Q96EP0 (RNF31_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RING finger protein 31
EC=6.3.2.-

Alternative name(s):
HOIL-1-interacting protein
Short name=HOIP
Zinc in-between-RING-finger ubiquitin-associated domain protein

Gene names

Name:	RNF31
Synonyms:	ZIBRA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1072 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner 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. Binds polyubiquitin of different linkage types. Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
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.
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.13
Sequence similarities	Contains 2 IBR-type zinc fingers. Contains 3 RanBP2-type zinc fingers. Contains 1 RING-type zinc finger. 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 process	Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	CD40 signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL T cell receptor signaling pathway Inferred from direct assay Ref.9. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay Ref.10Ref.11. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from direct assay Ref.10. Source: UniProtKB protein linear polyubiquitination Inferred from direct assay Ref.11Ref.12Ref.13. Source: UniProtKB
Cellular component	CD40 receptor complex Inferred from sequence or structural similarity. Source: BHF-UCL LUBAC complex Inferred from direct assay Ref.6Ref.11Ref.12Ref.13. Source: UniProtKB internal side of plasma membrane Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular function	ubiquitin binding Inferred from direct assay Ref.13. Source: UniProtKB ubiquitin-protein ligase activity Inferred from direct assay Ref.6. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMAD3	P84022	2	EBI-948111,EBI-347161

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1072

1072

RING finger protein 31

PRO_0000056069

Regions

Domain

564 – 615

52

UBA

Zinc finger

299 – 329

31

RanBP2-type 1

Zinc finger

350 – 379

30

RanBP2-type 2

Zinc finger

409 – 438

30

RanBP2-type 3

Zinc finger

699 – 747

49

RING-type; degenerate

Zinc finger

779 – 841

63

IBR-type 1

Zinc finger

853 – 930

78

IBR-type 2

Region

1 – 485

485

Polyubiquitin-binding

Region

563 – 616

54

Interaction with RBCK1

Amino acid modifications

Modified residue

466

1

Phosphoserine Ref.7 Ref.8

Natural variations

Alternative sequence

1 – 151

151

Missing in isoform 3.

VSP_014006

Alternative sequence

73 – 630

558

Missing in isoform 2.

VSP_009647

Alternative sequence

152 – 164

13

EVLLL…LSLLL → MDLCTRAGEPSLT in isoform 3.

VSP_014007

Alternative sequence

833 – 841

9

Missing in isoform 2.

VSP_009648

Natural variant

1061

1

V → I. Ref.2
Corresponds to variant rs2277484 [ dbSNP | Ensembl ].

VAR_052102

Experimental info

Mutagenesis

699

1

C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-702. Ref.6 Ref.13

Mutagenesis

702

1

C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-699. Ref.6 Ref.13

Mutagenesis

871

1

C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-874. Ref.6 Ref.13

Mutagenesis

874

1

C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-871. Ref.6 Ref.13

Sequence conflict

529

1

P → S in AAP12522. Ref.1

Sequence conflict

800

1

A → V in BAA91450. Ref.2

Sequence conflict

925

1

H → R in BAB15675. Ref.2

Sequence conflict

1005

1

Y → N in BAB15675. Ref.2

Sequence conflict

1018

1

A → S in BAB15675. Ref.2

Sequence conflict

1021

1

Y → D in BAB15675. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

1072

Helix Strand Turn

Details...

Beta strand

780 – 783

4

Beta strand

800 – 802

3

Turn

818 – 820

3

Beta strand

826 – 828

3

Turn

834 – 838

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: CFAD183A14F764BA	FASTA	1,072	119,652
	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
	Isoform 2 [UniParc]. Checksum: 04245E2E835AD19C	FASTA	505	57,633
	10 20 30 40 50 60 MPGEEEERAF LVAREELASA LRRDSGQAFS LEQLRPLLAS SLPLAARYLQ LDAARLVRCN 70 80 90 100 110 120 AHGEPRNYLN TLPTPSWDGP DKQSLVRRLL AVYALPSWGR AELALSLLQE TPRNYELGDV 130 140 150 160 170 180 VEAVRHSQDR AFLRRLLAQE CAVCGWALPH NRMQALTSCE CTICPDCFRQ HFTIALKEKH 190 200 210 220 230 240 ITDMVCPACG RPDLTDDTQL LSYFSTLDIQ LRESLEPDAY ALFHKKLTEG VLMRDPKFLW 250 260 270 280 290 300 CAQCSFGFIY EREQLEATCP QCHQTFCVRC KRQWEDFQNW KRMNDPEYQA QGLAMYLQEN 310 320 330 340 350 360 GIDCPKCKFS YALARGGCMH FHCTQCRHQF CSGCYNAFYA KNKCPEPNCR VKKSLHGHHP 370 380 390 400 410 420 RDCLFYLRDW TALRLQKLLQ DNNVMFNTEP PAGARAVPGG GCRVIEQKEV PNGLRDEACG 430 440 450 460 470 480 KETPAGYAGL CQAHYKEYLV SLINAHSLDP ATLYEVEELE TATERYLHVR PQPLAGEDPP 490 500 AYQARLLQKL TEEVPLGQSI PRRRK
	Isoform 3 [UniParc]. Checksum: 2149563718B64B0B	FASTA	921	102,496
	10 20 30 40 50 60 MDLCTRAGEP SLTQNTHPRQ QALEQLLEDK VEDDMLQLSE FDPLLREIAP GPLTTPSVPG 70 80 90 100 110 120 STPGPCFLCG SAPGTLHCPS CKQALCPACD HLFHGHPSRA HHLRQTLPGV LQGTHLSPSL 130 140 150 160 170 180 PASAQPRPQS TSLLALGDSS LSSPNPASAH LPWHCAACAM LNEPWAVLCV ACDRPRGCKG 190 200 210 220 230 240 LGLGTEGPQG TGGLEPDLAR GRWACQSCTF ENEAAAVLCS ICERPRLAQP PSLVVDSRDA 250 260 270 280 290 300 GICLQPLQQG DALLASAQSQ VWYCIHCTFC NSSPGWVCVM CNRTSSPIPA QHAPRPYASS 310 320 330 340 350 360 LEKGPPKPGP PRRLSAPLPS SCGDPEKQRQ DKMREEGLQL VSMIREGEAA GACPEEIFSA 370 380 390 400 410 420 LQYSGTEVPL QWLRSELPYV LEMVAELAGQ QDPGLGAFSC QEARRAWLDR HGNLDEAVEE 430 440 450 460 470 480 CVRTRRRKVQ ELQSLGFGPE EGSLQALFQH GGDVSRALTE LQRQRLEPFR QRLWDSGPEP 490 500 510 520 530 540 TPSWDGPDKQ SLVRRLLAVY ALPSWGRAEL ALSLLQETPR NYELGDVVEA VRHSQDRAFL 550 560 570 580 590 600 RRLLAQECAV CGWALPHNRM QALTSCECTI CPDCFRQHFT IALKEKHITD MVCPACGRPD 610 620 630 640 650 660 LTDDTQLLSY FSTLDIQLRE SLEPDAYALF HKKLTEGVLM RDPKFLWCAQ CSFGFIYERE 670 680 690 700 710 720 QLEATCPQCH QTFCVRCKRQ WEEQHRGRSC EDFQNWKRMN DPEYQAQGLA MYLQENGIDC 730 740 750 760 770 780 PKCKFSYALA RGGCMHFHCT QCRHQFCSGC YNAFYAKNKC PEPNCRVKKS LHGHHPRDCL 790 800 810 820 830 840 FYLRDWTALR LQKLLQDNNV MFNTEPPAGA RAVPGGGCRV IEQKEVPNGL RDEACGKETP 850 860 870 880 890 900 AGYAGLCQAH YKEYLVSLIN AHSLDPATLY EVEELETATE RYLHVRPQPL AGEDPPAYQA 910 920 RLLQKLTEEV PLGQSIPRRR K

References

	« Hide 'large scale' referencesShow '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: 15093743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, TISSUE SPECIFICITY. Tissue: Mammary carcinoma.
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 319-1072 (ISOFORMS 1/3), VARIANT ILE-1061. Tissue: Embryo and Hair follicle dermal papilla.
[3]	"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: 12508121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Ovary and Placenta.
[5]	"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: 12693554] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 526-1072 (ISOFORMS 1/3). Tissue: Spleen.
[6]	"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: 17006537] [Abstract] Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION OF THE LUBAC COMPLEX, MUTAGENESIS OF CYS-699; CYS-702; CYS-871 AND CYS-874.
[7]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, MASS SPECTROMETRY.
[8]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, MASS SPECTROMETRY.
[9]	"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: 20005846] [Abstract] Cited for: MASS SPECTROMETRY, POLYUBIQUITIN-BINDING, FUNCTION OF THE LUBAC COMPLEX, ASSOCIATION WITH TNF-RSC.
[10]	"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: 19136968] [Abstract] Cited for: FUNCTION OF THE LUBAC COMPLEX.
[11]	"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: 21455173] [Abstract] Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION.
[12]	"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: 21455180] [Abstract] Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION.
[13]	"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: 21455181] [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.
[14]	"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.
AK000973 mRNA. Translation: BAA91450.1.
AK027154 mRNA. Translation: BAB15675.1. Frameshift.
AK055542 mRNA. Translation: BAB70948.1. Different initiation.
AL136295 Genomic DNA. No translation available.
BC009821 mRNA. Translation: AAH09821.3.
BC012077 mRNA. Translation: AAH12077.1.
BC017376 mRNA. Translation: AAH17376.3.
AK074144 mRNA. Translation: BAB84970.1.

IPI

IPI00094740.
IPI00409629.
IPI00604409.

RefSeq

NP_060469.4. NM_017999.4.

UniGene

Hs.375217.
Hs.434081.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CT7	NMR	-	A	779-851	[»]

ProteinModelPortal

Q96EP0.

SMR

Q96EP0. Positions 70-146, 779-851, 864-917.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96EP0. 10 interactions.

MINT

MINT-3377714.

STRING

Q96EP0.

PTM databases

PhosphoSite

Q96EP0.

Polymorphism databases

DMDM

45477216.

Proteomic databases

PRIDE

Q96EP0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000324103; ENSP00000315112; ENSG00000092098.

GeneID

55072.

KEGG

hsa:55072.

UCSC

uc001wml.1. human.
uc001wmn.1. human.
uc001wmo.1. human.

Organism-specific databases

CTD

55072.

GeneCards

GC14P024616.

H-InvDB

HIX0019350.

HGNC

HGNC:16031. RNF31.

HPA

CAB009063.

MIM

612487. gene.

neXtProt

NX_Q96EP0.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00530000064112.

HOVERGEN

HBG063678.

InParanoid

Q96EP0.

OMA

NWKRTND.

OrthoDB

EOG45MN4P.

PhylomeDB

Q96EP0.

Gene expression databases

ArrayExpress

Q96EP0.

Bgee

Q96EP0.

CleanEx

HS_RNF31.

Genevestigator

Q96EP0.

Family and domain databases

InterPro

IPR018997. PUB_domain.
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]

KO

K11974.

Pfam

PF01485. IBR. 1 hit.
PF09409. PUB. 1 hit.
[Graphical view]

SMART

SM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
SM00547. ZnF_RBZ. 3 hits.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 1 hit.

PROSITE

PS50030. UBA. 1 hit.
PS01358. ZF_RANBP2_1. 3 hits.
PS50199. ZF_RANBP2_2. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

NextBio

58596.

SOURCE

Search...

Entry information

Entry name

RNF31_HUMAN

Accession

Primary (citable) accession number: Q96EP0
Secondary accession number(s): Q86VI2 , Q8TEI0, Q96GB4, Q96NF1, Q9H5F1, Q9NWD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.