SH3L3_HUMAN
ID SH3L3_HUMAN Reviewed; 93 AA.
AC Q9H299; Q5T122;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=SH3 domain-binding glutamic acid-rich-like protein 3;
DE AltName: Full=SH3 domain-binding protein 1;
DE Short=SH3BP-1;
GN Name=SH3BGRL3; ORFNames=P1725;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=11444877; DOI=10.1006/bbrc.2001.5169;
RA Mazzocco M., Arrigo P., Egeo A., Maffei M., Vergano A., Di Lisi R.,
RA Ghiotto F., Ciccone E., Cinti R., Ravazzolo R., Scartezzini P.;
RT "A novel human homologue of the SH3BGR gene encodes a small protein similar
RT to glutaredoxin 1 of Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 285:540-545(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li N., Wan T., Zhang W., Cao X.;
RT "Novel human SH3 domain binding protein SH3BP-1.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hair follicle dermal papilla;
RA Seo J.M., Kim M.K., Kim Y.H., Lee H.M., Hwang S.Y., Farooq M., Im S.U.,
RA Chung J.E., Kim J.C.;
RT "A catalog of genes in the human dermal papilla cells as identified by
RT expressed sequence tags.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP STRUCTURE BY NMR, AND SUBCELLULAR LOCATION.
RX PubMed=15907482; DOI=10.1016/j.febslet.2005.04.011;
RA Xu C., Zheng P., Shen S., Xu Y., Wei L., Gao H., Wang S., Zhu C., Tang Y.,
RA Wu J., Zhang Q., Shi Y.;
RT "NMR structure and regulated expression in APL cell of human SH3BGRL3.";
RL FEBS Lett. 579:2788-2794(2005).
CC -!- FUNCTION: Could act as a modulator of glutaredoxin biological activity.
CC -!- INTERACTION:
CC Q9H299; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-5234893, EBI-742054;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11444877}.
CC -!- SIMILARITY: Belongs to the SH3BGR 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; AJ297915; CAC35770.1; -; mRNA.
DR EMBL; AF247790; AAL95695.1; -; mRNA.
DR EMBL; AF304163; AAG41412.1; -; mRNA.
DR EMBL; AL451139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030135; AAH30135.1; -; mRNA.
DR CCDS; CCDS278.1; -.
DR PIR; JC7711; JC7711.
DR RefSeq; NP_112576.1; NM_031286.3.
DR PDB; 1SJ6; NMR; -; A=1-93.
DR PDBsum; 1SJ6; -.
DR AlphaFoldDB; Q9H299; -.
DR BMRB; Q9H299; -.
DR SMR; Q9H299; -.
DR BioGRID; 123644; 48.
DR IntAct; Q9H299; 5.
DR MINT; Q9H299; -.
DR STRING; 9606.ENSP00000270792; -.
DR iPTMnet; Q9H299; -.
DR PhosphoSitePlus; Q9H299; -.
DR BioMuta; SH3BGRL3; -.
DR DMDM; 24638222; -.
DR EPD; Q9H299; -.
DR jPOST; Q9H299; -.
DR MassIVE; Q9H299; -.
DR MaxQB; Q9H299; -.
DR PaxDb; Q9H299; -.
DR PeptideAtlas; Q9H299; -.
DR PRIDE; Q9H299; -.
DR ProteomicsDB; 80514; -.
DR TopDownProteomics; Q9H299; -.
DR Antibodypedia; 30595; 145 antibodies from 25 providers.
DR DNASU; 83442; -.
DR Ensembl; ENST00000270792.10; ENSP00000270792.5; ENSG00000142669.15.
DR GeneID; 83442; -.
DR KEGG; hsa:83442; -.
DR MANE-Select; ENST00000270792.10; ENSP00000270792.5; NM_031286.4; NP_112576.1.
DR UCSC; uc001blu.4; human.
DR CTD; 83442; -.
DR DisGeNET; 83442; -.
DR GeneCards; SH3BGRL3; -.
DR HGNC; HGNC:15568; SH3BGRL3.
DR HPA; ENSG00000142669; Low tissue specificity.
DR MIM; 615679; gene.
DR neXtProt; NX_Q9H299; -.
DR OpenTargets; ENSG00000142669; -.
DR PharmGKB; PA37979; -.
DR VEuPathDB; HostDB:ENSG00000142669; -.
DR eggNOG; KOG4023; Eukaryota.
DR GeneTree; ENSGT00940000157260; -.
DR HOGENOM; CLU_084862_3_1_1; -.
DR InParanoid; Q9H299; -.
DR OMA; FFNEDQY; -.
DR OrthoDB; 1508713at2759; -.
DR PhylomeDB; Q9H299; -.
DR TreeFam; TF105574; -.
DR PathwayCommons; Q9H299; -.
DR SignaLink; Q9H299; -.
DR BioGRID-ORCS; 83442; 19 hits in 1076 CRISPR screens.
DR ChiTaRS; SH3BGRL3; human.
DR EvolutionaryTrace; Q9H299; -.
DR GeneWiki; SH3BGRL3; -.
DR GenomeRNAi; 83442; -.
DR Pharos; Q9H299; Tbio.
DR PRO; PR:Q9H299; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H299; protein.
DR Bgee; ENSG00000142669; Expressed in granulocyte and 193 other tissues.
DR ExpressionAtlas; Q9H299; baseline and differential.
DR Genevisible; Q9H299; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR CDD; cd03030; GRX_SH3BGR; 1.
DR InterPro; IPR006993; Glut_rich_SH3-bd.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF04908; SH3BGR; 1.
DR PIRSF; PIRSF008142; SH3-bind_E-rich_L; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..93
FT /note="SH3 domain-binding glutamic acid-rich-like protein
FT 3"
FT /id="PRO_0000220749"
FT DOMAIN 2..93
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:1SJ6"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1SJ6"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:1SJ6"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1SJ6"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:1SJ6"
FT STRAND 63..73
FT /evidence="ECO:0007829|PDB:1SJ6"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:1SJ6"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:1SJ6"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:1SJ6"
SQ SEQUENCE 93 AA; 10438 MW; C30BE3251D5B82CC CRC64;
MSGLRVYSTS VTGSREIKSQ QSEVTRILDG KRIQYQLVDI SQDNALRDEM RALAGNPKAT
PPQIVNGDQY CGDYELFVEA VEQNTLQEFL KLA
