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Protein

SH3 domain-binding glutamic acid-rich-like protein

Gene

SH3BGRL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • SH3/SH2 adaptor activity Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
SH3 domain-binding glutamic acid-rich-like protein
Gene namesi
Name:SH3BGRL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:10823. SH3BGRL.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35731.

Polymorphism and mutation databases

BioMutaiSH3BGRL.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 114114SH3 domain-binding glutamic acid-rich-like proteinPRO_0000220745Add
BLAST

Proteomic databases

EPDiO75368.
PaxDbiO75368.
PeptideAtlasiO75368.
PRIDEiO75368.
TopDownProteomicsiO75368.

2D gel databases

DOSAC-COBS-2DPAGEO75368.
OGPiO75368.
REPRODUCTION-2DPAGEO75368.
SWISS-2DPAGEO75368.

PTM databases

iPTMnetiO75368.
PhosphoSiteiO75368.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO75368.
CleanExiHS_SH3BGRL.
ExpressionAtlasiO75368. baseline and differential.
GenevisibleiO75368. HS.

Organism-specific databases

HPAiHPA051248.

Interactioni

GO - Molecular functioni

  • SH3/SH2 adaptor activity Source: ProtInc

Protein-protein interaction databases

BioGridi112349. 15 interactions.
IntActiO75368. 2 interactions.
MINTiMINT-1562247.
STRINGi9606.ENSP00000362308.

Structurei

Secondary structure

1
114
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi14 – 2916Combined sources
Beta strandi34 – 385Combined sources
Helixi43 – 5210Combined sources
Helixi55 – 573Combined sources
Beta strandi60 – 634Combined sources
Beta strandi68 – 714Combined sources
Beta strandi74 – 785Combined sources
Helixi79 – 879Combined sources
Helixi91 – 955Combined sources
Helixi104 – 11411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U6TX-ray1.90A2-114[»]
1WRYNMR-A1-108[»]
ProteinModelPortaliO75368.
SMRiO75368. Positions 2-114.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75368.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi61 – 677SH3-bindingSequence analysis

Sequence similaritiesi

Belongs to the SH3BGR family.Curated

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiKOG4023. Eukaryota.
ENOG4111N7M. LUCA.
HOGENOMiHOG000095212.
HOVERGENiHBG054781.
InParanoidiO75368.
OMAiEEKYCGN.
OrthoDBiEOG7GTT63.
PhylomeDBiO75368.
TreeFamiTF105574.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

O75368-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVIRVYIASS SGSTAIKKKQ QDVLGFLEAN KIGFEEKDIA ANEENRKWMR
60 70 80 90 100
ENVPENSRPA TGYPLPPQIF NESQYRGDYD AFFEARENNA VYAFLGLTAP
110
PGSKEAEVQA KQQA
Length:114
Mass (Da):12,774
Last modified:November 1, 1998 - v1
Checksum:iD72AC2A095F1AA8B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351E → K (PubMed:11230166).Curated
Sequence conflicti35 – 351E → K (Ref. 3) Curated
Sequence conflicti113 – 1131Q → R (PubMed:11230166).Curated
Sequence conflicti113 – 1131Q → R (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042081 mRNA. Translation: AAC27445.1.
AL136718 mRNA. Translation: CAB66652.1.
CR533478 mRNA. Translation: CAG38509.1.
AL357115 Genomic DNA. Translation: CAI39436.1.
BC016709 mRNA. Translation: AAH16709.1.
BC103762 mRNA. Translation: AAI03763.1.
CCDSiCCDS14449.1.
PIRiJE0178.
RefSeqiNP_003013.1. NM_003022.2.
UniGeneiHs.108029.

Genome annotation databases

EnsembliENST00000373212; ENSP00000362308; ENSG00000131171.
GeneIDi6451.
KEGGihsa:6451.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042081 mRNA. Translation: AAC27445.1.
AL136718 mRNA. Translation: CAB66652.1.
CR533478 mRNA. Translation: CAG38509.1.
AL357115 Genomic DNA. Translation: CAI39436.1.
BC016709 mRNA. Translation: AAH16709.1.
BC103762 mRNA. Translation: AAI03763.1.
CCDSiCCDS14449.1.
PIRiJE0178.
RefSeqiNP_003013.1. NM_003022.2.
UniGeneiHs.108029.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U6TX-ray1.90A2-114[»]
1WRYNMR-A1-108[»]
ProteinModelPortaliO75368.
SMRiO75368. Positions 2-114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112349. 15 interactions.
IntActiO75368. 2 interactions.
MINTiMINT-1562247.
STRINGi9606.ENSP00000362308.

PTM databases

iPTMnetiO75368.
PhosphoSiteiO75368.

Polymorphism and mutation databases

BioMutaiSH3BGRL.

2D gel databases

DOSAC-COBS-2DPAGEO75368.
OGPiO75368.
REPRODUCTION-2DPAGEO75368.
SWISS-2DPAGEO75368.

Proteomic databases

EPDiO75368.
PaxDbiO75368.
PeptideAtlasiO75368.
PRIDEiO75368.
TopDownProteomicsiO75368.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373212; ENSP00000362308; ENSG00000131171.
GeneIDi6451.
KEGGihsa:6451.

Organism-specific databases

CTDi6451.
GeneCardsiSH3BGRL.
HGNCiHGNC:10823. SH3BGRL.
HPAiHPA051248.
MIMi300190. gene.
neXtProtiNX_O75368.
PharmGKBiPA35731.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4023. Eukaryota.
ENOG4111N7M. LUCA.
HOGENOMiHOG000095212.
HOVERGENiHBG054781.
InParanoidiO75368.
OMAiEEKYCGN.
OrthoDBiEOG7GTT63.
PhylomeDBiO75368.
TreeFamiTF105574.

Miscellaneous databases

ChiTaRSiSH3BGRL. human.
EvolutionaryTraceiO75368.
GeneWikiiSH3BGRL.
GenomeRNAii6451.
PROiO75368.
SOURCEiSearch...

Gene expression databases

BgeeiO75368.
CleanExiHS_SH3BGRL.
ExpressionAtlasiO75368. baseline and differential.
GenevisibleiO75368. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a new human gene encoding a small protein with high homology to the proline-rich region of the SH3BGR gene."
    Egeo A., Mazzocco M., Arrigo P., Vidal-Taboada J.M., Oliva R., Pirola B., Giglio S., Rasore-Quartino A., Scartezzini P.
    Biochem. Biophys. Res. Commun. 247:302-306(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [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: Bone marrow and PNS.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Crystal structure of human SH3BGRL protein: the first structure of the human SH3BGR family representing a novel class of thioredoxin fold proteins."
    Yin L., Xiang Y., Zhu D.Y., Yan N., Huang R.H., Zhang Y., Wang D.C.
    Proteins 61:213-216(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-114.
  8. "Solution structure of the SH3 domain-binding glutamic acid-rich-like protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-108.

Entry informationi

Entry nameiSH3L1_HUMAN
AccessioniPrimary (citable) accession number: O75368
Secondary accession number(s): Q3SYL1
, Q5JT50, Q6FIE8, Q9H0N8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 141 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 X
    Human chromosome X: 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.