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Q8IWV8

- UBR2_HUMAN

UniProt

Q8IWV8 - UBR2_HUMAN

Protein

E3 ubiquitin-protein ligase UBR2

Gene

UBR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    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.3 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri97 – 16872UBR-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1108 – 1214107RING-type; atypicalAdd
    BLAST

    GO - Molecular functioni

    1. leucine binding Source: UniProtKB
    2. ligase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. ubiquitin-protein transferase activity Source: Ensembl
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to leucine Source: UniProtKB
    2. chromatin silencing Source: UniProtKB
    3. histone H2A ubiquitination Source: UniProtKB
    4. male meiosis I Source: Ensembl
    5. negative regulation of TOR signaling Source: UniProtKB
    6. spermatogenesis Source: Ensembl
    7. ubiquitin-dependent protein catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase UBR2 (EC:6.3.2.-)
    Alternative name(s):
    N-recognin-2
    Ubiquitin-protein ligase E3-alpha-2
    Ubiquitin-protein ligase E3-alpha-II
    Gene namesi
    Name:UBR2
    Synonyms:C6orf133, KIAA0349
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21289. UBR2.

    Subcellular locationi

    Nucleus By similarity
    Note: Associated with chromatin during meiosis.

    GO - Cellular componenti

    1. chromatin Source: Ensembl
    2. nucleus Source: HPA
    3. plasma membrane Source: HPA
    4. ubiquitin ligase complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA128394621.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 17551754E3 ubiquitin-protein ligase UBR2PRO_0000056140Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8IWV8.
    PaxDbiQ8IWV8.
    PRIDEiQ8IWV8.

    PTM databases

    PhosphoSiteiQ8IWV8.

    Expressioni

    Tissue specificityi

    Broadly expressed, with highest levels in skeletal muscle, kidney and pancreas. Present in acinar cells of the pancreas (at protein level).2 Publications

    Developmental stagei

    Expressed in fetal pancreas.1 Publication

    Gene expression databases

    ArrayExpressiQ8IWV8.
    BgeeiQ8IWV8.
    CleanExiHS_UBR2.
    GenevestigatoriQ8IWV8.

    Organism-specific databases

    HPAiHPA027869.
    HPA027880.

    Interactioni

    Subunit structurei

    Interacts with UBE2B; promotes the UBE2B-H2A interaction and the ubiquitination of histone H2A by UBE2B and UBR2 By similarity. Interacts with RECQL4.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    vifP125043EBI-1237260,EBI-779991From a different organism.

    Protein-protein interaction databases

    BioGridi116896. 15 interactions.
    DIPiDIP-38165N.
    IntActiQ8IWV8. 7 interactions.
    STRINGi9606.ENSP00000361990.

    Structurei

    Secondary structure

    1
    1755
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi108 – 1125
    Turni113 – 1153
    Beta strandi116 – 1183
    Helixi125 – 1295
    Helixi132 – 1354
    Beta strandi138 – 1425
    Turni154 – 1563
    Beta strandi157 – 1593
    Turni164 – 1663

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NY2X-ray2.61A/B/C/D/E/F/G/H98-167[»]
    3NY3X-ray1.60A98-167[»]
    ProteinModelPortaliQ8IWV8.
    SMRiQ8IWV8. Positions 98-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IWV8.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1019 – 105436Sequence AnalysisAdd
    BLAST

    Domaini

    The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif.
    The UBR-type zinc finger forms a pocket that mediates recognition of type 1 N-degrons. It exhibits preference for Arginine in first position, has poor affinity for histidine, and doesn't bind acetylated peptides.

    Sequence similaritiesi

    Belongs to the UBR1 family.Curated
    Contains 1 RING-type zinc finger.Curated
    Contains 1 UBR-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri97 – 16872UBR-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1108 – 1214107RING-type; atypicalAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG310244.
    HOGENOMiHOG000231769.
    HOVERGENiHBG080426.
    KOiK10626.
    OMAiSHEELPC.
    OrthoDBiEOG7RNJZB.
    PhylomeDBiQ8IWV8.
    TreeFamiTF323875.

    Family and domain databases

    Gene3Di3.30.1390.10. 1 hit.
    InterProiIPR003769. ClpS_core.
    IPR014719. Ribosomal_L7/12_C/ClpS-like.
    IPR003126. Znf_N-recognin.
    IPR013993. Znf_N-recognin_met.
    IPR001841. Znf_RING.
    [Graphical view]
    PfamiPF02617. ClpS. 1 hit.
    PF02207. zf-UBR. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    SM00396. ZnF_UBR1. 1 hit.
    [Graphical view]
    SUPFAMiSSF54736. SSF54736. 1 hit.
    PROSITEiPS51157. ZF_UBR. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IWV8-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASELEPEVQ AIDRSLLECS AEEIAGKWLQ ATDLTREVYQ HLAHYVPKIY     50
    CRGPNPFPQK EDMLAQHVLL GPMEWYLCGE DPAFGFPKLE QANKPSHLCG 100
    RVFKVGEPTY SCRDCAVDPT CVLCMECFLG SIHRDHRYRM TTSGGGGFCD 150
    CGDTEAWKEG PYCQKHELNT SEIEEEEDPL VHLSEDVIAR TYNIFAITFR 200
    YAVEILTWEK ESELPADLEM VEKSDTYYCM LFNDEVHTYE QVIYTLQKAV 250
    NCTQKEAIGF ATTVDRDGRR SVRYGDFQYC EQAKSVIVRN TSRQTKPLKV 300
    QVMHSSIVAH QNFGLKLLSW LGSIIGYSDG LRRILCQVGL QEGPDGENSS 350
    LVDRLMLSDS KLWKGARSVY HQLFMSSLLM DLKYKKLFAV RFAKNYQQLQ 400
    RDFMEDDHER AVSVTALSVQ FFTAPTLARM LITEENLMSI IIKTFMDHLR 450
    HRDAQGRFQF ERYTALQAFK FRRVQSLILD LKYVLISKPT EWSDELRQKF 500
    LEGFDAFLEL LKCMQGMDPI TRQVGQHIEM EPEWEAAFTL QMKLTHVISM 550
    MQDWCASDEK VLIEAYKKCL AVLMQCHGGY TDGEQPITLS ICGHSVETIR 600
    YCVSQEKVSI HLPVSRLLAG LHVLLSKSEV AYKFPELLPL SELSPPMLIE 650
    HPLRCLVLCA QVHAGMWRRN GFSLVNQIYY YHNVKCRREM FDKDVVMLQT 700
    GVSMMDPNHF LMIMLSRFEL YQIFSTPDYG KRFSSEITHK DVVQQNNTLI 750
    EEMLYLIIML VGERFSPGVG QVNATDEIKR EIIHQLSIKP MAHSELVKSL 800
    PEDENKETGM ESVIEAVAHF KKPGLTGRGM YELKPECAKE FNLYFYHFSR 850
    AEQSKAEEAQ RKLKRQNRED TALPPPVLPP FCPLFASLVN ILQSDVMLCI 900
    MGTILQWAVE HNGYAWSESM LQRVLHLIGM ALQEEKQHLE NVTEEHVVTF 950
    TFTQKISKPG EAPKNSPSIL AMLETLQNAP YLEVHKDMIR WILKTFNAVK 1000
    KMRESSPTSP VAETEGTIME ESSRDKDKAE RKRKAEIARL RREKIMAQMS 1050
    EMQRHFIDEN KELFQQTLEL DASTSAVLDH SPVASDMTLT ALGPAQTQVP 1100
    EQRQFVTCIL CQEEQEVKVE SRAMVLAAFV QRSTVLSKNR SKFIQDPEKY 1150
    DPLFMHPDLS CGTHTSSCGH IMHAHCWQRY FDSVQAKEQR RQQRLRLHTS 1200
    YDVENGEFLC PLCECLSNTV IPLLLPPRNI FNNRLNFSDQ PNLTQWIRTI 1250
    SQQIKALQFL RKEESTPNNA STKNSENVDE LQLPEGFRPD FRPKIPYSES 1300
    IKEMLTTFGT ATYKVGLKVH PNEEDPRVPI MCWGSCAYTI QSIERILSDE 1350
    DKPLFGPLPC RLDDCLRSLT RFAAAHWTVA SVSVVQGHFC KLFASLVPND 1400
    SHEELPCILD IDMFHLLVGL VLAFPALQCQ DFSGISLGTG DLHIFHLVTM 1450
    AHIIQILLTS CTEENGMDQE NPPCEEESAV LALYKTLHQY TGSALKEIPS 1500
    GWHLWRSVRA GIMPFLKCSA LFFHYLNGVP SPPDIQVPGT SHFEHLCSYL 1550
    SLPNNLICLF QENSEIMNSL IESWCRNSEV KRYLEGERDA IRYPRESNKL 1600
    INLPEDYSSL INQASNFSCP KSGGDKSRAP TLCLVCGSLL CSQSYCCQTE 1650
    LEGEDVGACT AHTYSCGSGV GIFLRVRECQ VLFLAGKTKG CFYSPPYLDD 1700
    YGETDQGLRR GNPLHLCKER FKKIQKLWHQ HSVTEEIGHA QEANQTLVGI 1750
    DWQHL 1755
    Length:1,755
    Mass (Da):200,538
    Last modified:March 1, 2003 - v1
    Checksum:i04B14FCB13E21808
    GO
    Isoform 2 (identifier: Q8IWV8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         397-439: QQLQRDFMED...MLITEENLMS → ERLQSDYVTD...ISAGRSGSPL
         440-1755: Missing.

    Show »
    Length:439
    Mass (Da):49,978
    Checksum:iD1A9B29DF254AE1F
    GO
    Isoform 3 (identifier: Q8IWV8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-496: Missing.
         497-514: RQKFLEGFDAFLELLKCM → MYAGNIPIYKTESRSRNE
         1022-1071: SSRDKDKAER...ELFQQTLELD → HNFRVQGTKT...MKTKNSFSRH
         1072-1755: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:575
    Mass (Da):66,052
    Checksum:iEC2722AF55B26BD3
    GO
    Isoform 4 (identifier: Q8IWV8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         397-426: QQLQRDFMEDDHERAVSVTALSVQFFTAPT → ERLQSDYVTDDHDREFSVADLSVQIFTVPS

    Note: Derived from mouse cDNA data. No experimental confirmation available.

    Show »
    Length:1,755
    Mass (Da):200,540
    Checksum:i6FE8C7C600C162EE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti864 – 8641K → R in BAC86295. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti172 – 1721E → D.
    Corresponds to variant rs6905054 [ dbSNP | Ensembl ].
    VAR_052117
    Natural varianti1095 – 10951A → P.
    Corresponds to variant rs6917033 [ dbSNP | Ensembl ].
    VAR_059816
    Natural varianti1095 – 10951A → S.
    Corresponds to variant rs6917033 [ dbSNP | Ensembl ].
    VAR_059817
    Natural varianti1095 – 10951A → T.1 Publication
    Corresponds to variant rs6917033 [ dbSNP | Ensembl ].
    VAR_023283

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 496496Missing in isoform 3. 1 PublicationVSP_015166Add
    BLAST
    Alternative sequencei397 – 43943QQLQR…ENLMS → ERLQSDYVTDDHDREFSVAD LSVQIFTVPSLFSISAGRSG SPL in isoform 2. 1 PublicationVSP_015167Add
    BLAST
    Alternative sequencei397 – 42630QQLQR…FTAPT → ERLQSDYVTDDHDREFSVAD LSVQIFTVPS in isoform 4. CuratedVSP_017130Add
    BLAST
    Alternative sequencei440 – 17551316Missing in isoform 2. 1 PublicationVSP_015168Add
    BLAST
    Alternative sequencei497 – 51418RQKFL…LLKCM → MYAGNIPIYKTESRSRNE in isoform 3. 1 PublicationVSP_015169Add
    BLAST
    Alternative sequencei1022 – 107150SSRDK…TLELD → HNFRVQGTKTKLRGREKQRL PDCAEKRSWLRCLKCSGILL MKTKNSFSRH in isoform 3. 1 PublicationVSP_015170Add
    BLAST
    Alternative sequencei1072 – 1755684Missing in isoform 3. 1 PublicationVSP_015171Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY061884 mRNA. Translation: AAL32101.1.
    AK125795 mRNA. Translation: BAC86295.1.
    AL049843, AL136223, AL391814 Genomic DNA. Translation: CAI20399.1.
    AL049843, AL136223, AL391814 Genomic DNA. Translation: CAI95685.1.
    AL136223, AL391814 Genomic DNA. Translation: CAI19919.1.
    AL136223, AL049843, AL391814 Genomic DNA. Translation: CAI19920.1.
    AL136223, AL049843, AL391814 Genomic DNA. Translation: CAI95666.1.
    AL391814, AL136223 Genomic DNA. Translation: CAI14737.1.
    AL391814, AL136223, AL049843 Genomic DNA. Translation: CAI14738.1.
    AL391814, AL049843, AL136223 Genomic DNA. Translation: CAI95298.1.
    BC024217 mRNA. Translation: AAH24217.1.
    BC064512 mRNA. Translation: AAH64512.1.
    AB002347 mRNA. Translation: BAA20806.1.
    CCDSiCCDS4870.1. [Q8IWV8-1]
    CCDS55001.1. [Q8IWV8-2]
    RefSeqiNP_001171730.1. NM_001184801.1. [Q8IWV8-2]
    NP_056070.1. NM_015255.2. [Q8IWV8-1]
    XP_005249022.1. XM_005248965.2. [Q8IWV8-4]
    UniGeneiHs.529925.

    Genome annotation databases

    EnsembliENST00000372899; ENSP00000361990; ENSG00000024048. [Q8IWV8-1]
    ENST00000372901; ENSP00000361992; ENSG00000024048. [Q8IWV8-4]
    ENST00000372903; ENSP00000361994; ENSG00000024048. [Q8IWV8-2]
    GeneIDi23304.
    KEGGihsa:23304.
    UCSCiuc003osf.3. human. [Q8IWV8-2]
    uc011dur.2. human. [Q8IWV8-1]
    uc011dus.2. human. [Q8IWV8-4]

    Polymorphism databases

    DMDMi73622073.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY061884 mRNA. Translation: AAL32101.1 .
    AK125795 mRNA. Translation: BAC86295.1 .
    AL049843 , AL136223 , AL391814 Genomic DNA. Translation: CAI20399.1 .
    AL049843 , AL136223 , AL391814 Genomic DNA. Translation: CAI95685.1 .
    AL136223 , AL391814 Genomic DNA. Translation: CAI19919.1 .
    AL136223 , AL049843 , AL391814 Genomic DNA. Translation: CAI19920.1 .
    AL136223 , AL049843 , AL391814 Genomic DNA. Translation: CAI95666.1 .
    AL391814 , AL136223 Genomic DNA. Translation: CAI14737.1 .
    AL391814 , AL136223 , AL049843 Genomic DNA. Translation: CAI14738.1 .
    AL391814 , AL049843 , AL136223 Genomic DNA. Translation: CAI95298.1 .
    BC024217 mRNA. Translation: AAH24217.1 .
    BC064512 mRNA. Translation: AAH64512.1 .
    AB002347 mRNA. Translation: BAA20806.1 .
    CCDSi CCDS4870.1. [Q8IWV8-1 ]
    CCDS55001.1. [Q8IWV8-2 ]
    RefSeqi NP_001171730.1. NM_001184801.1. [Q8IWV8-2 ]
    NP_056070.1. NM_015255.2. [Q8IWV8-1 ]
    XP_005249022.1. XM_005248965.2. [Q8IWV8-4 ]
    UniGenei Hs.529925.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3NY2 X-ray 2.61 A/B/C/D/E/F/G/H 98-167 [» ]
    3NY3 X-ray 1.60 A 98-167 [» ]
    ProteinModelPortali Q8IWV8.
    SMRi Q8IWV8. Positions 98-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116896. 15 interactions.
    DIPi DIP-38165N.
    IntActi Q8IWV8. 7 interactions.
    STRINGi 9606.ENSP00000361990.

    PTM databases

    PhosphoSitei Q8IWV8.

    Polymorphism databases

    DMDMi 73622073.

    Proteomic databases

    MaxQBi Q8IWV8.
    PaxDbi Q8IWV8.
    PRIDEi Q8IWV8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372899 ; ENSP00000361990 ; ENSG00000024048 . [Q8IWV8-1 ]
    ENST00000372901 ; ENSP00000361992 ; ENSG00000024048 . [Q8IWV8-4 ]
    ENST00000372903 ; ENSP00000361994 ; ENSG00000024048 . [Q8IWV8-2 ]
    GeneIDi 23304.
    KEGGi hsa:23304.
    UCSCi uc003osf.3. human. [Q8IWV8-2 ]
    uc011dur.2. human. [Q8IWV8-1 ]
    uc011dus.2. human. [Q8IWV8-4 ]

    Organism-specific databases

    CTDi 23304.
    GeneCardsi GC06P042531.
    HGNCi HGNC:21289. UBR2.
    HPAi HPA027869.
    HPA027880.
    MIMi 609134. gene.
    neXtProti NX_Q8IWV8.
    PharmGKBi PA128394621.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG310244.
    HOGENOMi HOG000231769.
    HOVERGENi HBG080426.
    KOi K10626.
    OMAi SHEELPC.
    OrthoDBi EOG7RNJZB.
    PhylomeDBi Q8IWV8.
    TreeFami TF323875.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    EvolutionaryTracei Q8IWV8.
    GeneWikii UBR2.
    GenomeRNAii 23304.
    NextBioi 45149.
    PROi Q8IWV8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IWV8.
    Bgeei Q8IWV8.
    CleanExi HS_UBR2.
    Genevestigatori Q8IWV8.

    Family and domain databases

    Gene3Di 3.30.1390.10. 1 hit.
    InterProi IPR003769. ClpS_core.
    IPR014719. Ribosomal_L7/12_C/ClpS-like.
    IPR003126. Znf_N-recognin.
    IPR013993. Znf_N-recognin_met.
    IPR001841. Znf_RING.
    [Graphical view ]
    Pfami PF02617. ClpS. 1 hit.
    PF02207. zf-UBR. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    SM00396. ZnF_UBR1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54736. SSF54736. 1 hit.
    PROSITEi PS51157. ZF_UBR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Regulation of protein catabolism by muscle-specific and cytokine-inducible ubiquitin ligase E3alpha-II during cancer cachexia."
      Kwak K.S., Zhou X., Solomon V., Baracos V.E., Davis J., Bannon A.W., Boyle W.J., Lacey D.L., Han H.Q.
      Cancer Res. 64:8193-8198(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Testis.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Ovary.
    5. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 481-1755 (ISOFORMS 1/4), VARIANT THR-1095.
      Tissue: Brain.
    6. "RECQL4, mutated in the Rothmund-Thomson and RAPADILINO syndromes, interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway."
      Yin J., Kwon Y.T., Varshavsky A., Wang W.
      Hum. Mol. Genet. 13:2421-2430(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RECQL4, IDENTIFICATION BY MASS SPECTROMETRY.
    7. Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Role of N-end rule ubiquitin ligases UBR1 and UBR2 in regulating the leucine-mTOR signaling pathway."
      Kume K., Iizumi Y., Shimada M., Ito Y., Kishi T., Yamaguchi Y., Handa H.
      Genes Cells 15:339-349(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Structural basis of substrate recognition and specificity in the N-end rule pathway."
      Matta-Camacho E., Kozlov G., Li F.F., Gehring K.
      Nat. Struct. Mol. Biol. 17:1182-1187(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 98-167 ALONE AND IN COMPLEX WITH N-END RULE PEPTIDE, UBR-TYPE ZINC FINGER, FUNCTION.

    Entry informationi

    Entry nameiUBR2_HUMAN
    AccessioniPrimary (citable) accession number: Q8IWV8
    Secondary accession number(s): O15057
    , Q4VXK2, Q5TFH6, Q6P2I2, Q6ZUD0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3