| Tag | Content |
|---|
| CPLM ID | CPLM-015455 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | E3 ubiquitin-protein ligase UBR2 |
Protein Synonyms/Alias | N-recognin-2; Ubiquitin-protein ligase E3-alpha-2; Ubiquitin-protein ligase E3-alpha-II |
Gene Name | Ubr2 |
Gene Synonyms/Alias | Kiaa0349 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 361 | RLMLNDSKLWKGARS | ubiquitination | [1] | | 1187 | YFDSVQAKEQRRQQR | ubiquitination | [1] |
|
Reference | [1] 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] |
Functional Description | E3 ubiquitin-protein ligase 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. Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (By similarity). |
Sequence Annotation | ZN_FING 97 168 UBR-type.
ZN_FING 1108 1214 RING-type; atypical. |
Keyword | Alternative splicing; Coiled coil; Complete proteome; Ligase; Metal-binding; Nucleus; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1755 AA |
Protein Sequence | MASEMEPEVQ AIDRSLLECS AEEIAGRWLQ ATDLNREVYQ HLAHCVPKIY CRGPNPFPQK 60
EDTLAQHILL GPMEWYICAE DPALGFPKLE QANKPSHLCG RVFKVGEPTY SCRDCAVDPT 120
CVLCMECFLG SIHRDHRYRM TTSGGGGFCD CGDTEAWKEG PYCQKHKLSS SEVVEEEDPL 180
VHLSEDVIAR TYNIFAIMFR YAVDILTWEK ESELPEDLEV AEKSDTYYCM LFNDEVHTYE 240
QVIYTLQKAV NCTQKEAIGF ATTVDRDGRR SVRYGDFQYC DQAKTVIVRN TSRQTKPLKV 300
QVMHSSVAAH QNFGLKALSW LGSVIGYSDG LRRILCQVGL QEGPDGENSS LVDRLMLNDS 360
KLWKGARSVY HQLFMSSLLM DLKYKKLFAL RFAKNYRQLQ RDFMEDDHER AVSVTALSVQ 420
FFTAPTLARM LLTEENLMTV IIKAFMDHLK HRDAQGRFQF ERYTALQAFK FRRVQSLILD 480
LKYVLISKPT EWSDELRQKF LQGFDAFLEL LKCMQGMDPI TRQVGQHIEM EPEWEAAFTL 540
QMKLTHVISM VQDWCALDEK VLIEAYKKCL AVLTQCHGGF TDGEQPITLS ICGHSVETIR 600
YCVSQEKVSI HLPISRLLAG LHVLLSKSEV AYKFPELLPL SELSPPMLIE HPLRCLVLCA 660
QVHAGMWRRN GFSLVNQIYY YHNVKCRREM FDKDIVMLQT GVSMMDPNHF LMIMLSRFEL 720
YQLFSTPDYG KRFSSEVTHK DVVQQNNTLI EEMLYLIIML VGERFNPGVG QVAATDEIKR 780
EIIHQLSIKP MAHSELVKSL PEDENKETGM ESVIESVAHF KKPGLTGRGM YELKPECAKE 840
FNLYFYHFSR AEQSKAEEAQ RKLKRENKED TALPPPALPP FCPLFASLVN ILQCDVMLYI 900
MGTILQWAVE HHGSAWSESM LQRVLHLIGM ALQEEKHHLE NAVEGHVQTF TFTQKISKPG 960
DAPHNSPSIL AMLETLQNAP SLEAHKDMIR WLLKMFNAIK KIRECSSSSP VAEAEGTIME 1020
ESSRDKDKAE RKRKAEIARL RREKIMAQMS EMQRHFIDEN KELFQQTLEL DTSASATLDS 1080
SPPVSDAALT ALGPAQTQVP EPRQFVTCIL CQEEQEVTVG SRAMVLAAFV QRSTVLSKDR 1140
TKTIADPEKY DPLFMHPDLS CGTHTGSCGH VMHAHCWQRY FDSVQAKEQR RQQRLRLHTS 1200
YDVENGEFLC PLCECLSNTV IPLLLPPRSI LSRRLNFSDQ PDLAQWTRAV TQQIKVVQML 1260
RRKHNAADTS SSEDTEAMNI IPIPEGFRPD FYPRNPYSDS IKEMLTTFGT AAYKVGLKVH 1320
PNEGDPRVPI LCWGTCAYTI QSIERILSDE EKPVFGPLPC RLDDCLRSLT RFAAAHWTVA 1380
LLPVVQGHFC KLFASLVPSD SYEDLPCILD IDMFHLLVGL VLAFPALQCQ DFSGSSLATG 1440
DLHIFHLVTM AHIVQILLTS CTEENGMDQE NPTGEEELAI LSLHKTLHQY TGSALKEAPS 1500
GWHLWRSVRA AIMPFLKCSA LFFHYLNGVP APPDLQVSGT SHFEHLCNYL SLPTNLIHLF 1560
QENSDIMNSL IESWCQNSEV KRYLNGERGA ISYPRGANKL IDLPEDYSSL INQASNFSCP 1620
KSGGDKSRAP TLCLVCGSLL CSQSYCCQAE LEGEDVGACT AHTYSCGSGA GIFLRVRECQ 1680
VLFLAGKTKG CFYSPPYLDD YGETDQGLRR GNPLHLCQER FRKIQKLWQQ HSITEEIGHA 1740
QEANQTLVGI DWQHL 1755 |
Gene Ontology | GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0005886; C:plasma membrane; IEA:Compara. GO:0000151; C:ubiquitin ligase complex; IGI:MGI. GO:0070728; F:leucine binding; IEA:Compara. GO:0004842; F:ubiquitin-protein ligase activity; IDA:MGI. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0071233; P:cellular response to leucine; ISS:UniProtKB. GO:0006342; P:chromatin silencing; IDA:UniProtKB. GO:0033522; P:histone H2A ubiquitination; IDA:UniProtKB. GO:0007141; P:male meiosis I; IMP:MGI. GO:0032007; P:negative regulation of TOR signaling cascade; ISS:UniProtKB. GO:0007283; P:spermatogenesis; IMP:MGI. GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |