Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8CBW3 (ABI1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Abi1
Synonyms:Ssh3bp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 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. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.12

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.12

Subcellular location

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. Ref.8 Ref.10

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

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. Ref.5

Sequence similarities

Belongs to the ABI family.

Contains 1 SH3 domain.

Contains 1 t-SNARE coiled-coil homology domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Nucleus
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
SH3 domain
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular component movement

Inferred from electronic annotation. Source: Ensembl

cellular process

Inferred from direct assay Ref.5. Source: MGI

lamellipodium morphogenesis

Inferred from mutant phenotype PubMed 17664349. Source: MGI

megakaryocyte development

Inferred from mutant phenotype PubMed 17664349. Source: MGI

peptidyl-tyrosine phosphorylation

Inferred from sequence alignment PubMed 17101133. Source: MGI

positive regulation of protein tyrosine kinase activity

Inferred from direct assay Ref.7. Source: GOC

somitogenesis

Inferred from mutant phenotype PubMed 15755804. Source: MGI

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell leading edge

Inferred from direct assay PubMed 16831833PubMed 19200726. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

filopodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

growth cone

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred from sequence alignment PubMed 17101133. Source: MGI

lamellipodium

Inferred from direct assay Ref.7. Source: MGI

neuron projection

Inferred from direct assay PubMed 21795692. Source: BHF-UCL

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionprotein tyrosine kinase activator activity

Inferred from direct assay Ref.7. Source: MGI

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 481480Abl interactor 1
PRO_0000191788

Regions

Domain45 – 10763t-SNARE coiled-coil homology
Domain419 – 47860SH3
Region18 – 7962Required for binding to WASF1
Compositional bias337 – 39155Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue531Phosphotyrosine By similarity
Modified residue1831Phosphoserine Ref.14 Ref.15
Modified residue2131Phosphotyrosine; alternate Ref.15
Modified residue2131Phosphotyrosine; by ABL1; alternate By similarity
Modified residue2161Phosphoserine By similarity
Modified residue2221Phosphoserine By similarity
Modified residue2251Phosphoserine By similarity
Modified residue2961Phosphoserine By similarity
Modified residue4281Phosphotyrosine Ref.13
Modified residue4801Phosphothreonine By similarity

Natural variations

Alternative sequence154 – 1585Missing in isoform 2, isoform 3, isoform 4 and isoform 5.
VSP_010756
Alternative sequence274 – 36289AAPGA…VQENI → V in isoform 5.
VSP_022636
Alternative sequence2741Missing in isoform 2 and isoform 4.
VSP_010757
Alternative sequence333 – 36129Missing in isoform 2.
VSP_010758

Experimental info

Sequence conflict3131A → T in AAH04657. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1654A1E89438BC1D

FASTA48152,288
        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 

« Hide

Isoform 2 (short) [UniParc].

Checksum: 805A2F6072F1D24B
Show »

FASTA44648,512
Isoform 3 [UniParc].

Checksum: B7E38AA1E9ED7FA6
Show »

FASTA47651,661
Isoform 4 (long) [UniParc].

Checksum: A0A613AAD091B0F0
Show »

FASTA47551,590
Isoform 5 [UniParc].

Checksum: 27FAB95E05BCA655
Show »

FASTA38842,548

References

« Hide '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] [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. expand/collapse author list , 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]"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] [Europe PMC] [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] [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001070658.1. NM_001077190.2.
NP_001070660.1. NM_001077192.2.
NP_001070661.1. NM_001077193.2.
NP_031406.2. NM_007380.3.
UniGeneMm.205647.
Mm.249752.

3D structure databases

ProteinModelPortalQ8CBW3.
SMRQ8CBW3. Positions 1-154, 409-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197905. 7 interactions.
DIPDIP-29534N.
IntActQ8CBW3. 30 interactions.
MINTMINT-128698.

PTM databases

PhosphoSiteQ8CBW3.

Proteomic databases

PaxDbQ8CBW3.
PRIDEQ8CBW3.

Protocols and materials databases

DNASU11308.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000114544; ENSMUSP00000110191; ENSMUSG00000058835. [Q8CBW3-5]
ENSMUST00000123948; ENSMUSP00000118491; ENSMUSG00000058835. [Q8CBW3-1]
ENSMUST00000126112; ENSMUSP00000117335; ENSMUSG00000058835. [Q8CBW3-3]
ENSMUST00000140164; ENSMUSP00000120462; ENSMUSG00000058835. [Q8CBW3-4]
ENSMUST00000149719; ENSMUSP00000120621; ENSMUSG00000058835. [Q8CBW3-2]
GeneID11308.
KEGGmmu:11308.
UCSCuc008ins.1. mouse. [Q8CBW3-1]

Organism-specific databases

CTD10006.
MGIMGI:104913. Abi1.

Phylogenomic databases

eggNOGNOG262939.
GeneTreeENSGT00390000003756.
HOGENOMHOG000293213.
HOVERGENHBG050446.
InParanoidQ8CBW3.
OMAVGHGVKE.
OrthoDBEOG7J17ZT.
PhylomeDBQ8CBW3.
TreeFamTF314303.

Gene expression databases

ArrayExpressQ8CBW3.
BgeeQ8CBW3.
CleanExMM_ABI1.
GenevestigatorQ8CBW3.

Family and domain databases

InterProIPR028457. ABI.
IPR028456. ABI1.
IPR012849. Abl-interactor_HHR_dom.
IPR001452. SH3_domain.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERPTHR10460. PTHR10460. 1 hit.
PTHR10460:SF2. PTHR10460:SF2. 1 hit.
PfamPF07815. Abi_HHR. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50002. SH3. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSABI1. mouse.
NextBio278608.
PROQ8CBW3.
SOURCESearch...

Entry information

Entry nameABI1_MOUSE
AccessionPrimary (citable) accession number: Q8CBW3
Secondary accession number(s): Q3U8V0 expand/collapse secondary AC list , Q60747, Q91ZM5, Q923I9, Q99KH4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot