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Q9NYB9 (ABI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 2
Alternative name(s):
Abelson interactor 2
Short name=Abi-2
Abl-binding protein 3
Short name=AblBP3
Arg-binding protein 1
Short name=ArgBP1
Gene names
Name:ABI2
Synonyms:ARGBPIA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May act in regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Regulates ABL1/c-Abl-mediated phosphorylation of MENA. Ref.1 Ref.3 Ref.7

Subunit structure

Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterdimer containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by WAVE1, ABI2 and BRK1. CYFIP2 binds to activated RAC1 which causes the complex to dissociate, releasing activated WASF1. The complex can also be activated by NCK1 By similarity. Interacts with ABL1 and ABL2. Ref.1 Ref.3 Ref.14

Subcellular location

Cytoplasm By similarity Ref.1 Ref.8.

Isoform 1: Cell projectionlamellipodium By similarity. Cell projectionfilopodium By similarity. Cytoplasmcytoskeleton By similarity. Note: Isoform 1 but not isoform 3 is localized to protruding lamellipodia and filopodia tips By similarity. Ref.1 Ref.8

Post-translational modification

Is a substrate for ABL1.

Sequence similarities

Belongs to the ABI family.

Contains 1 SH3 domain.

Contains 1 t-SNARE coiled-coil homology domain.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
SH3 domain
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRac protein signal transduction

Inferred from direct assay Ref.14. Source: UniProt

actin polymerization or depolymerization

Non-traceable author statement Ref.8. Source: UniProtKB

camera-type eye development

Inferred from electronic annotation. Source: Ensembl

cell migration

Traceable author statement PubMed 12011975. Source: UniProtKB

cellular component movement

Inferred from direct assay Ref.8. Source: UniProtKB

cytoskeleton organization

Traceable author statement PubMed 12011975. Source: UniProtKB

dendrite development

Inferred from electronic annotation. Source: Ensembl

learning or memory

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 17101133. Source: MGI

positive regulation of Arp2/3 complex-mediated actin nucleation

Inferred from direct assay Ref.14. Source: UniProt

   Cellular_componentSCAR complex

Inferred from direct assay Ref.14. Source: UniProt

cell-cell adherens junction

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Traceable author statement Ref.3. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay PubMed 18632609. Source: BHF-UCL

dendrite

Inferred from electronic annotation. Source: Ensembl

filopodium

Inferred from direct assay Ref.8. Source: UniProtKB

lamellipodium

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement Ref.1. Source: ProtInc

SH3 domain binding

Inferred from physical interaction Ref.1. Source: UniProtKB

cytoskeletal adaptor activity

Traceable author statement PubMed 12011975. Source: UniProtKB

kinase binding

Non-traceable author statement Ref.3. Source: UniProtKB

proline-rich region binding

Inferred from physical interaction Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17101133PubMed 19523119. Source: IntAct

protein complex binding

Inferred from direct assay Ref.14. Source: UniProt

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 18632609. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABL1P005192EBI-743598,EBI-375543
Caskin1Q8VHK23EBI-743598,EBI-7049475From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NYB9-1)

Also known as: Abi-2b;

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: Q9NYB9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     154-159: Missing.
     284-344: Missing.
     399-399: S → SLAPPPPSILQVTPQLPLMGFVARVQENIS
Isoform 3 (identifier: Q9NYB9-3)

Also known as: Abi-2a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.
     46-95: ALEETKAYTT...MESSINHISQ → MSCRCWISRH...GNNCSLRLNE
     154-159: Missing.
     284-344: Missing.
Isoform 4 (identifier: Q9NYB9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     154-159: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 513513Abl interactor 2
PRO_0000191790

Regions

Domain45 – 10763t-SNARE coiled-coil homology
Domain451 – 51060SH3
Compositional bias172 – 423252Pro-rich

Amino acid modifications

Modified residue2271Phosphoserine Ref.9 Ref.10 Ref.12
Modified residue3681Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 4545Missing in isoform 3.
VSP_010759
Alternative sequence46 – 9550ALEET…NHISQ → MSCRCWISRHPSYEGWNLQS IIFHKQIRGVDLESTFVTKF GNNCSLRLNE in isoform 3.
VSP_010760
Alternative sequence154 – 1596Missing in isoform 2, isoform 3 and isoform 4.
VSP_010761
Alternative sequence284 – 34461Missing in isoform 2 and isoform 3.
VSP_010762
Alternative sequence3991S → SLAPPPPSILQVTPQLPLMG FVARVQENIS in isoform 2.
VSP_010763

Experimental info

Sequence conflict221S → R in CAA64885. Ref.3
Sequence conflict691A → D in CAA64885. Ref.3
Sequence conflict2431S → T in AAA75446. Ref.2
Sequence conflict2491G → P in AAA92289. Ref.1
Sequence conflict3171N → D in BAG61693. Ref.5
Sequence conflict324 – 3252PN → QT in BAG61693. Ref.5
Sequence conflict4321A → V in AAA75446. Ref.2
Sequence conflict5001F → S in AAA75446. Ref.2

Secondary structure

.................... 513
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Abi-2b) [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 822983A69E5EA512

FASTA51355,663
        10         20         30         40         50         60 
MAELQMLLEE EIPGGRRALF DSYTNLERVA DYCENNYIQS ADKQRALEET KAYTTQSLAS 

        70         80         90        100        110        120 
VAYLINTLAN NVLQMLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 

       130        140        150        160        170        180 
THKIIAPANL ERPVRYIRKP IDYTILDDIG HGVKWLLRFK VSTQNMKMGG LPRTTPPTQK 

       190        200        210        220        230        240 
PPSPPMSGKG TLGRHSPYRT LEPVRPPVVP NDYVPSPTRN MAPSQQSPVR TASVNQRNRT 

       250        260        270        280        290        300 
YSSSGSSGGS HPSSRSSSRE NSGSGSVGVP IAVPTPSPPS VFPAPAGSAG TPPLPATSAS 

       310        320        330        340        350        360 
APAPLVPATV PSSTAPNAAA GGAPNLADGF TSPTPPVVSS TPPTGHPVQF YSMNRPASRH 

       370        380        390        400        410        420 
TPPTIGGSLP YRRPPSITSQ TSLQNQMNGG PFYSQNPVSD TPPPPPPVEE PVFDESPPPP 

       430        440        450        460        470        480 
PPPEDYEEEE AAVVEYSDPY AEEDPPWAPR SYLEKVVAIY DYTKDKEDEL SFQEGAIIYV 

       490        500        510 
IKKNDDGWYE GVMNGVTGLF PGNYVESIMH YSE 

« Hide

Isoform 2 [UniParc].

Checksum: 3AF8B713FD40FA90
Show »

FASTA47552,446
Isoform 3 (Abi-2a) [UniParc].

Checksum: 5D009A269B2B2FFF
Show »

FASTA40144,409
Isoform 4 [UniParc].

Checksum: C0CE1E991D695FC1
Show »

FASTA50754,819

References

« Hide 'large scale' references
[1]"Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity."
Dai Z., Pendergast A.M.
Genes Dev. 9:2569-2582(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH ABL1.
[2]"Cloning of a binding substrate of the Abl protein tyrosine kinase."
Ren R.
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Identification of ArgBP1, an Arg protein tyrosine kinase binding protein that is the human homologue of a CNS-specific Xenopus gene."
Wang B., Mysliwiec T., Krainc D., Jensen R.A., Sonoda G., Testa J.R., Golemis E.A., Kruh G.D.
Oncogene 12:1921-1929(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH ABL2.
Tissue: Brain.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"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] (ISOFORM 4).
Tissue: Brain.
[6]"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 2).
Tissue: Placenta.
[7]"Drosophila abelson interacting protein (dAbi) is a positive regulator of abelson tyrosine kinase activity."
Juang J.L., Hoffmann F.M.
Oncogene 18:5138-5147(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"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.
[9]"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-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-227 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Solution structure of the SH3 domain of Abl interactor 2 (Abelson interactor 2)."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 444-508.
[14]"Structure and control of the actin regulatory WAVE complex."
Chen Z., Borek D., Padrick S.B., Gomez T.S., Metlagel Z., Ismail A.M., Umetani J., Billadeau D.D., Otwinowski Z., Rosen M.K.
Nature 468:533-538(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-164, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U23435 mRNA. Translation: AAA92289.1.
U31089 mRNA. Translation: AAA75446.1.
AF260261 mRNA. Translation: AAF70308.1.
X95632 mRNA. Translation: CAA64885.1.
BT009920 mRNA. Translation: AAP88922.1.
AK299824 mRNA. Translation: BAG61693.1.
BC001439 mRNA. Translation: AAH01439.1.
CCDSCCDS2358.1. [Q9NYB9-2]
CCDS63093.1. [Q9NYB9-1]
CCDS63094.1. [Q9NYB9-4]
CCDS63096.1. [Q9NYB9-3]
PIRG01936.
RefSeqNP_001269854.1. NM_001282925.1.
NP_001269855.1. NM_001282926.1.
NP_001269856.1. NM_001282927.1. [Q9NYB9-3]
NP_005750.4. NM_005759.5. [Q9NYB9-2]
XP_006712248.1. XM_006712185.1. [Q9NYB9-3]
UniGeneHs.471156.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ED0NMR-A444-508[»]
3P8CX-ray2.29F1-164[»]
4N78X-ray2.43F1-513[»]
ProteinModelPortalQ9NYB9.
SMRQ9NYB9. Positions 1-154, 444-508.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115454. 21 interactions.
DIPDIP-37566N.
IntActQ9NYB9. 23 interactions.
MINTMINT-252647.
STRING9606.ENSP00000261017.

PTM databases

PhosphoSiteQ9NYB9.

Polymorphism databases

DMDM50400673.

Proteomic databases

MaxQBQ9NYB9.
PaxDbQ9NYB9.
PRIDEQ9NYB9.

Protocols and materials databases

DNASU10152.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261016; ENSP00000261016; ENSG00000138443. [Q9NYB9-3]
ENST00000261017; ENSP00000261017; ENSG00000138443. [Q9NYB9-2]
ENST00000424558; ENSP00000391433; ENSG00000138443.
GeneID10152.
KEGGhsa:10152.
UCSCuc002uzz.3. human. [Q9NYB9-2]
uc002vab.3. human. [Q9NYB9-3]

Organism-specific databases

CTD10152.
GeneCardsGC02P204192.
H-InvDBHIX0002759.
HGNCHGNC:24011. ABI2.
MIM606442. gene.
neXtProtNX_Q9NYB9.
PharmGKBPA134977642.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262939.
HOGENOMHOG000293213.
HOVERGENHBG050446.
InParanoidQ9NYB9.
KOK05751.
PhylomeDBQ9NYB9.
TreeFamTF314303.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9NYB9.
BgeeQ9NYB9.
CleanExHS_ABI2.
GenevestigatorQ9NYB9.

Family and domain databases

InterProIPR028457. ABI.
IPR028454. Abi2.
IPR012849. Abl-interactor_HHR_dom.
IPR001452. SH3_domain.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERPTHR10460. PTHR10460. 1 hit.
PTHR10460:SF3. PTHR10460:SF3. 1 hit.
PfamPF07815. Abi_HHR. 1 hit.
PF14604. SH3_9. 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

ChiTaRSABI2. human.
EvolutionaryTraceQ9NYB9.
GeneWikiABI2.
GenomeRNAi10152.
NextBio38426.
PROQ9NYB9.
SOURCESearch...

Entry information

Entry nameABI2_HUMAN
AccessionPrimary (citable) accession number: Q9NYB9
Secondary accession number(s): B4DSN1 expand/collapse secondary AC list , Q13147, Q13249, Q13801, Q9BV70
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 122 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM