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Q96EP0 (RNF31_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RNF31
Synonyms:ZIBRA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1072 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17

Subunit structure

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. Ref.2 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17

Subcellular location

Cytoplasm By similarity.

Tissue specificity

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

Domain

The RanBP2-type zinc fingers mediate the specific interaction with ubiquitin. Ref.14 Ref.15

The UBA domain mediates association with RBCK1/HOIL1 via interaction with its UBL domain. Ref.14 Ref.15

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 (Ref.15). Ref.14 Ref.15

The linear ubiquitin chain determining domain (LDD) mediates the final transfer of ubiquitin from RING 2 onto the N-terminus of a target ubiquitin (Ref.15). Ref.14 Ref.15

Sequence similarities

Contains 1 IBR-type zinc finger.

Contains 3 RanBP2-type zinc fingers.

Contains 2 RING-type zinc fingers.

Contains 1 UBA domain.

Sequence caution

The sequence BAB15675.1 differs from that shown. Reason: Erroneous termination at position 1060. Translated as Glu.

The sequence BAB15675.1 differs from that shown. Reason: Frameshift at position 1036.

The sequence BAB15675.1 differs from that shown. Reason: Intron retention.

The sequence BAB70948.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCD40 signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

T cell receptor signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay Ref.11Ref.12. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay Ref.11. Source: UniProtKB

protein linear polyubiquitination

Inferred from direct assay Ref.12Ref.13Ref.14. Source: UniProtKB

protein polyubiquitination

Inferred from direct assay PubMed 12629548Ref.2. Source: UniProtKB

   Cellular_componentCD40 receptor complex

Inferred from sequence or structural similarity. Source: BHF-UCL

LUBAC complex

Inferred from direct assay Ref.2Ref.12Ref.13Ref.14. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity PubMed 20614026. Source: BHF-UCL

   Molecular_functionubiquitin binding

Inferred from direct assay Ref.14. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay Ref.2. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96EP0-1)

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.
Isoform 2 (identifier: Q96EP0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     73-630: Missing.
     833-841: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q96EP0-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10721072E3 ubiquitin-protein ligase RNF31
PRO_0000056069

Regions

Domain564 – 61552UBA
Zinc finger299 – 32931RanBP2-type 1
Zinc finger350 – 37930RanBP2-type 2
Zinc finger409 – 43830RanBP2-type 3
Zinc finger699 – 74749RING-type 1; degenerate
Zinc finger779 – 84163IBR-type
Zinc finger860 – 90950RING-type 2
Region1 – 485485Polyubiquitin-binding
Region563 – 61654Interaction with RBCK1
Region910 – 1072163LDD domain

Amino acid modifications

Modified residue4661Phosphoserine Ref.8 Ref.9

Natural variations

Alternative sequence1 – 151151Missing in isoform 3.
VSP_014006
Alternative sequence73 – 630558Missing in isoform 2.
VSP_009647
Alternative sequence152 – 16413EVLLL…LSLLL → MDLCTRAGEPSLT in isoform 3.
VSP_014007
Alternative sequence833 – 8419Missing in isoform 2.
VSP_009648
Natural variant10611V → I. Ref.3
Corresponds to variant rs2277484 [ dbSNP | Ensembl ].
VAR_052102

Experimental info

Mutagenesis6991C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-702. Ref.2 Ref.14
Mutagenesis7021C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-699. Ref.2 Ref.14
Mutagenesis8711C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-874. Ref.2 Ref.14
Mutagenesis8741C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-871. Ref.2 Ref.14
Sequence conflict5291P → S in AAP12522. Ref.1
Sequence conflict8001A → V in BAA91450. Ref.3
Sequence conflict9251H → R in BAB15675. Ref.3
Sequence conflict10051Y → N in BAB15675. Ref.3
Sequence conflict10181A → S in BAB15675. Ref.3
Sequence conflict10211Y → D in BAB15675. Ref.3

Secondary structure

........................................................................................................ 1072
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: CFAD183A14F764BA

FASTA1,072119,652
        10         20         30         40         50         60 
MPGEEEERAF LVAREELASA LRRDSGQAFS LEQLRPLLAS SLPLAARYLQ LDAARLVRCN 

        70         80         90        100        110        120 
AHGEPRNYLN TLSTALNILE KYGRNLLSPQ RPRYWRGVKF NNPVFRSTVD AVQGGRDVLR 

       130        140        150        160        170        180 
LYGYTEEQPD GLSFPEGQEE PDEHQVATVT LEVLLLRTEL SLLLQNTHPR QQALEQLLED 

       190        200        210        220        230        240 
KVEDDMLQLS EFDPLLREIA PGPLTTPSVP GSTPGPCFLC GSAPGTLHCP SCKQALCPAC 

       250        260        270        280        290        300 
DHLFHGHPSR AHHLRQTLPG VLQGTHLSPS LPASAQPRPQ STSLLALGDS SLSSPNPASA 

       310        320        330        340        350        360 
HLPWHCAACA MLNEPWAVLC VACDRPRGCK GLGLGTEGPQ GTGGLEPDLA RGRWACQSCT 

       370        380        390        400        410        420 
FENEAAAVLC SICERPRLAQ PPSLVVDSRD AGICLQPLQQ GDALLASAQS QVWYCIHCTF 

       430        440        450        460        470        480 
CNSSPGWVCV MCNRTSSPIP AQHAPRPYAS SLEKGPPKPG PPRRLSAPLP SSCGDPEKQR 

       490        500        510        520        530        540 
QDKMREEGLQ LVSMIREGEA AGACPEEIFS ALQYSGTEVP LQWLRSELPY VLEMVAELAG 

       550        560        570        580        590        600 
QQDPGLGAFS CQEARRAWLD RHGNLDEAVE ECVRTRRRKV QELQSLGFGP EEGSLQALFQ 

       610        620        630        640        650        660 
HGGDVSRALT ELQRQRLEPF RQRLWDSGPE PTPSWDGPDK QSLVRRLLAV YALPSWGRAE 

       670        680        690        700        710        720 
LALSLLQETP RNYELGDVVE AVRHSQDRAF LRRLLAQECA VCGWALPHNR MQALTSCECT 

       730        740        750        760        770        780 
ICPDCFRQHF TIALKEKHIT DMVCPACGRP DLTDDTQLLS YFSTLDIQLR ESLEPDAYAL 

       790        800        810        820        830        840 
FHKKLTEGVL MRDPKFLWCA QCSFGFIYER EQLEATCPQC HQTFCVRCKR QWEEQHRGRS 

       850        860        870        880        890        900 
CEDFQNWKRM NDPEYQAQGL AMYLQENGID CPKCKFSYAL ARGGCMHFHC TQCRHQFCSG 

       910        920        930        940        950        960 
CYNAFYAKNK CPEPNCRVKK SLHGHHPRDC LFYLRDWTAL RLQKLLQDNN VMFNTEPPAG 

       970        980        990       1000       1010       1020 
ARAVPGGGCR VIEQKEVPNG LRDEACGKET PAGYAGLCQA HYKEYLVSLI NAHSLDPATL 

      1030       1040       1050       1060       1070 
YEVEELETAT ERYLHVRPQP LAGEDPPAYQ ARLLQKLTEE VPLGQSIPRR RK 

« Hide

Isoform 2 [UniParc].

Checksum: 04245E2E835AD19C
Show »

FASTA50557,633
Isoform 3 [UniParc].

Checksum: 2149563718B64B0B
Show »

FASTA921102,496

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation."
Tokunaga F., Sakata S., Saeki Y., Satomi Y., Kirisako T., Kamei K., Nakagawa T., Kato M., Murata S., Yamaoka S., Yamamoto M., Akira S., Takao T., Tanaka K., Iwai K.
Nat. Cell Biol. 11:123-132(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE LUBAC COMPLEX.
[12]"Linear ubiquitination prevents inflammation and regulates immune signalling."
Gerlach B., Cordier S.M., Schmukle A.C., Emmerich C.H., Rieser E., Haas T.L., Webb A.I., Rickard J.A., Anderton H., Wong W.W., Nachbur U., Gangoda L., Warnken U., Purcell A.W., Silke J., Walczak H.
Nature 471:591-596(2011) [PubMed] [Europe PMC] [Abstract]
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]"SHARPIN forms a linear ubiquitin ligase complex regulating NF-kappaB activity and apoptosis."
Ikeda F., Deribe Y.L., Skanland S.S., Stieglitz B., Grabbe C., Franz-Wachtel M., van Wijk S.J., Goswami P., Nagy V., Terzic J., Tokunaga F., Androulidaki A., Nakagawa T., Pasparakis M., Iwai K., Sundberg J.P., Schaefer L., Rittinger K., Macek B., Dikic I.
Nature 471:637-641(2011) [PubMed] [Europe PMC] [Abstract]
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]"The linear ubiquitin-specific deubiquitinase gumby regulates angiogenesis."
Rivkin E., Almeida S.M., Ceccarelli D.F., Juang Y.C., Maclean T.A., Srikumar T., Huang H., Dunham W.H., Fukumura R., Xie G., Gondo Y., Raught B., Gingras A.C., Sicheri F., Cordes S.P.
Nature 498:318-324(2013) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_060469.4. NM_017999.4.
UniGeneHs.375217.
Hs.434081.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ96EP0.
SMRQ96EP0. Positions 1-179, 482-627, 690-1072.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120389. 30 interactions.
DIPDIP-44034N.
IntActQ96EP0. 21 interactions.
MINTMINT-3377714.
STRING9606.ENSP00000315112.

PTM databases

PhosphoSiteQ96EP0.

Polymorphism databases

DMDM45477216.

Proteomic databases

PaxDbQ96EP0.
PRIDEQ96EP0.

Protocols and materials databases

DNASU55072.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324103; ENSP00000315112; ENSG00000092098. [Q96EP0-1]
ENST00000382687; ENSP00000372134; ENSG00000092098. [Q96EP0-3]
ENST00000559275; ENSP00000453574; ENSG00000092098. [Q96EP0-3]
GeneID55072.
KEGGhsa:55072.
UCSCuc001wml.1. human. [Q96EP0-3]
uc001wmn.1. human. [Q96EP0-1]

Organism-specific databases

CTD55072.
GeneCardsGC14P024616.
HGNCHGNC:16031. RNF31.
HPACAB009063.
HPA048745.
MIM612487. gene.
neXtProtNX_Q96EP0.
PharmGKBPA134906471.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG269721.
HOVERGENHBG063678.
InParanoidQ96EP0.
KOK11974.
OMARTNDPEY.
PhylomeDBQ96EP0.
TreeFamTF350529.

Gene expression databases

BgeeQ96EP0.
CleanExHS_RNF31.
GenevestigatorQ96EP0.

Family and domain databases

InterProIPR018997. 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]
PANTHERPTHR16004. PTHR16004. 1 hit.
PfamPF01485. IBR. 1 hit.
PF09409. PUB. 1 hit.
[Graphical view]
SMARTSM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
SM00547. ZnF_RBZ. 3 hits.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
PROSITEPS50030. UBA. 1 hit.
PS01358. ZF_RANBP2_1. 3 hits.
PS50199. ZF_RANBP2_2. 2 hits.
PS00518. ZF_RING_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRNF31. human.
EvolutionaryTraceQ96EP0.
GeneWikiRNF31.
GenomeRNAi55072.
NextBio58596.
PROQ96EP0.
SOURCESearch...

Entry information

Entry nameRNF31_HUMAN
AccessionPrimary (citable) accession number: Q96EP0
Secondary accession number(s): A0A962 expand/collapse secondary AC list , Q86VI2, Q8TEI0, Q96GB4, Q96NF1, Q9H5F1, Q9NWD2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM