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Protein

SH3 domain-binding glutamic acid-rich-like protein 2

Gene

SH3BGRL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Names & Taxonomyi

Protein namesi
Recommended name:
SH3 domain-binding glutamic acid-rich-like protein 2
Alternative name(s):
Fovea-associated SH3 domain-binding protein
Gene namesi
Name:SH3BGRL2
Synonyms:FASH3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:15567. SH3BGRL2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37978.

Polymorphism and mutation databases

BioMutaiSH3BGRL2.
DMDMi24638476.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 107107SH3 domain-binding glutamic acid-rich-like protein 2PRO_0000220747Add
BLAST

Proteomic databases

EPDiQ9UJC5.
MaxQBiQ9UJC5.
PaxDbiQ9UJC5.
PeptideAtlasiQ9UJC5.
PRIDEiQ9UJC5.

2D gel databases

UCD-2DPAGEQ9UJC5.

PTM databases

iPTMnetiQ9UJC5.
PhosphoSiteiQ9UJC5.

Expressioni

Tissue specificityi

Highly expressed in brain, placenta, liver and kidney. Expressed in retina.1 Publication

Gene expression databases

BgeeiQ9UJC5.
CleanExiHS_SH3BGRL2.
GenevisibleiQ9UJC5. HS.

Organism-specific databases

HPAiHPA047486.

Interactioni

Protein-protein interaction databases

BioGridi123733. 5 interactions.
IntActiQ9UJC5. 2 interactions.
STRINGi9606.ENSP00000358853.

Structurei

Secondary structure

1
107
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi14 – 2916Combined sources
Beta strandi34 – 385Combined sources
Turni39 – 413Combined sources
Helixi43 – 519Combined sources
Turni55 – 573Combined sources
Beta strandi60 – 634Combined sources
Beta strandi68 – 714Combined sources
Beta strandi74 – 785Combined sources
Helixi79 – 868Combined sources
Turni87 – 893Combined sources
Helixi91 – 955Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CT6NMR-A1-98[»]
ProteinModelPortaliQ9UJC5.
SMRiQ9UJC5. Positions 1-98.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UJC5.

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.
GeneTreeiENSGT00440000039098.
HOVERGENiHBG054781.
InParanoidiQ9UJC5.
OMAiIFNEDHY.
OrthoDBiEOG7GTT63.
PhylomeDBiQ9UJC5.
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.

Q9UJC5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVIRVFIASS SGFVAIKKKQ QDVVRFLEAN KIEFEEVDIT MSEEQRQWMY
60 70 80 90 100
KNVPPEKKPT QGNPLPPQIF NGDRYCGDYD SFFESKESNT VFSFLGLKPR

LASKAEP
Length:107
Mass (Da):12,326
Last modified:November 1, 2002 - v2
Checksum:iD160736103FA8635
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71I → V in AAH70059 (PubMed:15489334).Curated
Sequence conflicti39 – 391I → T in AAH40489 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297972 mRNA. Translation: CAC35771.1.
AF340151 mRNA. Translation: AAK37526.1.
AK311757 mRNA. Translation: BAG34700.1.
AL035700, AL451064 Genomic DNA. Translation: CAB55867.2.
AL451064, AL035700 Genomic DNA. Translation: CAH70932.1.
CH471051 Genomic DNA. Translation: EAW48703.1.
BC040489 mRNA. Translation: AAH40489.2.
BC052987 mRNA. Translation: AAH52987.2.
BC060799 mRNA. Translation: AAH60799.2.
BC070059 mRNA. Translation: AAH70059.2.
BC109043 mRNA. Translation: AAI09044.2.
BC109044 mRNA. Translation: AAI09045.2.
CCDSiCCDS4991.1.
RefSeqiNP_113657.1. NM_031469.3.
UniGeneiHs.302772.

Genome annotation databases

EnsembliENST00000369838; ENSP00000358853; ENSG00000198478.
GeneIDi83699.
KEGGihsa:83699.
UCSCiuc003piz.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297972 mRNA. Translation: CAC35771.1.
AF340151 mRNA. Translation: AAK37526.1.
AK311757 mRNA. Translation: BAG34700.1.
AL035700, AL451064 Genomic DNA. Translation: CAB55867.2.
AL451064, AL035700 Genomic DNA. Translation: CAH70932.1.
CH471051 Genomic DNA. Translation: EAW48703.1.
BC040489 mRNA. Translation: AAH40489.2.
BC052987 mRNA. Translation: AAH52987.2.
BC060799 mRNA. Translation: AAH60799.2.
BC070059 mRNA. Translation: AAH70059.2.
BC109043 mRNA. Translation: AAI09044.2.
BC109044 mRNA. Translation: AAI09045.2.
CCDSiCCDS4991.1.
RefSeqiNP_113657.1. NM_031469.3.
UniGeneiHs.302772.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CT6NMR-A1-98[»]
ProteinModelPortaliQ9UJC5.
SMRiQ9UJC5. Positions 1-98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123733. 5 interactions.
IntActiQ9UJC5. 2 interactions.
STRINGi9606.ENSP00000358853.

PTM databases

iPTMnetiQ9UJC5.
PhosphoSiteiQ9UJC5.

Polymorphism and mutation databases

BioMutaiSH3BGRL2.
DMDMi24638476.

2D gel databases

UCD-2DPAGEQ9UJC5.

Proteomic databases

EPDiQ9UJC5.
MaxQBiQ9UJC5.
PaxDbiQ9UJC5.
PeptideAtlasiQ9UJC5.
PRIDEiQ9UJC5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369838; ENSP00000358853; ENSG00000198478.
GeneIDi83699.
KEGGihsa:83699.
UCSCiuc003piz.2. human.

Organism-specific databases

CTDi83699.
GeneCardsiSH3BGRL2.
HGNCiHGNC:15567. SH3BGRL2.
HPAiHPA047486.
MIMi615678. gene.
neXtProtiNX_Q9UJC5.
PharmGKBiPA37978.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4023. Eukaryota.
ENOG4111N7M. LUCA.
GeneTreeiENSGT00440000039098.
HOVERGENiHBG054781.
InParanoidiQ9UJC5.
OMAiIFNEDHY.
OrthoDBiEOG7GTT63.
PhylomeDBiQ9UJC5.
TreeFamiTF105574.

Miscellaneous databases

EvolutionaryTraceiQ9UJC5.
GenomeRNAii83699.
PROiQ9UJC5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UJC5.
CleanExiHS_SH3BGRL2.
GenevisibleiQ9UJC5. 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. "The identification of a novel human homologue of the SH3 binding glutamic acid-rich (SH3BGR) gene establishes a new family of highly conserved small proteins related to Thioredoxin Superfamily."
    Mazzocco M., Maffei M., Egeo A., Vergano A., Arrigo P., Di Lisi R., Ghiotto F., Scartezzini P.
    Gene 291:233-239(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Characterization of a novel candidate gene, FASH3, expressed in the primate fovea and linked to the disease gene, ELOVL4, associated with Stargardt-like dominant progressive macular dystrophy."
    Bowes Rickman C., Yarovinsky T.O., McKay B.S., Stone E.M., Ritter R., Rickman D.W., Edwards A.O.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Brain, Eye and Placenta.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Solution structure of the SH3 domain-binding glutamic acid-rich-like protein 2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-98.

Entry informationi

Entry nameiSH3L2_HUMAN
AccessioniPrimary (citable) accession number: Q9UJC5
Secondary accession number(s): A8MQU2
, Q2VPC2, Q5VV96, Q6NSK8, Q6P9E8, Q7Z734, Q8IWD3, Q9BPY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 2002
Last modified: June 8, 2016
This is version 124 of the entry and version 2 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 6
    Human chromosome 6: 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.