Reviewed, UniProtKB/Swiss-Prot Q8CBW3 (ABI1_MOUSE)

Names and origin

Protein names

Recommended name:
    Abl interactor 1
Alternative name(s):
    Abelson interactor 1
      Short name=Abi-1
    Spectrin SH3 domain-binding protein 1
    Eps8 SH3 domain-binding protein
      Short name=Eps8-binding protein
    e3B1
    Ablphilin-1

Gene names

Name:	Abi1
Synonyms:	Ssh3bp1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 MENA By similarity. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level.
Subunit structure	Interacts with MENA, 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.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Cell projection › lamellipodium By similarity. Cell projection › filopodium By similarity. Cell projection › growth cone By similarity. Cell junction › synapse › synaptosome By similarity. Cytoplasm › cytoskeleton By similarity. Note: Localized to protruding lamellipodia and filopodia tips. Also localized to neuronal growth cones and synaptosomes By similarity.
Tissue specificity	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. Ref.5 Ref.9
Developmental stage	Detected at E10 and E12 in developing brain, but does not appear more prominent in the neuroepithelium compared to the surrounding tissue. Ref.9
Domain	The t-SNARE coiled-coil homology domain is necessary and sufficient for interaction with STX1A.
Post-translational modification	In vitro substrate for v-Abl. Phosphorylated on tyrosine residues after serum stimulation or induction by v-Abl By similarity.
Sequence similarities	Belongs to the ABI family. Contains 1 SH3 domain. Contains 1 t-SNARE coiled-coil homology domain.

Ontologies

Keywords
Cellular component	Cell junction Cell projection Cytoplasm Cytoskeleton Nucleus Synapse Synaptosome
Coding sequence diversity	Alternative splicing
Domain	Coiled coil SH3 domain
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	cellular process Ref.5 Inferred from direct assay. Source: MGI somitogenesis Inferred from mutant phenotype. Source: MGI
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell filopodium Inferred from electronic annotation. Source: UniProtKB-SubCell growth cone Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Ref.7 Inferred from direct assay. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: UniProtKB-KW synaptosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct protein tyrosine kinase activator activity Ref.7 Inferred from direct assay. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABL1	P00519	1	EBI-375511,EBI-375543	From a different organism.
EPS8	Q12929	1	EBI-375511,EBI-375576	From a different organism.
Eps8	Q08509	1	EBI-375511,EBI-375596
Prpf40a	Q9R1C7-1	2	EBI-375511,EBI-645566

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8CBW3-1)

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.

Isoform 2 (identifier: Q8CBW3-2)

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.

Isoform 3 (identifier: Q8CBW3-3)

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

Isoform 4 (identifier: Q8CBW3-4)

Also known as: long;

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

Isoform 5 (identifier: Q8CBW3-5)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 481	480	Abl interactor 1		PRO_0000191788
Regions
	Domain	45 – 107	63	t-SNARE coiled-coil homology
	Domain	419 – 478	60	SH3
	Region	18 – 79	62	Required for binding to WASF1
	Compositional bias	337 – 391	55	Pro-rich
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	183	1	Phosphoserine Ref.14 Ref.15 Ref.16 Ref.17
	Modified residue	213	1	Phosphotyrosine Ref.17 Ref.12
	Modified residue	216	1	Phosphoserine By similarity
	Modified residue	222	1	Phosphoserine Ref.15 Ref.16
	Modified residue	225	1	Phosphoserine By similarity
	Modified residue	306	1	Phosphotyrosine By similarity
	Modified residue	428	1	Phosphotyrosine Ref.13
Natural variations
	Alternative sequence	154 – 158	5	Missing in isoform 2, isoform 3, isoform 4 and isoform 5.		VSP_010756
	Alternative sequence	274 – 362	89	AAPGA…VQENI → V in isoform 5.		VSP_022636
	Alternative sequence	274	1	Missing in isoform 2 and isoform 4.		VSP_010757
	Alternative sequence	333 – 361	29	Missing in isoform 2.		VSP_010758
Experimental info
	Sequence conflict	313	1	A → T in AAH04657. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1654A1E89438BC1D	FASTA	481	52,288
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK 190 200 210 220 230 240 PPSPPVSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS 250 260 270 280 290 300 GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT AGPAAPGAAP GSQYGTMTRQ ISRHNSTTSS 310 320 330 340 350 360 TSSGGYRRTP SVAAQFSAQP HVNGGPLYSQ NSISVAPPPP PMPQLTPQIP LTGFVARVQE 370 380 390 400 410 420 NIADSPTPPP PPPPDDIPMF DDSPPPPPPP PVDYEDEEAA VVQYSDPYAD GDPAWAPKNY 430 440 450 460 470 480 IEKVVAIYDY TKDKDDELSF KEGAIIYVIK KNDDGWFEGV CNRVTGLFPG NYVESIMHYT D
	Isoform 2 (short). Checksum: 805A2F6072F1D24B	FASTA	446	48,512
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKHGNNQP ARTGTLSRTN PPTQKPPSPP 190 200 210 220 230 240 VSGRGTLGRN TPYKTLEPVK PPTVPNDYMT SPARLGSQHS PGRTASLNQR PRTHSGSSGG 250 260 270 280 290 300 SGSRENSGSS SIGIPIAVPT PSPPTAGPAP GAAPGSQYGT MTRQISRHNS TTSSTSSGGY 310 320 330 340 350 360 RRTPSVAAQF SAQPHVNGGP LYSQNSIADS PTPPPPPPPD DIPMFDDSPP PPPPPPVDYE 370 380 390 400 410 420 DEEAAVVQYS DPYADGDPAW APKNYIEKVV AIYDYTKDKD DELSFKEGAI IYVIKKNDDG 430 440 WFEGVCNRVT GLFPGNYVES IMHYTD
	Isoform 3. Checksum: B7E38AA1E9ED7FA6	FASTA	476	51,661
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKHGNNQP ARTGTLSRTN PPTQKPPSPP 190 200 210 220 230 240 VSGRGTLGRN TPYKTLEPVK PPTVPNDYMT SPARLGSQHS PGRTASLNQR PRTHSGSSGG 250 260 270 280 290 300 SGSRENSGSS SIGIPIAVPT PSPPTAGPAA PGAAPGSQYG TMTRQISRHN STTSSTSSGG 310 320 330 340 350 360 YRRTPSVAAQ FSAQPHVNGG PLYSQNSISV APPPPPMPQL TPQIPLTGFV ARVQENIADS 370 380 390 400 410 420 PTPPPPPPPD DIPMFDDSPP PPPPPPVDYE DEEAAVVQYS DPYADGDPAW APKNYIEKVV 430 440 450 460 470 AIYDYTKDKD DELSFKEGAI IYVIKKNDDG WFEGVCNRVT GLFPGNYVES IMHYTD
	Isoform 4 (long). Checksum: A0A613AAD091B0F0	FASTA	475	51,590
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKHGNNQP ARTGTLSRTN PPTQKPPSPP 190 200 210 220 230 240 VSGRGTLGRN TPYKTLEPVK PPTVPNDYMT SPARLGSQHS PGRTASLNQR PRTHSGSSGG 250 260 270 280 290 300 SGSRENSGSS SIGIPIAVPT PSPPTAGPAP GAAPGSQYGT MTRQISRHNS TTSSTSSGGY 310 320 330 340 350 360 RRTPSVAAQF SAQPHVNGGP LYSQNSISVA PPPPPMPQLT PQIPLTGFVA RVQENIADSP 370 380 390 400 410 420 TPPPPPPPDD IPMFDDSPPP PPPPPVDYED EEAAVVQYSD PYADGDPAWA PKNYIEKVVA 430 440 450 460 470 IYDYTKDKDD ELSFKEGAII YVIKKNDDGW FEGVCNRVTG LFPGNYVESI MHYTD
	Isoform 5. Checksum: 27FAB95E05BCA655	FASTA	388	42,548
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKHGNNQP ARTGTLSRTN PPTQKPPSPP 190 200 210 220 230 240 VSGRGTLGRN TPYKTLEPVK PPTVPNDYMT SPARLGSQHS PGRTASLNQR PRTHSGSSGG 250 260 270 280 290 300 SGSRENSGSS SIGIPIAVPT PSPPTAGPVA DSPTPPPPPP PDDIPMFDDS PPPPPPPPVD 310 320 330 340 350 360 YEDEEAAVVQ YSDPYADGDP AWAPKNYIEK VVAIYDYTKD KDDELSFKEG AIIYVIKKND 370 380 DGWFEGVCNR VTGLFPGNYV ESIMHYTD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11526477] [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: 11477655] [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: 16141072] [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: 15489334] [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: 7590237] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 70-360 (ISOFORM 4), FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY, INTERACTION WITH ABL1 AND V-ABL.
[6]	"EPS8 and E3B1 transduce signals from Ras to Rac." Scita G., Nordstrom J., Carbone R., Tenca P., Giardina G., Gutkind S., Bjarnegard M., Betsholtz C., Di Fiore P.P. Nature 401:290-293(1999) [PubMed: 10499589] [Abstract] 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: 12672821] [Abstract] Cited for: FUNCTION, INTERACTION WITH MENA.
[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: 15143189] [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: 10995551] [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: 11516653] [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: 14765121] [Abstract] Cited for: COMPONENT OF WAVE2 COMPLEX. Strain: C57BL/6. Tissue: Brain.
[12]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213, MASS SPECTROMETRY.
[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: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-428, MASS SPECTROMETRY. Tissue: Brain.
[14]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, MASS SPECTROMETRY. Tissue: Brain cortex.
[15]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-222, MASS SPECTROMETRY.
[16]	"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: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-222, MASS SPECTROMETRY. Tissue: Macrophage.
[17]	"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: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND TYR-213, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00454179. IPI00551347. IPI00653749. IPI00659927. IPI00798483.
RefSeq	NP_001070658.1. NP_001070660.1. NP_001070661.1. NP_031406.2.
UniGene	Mm.205647 Mm.249752
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8CBW3. 22 interactions.
STRING	Q8CBW3.
PTM databases
PhosphoSite	Q8CBW3.
Proteomic databases
PRIDE	Q8CBW3.
Genome annotation databases
Ensembl	ENSMUST00000078977; ENSMUSP00000077997; ENSMUSG00000058835; Mus musculus. [Genome view] ENSMUST00000091394; ENSMUSP00000088957; ENSMUSG00000058835; Mus musculus. [Genome view] ENSMUST00000093171; ENSMUSP00000090860; ENSMUSG00000058835; Mus musculus. [Genome view] ENSMUST00000114544; ENSMUSP00000110191; ENSMUSG00000058835; Mus musculus. [Genome view]
GeneID	11308.
KEGG	mmu:11308.
UCSC	uc008ins.1. mouse. uc008int.1. mouse. uc008inu.1. mouse. uc008inv.1. mouse.
Organism-specific databases
CTD	11308.
MGI	MGI:104913. Abi1.
Phylogenomic databases
HOGENOM	Q8CBW3.
HOVERGEN	Q8CBW3.
OMA	IADSPTP
Gene expression databases
ArrayExpress	Q8CBW3.
Bgee	Q8CBW3.
CleanEx	MM_ABI1.
Genevestigator	Q8CBW3.
Family and domain databases
InterPro	IPR012849. Abl-interactor_HHR. IPR000108. Neu_cyt_fact_2. IPR001452. SH3_domain. IPR020473. SH3_region. IPR000727. T_SNARE. [Graphical view]
Pfam	PF07815. Abi_HHR. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00499. P67PHOX. PR00452. SH3DOMAIN.
SMART	SM00326. SH3. 1 hit. [Graphical view]
PROSITE	PS50002. SH3. 1 hit. PS50192. T_SNARE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	278608.
SOURCE	Search...

Entry information

Entry name

ABI1_MOUSE

Accession

Primary (citable) accession number: Q8CBW3
Secondary accession number(s): Q3U8V0 , Q60747, Q91ZM5, Q923I9, Q99KH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 81 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)