SH3L1_HUMAN
ID SH3L1_HUMAN Reviewed; 114 AA.
AC O75368; Q3SYL1; Q5JT50; Q6FIE8; Q9H0N8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=SH3 domain-binding glutamic acid-rich-like protein;
GN Name=SH3BGRL;
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].
RC TISSUE=Brain;
RX PubMed=9642120; DOI=10.1006/bbrc.1998.8763;
RA Egeo A., Mazzocco M., Arrigo P., Vidal-Taboada J.M., Oliva R., Pirola B.,
RA Giglio S., Rasore-Quartino A., Scartezzini P.;
RT "Identification and characterization of a new human gene encoding a small
RT protein with high homology to the proline-rich region of the SH3BGR gene.";
RL Biochem. Biophys. Res. Commun. 247:302-306(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and PNS;
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 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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-114.
RX PubMed=16080146; DOI=10.1002/prot.20523;
RA Yin L., Xiang Y., Zhu D.Y., Yan N., Huang R.H., Zhang Y., Wang D.C.;
RT "Crystal structure of human SH3BGRL protein: the first structure of the
RT human SH3BGR family representing a novel class of thioredoxin fold
RT proteins.";
RL Proteins 61:213-216(2005).
RN [8]
RP STRUCTURE BY NMR OF 1-108.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domain-binding glutamic acid-rich-like
RT protein.";
RL Submitted (APR-2005) to the PDB data bank.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
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; AF042081; AAC27445.1; -; mRNA.
DR EMBL; AL136718; CAB66652.1; -; mRNA.
DR EMBL; CR533478; CAG38509.1; -; mRNA.
DR EMBL; AL357115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016709; AAH16709.1; -; mRNA.
DR EMBL; BC103762; AAI03763.1; -; mRNA.
DR CCDS; CCDS14449.1; -.
DR PIR; JE0178; JE0178.
DR RefSeq; NP_003013.1; NM_003022.2.
DR PDB; 1U6T; X-ray; 1.90 A; A=2-114.
DR PDB; 1WRY; NMR; -; A=1-108.
DR PDBsum; 1U6T; -.
DR PDBsum; 1WRY; -.
DR AlphaFoldDB; O75368; -.
DR SMR; O75368; -.
DR BioGRID; 112349; 132.
DR IntAct; O75368; 86.
DR MINT; O75368; -.
DR STRING; 9606.ENSP00000362308; -.
DR iPTMnet; O75368; -.
DR PhosphoSitePlus; O75368; -.
DR BioMuta; SH3BGRL; -.
DR DOSAC-COBS-2DPAGE; O75368; -.
DR OGP; O75368; -.
DR REPRODUCTION-2DPAGE; O75368; -.
DR SWISS-2DPAGE; O75368; -.
DR CPTAC; CPTAC-584; -.
DR CPTAC; CPTAC-585; -.
DR EPD; O75368; -.
DR jPOST; O75368; -.
DR MassIVE; O75368; -.
DR PaxDb; O75368; -.
DR PeptideAtlas; O75368; -.
DR PRIDE; O75368; -.
DR ProteomicsDB; 49937; -.
DR TopDownProteomics; O75368; -.
DR Antibodypedia; 28352; 198 antibodies from 27 providers.
DR DNASU; 6451; -.
DR Ensembl; ENST00000373212.6; ENSP00000362308.5; ENSG00000131171.13.
DR GeneID; 6451; -.
DR KEGG; hsa:6451; -.
DR MANE-Select; ENST00000373212.6; ENSP00000362308.5; NM_003022.3; NP_003013.1.
DR CTD; 6451; -.
DR DisGeNET; 6451; -.
DR GeneCards; SH3BGRL; -.
DR HGNC; HGNC:10823; SH3BGRL.
DR HPA; ENSG00000131171; Low tissue specificity.
DR MIM; 300190; gene.
DR neXtProt; NX_O75368; -.
DR OpenTargets; ENSG00000131171; -.
DR PharmGKB; PA35731; -.
DR VEuPathDB; HostDB:ENSG00000131171; -.
DR eggNOG; KOG4023; Eukaryota.
DR GeneTree; ENSGT00940000156017; -.
DR HOGENOM; CLU_084862_3_0_1; -.
DR InParanoid; O75368; -.
DR OMA; NEKEFMQ; -.
DR OrthoDB; 1508713at2759; -.
DR PhylomeDB; O75368; -.
DR TreeFam; TF105574; -.
DR PathwayCommons; O75368; -.
DR SignaLink; O75368; -.
DR BioGRID-ORCS; 6451; 18 hits in 702 CRISPR screens.
DR ChiTaRS; SH3BGRL; human.
DR EvolutionaryTrace; O75368; -.
DR GeneWiki; SH3BGRL; -.
DR GenomeRNAi; 6451; -.
DR Pharos; O75368; Tbio.
DR PRO; PR:O75368; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O75368; protein.
DR Bgee; ENSG00000131171; Expressed in seminal vesicle and 213 other tissues.
DR ExpressionAtlas; O75368; baseline and differential.
DR Genevisible; O75368; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; SH3-binding.
FT CHAIN 1..114
FT /note="SH3 domain-binding glutamic acid-rich-like protein"
FT /id="PRO_0000220745"
FT MOTIF 61..67
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT CONFLICT 35
FT /note="E -> K (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="Q -> R (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1U6T"
FT HELIX 14..29
FT /evidence="ECO:0007829|PDB:1U6T"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1U6T"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:1U6T"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1U6T"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1U6T"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1U6T"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1U6T"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:1U6T"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:1U6T"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:1U6T"
SQ SEQUENCE 114 AA; 12774 MW; D72AC2A095F1AA8B CRC64;
MVIRVYIASS SGSTAIKKKQ QDVLGFLEAN KIGFEEKDIA ANEENRKWMR ENVPENSRPA
TGYPLPPQIF NESQYRGDYD AFFEARENNA VYAFLGLTAP PGSKEAEVQA KQQA