Q06649 (3BP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SH3 domain-binding protein 2
Short name=3BP-2

Gene names

Name:	Sh3bp2
Synonyms:	3bp2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds differentially to the SH3 domains of certain proteins of signal transduction pathways. Binds to phosphatidylinositols; linking the hemopoietic tyrosine kinase fes to the cytoplasmic membrane in a phosphorylation dependent mechanism By similarity.
Post-translational modification	Phosphorylated. Phosphorylation at Tyr-446 may stimulate the activity of the LYN kinase. Ref.2
Sequence similarities	Contains 1 PH domain. Contains 1 SH2 domain.

Ontologies

Keywords
Domain	SH2 domain SH3-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TNKS2	Q9H2K2	6	EBI-5323518,EBI-4398527	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 559	559	SH3 domain-binding protein 2		PRO_0000064366
Regions
	Domain	26 – 130	105	PH
	Domain	455 – 553	99	SH2
	Motif	201 – 210	10	SH3-binding
	Compositional bias	205 – 212	8	Poly-Pro
	Compositional bias	236 – 240	5	Poly-Pro
Amino acid modifications
	Modified residue	174	1	Phosphotyrosine; by SYK Ref.2
	Modified residue	183	1	Phosphotyrosine; by SYK Ref.2
	Modified residue	277	1	Phosphoserine By similarity
	Modified residue	442	1	Phosphoserine Ref.3
	Modified residue	446	1	Phosphotyrosine; by SYK Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q06649 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: EDFE1F11B259646E	FASTA	559	62,208
	10 20 30 40 50 60 MAAEEMQWPV PMKAIGAQNL LTMPGGVAKA GYLHKKGGTQ LQLLKWPLRF VIIHKRCIYY 70 80 90 100 110 120 FKSSTSASPQ GAFSLSGYNR VMRAAEETTS NNVFPFKIIH ISKKHRTWFF SASSEDERKS 130 140 150 160 170 180 WMAFVRREIG HFHEKKELPL DTSDSSSDTD SFYGAVERPI DISLSSYPMD NEDYEHEDED 190 200 210 220 230 240 DSYLEPDSPG PMKLEDALTY PPAYPPPPVP VPRKPAFSDL PRAHSFTSKS PSPLLPPPPP 250 260 270 280 290 300 KRGLPDTGSA PEDAKDALGL RRVEPGLRVP ATPRRMSDPP MSNVPTVPNL RKHPCFRDSV 310 320 330 340 350 360 NPGLEPWTPG HGTSSVSSST TMAVATSRNC DKLKSFHLSS RGPPTSEPPP VPANKPKFLK 370 380 390 400 410 420 IAEEPSPREA AKFAPVPPVA PRPPVQKMPM PEATVRPAVL PRPENTPLPH LQRSPPDGQS 430 440 450 460 470 480 FRGFSFEKAR QPSQADTGEE DSDEDYEKVP LPNSVFVNTT ESCEVERLFK ATDPRGEPQD 490 500 510 520 530 540 GLYCIRNSST KSGKVLVVWD ESSNKVRNYR IFEKDSKFYL EGEVLFASVG SMVEHYHTHV 550 LPSHQSLLLR HPYGYAGPR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a ten-amino acid proline-rich SH3 binding site." Ren R., Mayer B.J., Cicchetti P., Baltimore D. Science 259:1157-1161(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Adaptor protein 3BP2 is a potential ligand of Src homology 2 and 3 domains of Lyn protein-tyrosine kinase." Maeno K., Sada K., Kyo S., Miah S.M., Kawauchi-Kamata K., Qu X., Shi Y., Yamamura H. J. Biol. Chem. 278:24912-24920(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-174; TYR-183 AND TYR-446.
[3]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L14543 mRNA. Translation: AAA37121.1.
IPI	IPI00331306.
PIR	I49444.
UniGene	Mm.5012.
3D structure databases
ProteinModelPortal	Q06649.
SMR	Q06649. Positions 25-122, 442-558.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q06649. 3 interactions.
PTM databases
PhosphoSite	Q06649.
Proteomic databases
PaxDb	Q06649.
PRIDE	Q06649.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:1346349. Sh3bp2.
Phylogenomic databases
eggNOG	NOG42035.
HOGENOM	HOG000190359.
HOVERGEN	HBG000016.
InParanoid	Q06649.
OrthoDB	EOG4SN1P6.
Gene expression databases
CleanEx	MM_SH3BP2.
Genevestigator	Q06649.
GermOnline	ENSMUSG00000054520. Mus musculus.
Family and domain databases
Gene3D	2.30.29.30. 1 hit. 3.30.505.10. 1 hit.
InterPro	IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. IPR000980. SH2. [Graphical view]
Pfam	PF00169. PH. 1 hit. PF00017. SH2. 1 hit. [Graphical view]
SMART	SM00233. PH. 1 hit. SM00252. SH2. 1 hit. [Graphical view]
PROSITE	PS50003. PH_DOMAIN. 1 hit. PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

3BP2_MOUSE

Accession

Primary (citable) accession number: Q06649

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program