Reviewed, UniProtKB/Swiss-Prot Q8IZP0 (ABI1_HUMAN)

Names and origin

Protein names

Recommended name:
    Abl interactor 1
Alternative name(s):
    Abelson interactor 1
      Short name=Abi-1
    Spectrin SH3 domain-binding protein 1
    Eps8 SH3 domain-binding protein
      Short name=Eps8-binding protein
    e3B1
    Nap1-binding protein
      Short name=Nap1BP
    Abl-binding protein 4
      Short name=AblBP4

Gene names

Name:	ABI1
Synonyms:	SSH3BP1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	508 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of MENA. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level By similarity. Ref.13
Subunit structure	Interacts with ABL1, MENA, 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. Ref.13 Ref.1 Ref.2 Ref.3 Ref.4
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Cell projection › lamellipodium By similarity. Cell projection › filopodium By similarity. Cell projection › growth cone By similarity. Cell junction › synapse › synaptosome By similarity. Cytoplasm › cytoskeleton By similarity. Note: Localized to protruding lamellipodia and filopodia tips. Also localized to neuronal growth cones and synaptosomes By similarity. Ref.1
Tissue specificity	Widely expressed, with highest expression in brain. Ref.3
Domain	The t-SNARE coiled-coil homology domain is necessary and sufficient for interaction with STX1A By similarity.
Post-translational modification	In vitro substrate for v-Abl By similarity. Phosphorylated on tyrosine residues after serum stimulation or induction by v-Abl.
Involvement in disease	A chromosomal aberration involving ABI1 is a cause of acute leukemias. Translocation t(10;11)(p11.2;q23) with MLL. ABI1 isoform 2 was found to be present in acute leukemia MLL-ABI1 fusion transcript.
Sequence similarities	Belongs to the ABI family. Contains 1 SH3 domain. Contains 1 t-SNARE coiled-coil homology domain.

Ontologies

Keywords
Cellular component	Cell junction Cell projection Cytoplasm Cytoskeleton Nucleus Synapse Synaptosome
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Domain	Coiled coil SH3 domain
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	negative regulation of cell proliferation Ref.1 Traceable author statement. Source: ProtInc peptidyl-tyrosine phosphorylation Inferred from direct assay. Source: MGI transmembrane receptor protein tyrosine kinase signaling pathway Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Ref.1 Traceable author statement. Source: ProtInc endoplasmic reticulum Ref.2 Traceable author statement. Source: ProtInc filopodium Inferred from electronic annotation. Source: UniProtKB-SubCell growth cone Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Inferred from direct assay. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Ref.1 Traceable author statement. Source: ProtInc synapse Inferred from electronic annotation. Source: UniProtKB-KW synaptosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cytoskeletal protein binding Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABL1	P00519	2	EBI-375446,EBI-375543
BAIAP2	Q9UQB8	1	EBI-375446,EBI-525456
Eps8	Q08509	2	EBI-375446,EBI-375596	From a different organism.
NCF1	P14598	4	EBI-375446,EBI-395044
NCK1	P16333	1	EBI-375446,EBI-389883
NCKAP1	Q9Y2A7	2	EBI-375446,EBI-389845
PRKAA1	Q13131	1	EBI-375446,EBI-1181405
SPTA1	P02549	1	EBI-375446,EBI-375617

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q8IZP0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8IZP0-2)

Also known as: long; B48;

The sequence of this isoform differs from the canonical sequence as follows:
     154-158: Missing.
     274-300: Missing.
     301-301: Missing.
     360-388: Missing.

Isoform 3 (identifier: Q8IZP0-3)

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

Isoform 4 (identifier: Q8IZP0-4)

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

Isoform 5 (identifier: Q8IZP0-5)

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

Isoform 6 (identifier: Q8IZP0-6)

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

Isoform 7 (identifier: Q8IZP0-7)

Also known as: 4;

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

Isoform 8 (identifier: Q8IZP0-8)

Also known as: 5;

The sequence of this isoform differs from the canonical sequence as follows:
     274-300: Missing.
     301-301: Missing.
     302-359: Missing.
     360-388: Missing.

Isoform 9 (identifier: Q8IZP0-9)

Also known as: 2;

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

Isoform 10 (identifier: Q8IZP0-10)

Also known as: B30;

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.11
	Chain	2 – 508	507	Abl interactor 1		PRO_0000191787
Regions
	Domain	45 – 107	63	t-SNARE coiled-coil homology
	Domain	446 – 505	60	SH3
	Region	18 – 79	62	Required for binding to WASF1 By similarity
	Compositional bias	260 – 418	159	Pro-rich
Sites
	Site	95 – 96	2	Breakpoint for translocation to form MLL-ABI1
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.11
	Modified residue	183	1	Phosphoserine Ref.18 Ref.21
	Modified residue	213	1	Phosphotyrosine Ref.17 Ref.22
	Modified residue	216	1	Phosphoserine Ref.21
	Modified residue	222	1	Phosphoserine By similarity
	Modified residue	225	1	Phosphoserine Ref.16 Ref.19 Ref.20
	Modified residue	333	1	Phosphotyrosine Ref.15
	Modified residue	455	1	Phosphotyrosine By similarity
Natural variations
	Alternative sequence	154 – 158	5	Missing in isoform 2, isoform 5 and isoform 10.		VSP_010749
	Alternative sequence	274 – 300	27	Missing in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9 and isoform 10.		VSP_010750
	Alternative sequence	301	1	Missing in isoform 2, isoform 4, isoform 6, isoform 7, isoform 8 and isoform 10.		VSP_010751
	Alternative sequence	302 – 359	58	Missing in isoform 7, isoform 8 and isoform 10.		VSP_010754
	Alternative sequence	360 – 388	29	Missing in isoform 2, isoform 3, isoform 4, isoform 8 and isoform 10.		VSP_010752
	Alternative sequence	360	1	I → V in isoform 7.		VSP_010755
	Alternative sequence	389	1	I → V in isoform 10.		VSP_010753
	Natural variant	331	1	G → A: dbSNP rs2306236.		VAR_048159
Experimental info
	Sequence conflict	177	1	P → L in AAC39757. Ref.2
	Sequence conflict	410	1	S → F in AAC39757. Ref.2
	Sequence conflict	410	1	S → F in AAN28379. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 2D76F305934127CB	FASTA	508	55,081
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK 190 200 210 220 230 240 PPSPPMSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS 250 260 270 280 290 300 GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT IGPENISVPP PSGAPPAPPL APLLPVSTVI 310 320 330 340 350 360 AAPGSAPGSQ YGTMTRQISR HNSTTSSTSS GGYRRTPSVT AQFSAQPHVN GGPLYSQNSI 370 380 390 400 410 420 SIAPPPPPMP QLTPQIPLTG FVARVQENIA DSPTPPPPPP PDDIPMFDDS PPPPPPPPVD 430 440 450 460 470 480 YEDEEAAVVQ YNDPYADGDP AWAPKNYIEK VVAIYDYTKD KDDELSFMEG AIIYVIKKND 490 500 DGWYEGVCNR VTGLFPGNYV ESIMHYTD
	Isoform 2 (long) (B48). Checksum: FEDF9B1991B89955	FASTA	446	48,678
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKHGNNQP ARTGTLSRTN PPTQKPPSPP 190 200 210 220 230 240 MSGRGTLGRN TPYKTLEPVK PPTVPNDYMT SPARLGSQHS PGRTASLNQR PRTHSGSSGG 250 260 270 280 290 300 SGSRENSGSS SIGIPIAVPT PSPPTIGPAP GSAPGSQYGT MTRQISRHNS TTSSTSSGGY 310 320 330 340 350 360 RRTPSVTAQF SAQPHVNGGP LYSQNSIADS PTPPPPPPPD DIPMFDDSPP PPPPPPVDYE 370 380 390 400 410 420 DEEAAVVQYN DPYADGDPAW APKNYIEKVV AIYDYTKDKD DELSFMEGAI IYVIKKNDDG 430 440 WYEGVCNRVT GLFPGNYVES IMHYTD
	Isoform 3. Checksum: 558B171EB1EABED4	FASTA	452	49,376
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK 190 200 210 220 230 240 PPSPPMSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS 250 260 270 280 290 300 GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT IGPAAPGSAP GSQYGTMTRQ ISRHNSTTSS 310 320 330 340 350 360 TSSGGYRRTP SVTAQFSAQP HVNGGPLYSQ NSIADSPTPP PPPPPDDIPM FDDSPPPPPP 370 380 390 400 410 420 PPVDYEDEEA AVVQYNDPYA DGDPAWAPKN YIEKVVAIYD YTKDKDDELS FMEGAIIYVI 430 440 450 KKNDDGWYEG VCNRVTGLFP GNYVESIMHY TD
	Isoform 4. Checksum: 796AE1E3CA14C07B	FASTA	451	49,305
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK 190 200 210 220 230 240 PPSPPMSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS 250 260 270 280 290 300 GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT IGPAPGSAPG SQYGTMTRQI SRHNSTTSST 310 320 330 340 350 360 SSGGYRRTPS VTAQFSAQPH VNGGPLYSQN SIADSPTPPP PPPPDDIPMF DDSPPPPPPP 370 380 390 400 410 420 PVDYEDEEAA VVQYNDPYAD GDPAWAPKNY IEKVVAIYDY TKDKDDELSF MEGAIIYVIK 430 440 450 KNDDGWYEGV CNRVTGLFPG NYVESIMHYT D
	Isoform 5. Checksum: 0321298AEFF40B9D	FASTA	476	51,841
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKHGNNQP ARTGTLSRTN PPTQKPPSPP 190 200 210 220 230 240 MSGRGTLGRN TPYKTLEPVK PPTVPNDYMT SPARLGSQHS PGRTASLNQR PRTHSGSSGG 250 260 270 280 290 300 SGSRENSGSS SIGIPIAVPT PSPPTIGPAA PGSAPGSQYG TMTRQISRHN STTSSTSSGG 310 320 330 340 350 360 YRRTPSVTAQ FSAQPHVNGG PLYSQNSISI APPPPPMPQL TPQIPLTGFV ARVQENIADS 370 380 390 400 410 420 PTPPPPPPPD DIPMFDDSPP PPPPPPVDYE DEEAAVVQYN DPYADGDPAW APKNYIEKVV 430 440 450 460 470 AIYDYTKDKD DELSFMEGAI IYVIKKNDDG WYEGVCNRVT GLFPGNYVES IMHYTD
	Isoform 6. Checksum: 4EA3699ECE77EE0E	FASTA	480	52,397
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK 190 200 210 220 230 240 PPSPPMSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS 250 260 270 280 290 300 GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT IGPAPGSAPG SQYGTMTRQI SRHNSTTSST 310 320 330 340 350 360 SSGGYRRTPS VTAQFSAQPH VNGGPLYSQN SISIAPPPPP MPQLTPQIPL TGFVARVQEN 370 380 390 400 410 420 IADSPTPPPP PPPDDIPMFD DSPPPPPPPP VDYEDEEAAV VQYNDPYADG DPAWAPKNYI 430 440 450 460 470 480 EKVVAIYDYT KDKDDELSFM EGAIIYVIKK NDDGWYEGVC NRVTGLFPGN YVESIMHYTD
	Isoform 7 (4). Checksum: 16FAAB5B29D7E506	FASTA	422	46,386
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK 190 200 210 220 230 240 PPSPPMSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS 250 260 270 280 290 300 GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT IGPVSIAPPP PPMPQLTPQI PLTGFVARVQ 310 320 330 340 350 360 ENIADSPTPP PPPPPDDIPM FDDSPPPPPP PPVDYEDEEA AVVQYNDPYA DGDPAWAPKN 370 380 390 400 410 420 YIEKVVAIYD YTKDKDDELS FMEGAIIYVI KKNDDGWYEG VCNRVTGLFP GNYVESIMHY TD
	Isoform 8 (5). Checksum: 522FF3E0941EE851	FASTA	393	43,309
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK 190 200 210 220 230 240 PPSPPMSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS 250 260 270 280 290 300 GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT IGPIADSPTP PPPPPPDDIP MFDDSPPPPP 310 320 330 340 350 360 PPPVDYEDEE AAVVQYNDPY ADGDPAWAPK NYIEKVVAIY DYTKDKDDEL SFMEGAIIYV 370 380 390 IKKNDDGWYE GVCNRVTGLF PGNYVESIMH YTD
	Isoform 9 (2). Checksum: A29602C39221C826	FASTA	481	52,468
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK 190 200 210 220 230 240 PPSPPMSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS 250 260 270 280 290 300 GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT IGPAAPGSAP GSQYGTMTRQ ISRHNSTTSS 310 320 330 340 350 360 TSSGGYRRTP SVTAQFSAQP HVNGGPLYSQ NSISIAPPPP PMPQLTPQIP LTGFVARVQE 370 380 390 400 410 420 NIADSPTPPP PPPPDDIPMF DDSPPPPPPP PVDYEDEEAA VVQYNDPYAD GDPAWAPKNY 430 440 450 460 470 480 IEKVVAIYDY TKDKDDELSF MEGAIIYVIK KNDDGWYEGV CNRVTGLFPG NYVESIMHYT D
	Isoform 10 (B30). Checksum: E63747A11D358E42	FASTA	388	42,668
	10 20 30 40 50 60 MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 70 80 90 100 110 120 VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 130 140 150 160 170 180 THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKHGNNQP ARTGTLSRTN PPTQKPPSPP 190 200 210 220 230 240 MSGRGTLGRN TPYKTLEPVK PPTVPNDYMT SPARLGSQHS PGRTASLNQR PRTHSGSSGG 250 260 270 280 290 300 SGSRENSGSS SIGIPIAVPT PSPPTIGPVA DSPTPPPPPP PDDIPMFDDS PPPPPPPPVD 310 320 330 340 350 360 YEDEEAAVVQ YNDPYADGDP AWAPKNYIEK VVAIYDYTKD KDDELSFMEG AIIYVIKKND 370 380 DGWYEGVCNR VTGLFPGNYV ESIMHYTD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth." Biesova Z., Piccoli C., Wong W.T. Oncogene 14:233-241(1997) [PubMed: 9010225] [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: 9593709] [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: 11418237] [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: 12681507] [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]	"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: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). Tissue: Muscle.
[11]	"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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-17. Tissue: Platelet.
[12]	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, MASS SPECTROMETRY. Tissue: Hepatoma.
[13]	"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: 11003655] [Abstract] Cited for: FUNCTION, INTERACTION WITH SOS1; SOS2 AND GRB2.
[14]	"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: 9694699] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 2 AND 10), CHROMOSOMAL TRANSLOCATION WITH MLL.
[15]	"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry." Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C. Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed: 12522270] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-333, MASS SPECTROMETRY.
[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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213, MASS SPECTROMETRY.
[18]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, MASS SPECTROMETRY.
[19]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, MASS SPECTROMETRY. Tissue: Platelet.
[20]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, MASS SPECTROMETRY.
[21]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-216, MASS SPECTROMETRY.
[22]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[23]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF006516 mRNA. Translation: AAB62569.1. U87166 mRNA. Translation: AAC39757.1. AB040151 mRNA. Translation: BAB55675.1. AF540955 mRNA. Translation: AAN28379.1. AF001628 mRNA. Translation: AAD00897.1. AJ277065 , AJ277066, AJ277067, AJ277068, AJ277069, AJ277070, AJ277071, AJ277072, AJ277073, AJ277074 Genomic DNA. Translation: CAB88006.1. AF260262 mRNA. Translation: AAF70309.1. 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: CAH73119.1. 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: EAW86080.1. BC024254 mRNA. Translation: AAH24254.1.
IPI	IPI00431025. IPI00431026. IPI00431027. IPI00431029. IPI00431030. IPI00431031. IPI00431032. IPI00431033. IPI00827857. IPI00935670.
RefSeq	NP_001012768.1. NP_001012769.1. NP_001012770.1. NP_005461.2.
UniGene	Hs.508148
3D structure databases
SMR	Q8IZP0. Positions 436-503.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8IZP0. 8 interactions.
STRING	Q8IZP0.
PTM databases
PhosphoSite	Q8IZP0.
Proteomic databases
PRIDE	Q8IZP0.
Genome annotation databases
Ensembl	ENST00000376142; ENSP00000365312; ENSG00000136754; Homo sapiens. [Genome view]
GeneID	10006.
KEGG	hsa:10006.
UCSC	uc001isx.1. human. uc001isy.1. human. uc001isz.1. human. uc001ita.1. human. uc001itc.1. human. uc001ite.1. human.
Organism-specific databases
CTD	10006.
GeneCards	GC10M027075.
H-InvDB	HIX0008722.
HGNC	HGNC:11320. ABI1.
HPA	CAB008375.
MIM	603050. gene.
PharmGKB	PA36144.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16454.
HOVERGEN	Q8IZP0.
PhylomeDB	Q8IZP0.
Gene expression databases
ArrayExpress	Q8IZP0.
Bgee	Q8IZP0.
Genevestigator	Q8IZP0.
GermOnline	ENSG00000136754. Homo sapiens.
Family and domain databases
InterPro	IPR012849. Abl-interactor_HHR. IPR000108. Neu_cyt_fact_2. IPR001452. SH3_domain. IPR020473. SH3_region. IPR000727. T_SNARE_dom. [Graphical view]
Pfam	PF07815. Abi_HHR. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00499. P67PHOX. PR00452. SH3DOMAIN.
SMART	SM00326. SH3. 1 hit. [Graphical view]
PROSITE	PS50002. SH3. 1 hit. PS50192. T_SNARE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	37795.
SOURCE	Search...

Entry information

Entry name

ABI1_HUMAN

Accession

Primary (citable) accession number: Q8IZP0
Secondary accession number(s): A9Z1Y6 , O15147, O76049, O95060, Q5T2R3, Q5T2R4, Q5T2R6, Q5T2R7, Q5W070, Q5W072, Q8TB63, Q96S81, Q9NXZ9, Q9NYB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 85 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.