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Q96EP0

- RNF31_HUMAN

UniProt

Q96EP0 - RNF31_HUMAN

Protein

E3 ubiquitin-protein ligase RNF31

Gene

RNF31

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.8 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri299 – 32931RanBP2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri350 – 37930RanBP2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri409 – 43830RanBP2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri699 – 74749RING-type 1; degenerateAdd
    BLAST
    Zinc fingeri779 – 84163IBR-typeAdd
    BLAST
    Zinc fingeri860 – 90950RING-type 2Add
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. CD40 signaling pathway Source: BHF-UCL
    2. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    3. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    4. protein linear polyubiquitination Source: UniProtKB
    5. protein polyubiquitination Source: UniProtKB
    6. T cell receptor signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase RNF31 (EC:6.3.2.-)
    Alternative name(s):
    HOIL-1-interacting protein
    Short name:
    HOIP
    RING finger protein 31
    Zinc in-between-RING-finger ubiquitin-associated domain protein
    Gene namesi
    Name:RNF31
    Synonyms:ZIBRA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:16031. RNF31.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. CD40 receptor complex Source: BHF-UCL
    2. cytoplasm Source: UniProtKB-SubCell
    3. cytoplasmic side of plasma membrane Source: BHF-UCL
    4. LUBAC complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi699 – 6991C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-702. 2 Publications
    Mutagenesisi702 – 7021C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-699. 2 Publications
    Mutagenesisi871 – 8711C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-874. 2 Publications
    Mutagenesisi874 – 8741C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-871. 2 Publications

    Organism-specific databases

    PharmGKBiPA134906471.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10721072E3 ubiquitin-protein ligase RNF31PRO_0000056069Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei466 – 4661Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96EP0.
    PaxDbiQ96EP0.
    PRIDEiQ96EP0.

    PTM databases

    PhosphoSiteiQ96EP0.

    Expressioni

    Tissue specificityi

    Expressed in both normal and transformed breast epithelial cell lines.1 Publication

    Gene expression databases

    BgeeiQ96EP0.
    CleanExiHS_RNF31.
    GenevestigatoriQ96EP0.

    Organism-specific databases

    HPAiCAB009063.
    HPA048745.

    Interactioni

    Subunit structurei

    Interacts with MUSK By similarity. Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31. LUBAC has a MW of approximative 600 kDa suggesting a heteromultimeric assembly of its subunits. Associates with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent manner. Interacts with FAM105B/otulin; the interaction is direct.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Azi2Q9QYP62EBI-948111,EBI-6115874From a different organism.
    RBCK1Q9BYM820EBI-948111,EBI-2340624
    SHARPINQ9H0F62EBI-948111,EBI-3942966
    SMAD3P840222EBI-948111,EBI-347161
    Traf1Q4VA122EBI-948111,EBI-6116765From a different organism.

    Protein-protein interaction databases

    BioGridi120389. 41 interactions.
    DIPiDIP-44034N.
    IntActiQ96EP0. 21 interactions.
    MINTiMINT-3377714.
    STRINGi9606.ENSP00000315112.

    Structurei

    Secondary structure

    1
    1072
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 2320
    Helixi31 – 388
    Helixi44 – 474
    Beta strandi49 – 513
    Helixi53 – 586
    Helixi65 – 8622
    Beta strandi88 – 903
    Turni93 – 964
    Beta strandi97 – 1026
    Helixi103 – 1075
    Helixi109 – 1113
    Helixi115 – 1228
    Beta strandi126 – 1283
    Beta strandi131 – 1333
    Helixi143 – 16422
    Helixi171 – 1777
    Turni357 – 3593
    Turni371 – 3733
    Helixi483 – 49311
    Helixi505 – 51511
    Helixi521 – 5277
    Helixi531 – 54212
    Helixi544 – 5463
    Helixi551 – 56010
    Turni561 – 5633
    Helixi565 – 58521
    Helixi590 – 5923
    Helixi594 – 6007
    Turni601 – 6033
    Helixi605 – 61612
    Helixi618 – 6258
    Beta strandi780 – 7834
    Beta strandi800 – 8023
    Turni818 – 8203
    Beta strandi826 – 8283
    Turni834 – 8385
    Helixi841 – 85111
    Helixi859 – 8646
    Beta strandi868 – 8703
    Turni872 – 8743
    Beta strandi877 – 8793
    Beta strandi886 – 8894
    Turni891 – 8933
    Beta strandi896 – 8983
    Turni899 – 9013
    Beta strandi904 – 9063
    Turni917 – 9204
    Beta strandi921 – 9244
    Helixi931 – 9344
    Helixi939 – 94810
    Beta strandi965 – 9684
    Beta strandi972 – 9776
    Beta strandi980 – 9856
    Helixi999 – 101214
    Helixi1017 – 10204
    Helixi1023 – 103412
    Helixi1046 – 106015
    Beta strandi1065 – 10673

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CT7NMR-A779-851[»]
    4DBGX-ray2.71B480-636[»]
    4JUYX-ray2.40A/B1-180[»]
    4LJOX-ray1.56A853-1072[»]
    4LJPX-ray2.15A853-1072[»]
    4LJQX-ray2.45A/B/C/D853-1072[»]
    4OWFX-ray2.00G350-379[»]
    4OYJX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M1-184[»]
    4OYKX-ray2.00A/B3-179[»]
    4P09X-ray1.70A1-179[»]
    4P0AX-ray2.30A/C1-179[»]
    4P0BX-ray2.70A/C1-179[»]
    ProteinModelPortaliQ96EP0.
    SMRiQ96EP0. Positions 1-179, 302-327, 351-379, 482-627, 690-1072.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96EP0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini564 – 61552UBAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 485485Polyubiquitin-bindingAdd
    BLAST
    Regioni563 – 61654Interaction with RBCK1Add
    BLAST
    Regioni910 – 1072163LDD domainAdd
    BLAST

    Domaini

    The RanBP2-type zinc fingers mediate the specific interaction with ubiquitin.
    The UBA domain mediates association with RBCK1/HOIL1 via interaction with its UBL domain.
    RING 1 and IBR zinc-fingers catalyze the first step transfer of ubiquitin from the E2 onto RING 2, to transiently form a HECT-like covalent thioester intermediate.1 Publication
    The linear ubiquitin chain determining domain (LDD) mediates the final transfer of ubiquitin from RING 2 onto the N-terminus of a target ubiquitin.1 Publication

    Sequence similaritiesi

    Contains 1 IBR-type zinc finger.Curated
    Contains 3 RanBP2-type zinc fingers.PROSITE-ProRule annotation
    Contains 2 RING-type zinc fingers.Curated
    Contains 1 UBA domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri299 – 32931RanBP2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri350 – 37930RanBP2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri409 – 43830RanBP2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri699 – 74749RING-type 1; degenerateAdd
    BLAST
    Zinc fingeri779 – 84163IBR-typeAdd
    BLAST
    Zinc fingeri860 – 90950RING-type 2Add
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG269721.
    HOVERGENiHBG063678.
    InParanoidiQ96EP0.
    KOiK11974.
    OMAiRTNDPEY.
    PhylomeDBiQ96EP0.
    TreeFamiTF350529.

    Family and domain databases

    InterProiIPR018997. PUB_domain.
    IPR026254. RNF31.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR002867. Znf_C6HC.
    IPR001876. Znf_RanBP2.
    IPR001841. Znf_RING.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PANTHERiPTHR16004. PTHR16004. 1 hit.
    PfamiPF01485. IBR. 1 hit.
    PF09409. PUB. 1 hit.
    [Graphical view]
    SMARTiSM00647. IBR. 2 hits.
    SM00184. RING. 2 hits.
    SM00547. ZnF_RBZ. 3 hits.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    PROSITEiPS50030. UBA. 1 hit.
    PS01358. ZF_RANBP2_1. 3 hits.
    PS50199. ZF_RANBP2_2. 2 hits.
    PS00518. ZF_RING_1. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96EP0-1) [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

    MPGEEEERAF LVAREELASA LRRDSGQAFS LEQLRPLLAS SLPLAARYLQ     50
    LDAARLVRCN AHGEPRNYLN TLSTALNILE KYGRNLLSPQ RPRYWRGVKF 100
    NNPVFRSTVD AVQGGRDVLR LYGYTEEQPD GLSFPEGQEE PDEHQVATVT 150
    LEVLLLRTEL SLLLQNTHPR QQALEQLLED KVEDDMLQLS EFDPLLREIA 200
    PGPLTTPSVP GSTPGPCFLC GSAPGTLHCP SCKQALCPAC DHLFHGHPSR 250
    AHHLRQTLPG VLQGTHLSPS LPASAQPRPQ STSLLALGDS SLSSPNPASA 300
    HLPWHCAACA MLNEPWAVLC VACDRPRGCK GLGLGTEGPQ GTGGLEPDLA 350
    RGRWACQSCT FENEAAAVLC SICERPRLAQ PPSLVVDSRD AGICLQPLQQ 400
    GDALLASAQS QVWYCIHCTF CNSSPGWVCV MCNRTSSPIP AQHAPRPYAS 450
    SLEKGPPKPG PPRRLSAPLP SSCGDPEKQR QDKMREEGLQ LVSMIREGEA 500
    AGACPEEIFS ALQYSGTEVP LQWLRSELPY VLEMVAELAG QQDPGLGAFS 550
    CQEARRAWLD RHGNLDEAVE ECVRTRRRKV QELQSLGFGP EEGSLQALFQ 600
    HGGDVSRALT ELQRQRLEPF RQRLWDSGPE PTPSWDGPDK QSLVRRLLAV 650
    YALPSWGRAE LALSLLQETP RNYELGDVVE AVRHSQDRAF LRRLLAQECA 700
    VCGWALPHNR MQALTSCECT ICPDCFRQHF TIALKEKHIT DMVCPACGRP 750
    DLTDDTQLLS YFSTLDIQLR ESLEPDAYAL FHKKLTEGVL MRDPKFLWCA 800
    QCSFGFIYER EQLEATCPQC HQTFCVRCKR QWEEQHRGRS CEDFQNWKRM 850
    NDPEYQAQGL AMYLQENGID CPKCKFSYAL ARGGCMHFHC TQCRHQFCSG 900
    CYNAFYAKNK CPEPNCRVKK SLHGHHPRDC LFYLRDWTAL RLQKLLQDNN 950
    VMFNTEPPAG ARAVPGGGCR VIEQKEVPNG LRDEACGKET PAGYAGLCQA 1000
    HYKEYLVSLI NAHSLDPATL YEVEELETAT ERYLHVRPQP LAGEDPPAYQ 1050
    ARLLQKLTEE VPLGQSIPRR RK 1072
    Length:1,072
    Mass (Da):119,652
    Last modified:December 1, 2001 - v1
    Checksum:iCFAD183A14F764BA
    GO
    Isoform 2 (identifier: Q96EP0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         73-630: Missing.
         833-841: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:505
    Mass (Da):57,633
    Checksum:i04245E2E835AD19C
    GO
    Isoform 3 (identifier: Q96EP0-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-151: Missing.
         152-164: EVLLLRTELSLLL → MDLCTRAGEPSLT

    Show »
    Length:921
    Mass (Da):102,496
    Checksum:i2149563718B64B0B
    GO

    Sequence cautioni

    The sequence BAB15675.1 differs from that shown. Reason: Intron retention.
    The sequence BAB15675.1 differs from that shown. Reason: Frameshift at position 1036.
    The sequence BAB70948.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB15675.1 differs from that shown. Reason: Erroneous termination at position 1060. Translated as Glu.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti529 – 5291P → S in AAP12522. (PubMed:15093743)Curated
    Sequence conflicti800 – 8001A → V in BAA91450. (PubMed:14702039)Curated
    Sequence conflicti925 – 9251H → R in BAB15675. (PubMed:14702039)Curated
    Sequence conflicti1005 – 10051Y → N in BAB15675. (PubMed:14702039)Curated
    Sequence conflicti1018 – 10181A → S in BAB15675. (PubMed:14702039)Curated
    Sequence conflicti1021 – 10211Y → D in BAB15675. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1061 – 10611V → I.1 Publication
    Corresponds to variant rs2277484 [ dbSNP | Ensembl ].
    VAR_052102

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 151151Missing in isoform 3. 1 PublicationVSP_014006Add
    BLAST
    Alternative sequencei73 – 630558Missing in isoform 2. 1 PublicationVSP_009647Add
    BLAST
    Alternative sequencei152 – 16413EVLLL…LSLLL → MDLCTRAGEPSLT in isoform 3. 1 PublicationVSP_014007Add
    BLAST
    Alternative sequencei833 – 8419Missing in isoform 2. 1 PublicationVSP_009648

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY256461 mRNA. Translation: AAP12522.1.
    AB265810 mRNA. Translation: BAF35583.1.
    AK000973 mRNA. Translation: BAA91450.1.
    AK027154 mRNA. Translation: BAB15675.1. Frameshift.
    AK055542 mRNA. Translation: BAB70948.1. Different initiation.
    AK291247 mRNA. Translation: BAF83936.1.
    AL136295 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW66098.1.
    BC009821 mRNA. Translation: AAH09821.3.
    BC012077 mRNA. Translation: AAH12077.1.
    BC017376 mRNA. Translation: AAH17376.3.
    AK074144 mRNA. Translation: BAB84970.1.
    CCDSiCCDS41931.1. [Q96EP0-1]
    RefSeqiNP_060469.4. NM_017999.4. [Q96EP0-1]
    UniGeneiHs.375217.
    Hs.434081.

    Genome annotation databases

    EnsembliENST00000324103; ENSP00000315112; ENSG00000092098. [Q96EP0-1]
    ENST00000559275; ENSP00000453574; ENSG00000092098. [Q96EP0-3]
    GeneIDi55072.
    KEGGihsa:55072.
    UCSCiuc001wml.1. human. [Q96EP0-3]
    uc001wmn.1. human. [Q96EP0-1]

    Polymorphism databases

    DMDMi45477216.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY256461 mRNA. Translation: AAP12522.1 .
    AB265810 mRNA. Translation: BAF35583.1 .
    AK000973 mRNA. Translation: BAA91450.1 .
    AK027154 mRNA. Translation: BAB15675.1 . Frameshift.
    AK055542 mRNA. Translation: BAB70948.1 . Different initiation.
    AK291247 mRNA. Translation: BAF83936.1 .
    AL136295 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW66098.1 .
    BC009821 mRNA. Translation: AAH09821.3 .
    BC012077 mRNA. Translation: AAH12077.1 .
    BC017376 mRNA. Translation: AAH17376.3 .
    AK074144 mRNA. Translation: BAB84970.1 .
    CCDSi CCDS41931.1. [Q96EP0-1 ]
    RefSeqi NP_060469.4. NM_017999.4. [Q96EP0-1 ]
    UniGenei Hs.375217.
    Hs.434081.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CT7 NMR - A 779-851 [» ]
    4DBG X-ray 2.71 B 480-636 [» ]
    4JUY X-ray 2.40 A/B 1-180 [» ]
    4LJO X-ray 1.56 A 853-1072 [» ]
    4LJP X-ray 2.15 A 853-1072 [» ]
    4LJQ X-ray 2.45 A/B/C/D 853-1072 [» ]
    4OWF X-ray 2.00 G 350-379 [» ]
    4OYJ X-ray 3.00 A/B/C/D/E/F/G/H/I/J/K/L/M 1-184 [» ]
    4OYK X-ray 2.00 A/B 3-179 [» ]
    4P09 X-ray 1.70 A 1-179 [» ]
    4P0A X-ray 2.30 A/C 1-179 [» ]
    4P0B X-ray 2.70 A/C 1-179 [» ]
    ProteinModelPortali Q96EP0.
    SMRi Q96EP0. Positions 1-179, 302-327, 351-379, 482-627, 690-1072.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120389. 41 interactions.
    DIPi DIP-44034N.
    IntActi Q96EP0. 21 interactions.
    MINTi MINT-3377714.
    STRINGi 9606.ENSP00000315112.

    PTM databases

    PhosphoSitei Q96EP0.

    Polymorphism databases

    DMDMi 45477216.

    Proteomic databases

    MaxQBi Q96EP0.
    PaxDbi Q96EP0.
    PRIDEi Q96EP0.

    Protocols and materials databases

    DNASUi 55072.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324103 ; ENSP00000315112 ; ENSG00000092098 . [Q96EP0-1 ]
    ENST00000559275 ; ENSP00000453574 ; ENSG00000092098 . [Q96EP0-3 ]
    GeneIDi 55072.
    KEGGi hsa:55072.
    UCSCi uc001wml.1. human. [Q96EP0-3 ]
    uc001wmn.1. human. [Q96EP0-1 ]

    Organism-specific databases

    CTDi 55072.
    GeneCardsi GC14P024616.
    HGNCi HGNC:16031. RNF31.
    HPAi CAB009063.
    HPA048745.
    MIMi 612487. gene.
    neXtProti NX_Q96EP0.
    PharmGKBi PA134906471.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG269721.
    HOVERGENi HBG063678.
    InParanoidi Q96EP0.
    KOi K11974.
    OMAi RTNDPEY.
    PhylomeDBi Q96EP0.
    TreeFami TF350529.

    Miscellaneous databases

    ChiTaRSi RNF31. human.
    EvolutionaryTracei Q96EP0.
    GeneWikii RNF31.
    GenomeRNAii 55072.
    NextBioi 58596.
    PROi Q96EP0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96EP0.
    CleanExi HS_RNF31.
    Genevestigatori Q96EP0.

    Family and domain databases

    InterProi IPR018997. PUB_domain.
    IPR026254. RNF31.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR002867. Znf_C6HC.
    IPR001876. Znf_RanBP2.
    IPR001841. Znf_RING.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    PANTHERi PTHR16004. PTHR16004. 1 hit.
    Pfami PF01485. IBR. 1 hit.
    PF09409. PUB. 1 hit.
    [Graphical view ]
    SMARTi SM00647. IBR. 2 hits.
    SM00184. RING. 2 hits.
    SM00547. ZnF_RBZ. 3 hits.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    PROSITEi PS50030. UBA. 1 hit.
    PS01358. ZF_RANBP2_1. 3 hits.
    PS50199. ZF_RANBP2_2. 2 hits.
    PS00518. ZF_RING_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of the protein Zibra, its genomic organization, regulation, and expression in breast cancer cells."
      Thompson H.G.R., Harris J.W., Lin L., Brody J.P.
      Exp. Cell Res. 295:448-459(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
      Tissue: Mammary carcinoma.
    2. "A ubiquitin ligase complex assembles linear polyubiquitin chains."
      Kirisako T., Kamei K., Murata S., Kato M., Fukumoto H., Kanie M., Sano S., Tokunaga F., Tanaka K., Iwai K.
      EMBO J. 25:4877-4887(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION OF THE LUBAC COMPLEX, MUTAGENESIS OF CYS-699; CYS-702; CYS-871 AND CYS-874.
    3. "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] (ISOFORMS 1 AND 2), VARIANT ILE-1061.
      Tissue: Embryo and Hair follicle dermal papilla.
    4. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1).
      Tissue: Ovary and Placenta.
    7. "Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones."
      Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O.
      DNA Res. 10:49-57(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 526-1072 (ISOFORMS 1/3).
      Tissue: Spleen.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction."
      Haas T.L., Emmerich C.H., Gerlach B., Schmukle A.C., Cordier S.M., Rieser E., Feltham R., Vince J., Warnken U., Wenger T., Koschny R., Komander D., Silke J., Walczak H.
      Mol. Cell 36:831-844(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYUBIQUITIN-BINDING, FUNCTION OF THE LUBAC COMPLEX, ASSOCIATION WITH TNF-RSC, IDENTIFICATION BY MASS SPECTROMETRY.
    11. Cited for: FUNCTION OF THE LUBAC COMPLEX.
    12. Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION.
    13. "SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex."
      Tokunaga F., Nakagawa T., Nakahara M., Saeki Y., Taniguchi M., Sakata S., Tanaka K., Nakano H., Iwai K.
      Nature 471:633-636(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION.
    14. Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN RANBP2-TYPE, UBIQUITIN-BINDING, MUTAGENESIS OF CYS-699; CYS-702; CYS-871 AND CYS-874.
    15. "The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension."
      Smit J.J., Monteferrario D., Noordermeer S.M., van Dijk W.J., van der Reijden B.A., Sixma T.K.
      EMBO J. 31:3833-3844(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN RING, DOMAIN LDD, ENZYME MECHANISM.
    16. "A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex."
      Yagi H., Ishimoto K., Hiromoto T., Fujita H., Mizushima T., Uekusa Y., Yagi-Utsumi M., Kurimoto E., Noda M., Uchiyama S., Tokunaga F., Iwai K., Kato K.
      EMBO Rep. 13:462-468(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBCK1/HOIL1.
    17. Cited for: FUNCTION, INTERACTION WITH FAM105B.
    18. "Solution structure of the IBR domain of the RING finger protein 31."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 779-851.

    Entry informationi

    Entry nameiRNF31_HUMAN
    AccessioniPrimary (citable) accession number: Q96EP0
    Secondary accession number(s): A0A962
    , Q86VI2, Q8TEI0, Q96GB4, Q96NF1, Q9H5F1, Q9NWD2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2004
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 130 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 14
      Human chromosome 14: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3