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Q9NYB9

- ABI2_HUMAN

UniProt

Q9NYB9 - ABI2_HUMAN

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Protein

Abl interactor 2

Gene

ABI2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. cytoskeletal adaptor activity Source: UniProtKB
  2. DNA binding Source: ProtInc
  3. kinase binding Source: UniProtKB
  4. proline-rich region binding Source: UniProtKB
  5. protein complex binding Source: UniProt
  6. SH3 domain binding Source: UniProtKB
  7. ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

  1. actin polymerization or depolymerization Source: UniProtKB
  2. cell migration Source: UniProtKB
  3. cellular component movement Source: UniProtKB
  4. cytoskeleton organization Source: UniProtKB
  5. peptidyl-tyrosine phosphorylation Source: MGI
  6. positive regulation of Arp2/3 complex-mediated actin nucleation Source: UniProt
  7. Rac protein signal transduction Source: UniProt
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_228166. VEGFA-VEGFR2 Pathway.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ABI2
Synonyms:ARGBPIA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:24011. ABI2.

Subcellular locationi

Cytoplasm By similarity
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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
  3. cytosol Source: BHF-UCL
  4. filopodium Source: UniProtKB
  5. lamellipodium Source: UniProtKB
  6. SCAR complex Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134977642.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513Abl interactor 2PRO_0000191790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei227 – 2271Phosphoserine3 Publications
Modified residuei368 – 3681Phosphoserine1 Publication

Post-translational modificationi

Is a substrate for ABL1.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NYB9.
PaxDbiQ9NYB9.
PRIDEiQ9NYB9.

PTM databases

PhosphoSiteiQ9NYB9.

Expressioni

Gene expression databases

BgeeiQ9NYB9.
CleanExiHS_ABI2.
ExpressionAtlasiQ9NYB9. baseline and differential.
GenevestigatoriQ9NYB9.

Interactioni

Subunit structurei

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.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005192EBI-743598,EBI-375543
Caskin1Q8VHK23EBI-743598,EBI-7049475From a different organism.

Protein-protein interaction databases

BioGridi115454. 25 interactions.
DIPiDIP-37566N.
IntActiQ9NYB9. 23 interactions.
MINTiMINT-252647.
STRINGi9606.ENSP00000261017.

Structurei

Secondary structure

513
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 99Combined sources
Helixi11 – 3929Combined sources
Helixi43 – 11068Combined sources
Beta strandi123 – 1253Combined sources
Turni143 – 1519Combined sources
Beta strandi453 – 4586Combined sources
Beta strandi477 – 4837Combined sources
Beta strandi485 – 4939Combined sources
Beta strandi496 – 5016Combined sources
Beta strandi504 – 5074Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ED0NMR-A444-508[»]
3P8CX-ray2.29F1-164[»]
4N78X-ray2.43F1-513[»]
ProteinModelPortaliQ9NYB9.
SMRiQ9NYB9. Positions 1-154, 444-508.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NYB9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 10763t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST
Domaini451 – 51060SH3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi172 – 423252Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the ABI family.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG262939.
GeneTreeiENSGT00390000003756.
HOGENOMiHOG000293213.
HOVERGENiHBG050446.
InParanoidiQ9NYB9.
KOiK05751.
PhylomeDBiQ9NYB9.
TreeFamiTF314303.

Family and domain databases

InterProiIPR028457. ABI.
IPR028454. Abi2.
IPR012849. Abl-interactor_HHR_dom.
IPR001452. SH3_domain.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERiPTHR10460. PTHR10460. 1 hit.
PTHR10460:SF3. PTHR10460:SF3. 1 hit.
PfamiPF07815. Abi_HHR. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NYB9-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAELQMLLEE EIPGGRRALF DSYTNLERVA DYCENNYIQS ADKQRALEET
60 70 80 90 100
KAYTTQSLAS VAYLINTLAN NVLQMLDIQA SQLRRMESSI NHISQTVDIH
110 120 130 140 150
KEKVARREIG ILTTNKNTSR THKIIAPANL ERPVRYIRKP IDYTILDDIG
160 170 180 190 200
HGVKWLLRFK VSTQNMKMGG LPRTTPPTQK PPSPPMSGKG TLGRHSPYRT
210 220 230 240 250
LEPVRPPVVP NDYVPSPTRN MAPSQQSPVR TASVNQRNRT YSSSGSSGGS
260 270 280 290 300
HPSSRSSSRE NSGSGSVGVP IAVPTPSPPS VFPAPAGSAG TPPLPATSAS
310 320 330 340 350
APAPLVPATV PSSTAPNAAA GGAPNLADGF TSPTPPVVSS TPPTGHPVQF
360 370 380 390 400
YSMNRPASRH TPPTIGGSLP YRRPPSITSQ TSLQNQMNGG PFYSQNPVSD
410 420 430 440 450
TPPPPPPVEE PVFDESPPPP PPPEDYEEEE AAVVEYSDPY AEEDPPWAPR
460 470 480 490 500
SYLEKVVAIY DYTKDKEDEL SFQEGAIIYV IKKNDDGWYE GVMNGVTGLF
510
PGNYVESIMH YSE
Length:513
Mass (Da):55,663
Last modified:October 1, 2000 - v1
Checksum:i822983A69E5EA512
GO
Isoform 2 (identifier: Q9NYB9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     154-159: Missing.
     284-344: Missing.
     399-399: S → SLAPPPPSILQVTPQLPLMGFVARVQENIS

Show »
Length:475
Mass (Da):52,446
Checksum:i3AF8B713FD40FA90
GO
Isoform 3 (identifier: Q9NYB9-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:401
Mass (Da):44,409
Checksum:i5D009A269B2B2FFF
GO
Isoform 4 (identifier: Q9NYB9-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:507
Mass (Da):54,819
Checksum:iC0CE1E991D695FC1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221S → R in CAA64885. (PubMed:8649853)Curated
Sequence conflicti69 – 691A → D in CAA64885. (PubMed:8649853)Curated
Sequence conflicti243 – 2431S → T in AAA75446. 1 PublicationCurated
Sequence conflicti249 – 2491G → P in AAA92289. (PubMed:7590236)Curated
Sequence conflicti317 – 3171N → D in BAG61693. (PubMed:14702039)Curated
Sequence conflicti324 – 3252PN → QT in BAG61693. (PubMed:14702039)Curated
Sequence conflicti432 – 4321A → V in AAA75446. 1 PublicationCurated
Sequence conflicti500 – 5001F → S in AAA75446. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4545Missing in isoform 3. 1 PublicationVSP_010759Add
BLAST
Alternative sequencei46 – 9550ALEET…NHISQ → MSCRCWISRHPSYEGWNLQS IIFHKQIRGVDLESTFVTKF GNNCSLRLNE in isoform 3. 1 PublicationVSP_010760Add
BLAST
Alternative sequencei154 – 1596Missing in isoform 2, isoform 3 and isoform 4. 6 PublicationsVSP_010761
Alternative sequencei284 – 34461Missing in isoform 2 and isoform 3. 5 PublicationsVSP_010762Add
BLAST
Alternative sequencei399 – 3991S → SLAPPPPSILQVTPQLPLMG FVARVQENIS in isoform 2. 4 PublicationsVSP_010763

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2358.1. [Q9NYB9-2]
CCDS63093.1. [Q9NYB9-1]
CCDS63094.1. [Q9NYB9-4]
PIRiG01936.
RefSeqiNP_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]
UniGeneiHs.471156.

Genome annotation databases

EnsembliENST00000261017; ENSP00000261017; ENSG00000138443. [Q9NYB9-2]
ENST00000424558; ENSP00000391433; ENSG00000138443.
GeneIDi10152.
KEGGihsa:10152.
UCSCiuc002uzz.3. human. [Q9NYB9-2]
uc002vab.3. human. [Q9NYB9-3]

Polymorphism databases

DMDMi50400673.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS2358.1. [Q9NYB9-2 ]
CCDS63093.1. [Q9NYB9-1 ]
CCDS63094.1. [Q9NYB9-4 ]
PIRi G01936.
RefSeqi NP_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 ]
UniGenei Hs.471156.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ED0 NMR - A 444-508 [» ]
3P8C X-ray 2.29 F 1-164 [» ]
4N78 X-ray 2.43 F 1-513 [» ]
ProteinModelPortali Q9NYB9.
SMRi Q9NYB9. Positions 1-154, 444-508.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115454. 25 interactions.
DIPi DIP-37566N.
IntActi Q9NYB9. 23 interactions.
MINTi MINT-252647.
STRINGi 9606.ENSP00000261017.

PTM databases

PhosphoSitei Q9NYB9.

Polymorphism databases

DMDMi 50400673.

Proteomic databases

MaxQBi Q9NYB9.
PaxDbi Q9NYB9.
PRIDEi Q9NYB9.

Protocols and materials databases

DNASUi 10152.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261017 ; ENSP00000261017 ; ENSG00000138443 . [Q9NYB9-2 ]
ENST00000424558 ; ENSP00000391433 ; ENSG00000138443 .
GeneIDi 10152.
KEGGi hsa:10152.
UCSCi uc002uzz.3. human. [Q9NYB9-2 ]
uc002vab.3. human. [Q9NYB9-3 ]

Organism-specific databases

CTDi 10152.
GeneCardsi GC02P204192.
H-InvDB HIX0002759.
HGNCi HGNC:24011. ABI2.
MIMi 606442. gene.
neXtProti NX_Q9NYB9.
PharmGKBi PA134977642.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262939.
GeneTreei ENSGT00390000003756.
HOGENOMi HOG000293213.
HOVERGENi HBG050446.
InParanoidi Q9NYB9.
KOi K05751.
PhylomeDBi Q9NYB9.
TreeFami TF314303.

Enzyme and pathway databases

Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_228166. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

ChiTaRSi ABI2. human.
EvolutionaryTracei Q9NYB9.
GeneWikii ABI2.
GenomeRNAii 10152.
NextBioi 38426.
PROi Q9NYB9.
SOURCEi Search...

Gene expression databases

Bgeei Q9NYB9.
CleanExi HS_ABI2.
ExpressionAtlasi Q9NYB9. baseline and differential.
Genevestigatori Q9NYB9.

Family and domain databases

InterProi IPR028457. ABI.
IPR028454. Abi2.
IPR012849. Abl-interactor_HHR_dom.
IPR001452. SH3_domain.
IPR000727. T_SNARE_dom.
[Graphical view ]
PANTHERi PTHR10460. PTHR10460. 1 hit.
PTHR10460:SF3. PTHR10460:SF3. 1 hit.
Pfami PF07815. Abi_HHR. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50002. SH3. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-164, SUBUNIT.

Entry informationi

Entry nameiABI2_HUMAN
AccessioniPrimary (citable) accession number: Q9NYB9
Secondary accession number(s): B4DSN1
, Q13147, Q13249, Q13801, Q9BV70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3