Descriptions

(Annotation based on sequence homology with Q9UQB8)
BAIAP2 (IRSp53) is a SH3-containing protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. The N-terminal autoinhibitory region interacts intramolecularly with the central region containing CRIB motif and Cdc42 binding domain. When GTP-loaded Cdc42 binds to the CRIB motif, it abrogates the autoinhibitory, intramolecular interaction and allows the SH3 domain to interact with BAIAP2 effector proteins such as Mena. When the N-terminal autoinhibitory fragment is co-expressed with BAIAP2, the fragment inhibits the function of BAIAP2.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q5EAD0

Entry ID Method Resolution Chain Position Source
AF-Q5EAD0-F1 Predicted AlphaFoldDB

151 variants for Q5EAD0

Variant ID(s) Position Change Description Diseaes Association Provenance
rs439495013 2 S>L No EVA
rs458055016 2 S>P No EVA
rs442155045 6 S>A No EVA
rs442155045 6 S>P No EVA
rs475102910 7 E>G No EVA
rs456578642 8 E>D No EVA
rs444611710 9 M>V No EVA
rs470971145 10 H>P No EVA
rs452724177 11 R>G No EVA
rs465644505 12 L>H No EVA
rs465644505 12 L>P No EVA
rs453629247 13 T>P No EVA
rs468248259 14 E>D No EVA
rs435132854 14 E>K No EVA
rs449737803 15 N>H No EVA
rs464342475 15 N>K No EVA
rs482905547 15 N>S No EVA
rs478905046 16 V>A No EVA
rs445991055 16 V>F No EVA
rs478905046 16 V>G No EVA
rs481432417 17 Y>* No EVA
rs460578167 17 Y>H No EVA
rs442007072 17 Y>S No EVA
rs463023865 18 K>R No EVA
rs460651143 45 V>G No EVA
rs440815522 47 Y>D No EVA
rs461895017 54 D>G No EVA
rs476257784 58 K>Q No EVA
rs451535497 61 E>A No EVA
rs432919632 69 S>T No EVA
rs453926188 70 K>Q No EVA
rs437491174 74 D>E No EVA
rs470301581 77 F>C No EVA
rs468213930 98 H>P No EVA
rs450045551 115 Y>S No EVA
rs464530646 117 S>R No EVA
rs521541519 133 A>V No EVA
rs459394520 172 Q>E No EVA
rs461743547 174 E>G No EVA
rs476518482 175 L>R No EVA
rs443227215 175 L>V No EVA
rs451510089 177 S>G No EVA
rs432903828 177 S>R No EVA
rs472205631 178 Y>S No EVA
rs453824509 185 T>P No EVA
rs435673973 188 T>P No EVA
rs450044346 194 F>L No EVA
rs438006311 194 F>L No EVA
rs450044346 194 F>V No EVA
rs464826114 196 F>S No EVA
rs446364833 197 L>M No EVA
rs479354512 198 V>A No EVA
rs460728945 199 E>G No EVA
rs448737802 200 K>T No EVA
rs461842723 201 Q>P No EVA
rs461842723 201 Q>R No EVA
rs443180787 203 A>P No EVA
rs476213546 209 A>P No EVA
rs448750847 212 H>L No EVA
rs448750847 212 H>P No EVA
rs439458827 214 K>* No EVA
rs463462326 215 G>A No EVA
rs471392934 216 K>R No EVA
rs434668783 217 E>G No EVA
rs452877317 217 E>K No EVA
rs474137374 226 W>* No EVA
rs455495353 228 Q>P No EVA
rs473733323 230 C>W No EVA
rs436996344 232 D>H No EVA
rs470070918 237 P>A No EVA
rs445306599 238 D>A No EVA
rs433299145 240 A>G No EVA
rs465996065 242 Q>P No EVA
rs447621899 243 L>M No EVA
rs480927568 247 M>R No EVA
rs462443938 248 G>D No EVA
rs450228516 249 N>T No EVA
rs483215504 252 G>A No EVA
rs463400852 253 S>P No EVA
rs438514125 254 I>T No EVA
rs471532008 257 S>T No EVA
rs459327353 259 L>F No EVA
rs440816058 262 S>P No EVA
rs443124225 267 V>F No EVA
rs474093450 270 D>A No EVA
rs455562104 271 P>T No EVA
rs800794102 297 A>T No EVA
rs452832728 357 T>N No EVA
rs434322547 359 N>H No EVA
rs467130079 361 T>P No EVA
rs448702914 362 L>R No EVA
rs449555493 366 S>R No EVA
rs457831692 368 M>I No EVA
rs482432841 368 M>K No EVA
rs445901430 371 G>R No EVA
rs478994147 372 L>M No EVA
rs460286620 372 L>R No EVA
rs441834501 374 R>P No EVA
rs475074572 375 N>I No EVA
rs475074572 375 N>S No EVA
rs444400601 378 M>V No EVA
rs470981948 380 V>G No EVA
rs452570616 382 A>P No EVA
rs473757751 383 I>M No EVA
rs434263605 383 I>V No EVA
rs455018570 385 S>P No EVA
rs436602450 388 A>S No EVA
rs468062678 390 D>E No EVA
rs449694026 393 T>P No EVA
rs463979425 399 E>G No EVA
rs445656854 400 G>C No EVA
rs445656854 400 G>S No EVA
rs478926773 402 L>P No EVA
rs460476317 404 T>P No EVA
rs460476317 404 T>S No EVA
rs448146241 405 L>P No EVA
rs481216901 406 L>V No EVA
rs462797009 408 P>T No EVA
rs444537663 409 E>Q No EVA
rs458913079 414 W>C No EVA
rs440414488 419 S>R No EVA
rs473660752 423 K>T No EVA
rs473793205 427 W>L No EVA
rs455408557 428 F>V No EVA
rs437235667 429 P>H No EVA
rs451559495 431 S>F No EVA
rs466434758 433 T>N No EVA
rs433181406 433 T>P No EVA
rs480995322 434 R>P No EVA
rs468756588 436 L>P No EVA
rs481890043 437 D>A No EVA
rs463466242 437 D>E No EVA
rs450344722 437 D>H No EVA
rs438344693 439 D>H No EVA
rs459388869 442 D>G No EVA
rs459388869 442 D>V No EVA
rs441075851 444 L>V No EVA
rs473931911 445 H>L No EVA
rs455343500 445 H>Q No EVA
rs434181141 447 S>R No EVA
rs447297441 472 Y>S No EVA
rs467989099 487 F>S No EVA
rs449623120 490 R>S No EVA
rs482964940 496 V>G No EVA
rs464482506 497 P>L No EVA
rs460349982 499 F>S No EVA
rs478859124 499 F>V No EVA
rs442133039 501 Q>R No EVA
rs438065007 516 V>G No EVA
rs464663873 519 A>G No EVA
rs111023026 519 A>S No EVA

No associated diseases with Q5EAD0

4 regional properties for Q5EAD0

Type Name Position InterPro Accession
domain SH3 domain 375 - 438 IPR001452
domain IMD/I-BAR domain 1 - 250 IPR013606
domain I-BAR domain containing protein IRSp53, Inverse-Bin/Amphiphysin/Rvs domain 5 - 236 IPR030128
domain IRSp53, SH3 domain 378 - 436 IPR035594

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Membrane ; Peripheral membrane protein
  • Cell projection, filopodium
  • Cell projection, ruffle
  • Cytoplasm, cytoskeleton
  • 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)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
filopodium Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
ruffle Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork.

2 GO annotations of molecular function

Name Definition
cytoskeletal anchor activity The binding activity of a protein that brings together a cytoskeletal protein (either a microtubule or actin filament, spindle pole body, or protein directly bound to them) and one or more other molecules, permitting them to function in a coordinated way.
proline-rich region binding Binding to a proline-rich region, i.e. a region that contains a high proportion of proline residues, in a protein.

8 GO annotations of biological process

Name Definition
actin crosslink formation The process in which two or more actin filaments are connected together by proteins that act as crosslinks between the filaments. The crosslinked filaments may be on the same or differing axes.
actin filament bundle assembly The assembly of actin filament bundles; actin filaments are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
plasma membrane organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the plasma membrane.
positive regulation of actin cytoskeleton reorganization Any process that activates or increases the frequency, rate or extent of actin cytoskeleton reorganization.
positive regulation of actin filament polymerization Any process that activates or increases the frequency, rate or extent of actin polymerization.
regulation of actin cytoskeleton organization Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
regulation of cell shape Any process that modulates the surface configuration of a cell.
response to bacterium Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a bacterium.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9UQB8 BAIAP2 Brain-specific angiogenesis inhibitor 1-associated protein 2 Homo sapiens (Human) EV
Q8BKX1 Baiap2 BAR/IMD domain-containing adapter protein 2 Mus musculus (Mouse) SS
Q6GMN2 Baiap2 BAR/IMD domain-containing adapter protein 2 Rattus norvegicus (Rat) SS
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