SH3R2_MOUSE
ID SH3R2_MOUSE Reviewed; 735 AA.
AC Q8BZT2; B2RQJ2; Q80VJ1; Q8C122; Q8C1E3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=E3 ubiquitin-protein ligase SH3RF2;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8TEC5};
DE AltName: Full=Protein phosphatase 1 regulatory subunit 39;
DE AltName: Full=RING finger protein 158;
DE AltName: Full=RING-type E3 ubiquitin transferase SH3RF2 {ECO:0000305};
DE AltName: Full=SH3 domain-containing RING finger protein 2;
GN Name=Sh3rf2; Synonyms=Posh3, Ppp1r39, Rnf158;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cecum, Head, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP STRUCTURE BY NMR OF 385-441.
RG RIKEN structural genomics initiative (RSGI);
RT "solution structure of the SH3 domain of the mouse hypothetical protein
RT SH3RF2.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Has E3 ubiquitin-protein ligase activity. Acts as an anti-
CC apoptotic regulator of the JNK pathway by ubiquitinating and promoting
CC the degradation of SH3RF1, a scaffold protein that is required for pro-
CC apoptotic JNK activation. Facilitates TNF-alpha-mediated recruitment of
CC adapter proteins TRADD and RIPK1 to TNFRSF1A and regulates PAK4 protein
CC stability via inhibition of its ubiquitin-mediated proteasomal
CC degradation. Inhibits PPP1CA phosphatase activity (By similarity).
CC {ECO:0000250|UniProtKB:Q8TEC5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q8TEC5};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with FASLG and PPP1CA. Interacts with PAK4 and
CC TNFRSF1A. Interacts with DLK1, MAP3K10, MAPK8IP1/JIP1, MAPK8IP2/JIP2
CC and MAPK8IP3/JIP3. Interacts with RAC1 (both active GTP- or inactive
CC GDP-bound forms). {ECO:0000250|UniProtKB:Q498M5,
CC ECO:0000250|UniProtKB:Q8TEC5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TEC5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BZT2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BZT2-2; Sequence=VSP_022060;
CC -!- DOMAIN: The RING finger domain is required for ubiquitin ligase
CC activity and autoubiquitination. {ECO:0000250|UniProtKB:Q8TEC5}.
CC -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q8TEC5}.
CC -!- SIMILARITY: Belongs to the SH3RF family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK028153; BAC25780.1; -; mRNA.
DR EMBL; AK029168; BAC26334.1; -; mRNA.
DR EMBL; AK033601; BAC28382.1; -; mRNA.
DR EMBL; BC048400; AAH48400.1; -; mRNA.
DR EMBL; BC137955; AAI37956.1; -; mRNA.
DR EMBL; BC145060; AAI45061.1; -; mRNA.
DR CCDS; CCDS29210.1; -. [Q8BZT2-2]
DR CCDS; CCDS50265.1; -. [Q8BZT2-1]
DR RefSeq; NP_001139771.1; NM_001146299.1. [Q8BZT2-1]
DR RefSeq; NP_766554.2; NM_172966.3. [Q8BZT2-2]
DR RefSeq; XP_006526018.1; XM_006525955.2. [Q8BZT2-1]
DR RefSeq; XP_006526019.1; XM_006525956.3.
DR PDB; 2CUC; NMR; -; A=385-441.
DR PDB; 2DJQ; NMR; -; A=128-182.
DR PDBsum; 2CUC; -.
DR PDBsum; 2DJQ; -.
DR AlphaFoldDB; Q8BZT2; -.
DR SMR; Q8BZT2; -.
DR STRING; 10090.ENSMUSP00000071896; -.
DR iPTMnet; Q8BZT2; -.
DR PhosphoSitePlus; Q8BZT2; -.
DR MaxQB; Q8BZT2; -.
DR PaxDb; Q8BZT2; -.
DR PRIDE; Q8BZT2; -.
DR ProteomicsDB; 257221; -. [Q8BZT2-1]
DR ProteomicsDB; 257222; -. [Q8BZT2-2]
DR Antibodypedia; 27503; 141 antibodies from 26 providers.
DR DNASU; 269016; -.
DR Ensembl; ENSMUST00000072008; ENSMUSP00000071896; ENSMUSG00000057719. [Q8BZT2-1]
DR Ensembl; ENSMUST00000074679; ENSMUSP00000074247; ENSMUSG00000057719. [Q8BZT2-2]
DR GeneID; 269016; -.
DR KEGG; mmu:269016; -.
DR UCSC; uc008etk.2; mouse. [Q8BZT2-2]
DR UCSC; uc008etl.2; mouse. [Q8BZT2-1]
DR CTD; 153769; -.
DR MGI; MGI:2444628; Sh3rf2.
DR VEuPathDB; HostDB:ENSMUSG00000057719; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160067; -.
DR HOGENOM; CLU_015769_2_0_1; -.
DR InParanoid; Q8BZT2; -.
DR OMA; SVITQHM; -.
DR OrthoDB; 291531at2759; -.
DR PhylomeDB; Q8BZT2; -.
DR TreeFam; TF105571; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 269016; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Sh3rf2; mouse.
DR EvolutionaryTrace; Q8BZT2; -.
DR PRO; PR:Q8BZT2; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8BZT2; protein.
DR Bgee; ENSMUSG00000057719; Expressed in caudate-putamen and 99 other tissues.
DR Genevisible; Q8BZT2; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISS:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd11929; SH3_SH3RF2_1; 1.
DR CDD; cd11932; SH3_SH3RF2_2; 1.
DR CDD; cd11784; SH3_SH3RF2_3; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028511; SH3RF2.
DR InterPro; IPR035792; SH3RF2_SH3_1.
DR InterPro; IPR035794; SH3RF2_SH3_2.
DR InterPro; IPR035822; SH3RF2_SH3_3.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14167:SF60; PTHR14167:SF60; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50002; SH3; 3.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Metal-binding; Nucleus; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome; Repeat; SH3 domain;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..735
FT /note="E3 ubiquitin-protein ligase SH3RF2"
FT /id="PRO_0000269513"
FT DOMAIN 125..184
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 187..252
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 382..443
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 12..53
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 262..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..465
FT /note="Interaction with PAK4"
FT /evidence="ECO:0000250|UniProtKB:Q8TEC5"
FT REGION 497..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..652
FT /note="Interaction with PPP1CA"
FT /evidence="ECO:0000250"
FT COMPBIAS 266..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q498M5"
FT VAR_SEQ 217..248
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022060"
FT CONFLICT 127
FT /note="V -> G (in Ref. 1; BAC26334)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="E -> Q (in Ref. 1; BAC25780)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="S -> C (in Ref. 1; BAC28382)"
FT /evidence="ECO:0000305"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:2DJQ"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:2DJQ"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:2DJQ"
FT STRAND 170..180
FT /evidence="ECO:0007829|PDB:2DJQ"
FT STRAND 408..416
FT /evidence="ECO:0007829|PDB:2CUC"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:2CUC"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:2CUC"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:2CUC"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:2CUC"
SQ SEQUENCE 735 AA; 80066 MW; FAE1D97780289FCC CRC64;
MDDLTLLDLL ECPVCFEKLD VTAKVLPCQH TFCKPCLQRI FKAHKELRCP ECRTLVFCSI
EALPANLLLV RLLDGVRSGQ SSWKGGSFRR PRILTLQDNR KAKSSPRSLQ ASPFRLVPSV
RIHMDGVPRA KALCNYRGKN PGDLKFNKGD VILLRRQLDE NWYQGEINGV SGIFPASSVE
VIKQLPQPPP LCRALYNFDL RDKDKSENQD CLTFLKDDVI TVISRVDENW AEGKLGDKVG
IFPILFVEPN VSARHLLENK GHQLSRTRHL SLMSSPSRGK ATNTSSLRKS PGSRRKGSGQ
FSMTTALNTL NRTVHSPEGH QMVEISTPML ISSNSPSVLT QHGDKADFPT SSTGQVSSSQ
PAPASPGHST AMVSVPSSQQ HLSNNMFVAL HTYSAHRPEE LDLQKGEGIR VLGKYQDGWL
KGLSLLTGRT GIFPSDYVIP VFSSTARKTS SFPDSRSPTV CTTWALSTSS VSSQGSFAEG
DPRQSGPFKS VFVPTAVVNP SRSTPGPGSS GQGSLRKVRS SMRKNGSLQR PVQSGIPTFM
VGSLRCSPTM VIRPQRFQFY PPQGMTPSPT PIMVEMGSKS IYTGEPALTC INRGSKTRIH
SAGNSIIMEG KETPIKSEPP PKPPASAPPS ILVKPENSKN GTEKQVKTVR FQNYSPPPTK
HSASSPTSGK HDHPATLKGS QHEAVSSGGE MTILFAHRSG CHSGQQTDLR RKSAFGKTMP
LLSTASATQT LFPSK
