CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019200
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RNF31 
Protein Synonyms/Alias
 HOIL-1-interacting protein; HOIP; RING finger protein 31; Zinc in-between-RING-finger ubiquitin-associated domain protein 
Gene Name
 RNF31 
Gene Synonyms/Alias
 ZIBRA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
81TALNILEKYGRNLLSubiquitination[1]
99PRYWRGVKFNNPVFRubiquitination[1, 2, 3]
330CDRPRGCKGLGLGTEubiquitination[1, 2, 3, 4, 5]
454PYASSLEKGPPKPGPubiquitination[2, 3]
458SLEKGPPKPGPPRRLubiquitination[1, 2, 3, 6]
478SSCGDPEKQRQDKMRubiquitination[1]
483PEKQRQDKMREEGLQubiquitination[1]
579CVRTRRRKVQELQSLubiquitination[1, 6]
640PSWDGPDKQSLVRRLubiquitination[1, 2, 3, 6]
735QHFTIALKEKHITDMubiquitination[1]
783DAYALFHKKLTEGVLubiquitination[6]
784AYALFHKKLTEGVLMubiquitination[1, 6]
848CEDFQNWKRMNDPEYubiquitination[1]
873ENGIDCPKCKFSYALubiquitination[1]
910NAFYAKNKCPEPNCRubiquitination[1]
944WTALRLQKLLQDNNVubiquitination[1]
1056YQARLLQKLTEEVPLubiquitination[1, 6]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('M-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. 
Sequence Annotation
 DOMAIN 564 615 UBA.
 ZN_FING 299 329 RanBP2-type 1.
 ZN_FING 350 379 RanBP2-type 2.
 ZN_FING 409 438 RanBP2-type 3.
 ZN_FING 699 747 RING-type 1; degenerate.
 ZN_FING 779 841 IBR-type.
 ZN_FING 860 909 RING-type 2.
 REGION 1 485 Polyubiquitin-binding.
 REGION 563 616 Interaction with RBCK1.
 REGION 910 1072 LDD domain.
 MOD_RES 466 466 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Ligase; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1072 AA 
Protein Sequence
MPGEEEERAF LVAREELASA LRRDSGQAFS LEQLRPLLAS SLPLAARYLQ LDAARLVRCN 60
AHGEPRNYLN TLSTALNILE KYGRNLLSPQ RPRYWRGVKF NNPVFRSTVD AVQGGRDVLR 120
LYGYTEEQPD GLSFPEGQEE PDEHQVATVT LEVLLLRTEL SLLLQNTHPR QQALEQLLED 180
KVEDDMLQLS EFDPLLREIA PGPLTTPSVP GSTPGPCFLC GSAPGTLHCP SCKQALCPAC 240
DHLFHGHPSR AHHLRQTLPG VLQGTHLSPS LPASAQPRPQ STSLLALGDS SLSSPNPASA 300
HLPWHCAACA MLNEPWAVLC VACDRPRGCK GLGLGTEGPQ GTGGLEPDLA RGRWACQSCT 360
FENEAAAVLC SICERPRLAQ PPSLVVDSRD AGICLQPLQQ GDALLASAQS QVWYCIHCTF 420
CNSSPGWVCV MCNRTSSPIP AQHAPRPYAS SLEKGPPKPG PPRRLSAPLP SSCGDPEKQR 480
QDKMREEGLQ LVSMIREGEA AGACPEEIFS ALQYSGTEVP LQWLRSELPY VLEMVAELAG 540
QQDPGLGAFS CQEARRAWLD RHGNLDEAVE ECVRTRRRKV QELQSLGFGP EEGSLQALFQ 600
HGGDVSRALT ELQRQRLEPF RQRLWDSGPE PTPSWDGPDK QSLVRRLLAV YALPSWGRAE 660
LALSLLQETP RNYELGDVVE AVRHSQDRAF LRRLLAQECA VCGWALPHNR MQALTSCECT 720
ICPDCFRQHF TIALKEKHIT DMVCPACGRP DLTDDTQLLS YFSTLDIQLR ESLEPDAYAL 780
FHKKLTEGVL MRDPKFLWCA QCSFGFIYER EQLEATCPQC HQTFCVRCKR QWEEQHRGRS 840
CEDFQNWKRM NDPEYQAQGL AMYLQENGID CPKCKFSYAL ARGGCMHFHC TQCRHQFCSG 900
CYNAFYAKNK CPEPNCRVKK SLHGHHPRDC LFYLRDWTAL RLQKLLQDNN VMFNTEPPAG 960
ARAVPGGGCR VIEQKEVPNG LRDEACGKET PAGYAGLCQA HYKEYLVSLI NAHSLDPATL 1020
YEVEELETAT ERYLHVRPQP LAGEDPPAYQ ARLLQKLTEE VPLGQSIPRR RK 1072 
Gene Ontology
 GO:0035631; C:CD40 receptor complex; ISS:BHF-UCL.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0009898; C:internal side of plasma membrane; ISS:BHF-UCL.
 GO:0071797; C:LUBAC complex; IDA:UniProtKB.
 GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0023035; P:CD40 signaling pathway; ISS:BHF-UCL.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IDA:UniProtKB.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
 GO:0097039; P:protein linear polyubiquitination; IDA:UniProtKB.
 GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB. 
Interpro
 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. 
Pfam
 PF01485; IBR
 PF09409; PUB 
SMART
 SM00647; IBR
 SM00184; RING
 SM00547; ZnF_RBZ 
PROSITE
 PS50030; UBA
 PS01358; ZF_RANBP2_1
 PS50199; ZF_RANBP2_2
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS