Q9NYB9 (ABI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Protein existence	Evidence 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 projection › lamellipodium By similarity. Cell projection › filopodium By similarity. Cytoplasm › cytoskeleton 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 component	Cell projection Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	Coiled coil SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin polymerization or depolymerization Non-traceable author statement Ref.8. Source: UniProtKB camera-type eye development Inferred from electronic annotation. Source: Compara cell migration Traceable author statement PubMed 12011975. Source: UniProtKB dendrite development Inferred from electronic annotation. Source: Compara learning or memory Inferred from electronic annotation. Source: Compara peptidyl-tyrosine phosphorylation Inferred from direct assay PubMed 17101133. Source: MGI
Cellular_component	cell-cell adherens junction Inferred from electronic annotation. Source: Compara cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay PubMed 18632609. Source: BHF-UCL dendrite Inferred from electronic annotation. Source: Compara filopodium Inferred from direct assay Ref.8. Source: UniProtKB lamellipodium Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	DNA binding Traceable author statement Ref.1. Source: ProtInc SH3 domain binding Traceable author statement Ref.3. Source: UniProtKB cytoskeletal adaptor activity Traceable author statement PubMed 12011975. Source: UniProtKB kinase binding Non-traceable author statement Ref.3. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 513

513

Abl interactor 2

PRO_0000191790

Regions

Domain

45 – 107

63

t-SNARE coiled-coil homology

Domain

451 – 510

60

SH3

Compositional bias

172 – 423

252

Pro-rich

Amino acid modifications

Modified residue

227

1

Phosphoserine Ref.9 Ref.10 Ref.12

Modified residue

368

1

Phosphoserine Ref.10

Modified residue

462

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

1 – 45

45

Missing in isoform 3.

VSP_010759

Alternative sequence

46 – 95

50

ALEET…NHISQ → MSCRCWISRHPSYEGWNLQS IIFHKQIRGVDLESTFVTKF GNNCSLRLNE in isoform 3.

VSP_010760

Alternative sequence

154 – 159

6

Missing in isoform 2, isoform 3 and isoform 4.

VSP_010761

Alternative sequence

284 – 344

61

Missing in isoform 2 and isoform 3.

VSP_010762

Alternative sequence

399

1

S → SLAPPPPSILQVTPQLPLMG FVARVQENIS in isoform 2.

VSP_010763

Experimental info

Sequence conflict

22

1

S → R in CAA64885. Ref.3

Sequence conflict

69

1

A → D in CAA64885. Ref.3

Sequence conflict

243

1

S → T in AAA75446. Ref.2

Sequence conflict

249

1

G → P in AAA92289. Ref.1

Sequence conflict

317

1

N → D in BAG61693. Ref.5

Sequence conflict

324 – 325

2

PN → QT in BAG61693. Ref.5

Sequence conflict

432

1

A → V in AAA75446. Ref.2

Sequence conflict

500

1

F → S in AAA75446. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

513

Helix Strand Turn

Details...

Helix

1 – 9

9

Helix

11 – 39

29

Helix

43 – 110

68

Beta strand

123 – 125

3

Turn

143 – 151

9

Beta strand

453 – 458

6

Beta strand

477 – 483

7

Beta strand

485 – 493

9

Beta strand

496 – 501

6

Beta strand

504 – 507

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Abi-2b) [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 822983A69E5EA512	FASTA	513	55,663
	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
	Isoform 2 [UniParc]. Checksum: 3AF8B713FD40FA90	FASTA	475	52,446
	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 HGVKVSTQNM KMGGLPRTTP PTQKPPSPPM 190 200 210 220 230 240 SGKGTLGRHS PYRTLEPVRP PVVPNDYVPS PTRNMAPSQQ SPVRTASVNQ RNRTYSSSGS 250 260 270 280 290 300 SGGSHPSSRS SSRENSGSGS VGVPIAVPTP SPPSVFPGHP VQFYSMNRPA SRHTPPTIGG 310 320 330 340 350 360 SLPYRRPPSI TSQTSLQNQM NGGPFYSQNP VSLAPPPPSI LQVTPQLPLM GFVARVQENI 370 380 390 400 410 420 SDTPPPPPPV EEPVFDESPP PPPPPEDYEE EEAAVVEYSD PYAEEDPPWA PRSYLEKVVA 430 440 450 460 470 IYDYTKDKED ELSFQEGAII YVIKKNDDGW YEGVMNGVTG LFPGNYVESI MHYSE
	Isoform 3 (Abi-2a) [UniParc]. Checksum: 5D009A269B2B2FFF	FASTA	401	44,409
	10 20 30 40 50 60 MSCRCWISRH PSYEGWNLQS IIFHKQIRGV DLESTFVTKF GNNCSLRLNE TVDIHKEKVA 70 80 90 100 110 120 RREIGILTTN KNTSRTHKII APANLERPVR YIRKPIDYTI LDDIGHGVKV STQNMKMGGL 130 140 150 160 170 180 PRTTPPTQKP PSPPMSGKGT LGRHSPYRTL EPVRPPVVPN DYVPSPTRNM APSQQSPVRT 190 200 210 220 230 240 ASVNQRNRTY SSSGSSGGSH PSSRSSSREN SGSGSVGVPI AVPTPSPPSV FPGHPVQFYS 250 260 270 280 290 300 MNRPASRHTP PTIGGSLPYR RPPSITSQTS LQNQMNGGPF YSQNPVSDTP PPPPPVEEPV 310 320 330 340 350 360 FDESPPPPPP PEDYEEEEAA VVEYSDPYAE EDPPWAPRSY LEKVVAIYDY TKDKEDELSF 370 380 390 400 QEGAIIYVIK KNDDGWYEGV MNGVTGLFPG NYVESIMHYS E
	Isoform 4 [UniParc]. Checksum: C0CE1E991D695FC1	FASTA	507	54,819
	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 HGVKVSTQNM KMGGLPRTTP PTQKPPSPPM 190 200 210 220 230 240 SGKGTLGRHS PYRTLEPVRP PVVPNDYVPS PTRNMAPSQQ SPVRTASVNQ RNRTYSSSGS 250 260 270 280 290 300 SGGSHPSSRS SSRENSGSGS VGVPIAVPTP SPPSVFPAPA GSAGTPPLPA TSASAPAPLV 310 320 330 340 350 360 PATVPSSTAP NAAAGGAPNL ADGFTSPTPP VVSSTPPTGH PVQFYSMNRP ASRHTPPTIG 370 380 390 400 410 420 GSLPYRRPPS ITSQTSLQNQ MNGGPFYSQN PVSDTPPPPP PVEEPVFDES PPPPPPPEDY 430 440 450 460 470 480 EEEEAAVVEY SDPYAEEDPP WAPRSYLEKV VAIYDYTKDK EDELSFQEGA IIYVIKKNDD 490 500 GWYEGVMNGV TGLFPGNYVE SIMHYSE

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.

IPI

IPI00442210.
IPI00442211.
IPI00442214.
IPI00925810.

PIR

G01936.

RefSeq

NP_005750.4. NM_005759.4.

UniGene

Hs.471156.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ED0	NMR	-	A	444-508	[»]
3P8C	X-ray	2.29	F	1-154	[»]

ProteinModelPortal

Q9NYB9.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37566N.

IntAct

Q9NYB9. 10 interactions.

MINT

MINT-252647.

STRING

9606.ENSP00000261017.

PTM databases

PhosphoSite

Q9NYB9.

Polymorphism databases

DMDM

50400673.

Proteomic databases

PaxDb

Q9NYB9.

PRIDE

Q9NYB9.

Protocols and materials databases

DNASU

10152.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261016; ENSP00000261016; ENSG00000138443.
ENST00000261017; ENSP00000261017; ENSG00000138443.
ENST00000424558; ENSP00000391433; ENSG00000138443.

GeneID

10152.

KEGG

hsa:10152.

UCSC

uc002uzz.3. human.
uc002vab.3. human.
uc010zii.2. human.

Organism-specific databases

CTD

10152.

GeneCards

GC02P204192.

H-InvDB

HIX0002759.

HGNC

HGNC:24011. ABI2.

MIM

606442. gene.

neXtProt

NX_Q9NYB9.

PharmGKB

PA134977642.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG262939.

HOGENOM

HOG000293213.

HOVERGEN

HBG050446.

InParanoid

Q9NYB9.

KO

K05751.

OrthoDB

EOG4ZKJMQ.

Gene expression databases

ArrayExpress

Q9NYB9.

Bgee

Q9NYB9.

CleanEx

HS_ABI2.

Genevestigator

Q9NYB9.

GermOnline

ENSG00000138443. Homo sapiens.

Family and domain databases

InterPro

IPR012849. Abl-interactor_HHR_dom.
IPR001452. SH3_domain.
IPR000727. T_SNARE_dom.
[Graphical view]

Pfam

PF07815. Abi_HHR. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.

SMART

SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50002. SH3. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ABI2. human.

EvolutionaryTrace

Q9NYB9.

GenomeRNAi

10152.

NextBio

38426.

SOURCE

Search...

Entry information

Entry name

ABI2_HUMAN

Accession

Primary (citable) accession number: Q9NYB9
Secondary accession number(s): B4DSN1 , Q13147, Q13249, Q13801, Q9BV70

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.