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Q8CBW3

- ABI1_MOUSE

UniProt

Q8CBW3 - ABI1_MOUSE

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Protein
Abl interactor 1
Gene
Abi1, Ssh3bp1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. In vitro, at least isoform 2 and isoform 4 suppress the transforming activity of Abelson murine leukemia virus (v-Abl) after overexpression in fibroblasts. May play a role in regulation EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons.6 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. protein tyrosine kinase activator activity Source: MGI
Complete GO annotation...

GO - Biological processi

  1. cellular component movement Source: Ensembl
  2. cellular process Source: MGI
  3. lamellipodium morphogenesis Source: MGI
  4. megakaryocyte development Source: MGI
  5. peptidyl-tyrosine phosphorylation Source: MGI
  6. positive regulation of protein tyrosine kinase activity Source: GOC
  7. somitogenesis Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Abl interactor 1
Alternative name(s):
Abelson interactor 1
Short name:
Abi-1
Ablphilin-1
Eps8 SH3 domain-binding protein
Short name:
Eps8-binding protein
Spectrin SH3 domain-binding protein 1
e3B1
Gene namesi
Name:Abi1
Synonyms:Ssh3bp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:104913. Abi1.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. Cell projectionlamellipodium By similarity. Cell projectionfilopodium By similarity. Cell projectiongrowth cone By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Cytoplasmcytoskeleton By similarity
Note: Localized to protruding lamellipodia and filopodia tips. Also localized to neuronal growth cones and synaptosomes. May shuttle from the postsynaptic densities to the nucleus By similarity.2 Publications

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell leading edge Source: MGI
  3. cytoplasm Source: UniProtKB-SubCell
  4. filopodium Source: UniProtKB-SubCell
  5. growth cone Source: UniProtKB-SubCell
  6. intracellular Source: MGI
  7. lamellipodium Source: MGI
  8. neuron projection Source: BHF-UCL
  9. nucleus Source: UniProtKB-SubCell
  10. postsynaptic density Source: UniProtKB-SubCell
  11. postsynaptic membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus, Postsynaptic cell membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 481480Abl interactor 1
PRO_0000191788Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei53 – 531Phosphotyrosine By similarity
Modified residuei183 – 1831Phosphoserine2 Publications
Modified residuei213 – 2131Phosphotyrosine; alternate1 Publication
Modified residuei213 – 2131Phosphotyrosine; by ABL1; alternate By similarity
Modified residuei216 – 2161Phosphoserine By similarity
Modified residuei222 – 2221Phosphoserine By similarity
Modified residuei225 – 2251Phosphoserine By similarity
Modified residuei296 – 2961Phosphoserine By similarity
Modified residuei428 – 4281Phosphotyrosine1 Publication
Modified residuei480 – 4801Phosphothreonine By similarity

Post-translational modificationi

Phosphorylated on tyrosine residues after serum stimulation or induction by v-Abl. Seems to be phosphorylated at Tyr-53 by ABL1, required for nuclear but not for synaptic localization By similarity.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8CBW3.
PaxDbiQ8CBW3.
PRIDEiQ8CBW3.

PTM databases

PhosphoSiteiQ8CBW3.

Expressioni

Tissue specificityi

Widely expressed with highest levels in bone marrow, spleen, brain, testes, and embryonic brain. In adult brain prominently expressed in the neocortex, hippocampus and dentate gyrus.2 Publications

Developmental stagei

Detected at E10 and E12 in developing brain, but does not appear more prominent in the neuroepithelium compared to the surrounding tissue.1 Publication

Gene expression databases

ArrayExpressiQ8CBW3.
BgeeiQ8CBW3.
CleanExiMM_ABI1.
GenevestigatoriQ8CBW3.

Interactioni

Subunit structurei

Interacts with ENAH, Abelson murine leukemia virus V-ABL, ABL1, STX1A, SNAP25, VAMP2, and through its N-terminus with WASF1. Part of a complex consisting of ABI1, STX1A and SNAP25. Part of a complex consisting of ABI1, EPS8 and SOS1. Interacts with EPS8, SOS1, SOS2, GRB2, SPTA1, and the first SH3 domain of NCK1 By similarity. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. Interacts (via SH3 domain) with SHANK2 and SHANK3, but not SHANK1; the interaction is direct. Interacts with the heterodimer MYC:MAX; the interaction may enhance MYC:MAX transcriptional activity.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Eps8Q085092EBI-375511,EBI-375596
Sos2Q023842EBI-375511,EBI-395573

Protein-protein interaction databases

BioGridi197905. 7 interactions.
DIPiDIP-29534N.
IntActiQ8CBW3. 30 interactions.
MINTiMINT-128698.

Structurei

3D structure databases

ProteinModelPortaliQ8CBW3.
SMRiQ8CBW3. Positions 1-154, 409-476.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 10763t-SNARE coiled-coil homology
Add
BLAST
Domaini419 – 47860SH3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 7962Required for binding to WASF1
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi337 – 39155Pro-rich
Add
BLAST

Domaini

The t-SNARE coiled-coil homology domain is necessary and sufficient for interaction with STX1A.

Sequence similaritiesi

Belongs to the ABI family.
Contains 1 SH3 domain.

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG262939.
GeneTreeiENSGT00390000003756.
HOGENOMiHOG000293213.
HOVERGENiHBG050446.
InParanoidiQ8CBW3.
OMAiMPMFDDS.
OrthoDBiEOG7J17ZT.
PhylomeDBiQ8CBW3.
TreeFamiTF314303.

Family and domain databases

InterProiIPR028457. ABI.
IPR028456. ABI1.
IPR012849. Abl-interactor_HHR_dom.
IPR001452. SH3_domain.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERiPTHR10460. PTHR10460. 1 hit.
PTHR10460:SF2. PTHR10460:SF2. 1 hit.
PfamiPF07815. Abi_HHR. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8CBW3-1) [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

MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET    50
KAYTTQSLAS VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH 100
KEKVARREIG ILTTNKNTSR THKIIAPANM ERPVRYIRKP IDYTVLDDVG 150
HGVKWLKAKH GNNQPARTGT LSRTNPPTQK PPSPPVSGRG TLGRNTPYKT 200
LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS GSSGGSGSRE 250
NSGSSSIGIP IAVPTPSPPT AGPAAPGAAP GSQYGTMTRQ ISRHNSTTSS 300
TSSGGYRRTP SVAAQFSAQP HVNGGPLYSQ NSISVAPPPP PMPQLTPQIP 350
LTGFVARVQE NIADSPTPPP PPPPDDIPMF DDSPPPPPPP PVDYEDEEAA 400
VVQYSDPYAD GDPAWAPKNY IEKVVAIYDY TKDKDDELSF KEGAIIYVIK 450
KNDDGWFEGV CNRVTGLFPG NYVESIMHYT D 481
Length:481
Mass (Da):52,288
Last modified:January 23, 2007 - v3
Checksum:i1654A1E89438BC1D
GO
Isoform 2 (identifier: Q8CBW3-2) [UniParc]FASTAAdd to Basket

Also known as: short

The sequence of this isoform differs from the canonical sequence as follows:
     154-158: Missing.
     274-274: Missing.
     333-361: Missing.

Show »
Length:446
Mass (Da):48,512
Checksum:i805A2F6072F1D24B
GO
Isoform 3 (identifier: Q8CBW3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     154-158: Missing.

Show »
Length:476
Mass (Da):51,661
Checksum:iB7E38AA1E9ED7FA6
GO
Isoform 4 (identifier: Q8CBW3-4) [UniParc]FASTAAdd to Basket

Also known as: long

The sequence of this isoform differs from the canonical sequence as follows:
     154-158: Missing.
     274-274: Missing.

Show »
Length:475
Mass (Da):51,590
Checksum:iA0A613AAD091B0F0
GO
Isoform 5 (identifier: Q8CBW3-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     154-158: Missing.
     274-362: AAPGAAPGSQ...GFVARVQENI → V

Show »
Length:388
Mass (Da):42,548
Checksum:i27FAB95E05BCA655
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei154 – 1585Missing in isoform 2, isoform 3, isoform 4 and isoform 5.
VSP_010756
Alternative sequencei274 – 36289AAPGA…VQENI → V in isoform 5.
VSP_022636Add
BLAST
Alternative sequencei274 – 2741Missing in isoform 2 and isoform 4.
VSP_010757
Alternative sequencei333 – 36129Missing in isoform 2.
VSP_010758Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti313 – 3131A → T in AAH04657. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF420251 mRNA. Translation: AAL16036.1.
AY033645 mRNA. Translation: AAK59381.1.
AK034476 mRNA. Translation: BAC28722.1.
AK152061 mRNA. Translation: BAE30917.1.
AK152184 mRNA. Translation: BAE31015.1.
AK151026 mRNA. Translation: BAE30044.1.
BC004657 mRNA. Translation: AAH04657.1.
U17698 mRNA. Translation: AAB00373.1. Sequence problems.
CCDSiCCDS38058.1. [Q8CBW3-5]
CCDS38059.1. [Q8CBW3-3]
CCDS38060.1. [Q8CBW3-2]
CCDS38061.1. [Q8CBW3-1]
CCDS50513.1. [Q8CBW3-4]
RefSeqiNP_001070658.1. NM_001077190.2. [Q8CBW3-1]
NP_001070660.1. NM_001077192.2. [Q8CBW3-2]
NP_001070661.1. NM_001077193.2. [Q8CBW3-5]
NP_031406.2. NM_007380.3. [Q8CBW3-4]
UniGeneiMm.205647.
Mm.249752.

Genome annotation databases

EnsembliENSMUST00000114544; ENSMUSP00000110191; ENSMUSG00000058835. [Q8CBW3-5]
ENSMUST00000123948; ENSMUSP00000118491; ENSMUSG00000058835. [Q8CBW3-1]
ENSMUST00000126112; ENSMUSP00000117335; ENSMUSG00000058835. [Q8CBW3-3]
ENSMUST00000140164; ENSMUSP00000120462; ENSMUSG00000058835. [Q8CBW3-4]
ENSMUST00000149719; ENSMUSP00000120621; ENSMUSG00000058835. [Q8CBW3-2]
GeneIDi11308.
KEGGimmu:11308.
UCSCiuc008ins.1. mouse. [Q8CBW3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF420251 mRNA. Translation: AAL16036.1 .
AY033645 mRNA. Translation: AAK59381.1 .
AK034476 mRNA. Translation: BAC28722.1 .
AK152061 mRNA. Translation: BAE30917.1 .
AK152184 mRNA. Translation: BAE31015.1 .
AK151026 mRNA. Translation: BAE30044.1 .
BC004657 mRNA. Translation: AAH04657.1 .
U17698 mRNA. Translation: AAB00373.1 . Sequence problems.
CCDSi CCDS38058.1. [Q8CBW3-5 ]
CCDS38059.1. [Q8CBW3-3 ]
CCDS38060.1. [Q8CBW3-2 ]
CCDS38061.1. [Q8CBW3-1 ]
CCDS50513.1. [Q8CBW3-4 ]
RefSeqi NP_001070658.1. NM_001077190.2. [Q8CBW3-1 ]
NP_001070660.1. NM_001077192.2. [Q8CBW3-2 ]
NP_001070661.1. NM_001077193.2. [Q8CBW3-5 ]
NP_031406.2. NM_007380.3. [Q8CBW3-4 ]
UniGenei Mm.205647.
Mm.249752.

3D structure databases

ProteinModelPortali Q8CBW3.
SMRi Q8CBW3. Positions 1-154, 409-476.
ModBasei Search...

Protein-protein interaction databases

BioGridi 197905. 7 interactions.
DIPi DIP-29534N.
IntActi Q8CBW3. 30 interactions.
MINTi MINT-128698.

PTM databases

PhosphoSitei Q8CBW3.

Proteomic databases

MaxQBi Q8CBW3.
PaxDbi Q8CBW3.
PRIDEi Q8CBW3.

Protocols and materials databases

DNASUi 11308.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000114544 ; ENSMUSP00000110191 ; ENSMUSG00000058835 . [Q8CBW3-5 ]
ENSMUST00000123948 ; ENSMUSP00000118491 ; ENSMUSG00000058835 . [Q8CBW3-1 ]
ENSMUST00000126112 ; ENSMUSP00000117335 ; ENSMUSG00000058835 . [Q8CBW3-3 ]
ENSMUST00000140164 ; ENSMUSP00000120462 ; ENSMUSG00000058835 . [Q8CBW3-4 ]
ENSMUST00000149719 ; ENSMUSP00000120621 ; ENSMUSG00000058835 . [Q8CBW3-2 ]
GeneIDi 11308.
KEGGi mmu:11308.
UCSCi uc008ins.1. mouse. [Q8CBW3-1 ]

Organism-specific databases

CTDi 10006.
MGIi MGI:104913. Abi1.

Phylogenomic databases

eggNOGi NOG262939.
GeneTreei ENSGT00390000003756.
HOGENOMi HOG000293213.
HOVERGENi HBG050446.
InParanoidi Q8CBW3.
OMAi MPMFDDS.
OrthoDBi EOG7J17ZT.
PhylomeDBi Q8CBW3.
TreeFami TF314303.

Enzyme and pathway databases

Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.

Miscellaneous databases

ChiTaRSi ABI1. mouse.
NextBioi 278608.
PROi Q8CBW3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8CBW3.
Bgeei Q8CBW3.
CleanExi MM_ABI1.
Genevestigatori Q8CBW3.

Family and domain databases

InterProi IPR028457. ABI.
IPR028456. ABI1.
IPR012849. Abl-interactor_HHR_dom.
IPR001452. SH3_domain.
IPR000727. T_SNARE_dom.
[Graphical view ]
PANTHERi PTHR10460. PTHR10460. 1 hit.
PTHR10460:SF2. PTHR10460:SF2. 1 hit.
Pfami PF07815. Abi_HHR. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50002. SH3. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Inhibition of v-Abl transformation in 3T3 cells overexpressing different forms of the Abelson interactor protein Abi-1."
    Ikeguchi A., Yang H.-Y., Gao G., Goff S.P.
    Oncogene 20:4926-4934(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION.
    Strain: BALB/c.
  2. "t(10;11)-acute leukemias with MLL-AF10 and MLL-ABI1 chimeric transcripts: specific expression patterns of ABI1 gene in leukemia and solid tumor cell lines."
    Shibuya N., Taki T., Mugishima H., Chin M., Tsuchida M., Sako M., Kawa K., Ishii E., Miura I., Yanagisawa M., Hayashi Y.
    Genes Chromosomes Cancer 32:1-10(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "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] (ISOFORMS 1 AND 5).
    Strain: C57BL/6J.
    Tissue: Bone marrow and Diencephalon.
  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 3).
  5. "Abl-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the Abl protein, suppresses v-abl transforming activity."
    Shi Y., Alin K., Goff S.P.
    Genes Dev. 9:2583-2597(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 70-360 (ISOFORM 4), FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY, INTERACTION WITH ABL1 AND V-ABL.
  6. Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH EPS8 AND SOS1.
  7. "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase."
    Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H., Shishido T.
    J. Biol. Chem. 278:21685-21692(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ENAH.
  8. "Abl interactor 1 (Abi-1) wave-binding and SNARE domains regulate its nucleocytoplasmic shuttling, lamellipodium localization, and wave-1 levels."
    Echarri A., Lai M.J., Robinson M.R., Pendergast A.M.
    Mol. Cell. Biol. 24:4979-4993(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STX1A; SNAP25; VAMP2 AND WASF1.
  9. "Localization and phosphorylation of Abl-interactor proteins, Abi-1 and Abi-2, in the developing nervous system."
    Courtney K.D., Grove M., Vandongen H., Vandongen A., LaMantia A.-S., Pendergast A.M.
    Mol. Cell. Neurosci. 16:244-257(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  10. "The Abl interactor proteins localize to sites of actin polymerization at the tips of lamellipodia and filopodia."
    Stradal T.E.B., Courtney K.D., Rottner K., Hahne P., Small J.V., Pendergast A.M.
    Curr. Biol. 11:891-895(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia formation."
    Steffen A., Rottner K., Ehinger J., Innocenti M., Scita G., Wehland J., Stradal T.E.B.
    EMBO J. 23:749-759(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF WAVE2 COMPLEX.
    Strain: C57BL/6.
    Tissue: Brain.
  12. "Eps8 controls actin-based motility by capping the barbed ends of actin filaments."
    Disanza A., Carlier M.F., Stradal T.E., Didry D., Frittoli E., Confalonieri S., Croce A., Wehland J., Di Fiore P.P., Scita G.
    Nat. Cell Biol. 6:1180-1188(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EPS8.
  13. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  14. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND TYR-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiABI1_MOUSE
AccessioniPrimary (citable) accession number: Q8CBW3
Secondary accession number(s): Q3U8V0
, Q60747, Q91ZM5, Q923I9, Q99KH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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