSLDTLSR LFKPFTEENY RTINSIFSLM 1380
ISQCQGFDKA VRKRANFSHK DVSLILSVHW ANTISMLEIA SRLEKPYSIS FFRSREQKYK 1440
TLKNILVCIM LFTFVIGKPS MEFEPYPQQP DTVWNQNQLF QYIVRSALFS PVSLRQTVTE 1500
ALTTFSRQFL RDFLQGLSDA EQVTKLYAKA SKIGDVLKVS EQMLFALRTI SDVRMEGLDS 1560
ESIIYDLAYT FLLKSLLPTI RRCLVFIKVL HELVKDSENE TLVINGHEVE EELEFEDTAE 1620
FVNKALKMIT EKESLVDLLT TQESIVSHPY LENIPYEYCG IIKLIDLSKY LNTYVTQSKE 1680
IKLREERSQH MKNADNRLDF KICLTCGVKV HLRADRHEMT KHLNKNCFKP FGAFLMPNSS 1740
EVCLHLTQPP SNIFISAPYL NSHGEVGRNA MRRGDLTTLN LKRYEHLNRL WINNEIPGYI 1800
SRVMGDEFRV TILSNGFLFA FNREPRPRRI PPTDEDDEDM EEGEDGFFTE GNDEMDVDDE 1860
TGQAANLFGV GAEGIAGGGV RDFFQFFENF RNTLQPQGNG DDDAPQNPPP ILQFLGPQFD 1920
GATIIRNTNP RNLDEDDSDD NDDSDEREIW 1950 
Gene Ontology
 GO:0005737; C:cytoplasm; IMP:SGD.
 GO:0004842; F:ubiquitin-protein ligase activity; IMP:SGD.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0071629; P:cytoplasm-associated proteasomal ubiquitin-dependent protein catabolic process; IMP:SGD.
 GO:0000209; P:protein polyubiquitination; IMP:SGD.
 GO:0090089; P:regulation of dipeptide transport; IMP:SGD.
 GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IMP:SGD. 
Interpro
 IPR003769; ClpS_core.
 IPR003126; Znf_N-recognin.
 IPR013993; Znf_N-recognin_met.
 IPR001841; Znf_RING. 
Pfam
 PF02617; ClpS
 PF02207; zf-UBR 
SMART
 SM00184; RING
 SM00396; ZnF_UBR1 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2
 PS51157; ZF_UBR 
PRINTS