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P42684 (ABL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Abelson tyrosine-protein kinase 2

EC=2.7.10.2
Alternative name(s):
Abelson murine leukemia viral oncogene homolog 2
Abelson-related gene protein
Tyrosine-protein kinase ARG
Gene names
Name:ABL2
Synonyms:ABLL, ARG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1182 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-receptor tyrosine-protein kinase that plays an ABL1-overlapping role in key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion and receptor endocytosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and regulates actin cytoskeletal structure through its F-actin-bundling activity. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL, DOK1 or ARHGAP35. Adhesion-dependent phosphorylation of ARHGAP35 promotes its association with RASA1, resulting in recruitment of ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other substrates which are involved in endocytosis regulation such as RIN1. In brain, may regulate neurotransmission by phosphorylating proteins at the synapse. ABL2 acts also as a regulator of multiple pathological signaling cascades during infection. Pathogens can highjack ABL2 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Ref.11 Ref.12 Ref.13 Ref.15 Ref.17

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Cofactor

Magnesium or manganese.

Enzyme regulation

Stabilized in the inactive form by an association between the SH3 domain and the SH2-TK linker region, interactions of the N-terminal cap, and contributions from an N-terminal myristoyl group and phospholipids. Activated by autophosphorylation as well as by SRC-family kinase-mediated phosphorylation. Activated by RIN1 binding to the SH2 and SH3 domains. Inhibited by imatinib mesylate (Gleevec) which is used for the treatment of chronic myeloid leukemia (CML). Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant phosphoinositide known to regulate cytoskeletal and membrane proteins, inhibits the tyrosine kinase activity By similarity. Ref.10 Ref.11

Subunit structure

Interacts with PSMA7. Interacts with CTTN. Ref.11 Ref.13 Ref.31

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Widely expressed.

Domain

Contains two distinct classes of F-actin-binding domains. Although both can bind F-actin, the 2 are required to bundle actin filaments By similarity. Ref.27

Post-translational modification

Phosphorylated at Tyr-261 by ABL1 in response to oxidative stress. Phosphorylated by PDGFRB By similarity. Ref.10 Ref.12

Polyubiquitinated. Polyubiquitination of ABL2 leads to degradation.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Sequence caution

The sequence CAD98092.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament bundle assembly

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cellular protein modification process

Traceable author statement Ref.1. Source: ProtInc

cellular response to retinoic acid

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.11. Source: UniProtKB

positive regulation of neuron projection development

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

positive regulation of oxidoreductase activity

Inferred from direct assay PubMed 12893824. Source: BHF-UCL

regulation of actin cytoskeleton reorganization

Traceable author statement Ref.27. Source: UniProtKB

regulation of autophagy

Traceable author statement Ref.27. Source: UniProtKB

regulation of cell adhesion

Traceable author statement Ref.27. Source: UniProtKB

regulation of cell motility

Traceable author statement Ref.27. Source: UniProtKB

regulation of endocytosis

Traceable author statement Ref.27. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentactin cytoskeleton

Traceable author statement Ref.27. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

actin filament binding

Traceable author statement Ref.27. Source: UniProtKB

actin monomer binding

Traceable author statement Ref.27. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.11. Source: UniProtKB

manganese ion binding

Inferred from direct assay Ref.11. Source: UniProtKB

non-membrane spanning protein tyrosine kinase activity

Traceable author statement Ref.27. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11PubMed 16273093PubMed 17474147PubMed 19380743PubMed 20598684PubMed 24728074. Source: IntAct

protein kinase activity

Traceable author statement Ref.1. Source: ProtInc

protein tyrosine kinase activity

Inferred from direct assay Ref.11. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P42684-1)

Also known as: IB; 1BLCTL;

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: P42684-2)

Also known as: IA; 1ASCTL;

The sequence of this isoform differs from the canonical sequence as follows:
     2-73: GQQVGRVGEA...EGDKTGGSSP → MVLGTVLLPP...ASESALPDLT
Isoform 3 (identifier: P42684-3)

Also known as: IC; 1ALCTL;

The sequence of this isoform differs from the canonical sequence as follows:
     2-52: GQQVGRVGEA...ETGFNIFTQH → MVLGTVLLPP...ASESALPDLT
Isoform 4 (identifier: P42684-4)

Also known as: 1ASCTS;

The sequence of this isoform differs from the canonical sequence as follows:
     2-73: GQQVGRVGEA...EGDKTGGSSP → MVLGTVLLPP...ASESALPDLT
     688-790: Missing.
Note: Contains a phosphotyrosine at position 647.
Isoform 5 (identifier: P42684-5)

Also known as: 1BLCTS;

The sequence of this isoform differs from the canonical sequence as follows:
     688-790: Missing.
Note: Contains a phosphotyrosine at position 683.
Isoform 6 (identifier: P42684-6)

Also known as: 1BSCTL;

The sequence of this isoform differs from the canonical sequence as follows:
     53-73: Missing.
Isoform 7 (identifier: P42684-7)

Also known as: 1BSCTS;

The sequence of this isoform differs from the canonical sequence as follows:
     53-73: Missing.
     688-790: Missing.
Note: Contains a phosphotyrosine at position 662.
Isoform 10 (identifier: P42684-10)

Also known as: 1ALCTS;

The sequence of this isoform differs from the canonical sequence as follows:
     2-52: GQQVGRVGEA...ETGFNIFTQH → MVLGTVLLPP...ASESALPDLT
     688-790: Missing.
Note: Contains a phosphotyrosine at position 668.
Isoform 8 (identifier: P42684-8)

The sequence of this isoform differs from the canonical sequence as follows:
     53-73: Missing.
     550-564: EEVAEELGRAASSSS → EVLLHCANQTCITL
     565-1182: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 11821181Abelson tyrosine-protein kinase 2
PRO_0000088052

Regions

Domain107 – 16761SH3
Domain173 – 26391SH2
Domain288 – 539252Protein kinase
Nucleotide binding294 – 3029ATP By similarity
Nucleotide binding362 – 3687ATP By similarity
Region2 – 106105CAP
Region694 – 930237F-actin-binding By similarity
Region1020 – 1182163F-actin-binding By similarity
Motif427 – 45125Kinase activation loop By similarity
Motif658 – 6603Nuclear localization signal Potential
Compositional bias561 – 5644Poly-Ser
Compositional bias732 – 7398Poly-Gly
Compositional bias843 – 1055213Pro-rich
Compositional bias984 – 9885Poly-Pro

Sites

Active site4091Proton acceptor By similarity
Binding site3171ATP By similarity

Amino acid modifications

Modified residue2611Phosphotyrosine; by ABL1 and autocatalysis Ref.12
Modified residue2721Phosphotyrosine; by autocatalysis Ref.10
Modified residue2751Phosphoserine Ref.20
Modified residue4391Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases Ref.10
Modified residue5681Phosphotyrosine; by autocatalysis Ref.10
Modified residue6201Phosphoserine Ref.21
Modified residue6311Phosphoserine Ref.21 Ref.26 Ref.28
Modified residue6331Phosphoserine Ref.21
Modified residue6551Phosphoserine Ref.21
Modified residue6831Phosphotyrosine; by autocatalysis Ref.10 Ref.24
Modified residue7181Phosphotyrosine Ref.24
Modified residue8171Phosphoserine Ref.16 Ref.21
Modified residue8201Phosphoserine Ref.21 Ref.25
Modified residue9151Phosphoserine Ref.20
Modified residue9361Phosphoserine Ref.21 Ref.25 Ref.26
Lipidation21N-myristoyl glycine By similarity

Natural variations

Alternative sequence2 – 7372GQQVG…GGSSP → MVLGTVLLPPNSYGRDQDTS LCCLCTEASESALPDLT in isoform 2 and isoform 4.
VSP_004961
Alternative sequence2 – 5251GQQVG…IFTQH → MVLGTVLLPPNSYGRDQDTS LCCLCTEASESALPDLT in isoform 3 and isoform 10.
VSP_017112
Alternative sequence53 – 7321Missing in isoform 6, isoform 7 and isoform 8.
VSP_041772
Alternative sequence550 – 56415EEVAE…ASSSS → EVLLHCANQTCITL in isoform 8.
VSP_041773
Alternative sequence565 – 1182618Missing in isoform 8.
VSP_041774
Alternative sequence688 – 790103Missing in isoform 4, isoform 5, isoform 7 and isoform 10.
VSP_021308
Natural variant781R → H. Ref.32
Corresponds to variant rs55655202 [ dbSNP | Ensembl ].
VAR_055411
Natural variant991E → Q Somatic mutation in a breast cancer sample. Ref.32
VAR_055412
Natural variant5191R → I Somatic mutation in a lung squamous cell carcinoma. Ref.32
VAR_055413
Natural variant7691T → S. Ref.32
Corresponds to variant rs55892721 [ dbSNP | Ensembl ].
VAR_055414
Natural variant9301K → R. Ref.5 Ref.32
Corresponds to variant rs17277288 [ dbSNP | Ensembl ].
VAR_029232
Natural variant9461V → M. Ref.5
Corresponds to variant rs28913889 [ dbSNP | Ensembl ].
VAR_029233
Natural variant9961P → R. Ref.5 Ref.32
Corresponds to variant rs28913890 [ dbSNP | Ensembl ].
VAR_029234
Natural variant10851S → N. Ref.5
Corresponds to variant rs28913891 [ dbSNP | Ensembl ].
VAR_029235
Natural variant11011T → A. Ref.5
Corresponds to variant rs28913892 [ dbSNP | Ensembl ].
VAR_029236
Isoform 4:
Natural variant121N → T.
Corresponds to variant rs1318056 [ dbSNP | Ensembl ].

Experimental info

Sequence conflict343 – 3442NL → TI no nucleotide entry Ref.9
Sequence conflict4351T → I in AK311045. Ref.3
Sequence conflict9811K → R in CAD98092. Ref.4

Secondary structure

......................................................................................... 1182
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (IB) (1BLCTL) [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: ED93869BC2B14FAA

FASTA1,182128,343
        10         20         30         40         50         60 
MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TTETGFNIFT QHDHFASCVE 

        70         80         90        100        110        120 
DGFEGDKTGG SSPEALHRPY GCDVEPQALN EAIRWSSKEN LLGATESDPN LFVALYDFVA 

       130        140        150        160        170        180 
SGDNTLSITK GEKLRVLGYN QNGEWSEVRS KNGQGWVPSN YITPVNSLEK HSWYHGPVSR 

       190        200        210        220        230        240 
SAAEYLLSSL INGSFLVRES ESSPGQLSIS LRYEGRVYHY RINTTADGKV YVTAESRFST 

       250        260        270        280        290        300 
LAELVHHHST VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG 

       310        320        330        340        350        360 
EVYVGVWKKY SLTVAVKTLK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV CTLEPPFYIV 

       370        380        390        400        410        420 
TEYMPYGNLL DYLRECNREE VTAVVLLYMA TQISSAMEYL EKKNFIHRDL AARNCLVGEN 

       430        440        450        460        470        480 
HVVKVADFGL SRLMTGDTYT AHAGAKFPIK WTAPESLAYN TFSIKSDVWA FGVLLWEIAT 

       490        500        510        520        530        540 
YGMSPYPGID LSQVYDLLEK GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE 

       550        560        570        580        590        600 
TMFHDSSISE EVAEELGRAA SSSSVVPYLP RLPILPSKTR TLKKQVENKE NIEGAQDATE 

       610        620        630        640        650        660 
NSASSLAPGF IRGAQASSGS PALPRKQRDK SPSSLLEDAK ETCFTRDRKG GFFSSFMKKR 

       670        680        690        700        710        720 
NAPTPPKRSS SFREMENQPH KKYELTGNFS SVASLQHADG FSFTPAQQEA NLVPPKCYGG 

       730        740        750        760        770        780 
SFAQRNLCND DGGGGGGSGT AGGGWSGITG FFTPRLIKKT LGLRAGKPTA SDDTSKPFPR 

       790        800        810        820        830        840 
SNSTSSMSSG LPEQDRMAMT LPRNCQRSKL QLERTVSTSS QPEENVDRAN DMLPKKSEES 

       850        860        870        880        890        900 
AAPSRERPKA KLLPRGATAL PLRTPSGDLA ITEKDPPGVG VAGVAAAPKG KEKNGGARLG 

       910        920        930        940        950        960 
MAGVPEDGEQ PGWPSPAKAA PVLPTTHNHK VPVLISPTLK HTPADVQLIG TDSQGNKFKL 

       970        980        990       1000       1010       1020 
LSEHQVTSSG DKDRPRRVKP KCAPPPPPVM RLLQHPSICS DPTEEPTALT AGQSTSETQE 

      1030       1040       1050       1060       1070       1080 
GGKKAALGAV PISGKAGRPV MPPPQVPLPT SSISPAKMAN GTAGTKVALR KTKQAAEKIS 

      1090       1100       1110       1120       1130       1140 
ADKISKEALL ECADLLSSAL TEPVPNSQLV DTGHQLLDYC SGYVDCIPQT RNKFAFREAV 

      1150       1160       1170       1180 
SKLELSLQEL QVSSAAAGVP GTNPVLNNLL SCVQEISDVV QR 

« Hide

Isoform 2 (IA) (1ASCTL) [UniParc].

Checksum: 8A3D812B95967973
Show »

FASTA1,147124,691
Isoform 3 (IC) (1ALCTL) [UniParc].

Checksum: 5D5DD889471CAF96
Show »

FASTA1,168126,815
Isoform 4 (1ASCTS) [UniParc].

Checksum: D7A147578C36CBA0
Show »

FASTA1,044114,290
Isoform 5 (1BLCTS) [UniParc].

Checksum: 9916652E5DB8F74D
Show »

FASTA1,079117,942
Isoform 6 (1BSCTL) [UniParc].

Checksum: A54046CDF6770B1C
Show »

FASTA1,161126,219
Isoform 7 (1BSCTS) [UniParc].

Checksum: 28DCB354F9917898
Show »

FASTA1,058115,817
Isoform 10 (1ALCTS) [UniParc].

Checksum: ABED958129E9D74E
Show »

FASTA1,065116,414
Isoform 8 [UniParc].

Checksum: 89E988F0EFF2ABCF
Show »

FASTA54260,864

References

« Hide 'large scale' references
[1]"The complete coding sequence of arg defines the Abelson subfamily of cytoplasmic tyrosine kinases."
Kruh G.D., Perego R., Miki T., Aaronson S.A.
Proc. Natl. Acad. Sci. U.S.A. 87:5802-5806(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2).
[2]"Eight full-length abelson related gene (Arg) isoforms are constitutively expressed in caki-1 cell line and cell distribution of two isoforms has been analyzed after transfection."
Bianchi C., Torsello B., Angeloni V., Bombelli S., Soldi M., Invernizzi L., Brambilla P., Perego R.A.
J. Cell. Biochem. 105:1219-1227(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6 AND 7), ALTERNATIVE SPLICING (ISOFORM 10), VARIANT THR-12 (ISOFORM 4).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Uterine endothelium.
[5]NIEHS SNPs program
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-930; MET-946; ARG-996; ASN-1085 AND ALA-1101.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 3).
Tissue: Brain.
[9]"A novel human gene closely related to the abl proto-oncogene."
Kruh G.D., King C.R., Kraus M.H., Popescu N.C., Amsbaugh S.C., McBride W.O., Aaronson S.A.
Science 234:1545-1548(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 343-469.
[10]"Two distinct phosphorylation pathways have additive effects on Abl family kinase activation."
Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J.
Mol. Cell. Biol. 23:3884-3896(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION AT TYR-272; TYR-439; TYR-568 AND TYR-683, ENZYME REGULATION.
[11]"RIN1 is an ABL tyrosine kinase activator and a regulator of epithelial-cell adhesion and migration."
Hu H., Bliss J.M., Wang Y., Colicelli J.
Curr. Biol. 15:815-823(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RIN1, FUNCTION, ENZYME REGULATION.
[12]"Ubiquitination and degradation of the Arg tyrosine kinase is regulated by oxidative stress."
Cao C., Li Y., Leng Y., Li P., Ma Q., Kufe D.
Oncogene 24:2433-2440(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-261, UBIQUITINATION.
[13]"Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit PSMA7 regulates proteasome degradation."
Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q., Cao C.
Mol. Cell 22:317-327(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PSMA7.
[14]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"A critical role for cortactin phosphorylation by Abl-family kinases in PDGF-induced dorsal-wave formation."
Boyle S.N., Michaud G.A., Schweitzer B., Predki P.F., Koleske A.J.
Curr. Biol. 17:445-451(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[17]"Abl kinases regulate autophagy by promoting the trafficking and function of lysosomal components."
Yogalingam G., Pendergast A.M.
J. Biol. Chem. 283:35941-35953(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases."
Woodring P.J., Hunter T., Wang J.Y.
J. Cell Sci. 116:2613-2626(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[19]"How do Abl family kinases regulate cell shape and movement?"
Hernandez S.E., Krishnaswami M., Miller A.L., Koleske A.J.
Trends Cell Biol. 14:36-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-915, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620; SER-631; SER-633; SER-655; SER-817; SER-820 AND SER-936, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Emerging roles of Abl family tyrosine kinases in microbial pathogenesis."
Backert S., Feller S.M., Wessler S.
Trends Biochem. Sci. 33:80-90(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[23]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-718, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-668 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-647 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-683 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-662 (ISOFORM 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820 AND SER-936, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[26]"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-631 AND SER-936, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"ABL tyrosine kinases: evolution of function, regulation, and specificity."
Colicelli J.
Sci. Signal. 3:RE6-RE6(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION, DOMAIN.
[28]"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-631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Solution structure of the human ABL2 SH2 domain."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 163-268.
[30]"Crystal structures of ABL-related gene (ABL2) in complex with imatinib, tozasertib (VX-680), and a type I inhibitor of the triazole carbothioamide class."
Salah E., Ugochukwu E., Barr A.J., von Delft F., Knapp S., Elkins J.M.
J. Med. Chem. 54:2359-2367(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 279-546 IN COMPLEXES WITH INHIBITORS.
[31]"Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin-Arg-lysozyme complex."
Liu W., MacGrath S.M., Koleske A.J., Boggon T.J.
Acta Crystallogr. F 68:154-158(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 563-579 IN COMPLEX WITH CTTN, INTERACTION WITH CTTN.
[32]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-78; GLN-99; ILE-519; SER-769; ARG-930 AND ARG-996, VARIANT [LARGE SCALE ANALYSIS] THR-12 (ISOFORM 4).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35296 mRNA. Translation: AAA35553.1.
FJ542283 mRNA. Translation: ACK76601.1.
FJ542284 mRNA. Translation: ACK76602.1.
FJ542285 mRNA. Translation: ACK76603.1.
FJ542286 mRNA. Translation: ACK76604.1.
AK311045 mRNA. No translation available.
BX538317 mRNA. Translation: CAD98092.1. Different initiation.
DQ009672 Genomic DNA. Translation: AAY16984.1.
AL139132, AL359179, AL512326 Genomic DNA. Translation: CAH70921.1.
AL139132, AL359179, AL512326 Genomic DNA. Translation: CAH70925.1.
AL359179, AL139132, AL512326 Genomic DNA. Translation: CAI15584.1.
AL359179, AL139132, AL512326 Genomic DNA. Translation: CAI15585.1.
AL512326, AL359179, AL139132 Genomic DNA. Translation: CAI13566.1.
AL512326, AL359179, AL139132 Genomic DNA. Translation: CAI13570.1.
CH471067 Genomic DNA. Translation: EAW91040.1.
BC065912 mRNA. Translation: AAH65912.1.
CCDSCCDS30947.1. [P42684-1]
CCDS41441.2. [P42684-3]
CCDS44282.1. [P42684-10]
CCDS44283.1. [P42684-8]
CCDS53435.1. [P42684-4]
CCDS53436.1. [P42684-6]
CCDS53437.1. [P42684-7]
CCDS53438.1. [P42684-5]
PIRA35962.
B35962.
RefSeqNP_001129472.1. NM_001136000.2.
NP_001129473.1. NM_001136001.1. [P42684-8]
NP_001161708.1. NM_001168236.1. [P42684-6]
NP_001161709.1. NM_001168237.1. [P42684-5]
NP_001161710.1. NM_001168238.1. [P42684-7]
NP_001161711.1. NM_001168239.1.
NP_005149.4. NM_005158.4.
NP_009298.1. NM_007314.3. [P42684-1]
UniGeneHs.159472.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ECDNMR-A163-268[»]
2KK1NMR-A1058-1182[»]
2XYNX-ray2.81A/B/C279-546[»]
3GVUX-ray2.05A279-546[»]
3HMIX-ray1.65A279-546[»]
3ULRX-ray1.65C563-579[»]
4EIHX-ray1.20A165-273[»]
ProteinModelPortalP42684.
SMRP42684. Positions 108-558, 1058-1182.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106545. 25 interactions.
DIPDIP-91N.
IntActP42684. 34 interactions.
MINTMINT-1347081.
STRING9606.ENSP00000356595.

Chemistry

BindingDBP42684.
ChEMBLCHEMBL4014.
DrugBankDB00171. Adenosine triphosphate.
DB01254. Dasatinib.
GuidetoPHARMACOLOGY1924.

PTM databases

PhosphoSiteP42684.

Polymorphism databases

DMDM1168268.

Proteomic databases

MaxQBP42684.
PaxDbP42684.
PRIDEP42684.

Protocols and materials databases

DNASU27.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344730; ENSP00000339209; ENSG00000143322. [P42684-10]
ENST00000367623; ENSP00000356595; ENSG00000143322. [P42684-6]
ENST00000392043; ENSP00000375897; ENSG00000143322. [P42684-8]
ENST00000408940; ENSP00000386152; ENSG00000143322. [P42684-2]
ENST00000502732; ENSP00000427562; ENSG00000143322. [P42684-1]
ENST00000504405; ENSP00000426831; ENSG00000143322. [P42684-4]
ENST00000507173; ENSP00000423413; ENSG00000143322. [P42684-7]
ENST00000511413; ENSP00000424697; ENSG00000143322. [P42684-5]
ENST00000512653; ENSP00000423578; ENSG00000143322. [P42684-3]
GeneID27.
KEGGhsa:27.
UCSCuc001gmg.4. human. [P42684-10]
uc001gmi.4. human. [P42684-3]
uc001gmj.4. human. [P42684-1]
uc001gmk.3. human. [P42684-8]
uc010pne.2. human. [P42684-4]
uc010pnf.2. human. [P42684-5]
uc010png.2. human. [P42684-7]
uc010pnh.2. human. [P42684-6]

Organism-specific databases

CTD27.
GeneCardsGC01M179068.
HGNCHGNC:77. ABL2.
HPACAB017106.
HPA001866.
MIM164690. gene.
neXtProtNX_P42684.
PharmGKBPA24414.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG004162.
InParanoidP42684.
KOK08887.
OMAPPKCYGG.
OrthoDBEOG7GTT2V.
PhylomeDBP42684.
TreeFamTF105081.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111045. Developmental Biology.
SignaLinkP42684.

Gene expression databases

BgeeP42684.
CleanExHS_ABL2.
GenevestigatorP42684.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR015015. F-actin_binding.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTSM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSABL2. human.
EvolutionaryTraceP42684.
GeneWikiABL2.
GenomeRNAi27.
NextBio89.
PROP42684.
SOURCESearch...

Entry information

Entry nameABL2_HUMAN
AccessionPrimary (citable) accession number: P42684
Secondary accession number(s): A0M8X0 expand/collapse secondary AC list , B7UEF2, B7UEF3, B7UEF4, B7UEF5, Q5T0X6, Q5W0C5, Q6NZY6, Q7Z301
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM