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Protein

E3 ubiquitin-protein ligase RNF31

Gene

RNF31

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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). 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). Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed:21455173). 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 (PubMed:20005846). Together with otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types (PubMed:23708998).8 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri299 – 329RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri350 – 379RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri409 – 438RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri699 – 747RING-type 1; degenerateAdd BLAST49
Zinc fingeri779 – 841IBR-typeAdd BLAST63
Zinc fingeri860 – 909RING-type 2Add BLAST50

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • CD40 signaling pathway Source: BHF-UCL
  • I-kappaB kinase/NF-kappaB signaling Source: Reactome
  • 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
  • protein linear polyubiquitination Source: UniProtKB
  • protein polyubiquitination Source: UniProtKB
  • regulation of tumor necrosis factor-mediated signaling pathway Source: Reactome
  • T cell receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF31 (EC:6.3.2.-)
Alternative name(s):
HOIL-1-interacting protein1 Publication
Short name:
HOIP1 Publication
RING finger protein 31Imported
Zinc in-between-RING-finger ubiquitin-associated domain protein1 Publication
Gene namesi
Name:RNF31Imported
Synonyms:ZIBRA1 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:16031. RNF31.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

  • CD40 receptor complex Source: BHF-UCL
  • cytoplasmic side of plasma membrane Source: BHF-UCL
  • cytosol Source: Reactome
  • LUBAC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi82Y → A: Abolished interaction with OTULIN. 1 Publication1
Mutagenesisi82Y → F: Reduced interaction with OTULIN. 1 Publication1
Mutagenesisi85N → A: Reduced interaction with OTULIN. 1 Publication1
Mutagenesisi99K → E: Reduced interaction with OTULIN. 1 Publication1
Mutagenesisi101N → R: Does not affect interaction with OTULIN. 1 Publication1
Mutagenesisi102N → D: Abolished interaction with OTULIN. 1 Publication1
Mutagenesisi104V → A: Reduced interaction with OTULIN. 1 Publication1
Mutagenesisi699C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-702. 2 Publications1
Mutagenesisi702C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-699. 2 Publications1
Mutagenesisi871C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-874. 2 Publications1
Mutagenesisi874C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-871. 2 Publications1

Organism-specific databases

DisGeNETi55072.
OpenTargetsiENSG00000092098.
PharmGKBiPA134906471.

Polymorphism and mutation databases

BioMutaiRNF31.
DMDMi45477216.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000560691 – 1072E3 ubiquitin-protein ligase RNF31Add BLAST1072

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei383PhosphoserineCombined sources1
Modified residuei466PhosphoserineCombined sources1

Post-translational modificationi

Autoubiquitinated. Interaction with OTULIN is required to prevent formation of 'Met-1'-linked polyubiquitin chains.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96EP0.
MaxQBiQ96EP0.
PaxDbiQ96EP0.
PeptideAtlasiQ96EP0.
PRIDEiQ96EP0.

PTM databases

iPTMnetiQ96EP0.
PhosphoSitePlusiQ96EP0.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000092098.
CleanExiHS_RNF31.
ExpressionAtlasiQ96EP0. baseline and differential.
GenevisibleiQ96EP0. HS.

Organism-specific databases

HPAiCAB009063.
HPA048745.

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). LUBAC has a MW of approximative 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 with CYLD (PubMed:26997266). Interacts with MUSK (By similarity).By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AESQ081173EBI-10225152,EBI-717810
Azi2Q9QYP62EBI-948111,EBI-6115874From a different organism.
CCDC24Q8N4L83EBI-10225152,EBI-1104933
KRTAP9-2Q9BYQ43EBI-10225152,EBI-1044640
RBCK1Q9BYM820EBI-948111,EBI-2340624
SHARPINQ9H0F62EBI-948111,EBI-3942966
SMAD3P840222EBI-948111,EBI-347161
SNRPCQ5TAL43EBI-10225152,EBI-10246938
Traf1Q4VA122EBI-948111,EBI-6116765From a different organism.
TSSC4Q9Y5U23EBI-10225152,EBI-717229
VASNQ6EMK43EBI-10225152,EBI-10249550

GO - Molecular functioni

  • ubiquitin binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi120389. 72 interactors.
DIPiDIP-44034N.
IntActiQ96EP0. 28 interactors.
MINTiMINT-3377714.
STRINGi9606.ENSP00000315112.

Structurei

Secondary structure

11072
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 23Combined sources20
Helixi31 – 38Combined sources8
Helixi44 – 47Combined sources4
Beta strandi49 – 51Combined sources3
Helixi53 – 58Combined sources6
Helixi65 – 86Combined sources22
Beta strandi88 – 90Combined sources3
Turni93 – 96Combined sources4
Beta strandi97 – 102Combined sources6
Helixi103 – 107Combined sources5
Helixi109 – 111Combined sources3
Helixi115 – 122Combined sources8
Beta strandi126 – 128Combined sources3
Beta strandi131 – 133Combined sources3
Helixi143 – 164Combined sources22
Helixi171 – 177Combined sources7
Turni357 – 359Combined sources3
Turni371 – 373Combined sources3
Helixi483 – 493Combined sources11
Helixi505 – 515Combined sources11
Helixi521 – 527Combined sources7
Helixi531 – 542Combined sources12
Helixi544 – 546Combined sources3
Helixi551 – 560Combined sources10
Turni561 – 563Combined sources3
Helixi565 – 585Combined sources21
Helixi590 – 592Combined sources3
Helixi594 – 600Combined sources7
Turni601 – 603Combined sources3
Helixi605 – 616Combined sources12
Helixi618 – 625Combined sources8
Turni700 – 702Combined sources3
Turni715 – 717Combined sources3
Helixi723 – 735Combined sources13
Helixi739 – 741Combined sources3
Turni745 – 747Combined sources3
Turni756 – 759Combined sources4
Helixi760 – 772Combined sources13
Helixi775 – 790Combined sources16
Beta strandi792 – 798Combined sources7
Beta strandi800 – 803Combined sources4
Beta strandi805 – 811Combined sources7
Beta strandi813 – 816Combined sources4
Turni818 – 820Combined sources3
Beta strandi823 – 825Combined sources3
Turni826 – 828Combined sources3
Helixi834 – 836Combined sources3
Helixi841 – 851Combined sources11
Helixi859 – 864Combined sources6
Beta strandi868 – 870Combined sources3
Turni872 – 874Combined sources3
Beta strandi877 – 879Combined sources3
Beta strandi886 – 889Combined sources4
Turni891 – 893Combined sources3
Beta strandi896 – 898Combined sources3
Turni899 – 901Combined sources3
Beta strandi904 – 906Combined sources3
Turni917 – 920Combined sources4
Beta strandi921 – 924Combined sources4
Beta strandi928 – 930Combined sources3
Helixi931 – 934Combined sources4
Helixi939 – 948Combined sources10
Beta strandi965 – 968Combined sources4
Beta strandi972 – 977Combined sources6
Beta strandi980 – 985Combined sources6
Helixi999 – 1012Combined sources14
Helixi1017 – 1020Combined sources4
Helixi1023 – 1034Combined sources12
Helixi1046 – 1060Combined sources15
Beta strandi1065 – 1067Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5EDVX-ray3.48A/B696-1072[»]
5LJNX-ray2.70A/B5-176[»]
ProteinModelPortaliQ96EP0.
SMRiQ96EP0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96EP0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini71 – 142PUBSequence analysisAdd BLAST72
Domaini564 – 615UBAPROSITE-ProRule annotationAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 485Polyubiquitin-bindingAdd BLAST485
Regioni563 – 616Interaction with RBCK1Add BLAST54
Regioni910 – 1072LDD domainAdd BLAST163

Domaini

The PUB domain mediates interaction with the PIM motifs of VCP and RNF31, with a strong preference for RNF31.2 Publications
The RanBP2-type zinc fingers mediate the specific interaction with ubiquitin.1 Publication
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 1 PUB (PUG) domain.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)DescriptionActionsGraphical viewLength
Zinc fingeri299 – 329RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri350 – 379RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri409 – 438RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri699 – 747RING-type 1; degenerateAdd BLAST49
Zinc fingeri779 – 841IBR-typeAdd BLAST63
Zinc fingeri860 – 909RING-type 2Add BLAST50

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1812. Eukaryota.
ENOG410XS1H. LUCA.
GeneTreeiENSGT00530000064112.
HOVERGENiHBG063678.
InParanoidiQ96EP0.
KOiK11974.
OMAiRTNDPEY.
OrthoDBiEOG091G01NM.
PhylomeDBiQ96EP0.
TreeFamiTF350529.

Family and domain databases

InterProiIPR002867. IBR_dom.
IPR018997. PUB_domain.
IPR026254. RNF31.
IPR032065. RNF31-UBA.
IPR015940. UBA.
IPR001876. Znf_RanBP2.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR16004. PTHR16004. 1 hit.
PfamiPF16678. HOIP-UBA. 1 hit.
PF01485. IBR. 1 hit.
PF09409. PUB. 1 hit.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00547. ZnF_RBZ. 3 hits.
[Graphical view]
SUPFAMiSSF143503. SSF143503. 1 hit.
SSF90209. SSF90209. 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. AlignAdd to basket

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

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti529P → S in AAP12522 (PubMed:15093743).Curated1
Sequence conflicti800A → V in BAA91450 (PubMed:14702039).Curated1
Sequence conflicti925H → R in BAB15675 (PubMed:14702039).Curated1
Sequence conflicti1005Y → N in BAB15675 (PubMed:14702039).Curated1
Sequence conflicti1018A → S in BAB15675 (PubMed:14702039).Curated1
Sequence conflicti1021Y → D in BAB15675 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0521021061V → I.1 PublicationCorresponds to variant rs2277484dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0140061 – 151Missing in isoform 3. 1 PublicationAdd BLAST151
Alternative sequenceiVSP_00964773 – 630Missing in isoform 2. 1 PublicationAdd BLAST558
Alternative sequenceiVSP_014007152 – 164EVLLL…LSLLL → MDLCTRAGEPSLT in isoform 3. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_009648833 – 841Missing in isoform 2. 1 Publication9

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.
CCDSiCCDS41931.1. [Q96EP0-1]
CCDS81792.1. [Q96EP0-3]
RefSeqiNP_001297261.1. NM_001310332.1. [Q96EP0-3]
NP_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.2. human. [Q96EP0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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.
CCDSiCCDS41931.1. [Q96EP0-1]
CCDS81792.1. [Q96EP0-3]
RefSeqiNP_001297261.1. NM_001310332.1. [Q96EP0-3]
NP_060469.4. NM_017999.4. [Q96EP0-1]
UniGeneiHs.375217.
Hs.434081.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5EDVX-ray3.48A/B696-1072[»]
5LJNX-ray2.70A/B5-176[»]
ProteinModelPortaliQ96EP0.
SMRiQ96EP0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120389. 72 interactors.
DIPiDIP-44034N.
IntActiQ96EP0. 28 interactors.
MINTiMINT-3377714.
STRINGi9606.ENSP00000315112.

PTM databases

iPTMnetiQ96EP0.
PhosphoSitePlusiQ96EP0.

Polymorphism and mutation databases

BioMutaiRNF31.
DMDMi45477216.

Proteomic databases

EPDiQ96EP0.
MaxQBiQ96EP0.
PaxDbiQ96EP0.
PeptideAtlasiQ96EP0.
PRIDEiQ96EP0.

Protocols and materials databases

DNASUi55072.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324103; ENSP00000315112; ENSG00000092098. [Q96EP0-1]
ENST00000559275; ENSP00000453574; ENSG00000092098. [Q96EP0-3]
GeneIDi55072.
KEGGihsa:55072.
UCSCiuc001wml.2. human. [Q96EP0-1]

Organism-specific databases

CTDi55072.
DisGeNETi55072.
GeneCardsiRNF31.
HGNCiHGNC:16031. RNF31.
HPAiCAB009063.
HPA048745.
MIMi612487. gene.
neXtProtiNX_Q96EP0.
OpenTargetsiENSG00000092098.
PharmGKBiPA134906471.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1812. Eukaryota.
ENOG410XS1H. LUCA.
GeneTreeiENSGT00530000064112.
HOVERGENiHBG063678.
InParanoidiQ96EP0.
KOiK11974.
OMAiRTNDPEY.
OrthoDBiEOG091G01NM.
PhylomeDBiQ96EP0.
TreeFamiTF350529.

Enzyme and pathway databases

ReactomeiR-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.

Miscellaneous databases

ChiTaRSiRNF31. human.
EvolutionaryTraceiQ96EP0.
GeneWikiiRNF31.
GenomeRNAii55072.
PROiQ96EP0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000092098.
CleanExiHS_RNF31.
ExpressionAtlasiQ96EP0. baseline and differential.
GenevisibleiQ96EP0. HS.

Family and domain databases

InterProiIPR002867. IBR_dom.
IPR018997. PUB_domain.
IPR026254. RNF31.
IPR032065. RNF31-UBA.
IPR015940. UBA.
IPR001876. Znf_RanBP2.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR16004. PTHR16004. 1 hit.
PfamiPF16678. HOIP-UBA. 1 hit.
PF01485. IBR. 1 hit.
PF09409. PUB. 1 hit.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00547. ZnF_RBZ. 3 hits.
[Graphical view]
SUPFAMiSSF143503. SSF143503. 1 hit.
SSF90209. SSF90209. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 154 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.