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Q9UHR4

- BI2L1_HUMAN

UniProt

Q9UHR4 - BI2L1_HUMAN

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Protein

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

Gene

BAIAP2L1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. proline-rich region binding Source: UniProtKB

GO - Biological processi

  1. filopodium assembly Source: InterPro
  2. positive regulation of actin cytoskeleton reorganization Source: UniProtKB
  3. positive regulation of actin filament polymerization Source: UniProtKB
  4. response to bacterium Source: UniProtKB
  5. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:BAIAP2L1
Synonyms:IRTKS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:21649. BAIAP2L1.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication
Note: Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoskeleton Source: UniProtKB-KW
  3. cytosol Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. nucleus Source: HPA
  6. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi141 – 1411K → E: Loss ability to induce the formation of actin clusters; when associated with K-142; R-145 and K-146. 1 Publication
Mutagenesisi142 – 1421K → E: Loss ability to induce the formation of actin clusters; when associated with K-141; R-145 and K-146. 1 Publication
Mutagenesisi145 – 1451R → E: Loss ability to induce the formation of actin clusters; when associated with K-141; K-142 and K-146. 1 Publication
Mutagenesisi146 – 1461K → E: Loss ability to induce the formation of actin clusters; when associated with K-141; K-142 and R-145. 1 Publication
Mutagenesisi488 – 51124Missing: Loss ability to induce the formation of actin clusters; induce the formation of long filopodia. 1 PublicationAdd
BLAST

Organism-specific databases

PharmGKBiPA142672562.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 511511Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1PRO_0000247854Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei248 – 2481Phosphothreonine2 Publications
Modified residuei257 – 2571Phosphothreonine2 Publications
Modified residuei261 – 2611Phosphoserine3 Publications
Modified residuei281 – 2811Phosphoserine1 Publication
Modified residuei331 – 3311Phosphoserine1 Publication
Modified residuei412 – 4121Phosphothreonine2 Publications
Modified residuei422 – 4221PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on tyrosine in response to insulin.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UHR4.
PaxDbiQ9UHR4.
PeptideAtlasiQ9UHR4.
PRIDEiQ9UHR4.

PTM databases

PhosphoSiteiQ9UHR4.

Expressioni

Gene expression databases

BgeeiQ9UHR4.
CleanExiHS_BAIAP2L1.
GenevestigatoriQ9UHR4.

Organism-specific databases

HPAiHPA019484.
HPA021257.
HPA023874.
HPA029503.

Interactioni

Subunit structurei

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.5 Publications

Protein-protein interaction databases

BioGridi121017. 14 interactions.
DIPiDIP-53820N.
IntActiQ9UHR4. 5 interactions.
MINTiMINT-5006683.
STRINGi9606.ENSP00000005260.

Structurei

Secondary structure

1
511
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi343 – 3486Combined sources
Beta strandi356 – 3583Combined sources
Beta strandi366 – 3738Combined sources
Beta strandi378 – 3869Combined sources
Beta strandi389 – 3935Combined sources
Helixi394 – 3963Combined sources
Beta strandi397 – 4004Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KXCNMR-A339-402[»]
2LNHNMR-B339-402[»]
ProteinModelPortaliQ9UHR4.
SMRiQ9UHR4. Positions 6-227, 339-402.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 249249IMDPROSITE-ProRule annotationAdd
BLAST
Domaini339 – 40264SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni483 – 51129Binds F-actinAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili115 – 15440Sequence AnalysisAdd
BLAST

Domaini

The IMD domain is predicted to have a helical structure. It may induce actin bundling and filopodia formation (By similarity).By similarity

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG71665.
GeneTreeiENSGT00390000005995.
HOVERGENiHBG054462.
InParanoidiQ9UHR4.
OMAiYRNVMEQ.
OrthoDBiEOG7N0C3W.
PhylomeDBiQ9UHR4.
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]

Sequencei

Sequence statusi: Complete.

Q9UHR4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRGPEEVNR LTESTYRNVM EQFNPGLRNL INLGKNYEKA VNAMILAGKA
60 70 80 90 100
YYDGVAKIGE IATGSPVSTE LGHVLIEISS THKKLNESLD ENFKKFHKEI
110 120 130 140 150
IHELEKKIEL DVKYMNATLK RYQTEHKNKL ESLEKSQAEL KKIRRKSQGS
160 170 180 190 200
RNALKYEHKE IEYVETVTSR QSEIQKFIAD GCKEALLEEK RRFCFLVDKH
210 220 230 240 250
CGFANHIHYY HLQSAELLNS KLPRWQETCV DAIKVPEKIM NMIEEIKTPA
260 270 280 290 300
STPVSGTPQA SPMIERSNVV RKDYDTLSKC SPKMPPAPSG RAYTSPLIDM
310 320 330 340 350
FNNPATAAPN SQRVNNSTGT SEDPSLQRSV SVATGLNMMK KQKVKTIFPH
360 370 380 390 400
TAGSNKTLLS FAQGDVITLL IPEEKDGWLY GEHDVSKARG WFPSSYTKLL
410 420 430 440 450
EENETEAVTV PTPSPTPVRS ISTVNLSENS SVVIPPPDYL ECLSMGAAAD
460 470 480 490 500
RRADSARTTS TFKAPASKPE TAAPNDANGT AKPPFLSGEN PFATVKLRPT
510
VTNDRSAPII R
Length:511
Mass (Da):56,883
Last modified:March 1, 2004 - v2
Checksum:iC2304C4444B02F02
GO

Sequence cautioni

The sequence AAS07549.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAB15671.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAD20937.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti456 – 4561A → V in BAB15671. (PubMed:14702039)Curated
Sequence conflicti460 – 4601S → F in BAB15671. (PubMed:14702039)Curated
Sequence conflicti464 – 4641A → V in BAB15671. (PubMed:14702039)Curated
Sequence conflicti466 – 4661A → V in BAB15671. (PubMed:14702039)Curated
Sequence conflicti467 – 4671S → F in BAB15671. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti460 – 4601S → T.
Corresponds to variant rs2269966 [ dbSNP | Ensembl ].
VAR_033515

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34687.1.
RefSeqiNP_061330.2. NM_018842.4.
UniGeneiHs.656063.

Genome annotation databases

EnsembliENST00000005260; ENSP00000005260; ENSG00000006453.
GeneIDi55971.
KEGGihsa:55971.
UCSCiuc003upj.3. human.

Polymorphism databases

DMDMi74735022.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS34687.1.
RefSeqi NP_061330.2. NM_018842.4.
UniGenei Hs.656063.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KXC NMR - A 339-402 [» ]
2LNH NMR - B 339-402 [» ]
ProteinModelPortali Q9UHR4.
SMRi Q9UHR4. Positions 6-227, 339-402.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121017. 14 interactions.
DIPi DIP-53820N.
IntActi Q9UHR4. 5 interactions.
MINTi MINT-5006683.
STRINGi 9606.ENSP00000005260.

PTM databases

PhosphoSitei Q9UHR4.

Polymorphism databases

DMDMi 74735022.

Proteomic databases

MaxQBi Q9UHR4.
PaxDbi Q9UHR4.
PeptideAtlasi Q9UHR4.
PRIDEi Q9UHR4.

Protocols and materials databases

DNASUi 55971.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000005260 ; ENSP00000005260 ; ENSG00000006453 .
GeneIDi 55971.
KEGGi hsa:55971.
UCSCi uc003upj.3. human.

Organism-specific databases

CTDi 55971.
GeneCardsi GC07M097920.
H-InvDB HIX0167837.
HGNCi HGNC:21649. BAIAP2L1.
HPAi HPA019484.
HPA021257.
HPA023874.
HPA029503.
MIMi 611877. gene.
neXtProti NX_Q9UHR4.
PharmGKBi PA142672562.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG71665.
GeneTreei ENSGT00390000005995.
HOVERGENi HBG054462.
InParanoidi Q9UHR4.
OMAi YRNVMEQ.
OrthoDBi EOG7N0C3W.
PhylomeDBi Q9UHR4.
TreeFami TF325648.

Miscellaneous databases

ChiTaRSi BAIAP2L1. human.
GeneWikii BAIAP2L1.
GenomeRNAii 55971.
NextBioi 61407.
PROi Q9UHR4.
SOURCEi Search...

Gene expression databases

Bgeei Q9UHR4.
CleanExi HS_BAIAP2L1.
Genevestigatori Q9UHR4.

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. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [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. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248; THR-257; SER-261; SER-281; SER-331 AND THR-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FASLG.
  13. "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] [Europe PMC] [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.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248; THR-257; SER-261 AND THR-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 339-402 IN COMPLEX WITH E.COLI EFFECTOR PROTEIN ESPF(U), SUBUNIT.
  17. "Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly."
    Aitio O., Hellman M., Skehan B., Kesti T., Leong J.M., Saksela K., Permi P.
    Structure 20:1692-1703(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 339-402 IN COMPLEX WITH WASL AND E.COLI ESPF(U), FUNCTION, IDENTIFICATION IN A COMPLEX WITH WASL AND E.COLI ESPF(U).

Entry informationi

Entry nameiBI2L1_HUMAN
AccessioniPrimary (citable) accession number: Q9UHR4
Secondary accession number(s): A4D268
, Q75L21, Q75L22, Q96CV4, Q9H5F5, Q9Y2M8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2004
Last modified: October 29, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3