Details for: RNF31

Gene ID: 55072

Symbol: RNF31

Ensembl ID: ENSG00000092098

Description: ring finger protein 31

Associated with

Other Information

Genular Protein ID: 712479129

Symbol: RNF31_HUMAN

Name: E3 ubiquitin-protein ligase RNF31

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 15093743

Title: Identification of the protein Zibra, its genomic organization, regulation, and expression in breast cancer cells.

PubMed ID: 15093743

DOI: 10.1016/j.yexcr.2004.01.019

PubMed ID: 17006537

Title: A ubiquitin ligase complex assembles linear polyubiquitin chains.

PubMed ID: 17006537

DOI: 10.1038/sj.emboj.7601360

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 12508121

Title: The DNA sequence and analysis of human chromosome 14.

PubMed ID: 12508121

DOI: 10.1038/nature01348

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 12693554

Title: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones.

PubMed ID: 12693554

DOI: 10.1093/dnares/10.1.49

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 20005846

Title: Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction.

PubMed ID: 20005846

DOI: 10.1016/j.molcel.2009.10.013

PubMed ID: 19136968

Title: Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation.

PubMed ID: 19136968

DOI: 10.1038/ncb1821

PubMed ID: 21455173

Title: Linear ubiquitination prevents inflammation and regulates immune signalling.

PubMed ID: 21455173

DOI: 10.1038/nature09816

PubMed ID: 21455180

Title: SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex.

PubMed ID: 21455180

DOI: 10.1038/nature09815

PubMed ID: 21455181

Title: SHARPIN forms a linear ubiquitin ligase complex regulating NF-kappaB activity and apoptosis.

PubMed ID: 21455181

DOI: 10.1038/nature09814

PubMed ID: 22863777

Title: The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension.

PubMed ID: 22863777

DOI: 10.1038/emboj.2012.217

PubMed ID: 22430200

Title: A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex.

PubMed ID: 22430200

DOI: 10.1038/embor.2012.24

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23708998

Title: The linear ubiquitin-specific deubiquitinase gumby regulates angiogenesis.

PubMed ID: 23708998

DOI: 10.1038/nature12296

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 27458237

Title: SPATA2 promotes CYLD activity and regulates TNF-induced NF-kappaB signaling and cell death.

PubMed ID: 27458237

DOI: 10.15252/embr.201642592

PubMed ID: 27545878

Title: SPATA2-Mediated Binding of CYLD to HOIP Enables CYLD Recruitment to Signaling Complexes.

PubMed ID: 27545878

DOI: 10.1016/j.celrep.2016.07.086

PubMed ID: 26997266

Title: CYLD limits Lys63- and Met1-linked ubiquitin at receptor complexes to regulate innate immune signaling.

PubMed ID: 26997266

DOI: 10.1016/j.celrep.2016.02.062

PubMed ID: 27777308

Title: Molecular determinants of scaffold-induced linear ubiquitinylation of B Cell Lymphoma/Leukemia 10 (Bcl10) during T cell receptor and oncogenic caspase recruitment domain-containing protein 11 (CARD11) signaling.

PubMed ID: 27777308

DOI: 10.1074/jbc.m116.754028

PubMed ID: 27572974

Title: Shigella flexneri suppresses NF-kappaB activation by inhibiting linear ubiquitin chain ligation.

PubMed ID: 27572974

DOI: 10.1038/nmicrobiol.2016.84

PubMed ID: 28481331

Title: LUBAC-synthesized linear ubiquitin chains restrict cytosol-invading bacteria by activating autophagy and NF-kappaB.

PubMed ID: 28481331

DOI: 10.1038/nmicrobiol.2017.63

PubMed ID: 28189684

Title: Decreased linear ubiquitination of NEMO and FADD on apoptosis with caspase-mediated cleavage of HOIP.

PubMed ID: 28189684

DOI: 10.1016/j.bbrc.2017.02.040

PubMed ID: 34012115

Title: Ubiquitylation of lipopolysaccharide by RNF213 during bacterial infection.

PubMed ID: 34012115

DOI: 10.1038/s41586-021-03566-4

PubMed ID: 24726323

Title: Molecular basis and regulation of OTULIN-LUBAC interaction.

PubMed ID: 24726323

DOI: 10.1016/j.molcel.2014.03.018

PubMed ID: 24726327

Title: Binding of OTULIN to the PUB domain of HOIP controls NF-kappaB signaling.

PubMed ID: 24726327

DOI: 10.1016/j.molcel.2014.03.016

PubMed ID: 27591049

Title: SPATA2 links CYLD to LUBAC, activates CYLD, and controls LUBAC signaling.

PubMed ID: 27591049

DOI: 10.1016/j.molcel.2016.08.001

PubMed ID: 35294289

Title: Mechanistic insights into the subversion of the linear ubiquitin chain assembly complex by the E3 ligase IpaH1.4 of Shigella flexneri.

PubMed ID: 35294289

DOI: 10.1073/pnas.2116776119

Sequence Information:

  • Length: 1072
  • Mass: 119652
  • Checksum: CFAD183A14F764BA
  • Sequence:
  • MPGEEEERAF LVAREELASA LRRDSGQAFS LEQLRPLLAS SLPLAARYLQ LDAARLVRCN 
    AHGEPRNYLN TLSTALNILE KYGRNLLSPQ RPRYWRGVKF NNPVFRSTVD AVQGGRDVLR 
    LYGYTEEQPD GLSFPEGQEE PDEHQVATVT LEVLLLRTEL SLLLQNTHPR QQALEQLLED 
    KVEDDMLQLS EFDPLLREIA PGPLTTPSVP GSTPGPCFLC GSAPGTLHCP SCKQALCPAC 
    DHLFHGHPSR AHHLRQTLPG VLQGTHLSPS LPASAQPRPQ STSLLALGDS SLSSPNPASA 
    HLPWHCAACA MLNEPWAVLC VACDRPRGCK GLGLGTEGPQ GTGGLEPDLA RGRWACQSCT 
    FENEAAAVLC SICERPRLAQ PPSLVVDSRD AGICLQPLQQ GDALLASAQS QVWYCIHCTF 
    CNSSPGWVCV MCNRTSSPIP AQHAPRPYAS SLEKGPPKPG PPRRLSAPLP SSCGDPEKQR 
    QDKMREEGLQ LVSMIREGEA AGACPEEIFS ALQYSGTEVP LQWLRSELPY VLEMVAELAG 
    QQDPGLGAFS CQEARRAWLD RHGNLDEAVE ECVRTRRRKV QELQSLGFGP EEGSLQALFQ 
    HGGDVSRALT ELQRQRLEPF RQRLWDSGPE PTPSWDGPDK QSLVRRLLAV YALPSWGRAE 
    LALSLLQETP RNYELGDVVE AVRHSQDRAF LRRLLAQECA VCGWALPHNR MQALTSCECT 
    ICPDCFRQHF TIALKEKHIT DMVCPACGRP DLTDDTQLLS YFSTLDIQLR ESLEPDAYAL 
    FHKKLTEGVL MRDPKFLWCA QCSFGFIYER EQLEATCPQC HQTFCVRCKR QWEEQHRGRS 
    CEDFQNWKRM NDPEYQAQGL AMYLQENGID CPKCKFSYAL ARGGCMHFHC TQCRHQFCSG 
    CYNAFYAKNK CPEPNCRVKK SLHGHHPRDC LFYLRDWTAL RLQKLLQDNN VMFNTEPPAG 
    ARAVPGGGCR VIEQKEVPNG LRDEACGKET PAGYAGLCQA HYKEYLVSLI NAHSLDPATL 
    YEVEELETAT ERYLHVRPQP LAGEDPPAYQ ARLLQKLTEE VPLGQSIPRR RK

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.