Q9UHR4 (BI2L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1
Short name=BAI1-associated protein 2-like protein 1

Alternative name(s):
Insulin receptor tyrosine kinase substrate

Gene names

Name:	BAIAP2L1
Synonyms:	IRTKS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Ref.8 Ref.15
Subunit structure	Interacts with RAC1. Binds to F-actin. Interacts with FASLG. Interacts (via SH3 domain) with E.coli effector protein EspF(U) (via PXXP motifs). Identified in a complex containing at least WASL, BAIAP2L1 and E.coli EspF(U). Interacts with E.coli intimin receptor Tir. Ref.8 Ref.13 Ref.15 Ref.17
Subcellular location	Cytoplasm › cytoskeleton. Note: Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites. Ref.15
Domain	The IMD domain is predicted to have a helical structure. It may induce actin bundling and filopodia formation By similarity.
Post-translational modification	Phosphorylated on tyrosine in response to insulin. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14
Sequence similarities	Contains 1 IMD (IRSp53/MIM homology) domain. Contains 1 SH3 domain.
Sequence caution	The sequence AAD20937.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAS07549.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB15671.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Polymorphism
Domain	Coiled coil SH3 domain
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	filopodium assembly Inferred from electronic annotation. Source: InterPro positive regulation of actin cytoskeleton reorganization Inferred from mutant phenotype Ref.15. Source: UniProtKB positive regulation of actin filament polymerization Inferred from direct assay Ref.17. Source: UniProtKB response to bacterium Inferred from direct assay Ref.15. Source: UniProtKB signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cell junction Inferred from direct assay. Source: HPA cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay Ref.15. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular function	SH3 domain binding Inferred from electronic annotation. Source: InterPro actin binding Inferred from electronic annotation. Source: UniProtKB-KW cytoskeletal adaptor activity Inferred from electronic annotation. Source: InterPro proline-rich region binding Inferred from direct assay Ref.17. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 511

511

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

PRO_0000247854

Regions

Domain

1 – 249

249

IMD

Domain

339 – 402

64

SH3

Region

483 – 511

29

Binds F-actin

Coiled coil

115 – 154

40

Potential

Amino acid modifications

Modified residue

248

1

Phosphothreonine Ref.11

Modified residue

257

1

Phosphothreonine Ref.7 Ref.11 Ref.12

Modified residue

261

1

Phosphoserine Ref.7 Ref.9 Ref.11 Ref.12

Modified residue

274

1

Phosphotyrosine Ref.14

Modified residue

281

1

Phosphoserine Ref.11

Modified residue

329

1

Phosphoserine By similarity

Modified residue

331

1

Phosphoserine Ref.11

Modified residue

412

1

Phosphothreonine Ref.11 Ref.12

Modified residue

414

1

Phosphoserine Ref.10 Ref.11 Ref.12

Modified residue

416

1

Phosphothreonine Ref.12

Natural variations

Natural variant

460

1

S → T.
Corresponds to variant rs2269966 [ dbSNP | Ensembl ].

VAR_033515

Experimental info

Mutagenesis

141

1

K → E: Loss ability to induce the formation of actin clusters; when associated with K-142; R-145 and K-146. Ref.8

Mutagenesis

142

1

K → E: Loss ability to induce the formation of actin clusters; when associated with K-141; R-145 and K-146. Ref.8

Mutagenesis

145

1

R → E: Loss ability to induce the formation of actin clusters; when associated with K-141; K-142 and K-146. Ref.8

Mutagenesis

146

1

K → E: Loss ability to induce the formation of actin clusters; when associated with K-141; K-142 and R-145. Ref.8

Mutagenesis

488 – 511

24

Missing: Loss ability to induce the formation of actin clusters; induce the formation of long filopodia. Ref.8

Sequence conflict

456

1

A → V in BAB15671. Ref.6

Sequence conflict

460

1

S → F in BAB15671. Ref.6

Sequence conflict

464

1

A → V in BAB15671. Ref.6

Sequence conflict

466

1

A → V in BAB15671. Ref.6

Sequence conflict

467

1

S → F in BAB15671. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

511

Helix Strand Turn

Details...

Beta strand

343 – 348

6

Beta strand

366 – 368

3

Beta strand

370 – 373

4

Beta strand

383 – 386

4

Helix

394 – 396

3

Beta strand

397 – 400

4

Sequences

	Sequence		Length	Mass (Da)
	Q9UHR4 [UniParc]. Last modified March 1, 2004. Version 2. Checksum: C2304C4444B02F02	FASTA	511	56,883
	10 20 30 40 50 60 MSRGPEEVNR LTESTYRNVM EQFNPGLRNL INLGKNYEKA VNAMILAGKA YYDGVAKIGE 70 80 90 100 110 120 IATGSPVSTE LGHVLIEISS THKKLNESLD ENFKKFHKEI IHELEKKIEL DVKYMNATLK 130 140 150 160 170 180 RYQTEHKNKL ESLEKSQAEL KKIRRKSQGS RNALKYEHKE IEYVETVTSR QSEIQKFIAD 190 200 210 220 230 240 GCKEALLEEK RRFCFLVDKH CGFANHIHYY HLQSAELLNS KLPRWQETCV DAIKVPEKIM 250 260 270 280 290 300 NMIEEIKTPA STPVSGTPQA SPMIERSNVV RKDYDTLSKC SPKMPPAPSG RAYTSPLIDM 310 320 330 340 350 360 FNNPATAAPN SQRVNNSTGT SEDPSLQRSV SVATGLNMMK KQKVKTIFPH TAGSNKTLLS 370 380 390 400 410 420 FAQGDVITLL IPEEKDGWLY GEHDVSKARG WFPSSYTKLL EENETEAVTV PTPSPTPVRS 430 440 450 460 470 480 ISTVNLSENS SVVIPPPDYL ECLSMGAAAD RRADSARTTS TFKAPASKPE TAAPNDANGT 490 500 510 AKPPFLSGEN PFATVKLRPT VTNDRSAPII R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Adrenal gland.
[2]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed: 12690205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[6]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-511. Tissue: Lung.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257 AND SER-261, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with distinct filament bundling properties." Millard T.H., Dawson J., Machesky L.M. J. Cell Sci. 120:1663-1672(2007) [PubMed: 17430976] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAC1 AND F-ACTIN, PHOSPHORYLATION, MUTAGENESIS OF LYS-141; LYS-142; ARG-145; LYS-146 AND 488-GLY--ARG-511.
[9]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248; THR-257; SER-261; SER-281; SER-331; THR-412 AND SER-414, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-261; THR-412; SER-414 AND THR-416, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening." Voss M., Lettau M., Janssen O. BMC Immunol. 10:53-53(2009) [PubMed: 19807924] [Abstract] Cited for: INTERACTION WITH FASLG.
[14]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-274, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[15]	"Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspF(U) during pedestal formation." Vingadassalom D., Kazlauskas A., Skehan B., Cheng H.C., Magoun L., Robbins D., Rosen M.K., Saksela K., Leong J.M. Proc. Natl. Acad. Sci. U.S.A. 106:6754-6759(2009) [PubMed: 19366662] [Abstract] Cited for: FUNCTION, INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U), IDENTIFICATION IN A COMPLEX WITH WASL AND E.COLI EFFECTOR PROTEIN ESPF(U), INTERACTION WITH E.COLI INTIMIN RECEPTOR TIR, SUBCELLULAR LOCATION.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"Recognition of tandem PxxP motifs as a unique Src homology 3-binding mode triggers pathogen-driven actin assembly." Aitio O., Hellman M., Kazlauskas A., Vingadassalom D.F., Leong J.M., Saksela K., Permi P. Proc. Natl. Acad. Sci. U.S.A. 107:21743-21748(2010) [PubMed: 21098279] [Abstract] Cited for: STRUCTURE BY NMR OF 339-402 IN COMPLEX WITH E.COLI EFFECTOR PROTEIN ESPF(U), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF119666 mRNA. Translation: AAF17223.2.
AC004841 Genomic DNA. Translation: AAD20937.1. Sequence problems.
AC093169 Genomic DNA. No translation available.
AC093799 Genomic DNA. Translation: AAS07549.1. Different initiation.
AC093799 Genomic DNA. Translation: AAS07550.1.
CH236956 Genomic DNA. Translation: EAL23890.1.
CH471091 Genomic DNA. Translation: EAW76706.1.
BC013888 mRNA. Translation: AAH13888.1.
AK027142 mRNA. Translation: BAB15671.1. Different initiation.

IPI

IPI00179326.

RefSeq

NP_061330.2. NM_018842.4.

UniGene

Hs.656063.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KXC	NMR	-	A	339-402	[»]

ProteinModelPortal

Q9UHR4.

SMR

Q9UHR4. Positions 1-247, 339-402.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UHR4. 5 interactions.

STRING

Q9UHR4.

PTM databases

PhosphoSite

Q9UHR4.

Polymorphism databases

DMDM

74735022.

Proteomic databases

PeptideAtlas

Q9UHR4.

PRIDE

Q9UHR4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000005260; ENSP00000005260; ENSG00000006453.

GeneID

55971.

KEGG

hsa:55971.

NMPDR

fig|9606.3.peg.29028.

UCSC

uc003upj.1. human.

Organism-specific databases

CTD

55971.

GeneCards

GC07M097920.

H-InvDB

HIX0006880.

HGNC

HGNC:21649. BAIAP2L1.

HPA

HPA019484.
HPA021257.
HPA023874.
HPA029503.

MIM

611877. gene.

neXtProt

NX_Q9UHR4.

PharmGKB

PA142672562.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09659.

GeneTree

ENSGT00390000005995.

HOVERGEN

HBG054462.

InParanoid

Q9UHR4.

OMA

EKAVNAM.

OrthoDB

EOG4GXFMT.

PhylomeDB

Q9UHR4.

Gene expression databases

ArrayExpress

Q9UHR4.

Bgee

Q9UHR4.

CleanEx

HS_BAIAP2L1.

Genevestigator

Q9UHR4.

GermOnline

ENSG00000006453. Homo sapiens.

Family and domain databases

InterPro

IPR013606. IRSp53/MIM_homology_IMD.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

Gene3D

G3DSA:1.20.1270.80. IRSp53/MIM_homology_IMD. 1 hit.

Pfam

PF08397. IMD. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

SMART

SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS51338. IMD. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

61407.

SOURCE

Search...

Entry information

Entry name

BI2L1_HUMAN

Accession

Primary (citable) accession number: Q9UHR4
Secondary accession number(s): A4D268 , Q75L21, Q75L22, Q96CV4, Q9H5F5, Q9Y2M8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	March 1, 2004
Last modified:	January 25, 2012
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.