SH3R3_MOUSE
ID SH3R3_MOUSE Reviewed; 878 AA.
AC Q8C120; Q3V0K8; Q3V0Q0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=E3 ubiquitin-protein ligase SH3RF3;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8TEJ3};
DE AltName: Full=Plenty of SH3s 2;
DE AltName: Full=SH3 domain-containing RING finger protein 3;
DE AltName: Full=SH3 multiple domains protein 4;
GN Name=Sh3rf3; Synonyms=Posh2, Sh3md4;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Head, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Has E3 ubiquitin-protein ligase activity.
CC {ECO:0000250|UniProtKB:Q8TEJ3}.
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:Q8TEJ3};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via SH3 domain 3) with PAK2. Interacts with RAC1
CC (GTP-bound form). {ECO:0000250|UniProtKB:Q8TEJ3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8C120-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C120-2; Sequence=VSP_024719;
CC Name=3;
CC IsoId=Q8C120-3; Sequence=VSP_024718, VSP_024720, VSP_024721,
CC VSP_024722, VSP_024723;
CC Name=4;
CC IsoId=Q8C120-4; Sequence=VSP_024724, VSP_024725;
CC -!- DOMAIN: The RING finger domain is required for ubiquitin ligase
CC activity and autoubiquitination. {ECO:0000250|UniProtKB:Q8TEJ3}.
CC -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q8TEJ3}.
CC -!- SIMILARITY: Belongs to the SH3RF family. {ECO:0000305}.
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DR EMBL; AC153367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK029202; BAC26346.1; -; mRNA.
DR EMBL; AK132983; BAE21454.1; -; mRNA.
DR EMBL; AK133071; BAE21496.1; -; mRNA.
DR EMBL; BC057304; AAH57304.1; -; mRNA.
DR CCDS; CCDS35906.2; -. [Q8C120-1]
DR RefSeq; NP_766376.2; NM_172788.3. [Q8C120-1]
DR AlphaFoldDB; Q8C120; -.
DR SMR; Q8C120; -.
DR STRING; 10090.ENSMUSP00000120938; -.
DR iPTMnet; Q8C120; -.
DR PhosphoSitePlus; Q8C120; -.
DR MaxQB; Q8C120; -.
DR PaxDb; Q8C120; -.
DR PRIDE; Q8C120; -.
DR ProteomicsDB; 257142; -. [Q8C120-1]
DR ProteomicsDB; 257143; -. [Q8C120-2]
DR ProteomicsDB; 257144; -. [Q8C120-3]
DR ProteomicsDB; 257145; -. [Q8C120-4]
DR Antibodypedia; 64583; 85 antibodies from 18 providers.
DR DNASU; 237353; -.
DR Ensembl; ENSMUST00000135526; ENSMUSP00000114368; ENSMUSG00000037990. [Q8C120-4]
DR Ensembl; ENSMUST00000153031; ENSMUSP00000120938; ENSMUSG00000037990. [Q8C120-1]
DR GeneID; 237353; -.
DR KEGG; mmu:237353; -.
DR UCSC; uc007fdj.2; mouse. [Q8C120-4]
DR UCSC; uc007fdk.2; mouse. [Q8C120-1]
DR UCSC; uc007fdl.1; mouse. [Q8C120-3]
DR CTD; 344558; -.
DR MGI; MGI:2444637; Sh3rf3.
DR VEuPathDB; HostDB:ENSMUSG00000037990; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160405; -.
DR HOGENOM; CLU_015769_3_1_1; -.
DR InParanoid; Q8C120; -.
DR OMA; TTMHPGS; -.
DR OrthoDB; 291531at2759; -.
DR PhylomeDB; Q8C120; -.
DR TreeFam; TF105571; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 237353; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Sh3rf3; mouse.
DR PRO; PR:Q8C120; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8C120; protein.
DR Bgee; ENSMUSG00000037990; Expressed in secondary oocyte and 83 other tissues.
DR Genevisible; Q8C120; MM.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:InterPro.
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; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd11925; SH3_SH3RF3_3; 1.
DR CDD; cd11785; SH3_SH3RF_C; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035816; SH3RF1/SH3RF3_SH3_4.
DR InterPro; IPR028502; SH3RF3.
DR InterPro; IPR035612; SH3RF3_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:SF62; PTHR14167:SF62; 2.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF14604; SH3_9; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 4.
DR SUPFAM; SSF50044; SSF50044; 4.
DR PROSITE; PS50002; SH3; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..878
FT /note="E3 ubiquitin-protein ligase SH3RF3"
FT /id="PRO_0000284884"
FT DOMAIN 187..246
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 249..312
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 458..519
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 819..878
FT /note="SH3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 52..93
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 19..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..433
FT /note="Interaction with RAC1"
FT /evidence="ECO:0000250|UniProtKB:Q8TEJ3"
FT REGION 574..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEJ3"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEJ3"
FT VAR_SEQ 1..415
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024718"
FT VAR_SEQ 1..261
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_024719"
FT VAR_SEQ 416..428
FT /note="GELAHLSCTVPTQ -> MDAPEKYTERATP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024720"
FT VAR_SEQ 429..438
FT /note="DSSSAGPVPT -> VIPRAGGLCP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024724"
FT VAR_SEQ 439..878
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024725"
FT VAR_SEQ 518
FT /note="S -> SRSPHPSHSGEVRVRLAQE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024721"
FT VAR_SEQ 712..741
FT /note="KEKKSGLLKLLAGASTKKKSRSPPSVSPTH -> VSGPSWANPEPGAGWLLG
FT PSHTLANGAENR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024722"
FT VAR_SEQ 742..878
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024723"
SQ SEQUENCE 878 AA; 93130 MW; A1B274FE31334F3A CRC64;
MLLGASWLCA SKAAATAARG EGEDRQGEQQ RGAQARTEED MDESSLLDLL ECSVCLERLD
TTAKVLPCQH TFCRRCLESI VCSRHELRCP ECRILVGCGV DELPANILLV RLLDGIRQRP
RTGASPGSSP PARPGPGTFS ALAGGAGGAT GSPPCSPVFL SAAAGSSTSS LCDVATNRSV
PVAKTLSQLP YAKALYSYEG KEPGDLKFNK GDIIILRRKV DENWYHGELQ GMHGFLPASY
IQCVRPLPQA LPQGKALYDF EMKDRDQDKD CLTFTKDEVL TVIRRVDDNW AEGMLGDKIG
IFPLLYVELN DSAKQLIEMD KLCPAATTAY NYDALLSSDP STVASVAPGP TLSSSGAVSA
FQRRVDSKKN AKKRHSFTAL SVTHKSSQAA SHRHSMEISA PVLISSSDPR AAARIGELAH
LSCTVPTQDS SSAGPVPTAL PRAAAVAGEQ GMSPKVQLPL NVYLALYAYK PQKNDELELR
KGEMYRVLEK CQDGWFKGAS LKTGVSGVFP GNYVTPVSRV PGGGAGLPWN NVLGGSPLAK
GMATIMHPGG GSLSSPATAA RSALPLTTLQ DHMQHPATSL PTGSCLRHSA QPTASQAGDT
TIPTATHASA QALDRPTATV SPLRTQTSPS RLPSTGLRPR SVASPQHGQQ SPAQMCPRPA
IPFTSAASAI TPPNVSAANL SGEVGGTPIS GLSTPSLINT GFKPDDKKNE KKEKKSGLLK
LLAGASTKKK SRSPPSVSPT HDPQSAMDTS LQGAMGPEVS PLTVHGRAGS CPIESEMQGA
IGLEPLHRKA GSLDLNFSLS PSRQATLSMA SIRPEPKPLP RERYRVVVSY PPQSEAEIEL
KEGDIVFVHK KHEDGWFKGT LQRNGRTGLF PGSFVESF
