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Q80Y61

- BI2L2_MOUSE

UniProt

Q80Y61 - BI2L2_MOUSE

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Protein

Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2

Gene

Baiap2l2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Phosphoinositides-binding protein that induces the formation of planar or gently curved membrane structures. Binds to phosphoinositides, including to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) headgroups. There seems to be no clear preference for a specific phosphoinositide.1 Publication

GO - Molecular functioni

  1. phospholipid binding Source: UniProtKB

GO - Biological processi

  1. filopodium assembly Source: InterPro
  2. membrane organization Source: UniProtKB
  3. regulation of actin cytoskeleton organization Source: InterPro
  4. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2
Short name:
BAI1-associated protein 2-like protein 2
Alternative name(s):
Planar intestinal- and kidney-specific BAR domain protein
Short name:
Pinkbar
Gene namesi
Name:Baiap2l2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:2652819. Baiap2l2.

Subcellular locationi

Cell membrane By similarity; Peripheral membrane protein By similarity. Cell junction By similarity. Cytoplasmic vesicle membrane By similarity
Note: Localizes to RAB13-positive vesicles and to the plasma membrane at intercellular contacts.By similarity

GO - Cellular componenti

  1. cell-cell contact zone Source: UniProtKB
  2. clathrin complex Source: Ensembl
  3. cytoplasmic vesicle Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-KW
  5. vesicle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi109 – 1091K → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-116. 1 Publication
Mutagenesisi116 – 1161K → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-109. 1 Publication
Mutagenesisi124 – 1241I → S: Partially impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering. 1 Publication
Mutagenesisi127 – 1271R → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-135. 1 Publication
Mutagenesisi135 – 1351K → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-127. 1 Publication
Mutagenesisi141 – 1411W → S: Deficient in oligomerization (dimerization maintained). Inefficient formation of planar membrane structures. No effect on lipid-binding. 1 Publication
Mutagenesisi145 – 1451R → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-146 and A-147. 1 Publication
Mutagenesisi146 – 1461K → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-145 and A-147. 1 Publication
Mutagenesisi147 – 1471R → A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-145 and A-146. 1 Publication
Mutagenesisi149 – 1491K → A: No effect on lipid-binding; when associated with A-152 and A-155. 1 Publication
Mutagenesisi152 – 1521R → A: No effect on lipid-binding; when associated with A-149 and A-155. 1 Publication
Mutagenesisi155 – 1551K → A: No effect on lipid-binding; when associated with A-149 and A-152. 1 Publication
Mutagenesisi214 – 2141L → S: No effect on lipid-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2PRO_0000256131Add
BLAST

Proteomic databases

MaxQBiQ80Y61.
PaxDbiQ80Y61.
PRIDEiQ80Y61.

PTM databases

PhosphoSiteiQ80Y61.

Expressioni

Tissue specificityi

Expressed in the epithelial layer of the intestine and in the kidney.1 Publication

Gene expression databases

BgeeiQ80Y61.
CleanExiMM_BAIAP2L2.
ExpressionAtlasiQ80Y61. baseline.
GenevestigatoriQ80Y61.

Interactioni

Protein-protein interaction databases

DIPiDIP-59098N.

Structurei

Secondary structure

1
522
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2119
Helixi23 – 6442
Beta strandi65 – 673
Helixi69 – 9931
Helixi101 – 14545
Helixi151 – 21565

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OK8X-ray2.25A/B1-220[»]
ProteinModelPortaliQ80Y61.
SMRiQ80Y61. Positions 2-220, 323-383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 239239IMDPROSITE-ProRule annotationAdd
BLAST
Domaini324 – 38764SH3PROSITE-ProRule annotationAdd
BLAST

Domaini

The IMD domain consisting of an antiparallel dimer of three-helix bundles, featuring on one side a positively charged. The N-terminal alpha-helix inserts into the lipid bilayer. Also forms homodimers and homooligomers. The residue Trp-141 is essential for oligomer formation.

Sequence similaritiesi

Contains 1 IMD (IRSp53/MIM homology) domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG25242.
GeneTreeiENSGT00390000005995.
HOGENOMiHOG000038005.
HOVERGENiHBG100621.
InParanoidiQ80Y61.
OMAiRKRDKNV.
OrthoDBiEOG7N0C3W.
PhylomeDBiQ80Y61.
TreeFamiTF325648.

Family and domain databases

InterProiIPR027681. BAIAP2.
IPR013606. IRSp53/MIM_homology_IMD.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR14206. PTHR14206. 1 hit.
PfamiPF08397. IMD. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51338. IMD. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q80Y61-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPEMDQFYR STMAIYKSIM EQFNPALENL VYLGNNYLRA FHALSEAAEV
60 70 80 90 100
YFSAIQKIGE QALQSSTSQI LGEILVQMSD TQRHLNSDLE VVVQTFHGDL
110 120 130 140 150
LQHMEKNTKL DMQFIKDSCQ HYEIEYRHRA ANLEKCMSEL WRMERKRDKN
160 170 180 190 200
AREMKESVNR LHAQMQAFVS ESKRAAELEE KRRYRFLAEK HLLLSNTFLQ
210 220 230 240 250
FLGRARGMLQ NRVLLWKEQS EASRSPSRAH SPGLLGPALG PPYPSGRLTP
260 270 280 290 300
TRLDMPPRPL GEYGSPRSRH GSGSYGPEPA EARSASQLEP DRRSLPRTPS
310 320 330 340 350
ASSLYASSTQ RSRSNSFGER LGGGGARRVR ALVSHSEGAN HTLLRFSAGD
360 370 380 390 400
VVEVLVPEAQ NGWLYGKLEG SSASGWFPEA YVKPVEEIPV NPMNPVAPMN
410 420 430 440 450
SMAPMSPMNE LPSRSYPLRG SHSLDDLLDR PGNPTASSEY WDSQSRSRTP
460 470 480 490 500
SRVPSRAPSP APPPLPSSRR SSVGSMGAAT DVKKLMSWEQ NPPELFPRGT
510 520
NPFATVKLRP TVTNDRSAPL IR
Length:522
Mass (Da):58,402
Last modified:June 1, 2003 - v1
Checksum:i57403388931471FF
GO
Isoform 2 (identifier: Q80Y61-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     205-238: ARGMLQNRVLLWKEQSEASRSPSRAHSPGLLGPA → VSRAGESKPRPPGAVVRLRRTQEQERSFLPLCFL
     239-522: Missing.

Show »
Length:238
Mass (Da):27,954
Checksum:iED5F84192A0A2227
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei205 – 23834ARGML…LLGPA → VSRAGESKPRPPGAVVRLRR TQEQERSFLPLCFL in isoform 2. 1 PublicationVSP_021325Add
BLAST
Alternative sequencei239 – 522284Missing in isoform 2. 1 PublicationVSP_021326Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK143783 mRNA. Translation: BAE25539.1.
AL591913 Genomic DNA. No translation available.
CH466550 Genomic DNA. Translation: EDL04661.1.
BC048937 mRNA. Translation: AAH48937.1.
CCDSiCCDS37140.1. [Q80Y61-1]
RefSeqiNP_808248.1. NM_177580.3. [Q80Y61-1]
UniGeneiMm.309647.

Genome annotation databases

EnsembliENSMUST00000165408; ENSMUSP00000127816; ENSMUSG00000018126. [Q80Y61-1]
ENSMUST00000170955; ENSMUSP00000125946; ENSMUSG00000018126. [Q80Y61-2]
GeneIDi207495.
KEGGimmu:207495.
UCSCiuc007wtb.1. mouse. [Q80Y61-1]
uc007wtc.1. mouse. [Q80Y61-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK143783 mRNA. Translation: BAE25539.1 .
AL591913 Genomic DNA. No translation available.
CH466550 Genomic DNA. Translation: EDL04661.1 .
BC048937 mRNA. Translation: AAH48937.1 .
CCDSi CCDS37140.1. [Q80Y61-1 ]
RefSeqi NP_808248.1. NM_177580.3. [Q80Y61-1 ]
UniGenei Mm.309647.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3OK8 X-ray 2.25 A/B 1-220 [» ]
ProteinModelPortali Q80Y61.
SMRi Q80Y61. Positions 2-220, 323-383.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59098N.

PTM databases

PhosphoSitei Q80Y61.

Proteomic databases

MaxQBi Q80Y61.
PaxDbi Q80Y61.
PRIDEi Q80Y61.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000165408 ; ENSMUSP00000127816 ; ENSMUSG00000018126 . [Q80Y61-1 ]
ENSMUST00000170955 ; ENSMUSP00000125946 ; ENSMUSG00000018126 . [Q80Y61-2 ]
GeneIDi 207495.
KEGGi mmu:207495.
UCSCi uc007wtb.1. mouse. [Q80Y61-1 ]
uc007wtc.1. mouse. [Q80Y61-2 ]

Organism-specific databases

CTDi 80115.
MGIi MGI:2652819. Baiap2l2.

Phylogenomic databases

eggNOGi NOG25242.
GeneTreei ENSGT00390000005995.
HOGENOMi HOG000038005.
HOVERGENi HBG100621.
InParanoidi Q80Y61.
OMAi RKRDKNV.
OrthoDBi EOG7N0C3W.
PhylomeDBi Q80Y61.
TreeFami TF325648.

Miscellaneous databases

ChiTaRSi BAIAP2L2. mouse.
NextBioi 371953.
PROi Q80Y61.
SOURCEi Search...

Gene expression databases

Bgeei Q80Y61.
CleanExi MM_BAIAP2L2.
ExpressionAtlasi Q80Y61. baseline.
Genevestigatori Q80Y61.

Family and domain databases

InterProi IPR027681. BAIAP2.
IPR013606. IRSp53/MIM_homology_IMD.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR14206. PTHR14206. 1 hit.
Pfami PF08397. IMD. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS51338. IMD. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Spleen.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Colon.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-220, FUNCTION, TISSUE SPECIFICITY, PHOSPHOINOSITIDES-BINDING, MUTAGENESIS OF LYS-109; LYS-116; ILE-124; ARG-127; LYS-135; TRP-141; ARG-145; LYS-146; ARG-147; LYS-149; ARG-152; LYS-155 AND LEU-214.

Entry informationi

Entry nameiBI2L2_MOUSE
AccessioniPrimary (citable) accession number: Q80Y61
Secondary accession number(s): Q3UP58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2003
Last modified: October 29, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3