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Protein

SH3 domain-binding glutamic acid-rich-like protein 3

Gene

SH3BGRL3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Could act as a modulator of glutaredoxin biological activity.

GO - Molecular functioni

  • electron carrier activity Source: InterPro
  • GTPase activator activity Source: UniProtKB
  • protein disulfide oxidoreductase activity Source: InterPro
  • semaphorin receptor binding Source: UniProtKB

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • positive regulation of GTPase activity Source: UniProtKB
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of actin filament depolymerization Source: UniProtKB
  • regulation of blood vessel endothelial cell migration Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
SH3 domain-binding glutamic acid-rich-like protein 3
Alternative name(s):
SH3 domain-binding protein 1
Short name:
SH3BP-1
Gene namesi
ORF Names:P1725
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:15568. SH3BGRL3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37979.

Polymorphism and mutation databases

BioMutaiSH3BGRL3.
DMDMi24638222.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 9392SH3 domain-binding glutamic acid-rich-like protein 3PRO_0000220749Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9H299.
MaxQBiQ9H299.
PaxDbiQ9H299.
PeptideAtlasiQ9H299.
PRIDEiQ9H299.
TopDownProteomicsiQ9H299.

PTM databases

iPTMnetiQ9H299.
PhosphoSiteiQ9H299.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9H299.
CleanExiHS_SH3BGRL3.
ExpressionAtlasiQ9H299. baseline and differential.
GenevisibleiQ9H299. HS.

Organism-specific databases

HPAiHPA030848.

Interactioni

GO - Molecular functioni

  • semaphorin receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi123644. 5 interactions.
IntActiQ9H299. 1 interaction.
MINTiMINT-1547823.
STRINGi9606.ENSP00000270792.

Structurei

Secondary structure

1
93
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Beta strandi14 – 163Combined sources
Helixi17 – 3014Combined sources
Beta strandi36 – 394Combined sources
Helixi44 – 5310Combined sources
Beta strandi63 – 7311Combined sources
Helixi74 – 818Combined sources
Turni82 – 843Combined sources
Helixi86 – 905Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SJ6NMR-A1-93[»]
ProteinModelPortaliQ9H299.
SMRiQ9H299. Positions 1-93.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H299.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 9392GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the SH3BGR family.Curated
Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4023. Eukaryota.
ENOG4111N7M. LUCA.
GeneTreeiENSGT00440000039098.
HOGENOMiHOG000095212.
HOVERGENiHBG054781.
InParanoidiQ9H299.
OrthoDBiEOG7GTT63.
PhylomeDBiQ9H299.
TreeFamiTF105574.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR006993. Glut_rich_SH3-bd.
IPR002109. Glutaredoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF04908. SH3BGR. 1 hit.
[Graphical view]
PIRSFiPIRSF008142. SH3-bind_E-rich_L. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9H299-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGLRVYSTS VTGSREIKSQ QSEVTRILDG KRIQYQLVDI SQDNALRDEM
60 70 80 90
RALAGNPKAT PPQIVNGDQY CGDYELFVEA VEQNTLQEFL KLA
Length:93
Mass (Da):10,438
Last modified:March 1, 2001 - v1
Checksum:iC30BE3251D5B82CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297915 mRNA. Translation: CAC35770.1.
AF247790 mRNA. Translation: AAL95695.1.
AF304163 mRNA. Translation: AAG41412.1.
AL451139 Genomic DNA. Translation: CAI15827.1.
BC030135 mRNA. Translation: AAH30135.1.
CCDSiCCDS278.1.
PIRiJC7711.
RefSeqiNP_112576.1. NM_031286.3.
UniGeneiHs.109051.

Genome annotation databases

EnsembliENST00000270792; ENSP00000270792; ENSG00000142669.
GeneIDi83442.
KEGGihsa:83442.
UCSCiuc001blu.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297915 mRNA. Translation: CAC35770.1.
AF247790 mRNA. Translation: AAL95695.1.
AF304163 mRNA. Translation: AAG41412.1.
AL451139 Genomic DNA. Translation: CAI15827.1.
BC030135 mRNA. Translation: AAH30135.1.
CCDSiCCDS278.1.
PIRiJC7711.
RefSeqiNP_112576.1. NM_031286.3.
UniGeneiHs.109051.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SJ6NMR-A1-93[»]
ProteinModelPortaliQ9H299.
SMRiQ9H299. Positions 1-93.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123644. 5 interactions.
IntActiQ9H299. 1 interaction.
MINTiMINT-1547823.
STRINGi9606.ENSP00000270792.

PTM databases

iPTMnetiQ9H299.
PhosphoSiteiQ9H299.

Polymorphism and mutation databases

BioMutaiSH3BGRL3.
DMDMi24638222.

Proteomic databases

EPDiQ9H299.
MaxQBiQ9H299.
PaxDbiQ9H299.
PeptideAtlasiQ9H299.
PRIDEiQ9H299.
TopDownProteomicsiQ9H299.

Protocols and materials databases

DNASUi83442.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000270792; ENSP00000270792; ENSG00000142669.
GeneIDi83442.
KEGGihsa:83442.
UCSCiuc001blu.4. human.

Organism-specific databases

CTDi83442.
GeneCardsiSH3BGRL3.
HGNCiHGNC:15568. SH3BGRL3.
HPAiHPA030848.
MIMi615679. gene.
neXtProtiNX_Q9H299.
PharmGKBiPA37979.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4023. Eukaryota.
ENOG4111N7M. LUCA.
GeneTreeiENSGT00440000039098.
HOGENOMiHOG000095212.
HOVERGENiHBG054781.
InParanoidiQ9H299.
OrthoDBiEOG7GTT63.
PhylomeDBiQ9H299.
TreeFamiTF105574.

Miscellaneous databases

ChiTaRSiSH3BGRL3. human.
EvolutionaryTraceiQ9H299.
GeneWikiiSH3BGRL3.
GenomeRNAii83442.
PROiQ9H299.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H299.
CleanExiHS_SH3BGRL3.
ExpressionAtlasiQ9H299. baseline and differential.
GenevisibleiQ9H299. HS.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR006993. Glut_rich_SH3-bd.
IPR002109. Glutaredoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF04908. SH3BGR. 1 hit.
[Graphical view]
PIRSFiPIRSF008142. SH3-bind_E-rich_L. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel human homologue of the SH3BGR gene encodes a small protein similar to glutaredoxin 1 of Escherichia coli."
    Mazzocco M., Arrigo P., Egeo A., Maffei M., Vergano A., Di Lisi R., Ghiotto F., Ciccone E., Cinti R., Ravazzolo R., Scartezzini P.
    Biochem. Biophys. Res. Commun. 285:540-545(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Pancreas.
  2. "Novel human SH3 domain binding protein SH3BP-1."
    Li N., Wan T., Zhang W., Cao X.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "A catalog of genes in the human dermal papilla cells as identified by expressed sequence tags."
    Seo J.M., Kim M.K., Kim Y.H., Lee H.M., Hwang S.Y., Farooq M., Im S.U., Chung J.E., Kim J.C.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Hair follicle dermal papilla.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "NMR structure and regulated expression in APL cell of human SH3BGRL3."
    Xu C., Zheng P., Shen S., Xu Y., Wei L., Gao H., Wang S., Zhu C., Tang Y., Wu J., Zhang Q., Shi Y.
    FEBS Lett. 579:2788-2794(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSH3L3_HUMAN
AccessioniPrimary (citable) accession number: Q9H299
Secondary accession number(s): Q5T122
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.