SH3R3_HUMAN
ID SH3R3_HUMAN Reviewed; 882 AA.
AC Q8TEJ3; A0SDZ7; A8MPR1; Q8NDU1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=E3 ubiquitin-protein ligase SH3RF3;
DE EC=2.3.2.27 {ECO:0000269|PubMed:20696164};
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 {ECO:0000303|PubMed:20696164}, SH3MD4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-314, AND INTERACTION WITH PAK2.
RX PubMed=16374509; DOI=10.1038/sj.embor.7400596;
RA Kaerkkaeinen S., Hiipakka M., Wang J.-H., Kleino I., Vaehae-Jaakkola M.,
RA Renkema G.H., Liss M., Wagner R., Saksela K.;
RT "Identification of preferred protein interactions by phage-display of the
RT human Src homology-3 proteome.";
RL EMBO Rep. 7:186-191(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 310-882.
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 672-882.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400 AND SER-797, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, CATALYTIC ACTIVITY,
RP AUTOUBIQUITINATION, INTERACTION WITH RAC1, AND MUTAGENESIS OF CYS-73;
RP HIS-75; ILE-403; SER-404 AND PRO-406.
RX PubMed=20696164; DOI=10.1016/j.febslet.2010.07.060;
RA Kaerkkaeinen S., van der Linden M., Renkema G.H.;
RT "POSH2 is a RING finger E3 ligase with Rac1 binding activity through a
RT partial CRIB domain.";
RL FEBS Lett. 584:3867-3872(2010).
CC -!- FUNCTION: Has E3 ubiquitin-protein ligase activity.
CC {ECO:0000269|PubMed:20696164}.
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:0000269|PubMed:20696164};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via SH3 domain 3) with PAK2 (PubMed:16374509).
CC Interacts with RAC1 (GTP-bound form) (PubMed:20696164).
CC {ECO:0000269|PubMed:16374509, ECO:0000269|PubMed:20696164}.
CC -!- INTERACTION:
CC Q8TEJ3; Q13177: PAK2; NbExp=2; IntAct=EBI-7975674, EBI-1045887;
CC Q8TEJ3; P63000: RAC1; NbExp=6; IntAct=EBI-7975674, EBI-413628;
CC -!- DOMAIN: The RING finger domain is required for ubiquitin ligase
CC activity and autoubiquitination. {ECO:0000269|PubMed:20696164}.
CC -!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:20696164}.
CC -!- SIMILARITY: Belongs to the SH3RF family. {ECO:0000305}.
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DR EMBL; AC010906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ307286; ABC25188.1; -; mRNA.
DR EMBL; AK074131; BAB84957.1; -; mRNA.
DR EMBL; AL831825; CAD38539.1; -; mRNA.
DR CCDS; CCDS74557.1; -.
DR RefSeq; NP_001092759.1; NM_001099289.2.
DR AlphaFoldDB; Q8TEJ3; -.
DR SMR; Q8TEJ3; -.
DR BioGRID; 131307; 48.
DR DIP; DIP-43763N; -.
DR IntAct; Q8TEJ3; 9.
DR MINT; Q8TEJ3; -.
DR STRING; 9606.ENSP00000309186; -.
DR iPTMnet; Q8TEJ3; -.
DR PhosphoSitePlus; Q8TEJ3; -.
DR BioMuta; SH3RF3; -.
DR DMDM; 146325718; -.
DR EPD; Q8TEJ3; -.
DR jPOST; Q8TEJ3; -.
DR MassIVE; Q8TEJ3; -.
DR MaxQB; Q8TEJ3; -.
DR PaxDb; Q8TEJ3; -.
DR PeptideAtlas; Q8TEJ3; -.
DR PRIDE; Q8TEJ3; -.
DR ProteomicsDB; 74467; -.
DR ABCD; Q8TEJ3; 1 sequenced antibody.
DR Antibodypedia; 64583; 85 antibodies from 18 providers.
DR DNASU; 344558; -.
DR Ensembl; ENST00000309415.8; ENSP00000309186.6; ENSG00000172985.11.
DR GeneID; 344558; -.
DR KEGG; hsa:344558; -.
DR MANE-Select; ENST00000309415.8; ENSP00000309186.6; NM_001099289.3; NP_001092759.1.
DR UCSC; uc010ywt.2; human.
DR CTD; 344558; -.
DR DisGeNET; 344558; -.
DR GeneCards; SH3RF3; -.
DR HGNC; HGNC:24699; SH3RF3.
DR HPA; ENSG00000172985; Low tissue specificity.
DR MIM; 618933; gene.
DR neXtProt; NX_Q8TEJ3; -.
DR OpenTargets; ENSG00000172985; -.
DR PharmGKB; PA162403291; -.
DR VEuPathDB; HostDB:ENSG00000172985; -.
DR eggNOG; KOG2177; Eukaryota.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00940000160405; -.
DR HOGENOM; CLU_015769_1_0_1; -.
DR InParanoid; Q8TEJ3; -.
DR OMA; TTMHPGS; -.
DR OrthoDB; 291531at2759; -.
DR PhylomeDB; Q8TEJ3; -.
DR TreeFam; TF105571; -.
DR PathwayCommons; Q8TEJ3; -.
DR SignaLink; Q8TEJ3; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 344558; 6 hits in 267 CRISPR screens.
DR GenomeRNAi; 344558; -.
DR Pharos; Q8TEJ3; Tbio.
DR PRO; PR:Q8TEJ3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8TEJ3; protein.
DR Bgee; ENSG00000172985; Expressed in pancreatic ductal cell and 166 other tissues.
DR Genevisible; Q8TEJ3; HS.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP: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; IMP: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 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 Metal-binding; Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..882
FT /note="E3 ubiquitin-protein ligase SH3RF3"
FT /id="PRO_0000284883"
FT DOMAIN 194..253
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 256..319
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 464..525
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 823..882
FT /note="SH3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 57..98
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 18..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..439
FT /note="Interaction with RAC1"
FT /evidence="ECO:0000269|PubMed:20696164"
FT REGION 433..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648"
FT MUTAGEN 73
FT /note="C->A: Significant reduction in autoubiquitination;
FT when associated with A-75."
FT /evidence="ECO:0000269|PubMed:20696164"
FT MUTAGEN 75
FT /note="H->A: Significant reduction in autoubiquitination;
FT when associated with A-73."
FT /evidence="ECO:0000269|PubMed:20696164"
FT MUTAGEN 403
FT /note="I->N: Significant loss of interaction with RAC1;
FT alone or when associated with P-404 and A-406."
FT /evidence="ECO:0000269|PubMed:20696164"
FT MUTAGEN 404
FT /note="S->P: Reduced JNK activation. Significant loss of
FT interaction with RAC1; alone or when associated with N-403
FT and A-406."
FT /evidence="ECO:0000269|PubMed:20696164"
FT MUTAGEN 406
FT /note="P->A: Significant loss of interaction with RAC1;
FT when associated with N-403 and P-404."
FT /evidence="ECO:0000269|PubMed:20696164"
SQ SEQUENCE 882 AA; 92776 MW; 07DF961AF2C80A08 CRC64;
MLLGASWLCA SKAAAAAAQS EGDEDRPGER RRRRAAATAA GAGEDMDESS LLDLLECSVC
LERLDTTAKV LPCQHTFCRR CLESIVCSRH ELRCPECRIL VGCGVDELPA NILLVRLLDG
IRQRPRAGTS PGGSPPARPI PGQSAAPTLA GGGGGAAGST PGSPVFLSAA AGSTAGSLRE
LATSRTAPAA KNPCLLPYGK ALYSYEGKEP GDLKFNKGDI IVLRRKVDEQ WYHGELHGTQ
GFLPASYIQC IQPLPHAPPQ GKALYDFEMK DKDQDKDCLT FTKDEILTVL RRVDENWAEG
MLGDKIGIFP LLYVELNDSA KQLIEMDKPC PAAASSCNAS LPSDSGAVAS VAPSPTLSSS
GAVSAFQRRV DGKKNTKKRH SFTALSVTHR SSQAASHRHS MEISAPVLIS SSDPRAAARI
GDLAHLSCAA PTQDVSSSAG STPTAVPRAA SVSGEQGTPP KVQLPLNVYL ALYAYKPQKS
DELELHKGEM YRVLEKCQDG WFKGASLRTG VSGVFPGNYV TPVSRVPAGG AGPPRNNVVG
GSPLAKGITT TMHPGSGSLS SLATATRPAL PITTPQAHAQ HPTASPPTGS CLRHSAQPTA
SQARSTISTA AHSAAQAQDR PTATVSPLRT QNSPSRLPAT SLRPHSVVSP QHSHQPPVQM
CPRPAIPLTS AASAITPPNV SAANLNGEAG GGPIGVLSTS SPTNTGCKLD EKKSEKKEKK
SGLLKLLAGA STKKKSRSPP SVSPTHDPQV AVDALLQGAV GPEVSSLSIH GRAGSCPIES
EMQGAMGMEP LHRKAGSLDL NFTSPSRQAP LSMAAIRPEP KLLPRERYRV VVSYPPQSEA
EIELKEGDIV FVHKKREDGW YKGTLQRNGR TGLFPGSFVE SF
