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Q5EAD0 (BAIP2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Brain-specific angiogenesis inhibitor 1-associated protein 2

Short name=BAI-associated protein 2
Short name=BAI1-associated protein 2
Gene names
Name:BAIAP2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Participates in actin bundling when associated with EPS8, promoting filopodial protrusions By similarity.

Subunit structure

Homodimer. Interacts with CDC42 and RAC1 that have been activated by GTP binding. Interacts with ATN1, BAI1, DIAPH1, EPS8, SHANK1, SHANK2, SHANK3, TIAM1, WASF1 and WASF2. Interacts with ENAH after recruitment of CDC42 By similarity.

Subcellular location

Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity. Cell projectionfilopodium By similarity. Cell projectionruffle By similarity. Cytoplasmcytoskeleton By similarity. Note: Detected throughout the cytoplasm in the absence of specific binding partners. Detected in filopodia and close to membrane ruffles. Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites By similarity.

Domain

The IMD domain forms a coiled coil. The isolated domain can induce actin bundling and filopodia formation. In the absence of G-proteins intramolecular interaction between the IMD and the SH3 domain gives rise to an auto-inhibited state of the protein. Interaction of the IMD with RAC1 or CDC42 leads to activation By similarity.

The SH3 domain interacts with ATN1, BAI1, WASF1, WASF2, SHANK1, DIAPH1 and ENAH By similarity.

Post-translational modification

Phosphorylated on tyrosine residues by INSR in response to insulin treatment By similarity.

Sequence similarities

Contains 1 IMD (IRSp53/MIM homology) domain.

Contains 1 SH3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521Brain-specific angiogenesis inhibitor 1-associated protein 2
PRO_0000064814

Regions

Domain1 – 250250IMD
Domain375 – 43864SH3
Coiled coil132 – 15322 Potential

Amino acid modifications

Modified residue3241Phosphoserine By similarity
Modified residue3261Phosphoserine By similarity
Modified residue3411Phosphothreonine By similarity
Modified residue3471Phosphoserine By similarity
Modified residue3671Phosphoserine By similarity
Modified residue4551Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5EAD0 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 283D43FE6B9FD1D7

FASTA52157,566
        10         20         30         40         50         60 
MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK GYFDALVKMG 

        70         80         90        100        110        120 
ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE LLTQLEQKVE LDSRYLSAAL 

       130        140        150        160        170        180 
KKYQTEQRSK GDALDKCQAE LKKLRKKSQG SKNPQKYSDK ELQYIDAIGN KQGELESYVS 

       190        200        210        220        230        240 
DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPNKIPDRA 

       250        260        270        280        290        300 
VQLMQQMGNS NGSILPSGLS ASKSNLVISD PIPGAKPLPV PPELAPFVGR LSAQENAPVM 

       310        320        330        340        350        360 
NGVSGPDSED YNPWADRKAT QPKSTSPPQS QSKLSDSYSN TLPVRKSVAP KNSYATTENK 

       370        380        390        400        410        420 
TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG DLITLLVPEA RDGWHYGESE 

       430        440        450        460        470        480 
KTKMRGWFPF SYTRVLDNDG GDRLHMSLQQ GKSSSTGNLL DKEDLALPPP DYGTSSRAFP 

       490        500        510        520 
TQTAGAFKQR PYSVAVPAFS QGLDDYGARA VSSADVEVAR F 

« Hide

References

[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT020639 mRNA. Translation: AAX08656.1.
RefSeqNP_001017937.1. NM_001017937.1.
XP_005221080.1. XM_005221023.1.
UniGeneBt.17140.

3D structure databases

ProteinModelPortalQ5EAD0.
SMRQ5EAD0. Positions 1-248, 379-436.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5EAD0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000025350; ENSBTAP00000025350; ENSBTAG00000019044.
GeneID507837.
KEGGbta:507837.

Organism-specific databases

CTD10458.

Phylogenomic databases

eggNOGNOG71665.
GeneTreeENSGT00390000005995.
HOGENOMHOG000038005.
HOVERGENHBG054462.
KOK05627.
OrthoDBEOG7N0C3W.

Family and domain databases

InterProIPR027681. BAIAP2.
IPR013606. IRSp53/MIM_homology_IMD.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR14206. PTHR14206. 1 hit.
PfamPF08397. IMD. 1 hit.
[Graphical view]
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51338. IMD. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20868241.

Entry information

Entry nameBAIP2_BOVIN
AccessionPrimary (citable) accession number: Q5EAD0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 15, 2005
Last modified: April 16, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families