UniProtKB - Q96EP0 (RNF31_HUMAN)
E3 ubiquitin-protein ligase RNF31
RNF31
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 (PubMed:17006537, PubMed:19136968, PubMed:20005846, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22863777, PubMed:28481331, PubMed:28189684).
LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (PubMed:17006537, PubMed:19136968, PubMed:20005846, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22863777, PubMed:28189684).
Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed:21455173, PubMed:28189684).
LUBAC is 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 (PubMed:20005846, PubMed:27458237).
The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria (PubMed:28481331, PubMed:34012115).
LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin (PubMed:28481331).
Recruited to the surface of bacteria by RNF213, which initiates the bacterial ubiquitin coat (PubMed:34012115).
The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:28481331, PubMed:34012115).
Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (PubMed:23708998).
RNF31 is required for linear ubiquitination of BCL10, thereby promoting TCR-induced NF-kappa-B activation (PubMed:27777308).
Binds polyubiquitin of different linkage types (PubMed:23708998).
13 PublicationsCatalytic activityi
- [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.4 Publications EC:2.3.2.31
: protein ubiquitination Pathwayi
This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.4 PublicationsView all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 699 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 702 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 722 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 725 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 799 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 802 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 817 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 820 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 825 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 828 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 836 | Zinc 3; via tele nitrogenPROSITE-ProRule annotation | 1 | |
Metal bindingi | 841 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 871 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 874 | Zinc 4PROSITE-ProRule annotation | 1 | |
Active sitei | 885 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 890 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 893 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 898 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 901 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 916 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 925 | Zinc 5; via tele nitrogenPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 299 – 329 | RanBP2-type 1PROSITE-ProRule annotationAdd BLAST | 31 | |
Zinc fingeri | 350 – 379 | RanBP2-type 2PROSITE-ProRule annotationAdd BLAST | 30 | |
Zinc fingeri | 409 – 438 | RanBP2-type 3PROSITE-ProRule annotationAdd BLAST | 30 | |
Zinc fingeri | 699 – 749 | RING-type 1PROSITE-ProRule annotationAdd BLAST | 51 | |
Zinc fingeri | 779 – 841 | IBR-typePROSITE-ProRule annotationAdd BLAST | 63 | |
Zinc fingeri | 871 – 901 | RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST | 31 |
GO - Molecular functioni
- identical protein binding Source: IntAct
- K48-linked polyubiquitin modification-dependent protein binding Source: GO_Central
- K63-linked polyubiquitin modification-dependent protein binding Source: GO_Central
- linear polyubiquitin binding Source: GO_Central
- metal ion binding Source: UniProtKB-KW
- ubiquitin binding Source: UniProtKB
- ubiquitin protein ligase activity Source: UniProtKB
- ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
- ubiquitin-protein transferase activity Source: UniProtKB
GO - Biological processi
- CD40 signaling pathway Source: BHF-UCL
- defense response to bacterium Source: UniProtKB
- positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
- positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
- positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
- positive regulation of xenophagy Source: UniProtKB
- protein linear polyubiquitination Source: UniProtKB
- protein polyubiquitination Source: UniProtKB
- T cell receptor signaling pathway Source: UniProtKB
Keywordsi
Molecular function | Transferase |
Biological process | Ubl conjugation pathway |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 2.3.2.31, 2681 |
PathwayCommonsi | Q96EP0 |
Reactomei | R-HSA-5357905, Regulation of TNFR1 signaling R-HSA-5357956, TNFR1-induced NFkappaB signaling pathway |
SignaLinki | Q96EP0 |
UniPathwayi | UPA00143 |
Names & Taxonomyi
Protein namesi | Recommended name: E3 ubiquitin-protein ligase RNF31 (EC:2.3.2.314 Publications)Alternative name(s): HOIL-1-interacting protein1 Publication Short name: HOIP1 Publication RING finger protein 31Imported RING-type E3 ubiquitin transferase RNF31Curated Zinc in-between-RING-finger ubiquitin-associated domain protein1 Publication |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:16031, RNF31 |
MIMi | 612487, gene |
neXtProti | NX_Q96EP0 |
VEuPathDBi | HostDB:ENSG00000092098 |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Cytosol
- cytosol Source: Reactome
Plasma Membrane
- CD40 receptor complex Source: BHF-UCL
- cytoplasmic side of plasma membrane Source: BHF-UCL
Other locations
- LUBAC complex Source: UniProtKB
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 82 | Y → A: Abolished interaction with OTULIN. 1 Publication | 1 | |
Mutagenesisi | 82 | Y → F: Reduced interaction with OTULIN. 1 Publication | 1 | |
Mutagenesisi | 85 | N → A: Reduced interaction with OTULIN. 1 Publication | 1 | |
Mutagenesisi | 99 | K → E: Reduced interaction with OTULIN. 1 Publication | 1 | |
Mutagenesisi | 101 | N → R: Does not affect interaction with OTULIN. 1 Publication | 1 | |
Mutagenesisi | 102 | N → A: Abolished interaction with SPATA2. 1 Publication | 1 | |
Mutagenesisi | 102 | N → D: Abolished interaction with OTULIN. 1 Publication | 1 | |
Mutagenesisi | 104 | V → A: Reduced interaction with OTULIN. 1 Publication | 1 | |
Mutagenesisi | 360 | T → A: Decreased ubiquitin-binding and ability to promote formation of the bacterial ubiquitin coat. 1 Publication | 1 | |
Mutagenesisi | 390 | D → A: Abolishes cleavage by caspase. 1 Publication | 1 | |
Mutagenesisi | 699 | C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-702. 2 Publications | 1 | |
Mutagenesisi | 702 | C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-699. 2 Publications | 1 | |
Mutagenesisi | 735 | K → R: Reduced ubiquitination; when associated with R-783 and R-875. 1 Publication | 1 | |
Mutagenesisi | 783 | K → R: Reduced ubiquitination; when associated with R-735 and R-875. 1 Publication | 1 | |
Mutagenesisi | 871 | C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-874. 2 Publications | 1 | |
Mutagenesisi | 874 | C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-871. 2 Publications | 1 | |
Mutagenesisi | 875 | K → R: Reduced ubiquitination; when associated with R-735 and R-783. 1 Publication | 1 | |
Mutagenesisi | 885 | C → A: Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-935 and A-983. 1 Publication | 1 | |
Mutagenesisi | 935 | R → A: Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-885 and A-983. 1 Publication | 1 | |
Mutagenesisi | 983 | D → A: Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-885 and A-935. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 55072 |
MalaCardsi | RNF31 |
OpenTargetsi | ENSG00000092098 ENSG00000259529 |
Orphaneti | 329173, Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis |
PharmGKBi | PA134906471 |
Miscellaneous databases
Pharosi | Q96EP0, Tbio |
Chemistry databases
ChEMBLi | CHEMBL4296109 |
Genetic variation databases
BioMutai | RNF31 |
DMDMi | 45477216 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000056069 | 1 – 1072 | E3 ubiquitin-protein ligase RNF31Add BLAST | 1072 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 383 | PhosphoserineCombined sources | 1 | |
Modified residuei | 466 | PhosphoserineCombined sources | 1 | |
Cross-linki | 735 | (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Cross-linki | 783 | (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Cross-linki | 875 | (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 390 – 391 | Cleavage; by caspase1 Publication | 2 |
Keywords - PTMi
Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | Q96EP0 |
jPOSTi | Q96EP0 |
MassIVEi | Q96EP0 |
MaxQBi | Q96EP0 |
PaxDbi | Q96EP0 |
PeptideAtlasi | Q96EP0 |
PRIDEi | Q96EP0 |
ProteomicsDBi | 76429 [Q96EP0-1] 76430 [Q96EP0-2] 76431 [Q96EP0-3] |
PTM databases
iPTMneti | Q96EP0 |
MetOSitei | Q96EP0 |
PhosphoSitePlusi | Q96EP0 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000092098, Expressed in muscle tissue and 119 other tissues |
ExpressionAtlasi | Q96EP0, baseline and differential |
Genevisiblei | Q96EP0, HS |
Organism-specific databases
HPAi | ENSG00000092098, Low tissue specificity |
Interactioni
Subunit structurei
Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31 (PubMed:17006537, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:28481331). LUBAC has a MW of approximately 600 kDa suggesting a heteromultimeric assembly of its subunits (PubMed:17006537, PubMed:21455173, PubMed:21455180, PubMed:21455181). Associates with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent manner (PubMed:20005846).
Interacts (via the PUB domain) with OTULIN (via the PIM motif); the interaction is direct (PubMed:23708998, PubMed:24726323, PubMed:24726327).
Interacts (via the PUB domain) with VCP (via the PIM motif) (PubMed:24726327).
Interacts (via the PUB domain) with SPATA2 (via the PIM motif); interaction is direct and bridges RNF31 and CYLD (PubMed:27458237, PubMed:27545878, PubMed:28189684, PubMed:27591049).
Interacts with CYLD; the interaction is indirect and is mediated via SPATA2 (PubMed:27458237, PubMed:27545878, PubMed:26997266).
Interacts with MUSK (By similarity).
Interacts with CARD11, promoting linear ubiquitination of BCL10 (PubMed:27777308).
By similarity16 Publications(Microbial infection) Interacts with S.flexneri E3 ubiquitin-protein ligases IpaH1.4 and IpaH2.5, leading to its ubiquitination.
1 PublicationBinary interactionsi
Q96EP0
Isoform 3 [Q96EP0-3]
GO - Molecular functioni
- identical protein binding Source: IntAct
- K48-linked polyubiquitin modification-dependent protein binding Source: GO_Central
- K63-linked polyubiquitin modification-dependent protein binding Source: GO_Central
- linear polyubiquitin binding Source: GO_Central
- ubiquitin binding Source: UniProtKB
- ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
Protein-protein interaction databases
BioGRIDi | 120389, 383 interactors |
ComplexPortali | CPX-1877, LUBAC ubiquitin ligase complex |
CORUMi | Q96EP0 |
DIPi | DIP-44034N |
IntActi | Q96EP0, 69 interactors |
MINTi | Q96EP0 |
STRINGi | 9606.ENSP00000315112 |
Chemistry databases
BindingDBi | Q96EP0 |
Miscellaneous databases
RNActi | Q96EP0, protein |
Structurei
Secondary structure
3D structure databases
BMRBi | Q96EP0 |
SMRi | Q96EP0 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q96EP0 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 71 – 142 | PUBSequence analysisAdd BLAST | 72 | |
Domaini | 564 – 615 | UBAPROSITE-ProRule annotationAdd BLAST | 52 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 485 | Polyubiquitin-bindingAdd BLAST | 485 | |
Regioni | 263 – 290 | DisorderedSequence analysisAdd BLAST | 28 | |
Regioni | 443 – 484 | DisorderedSequence analysisAdd BLAST | 42 | |
Regioni | 563 – 616 | Interaction with RBCK1Add BLAST | 54 | |
Regioni | 695 – 929 | TRIAD supradomainPROSITE-ProRule annotationAdd BLAST | 235 | |
Regioni | 910 – 1072 | LDD domainAdd BLAST | 163 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 452 – 466 | Pro residuesSequence analysisAdd BLAST | 15 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 299 – 329 | RanBP2-type 1PROSITE-ProRule annotationAdd BLAST | 31 | |
Zinc fingeri | 350 – 379 | RanBP2-type 2PROSITE-ProRule annotationAdd BLAST | 30 | |
Zinc fingeri | 409 – 438 | RanBP2-type 3PROSITE-ProRule annotationAdd BLAST | 30 | |
Zinc fingeri | 699 – 749 | RING-type 1PROSITE-ProRule annotationAdd BLAST | 51 | |
Zinc fingeri | 779 – 841 | IBR-typePROSITE-ProRule annotationAdd BLAST | 63 | |
Zinc fingeri | 871 – 901 | RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST | 31 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | KOG1812, Eukaryota |
GeneTreei | ENSGT00530000064112 |
InParanoidi | Q96EP0 |
OMAi | AVLCAMC |
OrthoDBi | 1188714at2759 |
PhylomeDBi | Q96EP0 |
TreeFami | TF350529 |
Family and domain databases
Gene3Di | 3.30.40.10, 1 hit |
IDEALi | IID00576 |
InterProi | View protein in InterPro IPR002867, IBR_dom IPR036339, PUB-like_dom_sf IPR018997, PUB_domain IPR026254, RNF31-like IPR032065, RNF31-UBA IPR041031, RNF31_C IPR040641, RNF31_PUB IPR044066, TRIAD_supradom IPR015940, UBA IPR001876, Znf_RanBP2 IPR036443, Znf_RanBP2_sf IPR013083, Znf_RING/FYVE/PHD IPR017907, Znf_RING_CS |
PANTHERi | PTHR16004, PTHR16004, 2 hits |
Pfami | View protein in Pfam PF18091, E3_UbLigase_RBR, 1 hit PF16678, HOIP-UBA, 1 hit PF01485, IBR, 1 hit PF09409, PUB, 1 hit PF18486, PUB_1, 1 hit |
SMARTi | View protein in SMART SM00647, IBR, 2 hits SM00547, ZnF_RBZ, 3 hits |
SUPFAMi | SSF143503, SSF143503, 1 hit SSF90209, SSF90209, 1 hit |
PROSITEi | View protein in PROSITE PS51873, TRIAD, 1 hit PS50030, UBA, 1 hit PS01358, ZF_RANBP2_1, 3 hits PS50199, ZF_RANBP2_2, 2 hits PS00518, ZF_RING_1, 1 hit |
s (3+)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 3 described isoforms and 13 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MPGEEEERAF LVAREELASA LRRDSGQAFS LEQLRPLLAS SLPLAARYLQ
60 70 80 90 100
LDAARLVRCN AHGEPRNYLN TLSTALNILE KYGRNLLSPQ RPRYWRGVKF
110 120 130 140 150
NNPVFRSTVD AVQGGRDVLR LYGYTEEQPD GLSFPEGQEE PDEHQVATVT
160 170 180 190 200
LEVLLLRTEL SLLLQNTHPR QQALEQLLED KVEDDMLQLS EFDPLLREIA
210 220 230 240 250
PGPLTTPSVP GSTPGPCFLC GSAPGTLHCP SCKQALCPAC DHLFHGHPSR
260 270 280 290 300
AHHLRQTLPG VLQGTHLSPS LPASAQPRPQ STSLLALGDS SLSSPNPASA
310 320 330 340 350
HLPWHCAACA MLNEPWAVLC VACDRPRGCK GLGLGTEGPQ GTGGLEPDLA
360 370 380 390 400
RGRWACQSCT FENEAAAVLC SICERPRLAQ PPSLVVDSRD AGICLQPLQQ
410 420 430 440 450
GDALLASAQS QVWYCIHCTF CNSSPGWVCV MCNRTSSPIP AQHAPRPYAS
460 470 480 490 500
SLEKGPPKPG PPRRLSAPLP SSCGDPEKQR QDKMREEGLQ LVSMIREGEA
510 520 530 540 550
AGACPEEIFS ALQYSGTEVP LQWLRSELPY VLEMVAELAG QQDPGLGAFS
560 570 580 590 600
CQEARRAWLD RHGNLDEAVE ECVRTRRRKV QELQSLGFGP EEGSLQALFQ
610 620 630 640 650
HGGDVSRALT ELQRQRLEPF RQRLWDSGPE PTPSWDGPDK QSLVRRLLAV
660 670 680 690 700
YALPSWGRAE LALSLLQETP RNYELGDVVE AVRHSQDRAF LRRLLAQECA
710 720 730 740 750
VCGWALPHNR MQALTSCECT ICPDCFRQHF TIALKEKHIT DMVCPACGRP
760 770 780 790 800
DLTDDTQLLS YFSTLDIQLR ESLEPDAYAL FHKKLTEGVL MRDPKFLWCA
810 820 830 840 850
QCSFGFIYER EQLEATCPQC HQTFCVRCKR QWEEQHRGRS CEDFQNWKRM
860 870 880 890 900
NDPEYQAQGL AMYLQENGID CPKCKFSYAL ARGGCMHFHC TQCRHQFCSG
910 920 930 940 950
CYNAFYAKNK CPEPNCRVKK SLHGHHPRDC LFYLRDWTAL RLQKLLQDNN
960 970 980 990 1000
VMFNTEPPAG ARAVPGGGCR VIEQKEVPNG LRDEACGKET PAGYAGLCQA
1010 1020 1030 1040 1050
HYKEYLVSLI NAHSLDPATL YEVEELETAT ERYLHVRPQP LAGEDPPAYQ
1060 1070
ARLLQKLTEE VPLGQSIPRR RK
Computationally mapped potential isoform sequencesi
There are 13 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketH0YKX0 | H0YKX0_HUMAN | RBR-type E3 ubiquitin transferase | RNF31 | 917 | Annotation score: | ||
H0YMG4 | H0YMG4_HUMAN | E3 ubiquitin-protein ligase RNF31 | RNF31 | 623 | Annotation score: | ||
H0YNK5 | H0YNK5_HUMAN | E3 ubiquitin-protein ligase RNF31 | RNF31 | 149 | Annotation score: | ||
H0YMN0 | H0YMN0_HUMAN | E3 ubiquitin-protein ligase RNF31 | RNF31 | 143 | Annotation score: | ||
H0YNT1 | H0YNT1_HUMAN | E3 ubiquitin-protein ligase RNF31 | RNF31 | 140 | Annotation score: | ||
H0YM13 | H0YM13_HUMAN | E3 ubiquitin-protein ligase RNF31 | RNF31 | 170 | Annotation score: | ||
H0YKI4 | H0YKI4_HUMAN | E3 ubiquitin-protein ligase RNF31 | RNF31 | 165 | Annotation score: | ||
H0YMG8 | H0YMG8_HUMAN | E3 ubiquitin-protein ligase RNF31 | RNF31 | 152 | Annotation score: | ||
A0A494C1G4 | A0A494C1G4_HUMAN | E3 ubiquitin-protein ligase RNF31 | RNF31 | 161 | Annotation score: | ||
H0YMK6 | H0YMK6_HUMAN | E3 ubiquitin-protein ligase RNF31 | RNF31 | 32 | Annotation score: | ||
There are more potential isoformsShow all |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 529 | P → S in AAP12522 (PubMed:15093743).Curated | 1 | |
Sequence conflicti | 800 | A → V in BAA91450 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 925 | H → R in BAB15675 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 1005 | Y → N in BAB15675 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 1018 | A → S in BAB15675 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 1021 | Y → D in BAB15675 (PubMed:14702039).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_052102 | 1061 | V → I1 PublicationCorresponds to variant dbSNP:rs2277484Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_014006 | 1 – 151 | Missing in isoform 3. 1 PublicationAdd BLAST | 151 | |
Alternative sequenceiVSP_009647 | 73 – 630 | Missing in isoform 2. 1 PublicationAdd BLAST | 558 | |
Alternative sequenceiVSP_014007 | 152 – 164 | EVLLL…LSLLL → MDLCTRAGEPSLT in isoform 3. 1 PublicationAdd BLAST | 13 | |
Alternative sequenceiVSP_009648 | 833 – 841 | Missing in isoform 2. 1 Publication | 9 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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] CCDS81792.1 [Q96EP0-3] |
RefSeqi | NP_001297261.1, NM_001310332.1 [Q96EP0-3] NP_060469.4, NM_017999.4 [Q96EP0-1] |
Genome annotation databases
Ensembli | ENST00000324103; ENSP00000315112; ENSG00000092098 ENST00000559275; ENSP00000453574; ENSG00000092098 [Q96EP0-3] ENST00000642631; ENSP00000494011; ENSG00000285152 [Q96EP0-3] ENST00000647495; ENSP00000496609; ENSG00000285152 |
GeneIDi | 55072 |
KEGGi | hsa:55072 |
MANE-Selecti | ENST00000324103.11; ENSP00000315112.6; NM_017999.5; NP_060469.4 |
UCSCi | uc001wml.2, human [Q96EP0-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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] CCDS81792.1 [Q96EP0-3] |
RefSeqi | NP_001297261.1, NM_001310332.1 [Q96EP0-3] NP_060469.4, NM_017999.4 [Q96EP0-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
5EDV | X-ray | 3.48 | A/B | 696-1072 | [»] | |
5LJN | X-ray | 2.70 | A/B | 5-176 | [»] | |
5X0W | X-ray | 3.00 | A/C/E/G | 480-639 | [»] | |
6GZY | X-ray | 2.15 | A/B | 853-1072 | [»] | |
6KC5 | X-ray | 1.54 | B | 853-1072 | [»] | |
6KC6 | X-ray | 2.12 | A/C/E/G/I/K | 853-1072 | [»] | |
6SC5 | X-ray | 2.10 | A | 697-1072 | [»] | |
6SC6 | X-ray | 2.25 | A | 697-1072 | [»] | |
6SC7 | X-ray | 2.56 | A | 697-1072 | [»] | |
6SC8 | X-ray | 2.11 | A | 697-1072 | [»] | |
6SC9 | X-ray | 2.47 | A | 697-1072 | [»] | |
BMRBi | Q96EP0 | |||||
SMRi | Q96EP0 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 120389, 383 interactors |
ComplexPortali | CPX-1877, LUBAC ubiquitin ligase complex |
CORUMi | Q96EP0 |
DIPi | DIP-44034N |
IntActi | Q96EP0, 69 interactors |
MINTi | Q96EP0 |
STRINGi | 9606.ENSP00000315112 |
Chemistry databases
BindingDBi | Q96EP0 |
ChEMBLi | CHEMBL4296109 |
PTM databases
iPTMneti | Q96EP0 |
MetOSitei | Q96EP0 |
PhosphoSitePlusi | Q96EP0 |
Genetic variation databases
BioMutai | RNF31 |
DMDMi | 45477216 |
Proteomic databases
EPDi | Q96EP0 |
jPOSTi | Q96EP0 |
MassIVEi | Q96EP0 |
MaxQBi | Q96EP0 |
PaxDbi | Q96EP0 |
PeptideAtlasi | Q96EP0 |
PRIDEi | Q96EP0 |
ProteomicsDBi | 76429 [Q96EP0-1] 76430 [Q96EP0-2] 76431 [Q96EP0-3] |
Protocols and materials databases
ABCDi | Q96EP0, 10 sequenced antibodies |
Antibodypediai | 22671, 257 antibodies from 36 providers |
DNASUi | 55072 |
Genome annotation databases
Ensembli | ENST00000324103; ENSP00000315112; ENSG00000092098 ENST00000559275; ENSP00000453574; ENSG00000092098 [Q96EP0-3] ENST00000642631; ENSP00000494011; ENSG00000285152 [Q96EP0-3] ENST00000647495; ENSP00000496609; ENSG00000285152 |
GeneIDi | 55072 |
KEGGi | hsa:55072 |
MANE-Selecti | ENST00000324103.11; ENSP00000315112.6; NM_017999.5; NP_060469.4 |
UCSCi | uc001wml.2, human [Q96EP0-1] |
Organism-specific databases
CTDi | 55072 |
DisGeNETi | 55072 |
GeneCardsi | RNF31 |
HGNCi | HGNC:16031, RNF31 |
HPAi | ENSG00000092098, Low tissue specificity |
MalaCardsi | RNF31 |
MIMi | 612487, gene |
neXtProti | NX_Q96EP0 |
OpenTargetsi | ENSG00000092098 ENSG00000259529 |
Orphaneti | 329173, Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis |
PharmGKBi | PA134906471 |
VEuPathDBi | HostDB:ENSG00000092098 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1812, Eukaryota |
GeneTreei | ENSGT00530000064112 |
InParanoidi | Q96EP0 |
OMAi | AVLCAMC |
OrthoDBi | 1188714at2759 |
PhylomeDBi | Q96EP0 |
TreeFami | TF350529 |
Enzyme and pathway databases
UniPathwayi | UPA00143 |
BRENDAi | 2.3.2.31, 2681 |
PathwayCommonsi | Q96EP0 |
Reactomei | R-HSA-5357905, Regulation of TNFR1 signaling R-HSA-5357956, TNFR1-induced NFkappaB signaling pathway |
SignaLinki | Q96EP0 |
Miscellaneous databases
BioGRID-ORCSi | 55072, 76 hits in 1088 CRISPR screens |
ChiTaRSi | RNF31, human |
EvolutionaryTracei | Q96EP0 |
GeneWikii | RNF31 |
GenomeRNAii | 55072 |
Pharosi | Q96EP0, Tbio |
PROi | PR:Q96EP0 |
RNActi | Q96EP0, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000092098, Expressed in muscle tissue and 119 other tissues |
ExpressionAtlasi | Q96EP0, baseline and differential |
Genevisiblei | Q96EP0, HS |
Family and domain databases
Gene3Di | 3.30.40.10, 1 hit |
IDEALi | IID00576 |
InterProi | View protein in InterPro IPR002867, IBR_dom IPR036339, PUB-like_dom_sf IPR018997, PUB_domain IPR026254, RNF31-like IPR032065, RNF31-UBA IPR041031, RNF31_C IPR040641, RNF31_PUB IPR044066, TRIAD_supradom IPR015940, UBA IPR001876, Znf_RanBP2 IPR036443, Znf_RanBP2_sf IPR013083, Znf_RING/FYVE/PHD IPR017907, Znf_RING_CS |
PANTHERi | PTHR16004, PTHR16004, 2 hits |
Pfami | View protein in Pfam PF18091, E3_UbLigase_RBR, 1 hit PF16678, HOIP-UBA, 1 hit PF01485, IBR, 1 hit PF09409, PUB, 1 hit PF18486, PUB_1, 1 hit |
SMARTi | View protein in SMART SM00647, IBR, 2 hits SM00547, ZnF_RBZ, 3 hits |
SUPFAMi | SSF143503, SSF143503, 1 hit SSF90209, SSF90209, 1 hit |
PROSITEi | View protein in PROSITE PS51873, TRIAD, 1 hit PS50030, UBA, 1 hit PS01358, ZF_RANBP2_1, 3 hits PS50199, ZF_RANBP2_2, 2 hits PS00518, ZF_RING_1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RNF31_HUMAN | |
Accessioni | Q96EP0Primary (citable) accession number: Q96EP0 Secondary accession number(s): A0A962 Q9NWD2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 15, 2004 |
Last sequence update: | December 1, 2001 | |
Last modified: | February 23, 2022 | |
This is version 195 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families