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Q8IZP0 (ABI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
Abl-binding protein 4
Short name=AblBP4
Eps8 SH3 domain-binding protein
Short name=Eps8-binding protein
Nap1-binding protein
Short name=Nap1BP
Spectrin SH3 domain-binding protein 1
e3B1
Gene names
Name:ABI1
Synonyms:SSH3BP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length508 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. May play a role in regulation of 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.14 Ref.17

Subunit structure

Interacts with ABL1, ENAH, STX1A, SNAP25, VAMP2, EPS8, 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 By similarity. Interacts with SOS1, SOS2, GRB2, SPTA1 and the first SH3 domain of NCK1. Isoform 6 does not interact with NCK1. 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.1 Ref.2 Ref.3 Ref.4 Ref.14

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.1

Tissue specificity

Widely expressed, with highest expression in brain. Ref.3

Domain

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

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. Ref.1 Ref.17

Involvement in disease

A chromosomal aberration involving ABI1 is a cause of acute leukemias. Translocation t(10;11)(p11.2;q23) with KMT2A/MLL1. ABI1 isoform 2 was found to be present in acute leukemia KMT2A/MLL1-ABI1 fusion transcript.

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
Chromosomal rearrangement
Polymorphism
   DomainCoiled coil
SH3 domain
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

actin polymerization or depolymerization

Non-traceable author statement PubMed 11516653. Source: UniProtKB

cellular component movement

Inferred from direct assay PubMed 11516653. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

lamellipodium morphogenesis

Inferred from electronic annotation. Source: Ensembl

megakaryocyte development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Traceable author statement Ref.1. Source: ProtInc

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 17101133. Source: MGI

somitogenesis

Inferred from electronic annotation. Source: Ensembl

transmembrane receptor protein tyrosine kinase signaling pathway

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentSCAR complex

Inferred from direct assay PubMed 21107423. Source: UniProt

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum

Traceable author statement Ref.2. Source: ProtInc

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

filopodium

Inferred from direct assay PubMed 11516653. Source: UniProtKB

growth cone

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred from direct assay PubMed 17101133. Source: MGI

lamellipodium

Inferred from direct assay PubMed 11516653. Source: UniProtKB

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_functioncytoskeletal protein binding

Traceable author statement Ref.2. Source: ProtInc

protein complex binding

Inferred from direct assay PubMed 18560548. Source: UniProt

protein tyrosine kinase activator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q8IZP0-1)

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: Q8IZP0-2)

Also known as: long; B48;

The sequence of this isoform differs from the canonical sequence as follows:
     154-158: Missing.
     274-300: Missing.
     301-301: Missing.
     360-388: Missing.
Isoform 3 (identifier: Q8IZP0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     274-300: Missing.
     360-388: Missing.
Isoform 4 (identifier: Q8IZP0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     274-300: Missing.
     301-301: Missing.
     360-388: Missing.
Isoform 5 (identifier: Q8IZP0-5)

The sequence of this isoform differs from the canonical sequence as follows:
     154-158: Missing.
     274-300: Missing.
Isoform 6 (identifier: Q8IZP0-6)

The sequence of this isoform differs from the canonical sequence as follows:
     274-300: Missing.
     301-301: Missing.
Isoform 7 (identifier: Q8IZP0-7)

Also known as: 4;

The sequence of this isoform differs from the canonical sequence as follows:
     274-300: Missing.
     301-301: Missing.
     302-359: Missing.
     360-360: I → V
Isoform 8 (identifier: Q8IZP0-8)

Also known as: 5;

The sequence of this isoform differs from the canonical sequence as follows:
     274-300: Missing.
     301-301: Missing.
     302-359: Missing.
     360-388: Missing.
Isoform 9 (identifier: Q8IZP0-9)

Also known as: 2;

The sequence of this isoform differs from the canonical sequence as follows:
     274-300: Missing.
Isoform 10 (identifier: Q8IZP0-10)

Also known as: B30;

The sequence of this isoform differs from the canonical sequence as follows:
     154-158: Missing.
     274-300: Missing.
     301-301: Missing.
     302-359: Missing.
     360-388: Missing.
     389-389: I → V
Isoform 11 (identifier: Q8IZP0-11)

The sequence of this isoform differs from the canonical sequence as follows:
     96-159: Missing.
     274-300: Missing.
     301-301: Missing.
     302-359: Missing.
     360-388: Missing.
     389-389: I → V
Note: No experimental confirmation available.
Isoform 12 (identifier: Q8IZP0-12)

The sequence of this isoform differs from the canonical sequence as follows:
     38-38: I → IQRHGFAVLLCLLSNSWP
     360-388: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12 Ref.13
Chain2 – 508507Abl interactor 1
PRO_0000191787

Regions

Domain45 – 10763t-SNARE coiled-coil homology
Domain446 – 50560SH3
Region18 – 7962Required for binding to WASF1 By similarity
Compositional bias260 – 418159Pro-rich

Sites

Site95 – 962Breakpoint for translocation to form KMT2A/MLL1-ABI1

Amino acid modifications

Modified residue21N-acetylalanine Ref.13 Ref.24 Ref.25
Modified residue531Phosphotyrosine By similarity
Modified residue1831Phosphoserine Ref.20
Modified residue2131Phosphotyrosine; by ABL1 Ref.17
Modified residue2161Phosphoserine Ref.20
Modified residue2221Phosphoserine Ref.23
Modified residue2251Phosphoserine Ref.16 Ref.18 Ref.19 Ref.21 Ref.23
Modified residue3231Phosphoserine Ref.23
Modified residue4551Phosphotyrosine By similarity
Modified residue5071Phosphothreonine Ref.21

Natural variations

Alternative sequence381I → IQRHGFAVLLCLLSNSWP in isoform 12.
VSP_044604
Alternative sequence96 – 15964Missing in isoform 11.
VSP_043403
Alternative sequence154 – 1585Missing in isoform 2, isoform 5 and isoform 10.
VSP_010749
Alternative sequence274 – 30027Missing in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 11.
VSP_010750
Alternative sequence3011Missing in isoform 2, isoform 4, isoform 6, isoform 7, isoform 8, isoform 10 and isoform 11.
VSP_010751
Alternative sequence302 – 35958Missing in isoform 7, isoform 8, isoform 10 and isoform 11.
VSP_010754
Alternative sequence360 – 38829Missing in isoform 2, isoform 3, isoform 4, isoform 8, isoform 10, isoform 11 and isoform 12.
VSP_010752
Alternative sequence3601I → V in isoform 7.
VSP_010755
Alternative sequence3891I → V in isoform 10 and isoform 11.
VSP_010753
Natural variant3311G → A.
Corresponds to variant rs2306236 [ dbSNP | Ensembl ].
VAR_048159

Experimental info

Sequence conflict1771P → L in AAC39757. Ref.2
Sequence conflict4101S → F in AAC39757. Ref.2
Sequence conflict4101S → F in AAN28379. Ref.4
Sequence conflict4371D → G in BAG54374. Ref.8

Sequences

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

Last modified January 23, 2007. Version 4.
Checksum: 2D76F305934127CB

FASTA50855,081
        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 
PPSPPMSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS 

       250        260        270        280        290        300 
GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT IGPENISVPP PSGAPPAPPL APLLPVSTVI 

       310        320        330        340        350        360 
AAPGSAPGSQ YGTMTRQISR HNSTTSSTSS GGYRRTPSVT AQFSAQPHVN GGPLYSQNSI 

       370        380        390        400        410        420 
SIAPPPPPMP QLTPQIPLTG FVARVQENIA DSPTPPPPPP PDDIPMFDDS PPPPPPPPVD 

       430        440        450        460        470        480 
YEDEEAAVVQ YNDPYADGDP AWAPKNYIEK VVAIYDYTKD KDDELSFMEG AIIYVIKKND 

       490        500 
DGWYEGVCNR VTGLFPGNYV ESIMHYTD 

« Hide

Isoform 2 (long) (B48) [UniParc].

Checksum: FEDF9B1991B89955
Show »

FASTA44648,678
Isoform 3 [UniParc].

Checksum: 558B171EB1EABED4
Show »

FASTA45249,376
Isoform 4 [UniParc].

Checksum: 796AE1E3CA14C07B
Show »

FASTA45149,305
Isoform 5 [UniParc].

Checksum: 0321298AEFF40B9D
Show »

FASTA47651,841
Isoform 6 [UniParc].

Checksum: 4EA3699ECE77EE0E
Show »

FASTA48052,397
Isoform 7 (4) [UniParc].

Checksum: 16FAAB5B29D7E506
Show »

FASTA42246,386
Isoform 8 (5) [UniParc].

Checksum: 522FF3E0941EE851
Show »

FASTA39343,309
Isoform 9 (2) [UniParc].

Checksum: A29602C39221C826
Show »

FASTA48152,468
Isoform 10 (B30) [UniParc].

Checksum: E63747A11D358E42
Show »

FASTA38842,668
Isoform 11 [UniParc].

Checksum: 5895AC905A5773F7
Show »

FASTA32935,920
Isoform 12 [UniParc].

Checksum: B6D85C58732FB5E2
Show »

FASTA49653,912

References

« Hide 'large scale' references
[1]"Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth."
Biesova Z., Piccoli C., Wong W.T.
Oncogene 14:233-241(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH EPS8 AND ABL1.
[2]"Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton."
Ziemnicka-Kotula D., Xu J., Gu H., Potempska A., Kim K.S., Jenkins E.C., Trenkner E., Kotula L.
J. Biol. Chem. 273:13681-13692(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS 3; 7; 8 AND 9), INTERACTION WITH SPTA1.
[3]"Isolation of hNap1BP which interacts with human Nap 1 (NCKAP1) whose expression is down-regulated in Alzheimer's disease."
Yamamoto A., Suzuki T., Sakaki Y.
Gene 271:159-169(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, INTERACTION WITH ABL1; NAP1 AND NCK1.
[4]"Induction of colonic epithelial cell apoptosis by p47-dependent oxidants(1)."
Gu Y., Souza R.F., Wu R.F., Xu Y.C., Terada L.S.
FEBS Lett. 540:195-200(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH NCF1.
Tissue: Umbilical vein endothelial cell.
[5]"A new member of the Abl interactor protein family, AblBP4."
Wilson L.A., Fields D., Cruz L., Friesen J., Siminovitch K.A.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: T-cell.
[6]"In silico cloning of the human SSH3BP1/e3B1 gene."
Chikri M.M., Boutin M.P., Vaxillaire M.M., Froguel M.P.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]Quackenbush R.C., Pendergast A.M.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[8]"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. expand/collapse author list , 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] (ISOFORMS 2; 11 AND 12).
Tissue: Cerebellum.
[9]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]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. expand/collapse author list , 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].
[11]"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 5).
Tissue: Muscle.
[12]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-17.
Tissue: Platelet.
[13]Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-17; 139-154; 229-237 AND 451-477, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hepatoma.
[14]"Abl interactor 1 binds to sos and inhibits epidermal growth factor- and v-Abl-induced activation of extracellular signal-regulated kinases."
Fan P.-D., Goff S.P.
Mol. Cell. Biol. 20:7591-7601(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SOS1; SOS2 AND GRB2.
[15]"ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL gene in acute myeloid leukemia with t(10;11)(p11.2;q23)."
Taki T., Shibuya N., Taniwaki M., Hanada R., Morishita K., Bessho F., Yanagisawa M., Hayashi Y.
Blood 92:1125-1130(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 2 AND 10), CHROMOSOMAL TRANSLOCATION WITH KMT2A.
[16]"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-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinase by phosphopeptides derived from Abi1/Hssh3bp1."
Xiong X., Cui P., Hossain S., Xu R., Warner B., Guo X., An X., Debnath A.K., Cowburn D., Kotula L.
Biochim. Biophys. Acta 1783:737-747(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-213.
[18]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[19]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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 SER-225 AND THR-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-225 AND SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF006516 mRNA. Translation: AAB62569.1.
U87166 mRNA. Translation: AAC39757.1.
AB040151 mRNA. Translation: BAB55675.1.
AF540955 mRNA. Translation: AAN28379.1.
AF001628 mRNA. Translation: AAD00897.1.
AJ277065 expand/collapse EMBL AC list , AJ277066, AJ277067, AJ277068, AJ277069, AJ277070, AJ277071, AJ277072, AJ277073, AJ277074 Genomic DNA. Translation: CAB88006.1.
AF260262 mRNA. Translation: AAF70309.1.
AK126803 mRNA. Translation: BAG54374.1.
AK298646 mRNA. Translation: BAG60820.1.
AK291823 mRNA. Translation: BAF84512.1.
AL139404, AL390961 Genomic DNA. Translation: CAH73112.1.
AL139404, AL390961 Genomic DNA. Translation: CAH73113.1.
AL139404, AL390961 Genomic DNA. Translation: CAH73114.1.
AL139404, AL390961 Genomic DNA. Translation: CAH73115.1.
AL139404, AL390961 Genomic DNA. Translation: CAH73116.1.
AL139404, AL390961 Genomic DNA. Translation: CAH73117.1.
AL139404, AL390961 Genomic DNA. Translation: CAH73118.1.
AL139404, AL390961 Genomic DNA. Translation: CAH73119.1.
AL390961, AL139404 Genomic DNA. Translation: CAI17272.1.
AL390961, AL139404 Genomic DNA. Translation: CAI17273.1.
AL390961, AL139404 Genomic DNA. Translation: CAI17274.1.
AL390961, AL139404 Genomic DNA. Translation: CAI17275.1.
AL390961, AL139404 Genomic DNA. Translation: CAI17276.1.
AL390961, AL139404 Genomic DNA. Translation: CAI17277.1.
AL390961, AL139404 Genomic DNA. Translation: CAI17278.1.
AL390961, AL139404 Genomic DNA. Translation: CAI17279.1.
CH471072 Genomic DNA. Translation: EAW86079.1.
CH471072 Genomic DNA. Translation: EAW86080.1.
BC024254 mRNA. Translation: AAH24254.1.
RefSeqNP_001012768.1. NM_001012750.2.
NP_001012769.1. NM_001012751.2.
NP_001012770.1. NM_001012752.2.
NP_001171587.1. NM_001178116.1.
NP_001171590.1. NM_001178119.1.
NP_001171591.1. NM_001178120.1.
NP_001171592.1. NM_001178121.1.
NP_001171593.1. NM_001178122.1.
NP_001171594.1. NM_001178123.1.
NP_001171595.1. NM_001178124.1.
NP_001171596.1. NM_001178125.1.
NP_005461.2. NM_005470.3.
UniGeneHs.508148.

3D structure databases

ProteinModelPortalQ8IZP0.
SMRQ8IZP0. Positions 1-154, 436-503.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115324. 24 interactions.
DIPDIP-31118N.
IntActQ8IZP0. 61 interactions.
MINTMINT-106609.

PTM databases

PhosphoSiteQ8IZP0.

Polymorphism databases

DMDM50400546.

Proteomic databases

PaxDbQ8IZP0.
PRIDEQ8IZP0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346832; ENSP00000279599; ENSG00000136754. [Q8IZP0-12]
ENST00000359188; ENSP00000352114; ENSG00000136754. [Q8IZP0-6]
ENST00000376138; ENSP00000365308; ENSG00000136754. [Q8IZP0-3]
ENST00000376139; ENSP00000365309; ENSG00000136754. [Q8IZP0-5]
ENST00000376140; ENSP00000365310; ENSG00000136754. [Q8IZP0-9]
ENST00000376142; ENSP00000365312; ENSG00000136754. [Q8IZP0-1]
ENST00000376166; ENSP00000365336; ENSG00000136754. [Q8IZP0-2]
ENST00000376170; ENSP00000365340; ENSG00000136754. [Q8IZP0-4]
ENST00000490841; ENSP00000440101; ENSG00000136754. [Q8IZP0-11]
GeneID10006.
KEGGhsa:10006.
UCSCuc001isx.3. human. [Q8IZP0-1]
uc001isy.3. human. [Q8IZP0-9]
uc001isz.3. human. [Q8IZP0-5]
uc001ita.3. human. [Q8IZP0-3]
uc001itc.3. human. [Q8IZP0-6]
uc001itd.3. human. [Q8IZP0-4]
uc001ite.3. human. [Q8IZP0-2]
uc010qdh.2. human. [Q8IZP0-10]
uc010qdi.2. human. [Q8IZP0-11]

Organism-specific databases

CTD10006.
GeneCardsGC10M027075.
HGNCHGNC:11320. ABI1.
HPACAB008375.
HPA029973.
MIM603050. gene.
neXtProtNX_Q8IZP0.
PharmGKBPA36144.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262939.
HOVERGENHBG050446.
OrthoDBEOG7J17ZT.
PhylomeDBQ8IZP0.
TreeFamTF314303.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ8IZP0.

Gene expression databases

ArrayExpressQ8IZP0.
BgeeQ8IZP0.
GenevestigatorQ8IZP0.

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. human.
GeneWikiABI1.
GenomeRNAi10006.
NextBio37795.
PROQ8IZP0.
SOURCESearch...

Entry information

Entry nameABI1_HUMAN
AccessionPrimary (citable) accession number: Q8IZP0
Secondary accession number(s): A9Z1Y6 expand/collapse secondary AC list , B3KX62, B4DQ58, H7BXI6, O15147, O76049, O95060, Q5T2R3, Q5T2R4, Q5T2R6, Q5T2R7, Q5T2R9, Q5W070, Q5W072, Q8TB63, Q96S81, Q9NXZ9, Q9NYB8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 125 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM