SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8IZP0

- ABI1_HUMAN

UniProt

Q8IZP0 - ABI1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Abl interactor 1

Gene
ABI1, SSH3BP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei95 – 962Breakpoint for translocation to form KMT2A/MLL1-ABI1

GO - Molecular functioni

  1. cytoskeletal protein binding Source: ProtInc
  2. protein binding Source: IntAct
  3. protein complex binding Source: UniProt
  4. protein tyrosine kinase activator activity Source: Ensembl

GO - Biological processi

  1. actin polymerization or depolymerization Source: UniProtKB
  2. cellular component movement Source: UniProtKB
  3. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  4. innate immune response Source: Reactome
  5. lamellipodium morphogenesis Source: Ensembl
  6. megakaryocyte development Source: Ensembl
  7. negative regulation of cell proliferation Source: ProtInc
  8. peptidyl-tyrosine phosphorylation Source: MGI
  9. somitogenesis Source: Ensembl
  10. transmembrane receptor protein tyrosine kinase signaling pathway Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
SignaLinkiQ8IZP0.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ABI1
Synonyms:SSH3BP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:11320. ABI1.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytosol Source: Reactome
  3. endoplasmic reticulum Source: ProtInc
  4. extracellular vesicular exosome Source: UniProt
  5. filopodium Source: UniProtKB
  6. growth cone Source: UniProtKB-SubCell
  7. intracellular Source: MGI
  8. lamellipodium Source: UniProtKB
  9. nucleus Source: UniProtKB-SubCell
  10. postsynaptic density Source: UniProtKB-SubCell
  11. postsynaptic membrane Source: UniProtKB-KW
  12. SCAR complex Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Involvement in diseasei

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.

Organism-specific databases

PharmGKBiPA36144.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 508507Abl interactor 1PRO_0000191787Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei53 – 531Phosphotyrosine By similarity
Modified residuei183 – 1831Phosphoserine1 Publication
Modified residuei213 – 2131Phosphotyrosine; by ABL11 Publication
Modified residuei216 – 2161Phosphoserine1 Publication
Modified residuei222 – 2221Phosphoserine1 Publication
Modified residuei225 – 2251Phosphoserine5 Publications
Modified residuei323 – 3231Phosphoserine1 Publication
Modified residuei455 – 4551Phosphotyrosine By similarity
Modified residuei507 – 5071Phosphothreonine1 Publication

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8IZP0.
PaxDbiQ8IZP0.
PRIDEiQ8IZP0.

PTM databases

PhosphoSiteiQ8IZP0.

Expressioni

Tissue specificityi

Widely expressed, with highest expression in brain.1 Publication

Gene expression databases

ArrayExpressiQ8IZP0.
BgeeiQ8IZP0.
GenevestigatoriQ8IZP0.

Organism-specific databases

HPAiCAB008375.
HPA029973.

Interactioni

Subunit structurei

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P0051911EBI-375446,EBI-375543
Abl1P00520-45EBI-8593095,EBI-8593082From a different organism.
ABL2P426842EBI-375446,EBI-1102694
CACNA1AO005552EBI-375446,EBI-766279
CBLP226813EBI-7358775,EBI-518228
Eps8Q085092EBI-375446,EBI-375596From a different organism.
NCF1P145985EBI-375446,EBI-395044
NCKAP1Q9Y2A72EBI-375446,EBI-389845
PIK3R1P279868EBI-375446,EBI-79464
Pik3r1P264503EBI-375446,EBI-641764From a different organism.
PIK3R3Q925692EBI-375446,EBI-79893
RASA1P209362EBI-375446,EBI-1026476
SOCS7O145122EBI-375446,EBI-1539606
SPTA1P025492EBI-375446,EBI-375617
VAV1P154982EBI-375446,EBI-625518
VAV2P527352EBI-375446,EBI-297549

Protein-protein interaction databases

BioGridi115324. 24 interactions.
DIPiDIP-31118N.
IntActiQ8IZP0. 61 interactions.
MINTiMINT-106609.

Structurei

3D structure databases

ProteinModelPortaliQ8IZP0.
SMRiQ8IZP0. Positions 1-154, 436-503.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 10763t-SNARE coiled-coil homologyAdd
BLAST
Domaini446 – 50560SH3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 7962Required for binding to WASF1 By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi260 – 418159Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the ABI family.
Contains 1 SH3 domain.

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG262939.
HOVERGENiHBG050446.
OrthoDBiEOG7J17ZT.
PhylomeDBiQ8IZP0.
TreeFamiTF314303.

Family and domain databases

InterProiIPR028457. ABI.
IPR028456. ABI1.
IPR012849. Abl-interactor_HHR_dom.
IPR001452. SH3_domain.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERiPTHR10460. PTHR10460. 1 hit.
PTHR10460:SF2. PTHR10460:SF2. 1 hit.
PfamiPF07815. Abi_HHR. 1 hit.
PF00018. SH3_1. 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 (12)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 12 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q8IZP0-1) [UniParc]FASTAAdd to Basket

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

MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET    50
KAYTTQSLAS VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH 100
KEKVARREIG ILTTNKNTSR THKIIAPANM ERPVRYIRKP IDYTVLDDVG 150
HGVKWLKAKH GNNQPARTGT LSRTNPPTQK PPSPPMSGRG TLGRNTPYKT 200
LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS GSSGGSGSRE 250
NSGSSSIGIP IAVPTPSPPT IGPENISVPP PSGAPPAPPL APLLPVSTVI 300
AAPGSAPGSQ YGTMTRQISR HNSTTSSTSS GGYRRTPSVT AQFSAQPHVN 350
GGPLYSQNSI SIAPPPPPMP QLTPQIPLTG FVARVQENIA DSPTPPPPPP 400
PDDIPMFDDS PPPPPPPPVD YEDEEAAVVQ YNDPYADGDP AWAPKNYIEK 450
VVAIYDYTKD KDDELSFMEG AIIYVIKKND DGWYEGVCNR VTGLFPGNYV 500
ESIMHYTD 508
Length:508
Mass (Da):55,081
Last modified:January 23, 2007 - v4
Checksum:i2D76F305934127CB
GO
Isoform 2 (identifier: Q8IZP0-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:446
Mass (Da):48,678
Checksum:iFEDF9B1991B89955
GO
Isoform 3 (identifier: Q8IZP0-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     274-300: Missing.
     360-388: Missing.

Show »
Length:452
Mass (Da):49,376
Checksum:i558B171EB1EABED4
GO
Isoform 4 (identifier: Q8IZP0-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     274-300: Missing.
     301-301: Missing.
     360-388: Missing.

Show »
Length:451
Mass (Da):49,305
Checksum:i796AE1E3CA14C07B
GO
Isoform 5 (identifier: Q8IZP0-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     154-158: Missing.
     274-300: Missing.

Show »
Length:476
Mass (Da):51,841
Checksum:i0321298AEFF40B9D
GO
Isoform 6 (identifier: Q8IZP0-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     274-300: Missing.
     301-301: Missing.

Show »
Length:480
Mass (Da):52,397
Checksum:i4EA3699ECE77EE0E
GO
Isoform 7 (identifier: Q8IZP0-7) [UniParc]FASTAAdd to Basket

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

Show »
Length:422
Mass (Da):46,386
Checksum:i16FAAB5B29D7E506
GO
Isoform 8 (identifier: Q8IZP0-8) [UniParc]FASTAAdd to Basket

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.

Show »
Length:393
Mass (Da):43,309
Checksum:i522FF3E0941EE851
GO
Isoform 9 (identifier: Q8IZP0-9) [UniParc]FASTAAdd to Basket

Also known as: 2

The sequence of this isoform differs from the canonical sequence as follows:
     274-300: Missing.

Show »
Length:481
Mass (Da):52,468
Checksum:iA29602C39221C826
GO
Isoform 10 (identifier: Q8IZP0-10) [UniParc]FASTAAdd to Basket

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

Show »
Length:388
Mass (Da):42,668
Checksum:iE63747A11D358E42
GO
Isoform 11 (identifier: Q8IZP0-11) [UniParc]FASTAAdd to Basket

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.

Show »
Length:329
Mass (Da):35,920
Checksum:i5895AC905A5773F7
GO
Isoform 12 (identifier: Q8IZP0-12) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     38-38: I → IQRHGFAVLLCLLSNSWP
     360-388: Missing.

Note: No experimental confirmation available.

Show »
Length:496
Mass (Da):53,912
Checksum:iB6D85C58732FB5E2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti331 – 3311G → A.
Corresponds to variant rs2306236 [ dbSNP | Ensembl ].
VAR_048159

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei38 – 381I → IQRHGFAVLLCLLSNSWP in isoform 12. VSP_044604
Alternative sequencei96 – 15964Missing in isoform 11. VSP_043403Add
BLAST
Alternative sequencei154 – 1585Missing in isoform 2, isoform 5 and isoform 10. VSP_010749
Alternative sequencei274 – 30027Missing in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 11. VSP_010750Add
BLAST
Alternative sequencei301 – 3011Missing in isoform 2, isoform 4, isoform 6, isoform 7, isoform 8, isoform 10 and isoform 11. VSP_010751
Alternative sequencei302 – 35958Missing in isoform 7, isoform 8, isoform 10 and isoform 11. VSP_010754Add
BLAST
Alternative sequencei360 – 38829Missing in isoform 2, isoform 3, isoform 4, isoform 8, isoform 10, isoform 11 and isoform 12. VSP_010752Add
BLAST
Alternative sequencei360 – 3601I → V in isoform 7. VSP_010755
Alternative sequencei389 – 3891I → V in isoform 10 and isoform 11. VSP_010753

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti177 – 1771P → L in AAC39757. 1 Publication
Sequence conflicti410 – 4101S → F in AAC39757. 1 Publication
Sequence conflicti410 – 4101S → F in AAN28379. 1 Publication
Sequence conflicti437 – 4371D → G in BAG54374. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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
, 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.
CCDSiCCDS31169.1. [Q8IZP0-5]
CCDS31170.1. [Q8IZP0-3]
CCDS31171.1. [Q8IZP0-9]
CCDS53497.1. [Q8IZP0-11]
CCDS53498.1. [Q8IZP0-2]
CCDS53499.1. [Q8IZP0-4]
CCDS53500.1. [Q8IZP0-6]
CCDS53501.1. [Q8IZP0-12]
CCDS7150.1. [Q8IZP0-1]
RefSeqiNP_001012768.1. NM_001012750.2. [Q8IZP0-9]
NP_001012769.1. NM_001012751.2. [Q8IZP0-3]
NP_001012770.1. NM_001012752.2. [Q8IZP0-5]
NP_001171587.1. NM_001178116.1. [Q8IZP0-12]
NP_001171590.1. NM_001178119.1. [Q8IZP0-6]
NP_001171591.1. NM_001178120.1. [Q8IZP0-4]
NP_001171592.1. NM_001178121.1. [Q8IZP0-2]
NP_001171593.1. NM_001178122.1. [Q8IZP0-7]
NP_001171594.1. NM_001178123.1.
NP_001171595.1. NM_001178124.1. [Q8IZP0-10]
NP_001171596.1. NM_001178125.1. [Q8IZP0-11]
NP_005461.2. NM_005470.3. [Q8IZP0-1]
UniGeneiHs.508148.

Genome annotation databases

EnsembliENST00000346832; 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]
GeneIDi10006.
KEGGihsa:10006.
UCSCiuc001isx.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]

Polymorphism databases

DMDMi50400546.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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
, 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 .
CCDSi CCDS31169.1. [Q8IZP0-5 ]
CCDS31170.1. [Q8IZP0-3 ]
CCDS31171.1. [Q8IZP0-9 ]
CCDS53497.1. [Q8IZP0-11 ]
CCDS53498.1. [Q8IZP0-2 ]
CCDS53499.1. [Q8IZP0-4 ]
CCDS53500.1. [Q8IZP0-6 ]
CCDS53501.1. [Q8IZP0-12 ]
CCDS7150.1. [Q8IZP0-1 ]
RefSeqi NP_001012768.1. NM_001012750.2. [Q8IZP0-9 ]
NP_001012769.1. NM_001012751.2. [Q8IZP0-3 ]
NP_001012770.1. NM_001012752.2. [Q8IZP0-5 ]
NP_001171587.1. NM_001178116.1. [Q8IZP0-12 ]
NP_001171590.1. NM_001178119.1. [Q8IZP0-6 ]
NP_001171591.1. NM_001178120.1. [Q8IZP0-4 ]
NP_001171592.1. NM_001178121.1. [Q8IZP0-2 ]
NP_001171593.1. NM_001178122.1. [Q8IZP0-7 ]
NP_001171594.1. NM_001178123.1.
NP_001171595.1. NM_001178124.1. [Q8IZP0-10 ]
NP_001171596.1. NM_001178125.1. [Q8IZP0-11 ]
NP_005461.2. NM_005470.3. [Q8IZP0-1 ]
UniGenei Hs.508148.

3D structure databases

ProteinModelPortali Q8IZP0.
SMRi Q8IZP0. Positions 1-154, 436-503.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115324. 24 interactions.
DIPi DIP-31118N.
IntActi Q8IZP0. 61 interactions.
MINTi MINT-106609.

PTM databases

PhosphoSitei Q8IZP0.

Polymorphism databases

DMDMi 50400546.

Proteomic databases

MaxQBi Q8IZP0.
PaxDbi Q8IZP0.
PRIDEi Q8IZP0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000346832 ; 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 ]
GeneIDi 10006.
KEGGi hsa:10006.
UCSCi uc001isx.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

CTDi 10006.
GeneCardsi GC10M027075.
HGNCi HGNC:11320. ABI1.
HPAi CAB008375.
HPA029973.
MIMi 603050. gene.
neXtProti NX_Q8IZP0.
PharmGKBi PA36144.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262939.
HOVERGENi HBG050446.
OrthoDBi EOG7J17ZT.
PhylomeDBi Q8IZP0.
TreeFami TF314303.

Enzyme and pathway databases

Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
SignaLinki Q8IZP0.

Miscellaneous databases

ChiTaRSi ABI1. human.
GeneWikii ABI1.
GenomeRNAii 10006.
NextBioi 37795.
PROi Q8IZP0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8IZP0.
Bgeei Q8IZP0.
Genevestigatori Q8IZP0.

Family and domain databases

InterProi IPR028457. ABI.
IPR028456. ABI1.
IPR012849. Abl-interactor_HHR_dom.
IPR001452. SH3_domain.
IPR000727. T_SNARE_dom.
[Graphical view ]
PANTHERi PTHR10460. PTHR10460. 1 hit.
PTHR10460:SF2. PTHR10460:SF2. 1 hit.
Pfami PF07815. Abi_HHR. 1 hit.
PF00018. SH3_1. 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. "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.
    , 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.
    , 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. 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. 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiABI1_HUMAN
AccessioniPrimary (citable) accession number: Q8IZP0
Secondary accession number(s): A9Z1Y6
, B3KX62, B4DQ58, H7BXI6, O15147, O76049, O95060, Q5T2R3, Q5T2R4, Q5T2R6, Q5T2R7, Q5T2R9, Q5W070, Q5W072, Q8TB63, Q96S81, Q9NXZ9, Q9NYB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 129 of the entry and version 4 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi