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Q96EP0

- RNF31_HUMAN

UniProt

Q96EP0 - RNF31_HUMAN

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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

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. ubiquitin binding Source: UniProtKB
  3. ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
  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
Complete GO annotation...

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-KW
  3. cytoplasmic side of plasma membrane Source: BHF-UCL
  4. LUBAC complex Source: UniProtKB
Complete GO annotation...

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.
ExpressionAtlasiQ96EP0. baseline.
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. 49 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 2-178, 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.
GeneTreeiENSGT00530000064112.
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

        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 BAB15675.1 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 2-178, 351-379, 482-627, 690-1072.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120389. 49 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.
GeneTreei ENSGT00530000064112.
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.
ExpressionAtlasi Q96EP0. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 131 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