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P42684

- ABL2_HUMAN

UniProt

P42684 - ABL2_HUMAN

Protein

Abelson tyrosine-protein kinase 2

Gene

ABL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    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, ABI1.5 Publications

    Catalytic activityi

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

    Cofactori

    Magnesium or manganese.

    Enzyme regulationi

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei317 – 3171ATPPROSITE-ProRule annotation
    Active sitei409 – 4091Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi294 – 3029ATPPROSITE-ProRule annotation
    Nucleotide bindingi362 – 3687ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. actin filament binding Source: UniProtKB
    2. actin monomer binding Source: UniProtKB
    3. ATP binding Source: UniProtKB-KW
    4. magnesium ion binding Source: UniProtKB
    5. manganese ion binding Source: UniProtKB
    6. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
    7. protein binding Source: IntAct
    8. protein kinase activity Source: ProtInc
    9. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. actin filament bundle assembly Source: Ensembl
    2. axon guidance Source: Reactome
    3. cell adhesion Source: UniProtKB-KW
    4. cellular protein modification process Source: ProtInc
    5. cellular response to retinoic acid Source: BHF-UCL
    6. peptidyl-tyrosine phosphorylation Source: UniProtKB
    7. positive regulation of neuron projection development Source: BHF-UCL
    8. positive regulation of oxidoreductase activity Source: BHF-UCL
    9. regulation of actin cytoskeleton reorganization Source: UniProtKB
    10. regulation of autophagy Source: UniProtKB
    11. regulation of cell adhesion Source: UniProtKB
    12. regulation of cell motility Source: UniProtKB
    13. regulation of endocytosis Source: UniProtKB
    14. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 2681.
    ReactomeiREACT_19230. Role of Abl in Robo-Slit signaling.
    SignaLinkiP42684.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:ABL2
    Synonyms:ABLL, ARG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:77. ABL2.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24414.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 11821181Abelson tyrosine-protein kinase 2PRO_0000088052Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Modified residuei261 – 2611Phosphotyrosine; by ABL1 and autocatalysis1 Publication
    Modified residuei272 – 2721Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei275 – 2751Phosphoserine1 Publication
    Modified residuei439 – 4391Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases1 Publication
    Modified residuei568 – 5681Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei620 – 6201Phosphoserine1 Publication
    Modified residuei631 – 6311Phosphoserine3 Publications
    Modified residuei633 – 6331Phosphoserine1 Publication
    Modified residuei655 – 6551Phosphoserine1 Publication
    Modified residuei683 – 6831Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei718 – 7181Phosphotyrosine1 Publication
    Modified residuei817 – 8171Phosphoserine2 Publications
    Modified residuei820 – 8201Phosphoserine2 Publications
    Modified residuei915 – 9151Phosphoserine1 Publication
    Modified residuei936 – 9361Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated at Tyr-261 by ABL1 in response to oxidative stress. Phosphorylated by PDGFRB By similarity.By similarity
    Polyubiquitinated. Polyubiquitination of ABL2 leads to degradation.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP42684.
    PaxDbiP42684.
    PRIDEiP42684.

    PTM databases

    PhosphoSiteiP42684.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    BgeeiP42684.
    CleanExiHS_ABL2.
    GenevestigatoriP42684.

    Organism-specific databases

    HPAiCAB017106.
    HPA001866.

    Interactioni

    Subunit structurei

    Interacts with PSMA7. Interacts with CTTN. Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABI1Q8IZP02EBI-1102694,EBI-375446
    CRKP461085EBI-1102694,EBI-886
    EGFRP005337EBI-1102694,EBI-297353
    ERBB2P046266EBI-1102694,EBI-641062
    ERBB3P2186010EBI-1102694,EBI-720706
    ERBB4Q153034EBI-1102694,EBI-80371
    FYNP062412EBI-1102694,EBI-515315
    GRB2P629932EBI-1102694,EBI-401755
    KITP107212EBI-1102694,EBI-1379503
    NCK1P163334EBI-1102694,EBI-389883
    PIK3R1P279862EBI-1102694,EBI-79464
    PLCG1P191744EBI-1102694,EBI-79387
    RIN1Q136714EBI-1102694,EBI-366017
    SRCP129312EBI-1102694,EBI-621482

    Protein-protein interaction databases

    BioGridi106545. 25 interactions.
    DIPiDIP-91N.
    IntActiP42684. 37 interactions.
    MINTiMINT-1347081.
    STRINGi9606.ENSP00000356595.

    Structurei

    Secondary structure

    1
    1182
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi168 – 1703
    Beta strandi174 – 1774
    Helixi180 – 1878
    Beta strandi194 – 1996
    Beta strandi207 – 2137
    Beta strandi216 – 2216
    Beta strandi226 – 2283
    Beta strandi230 – 2334
    Beta strandi236 – 2405
    Helixi241 – 2488
    Beta strandi255 – 2573
    Beta strandi280 – 2823
    Helixi285 – 2873
    Beta strandi288 – 2936
    Helixi294 – 2974
    Beta strandi300 – 3078
    Helixi308 – 3103
    Beta strandi312 – 3187
    Helixi326 – 33712
    Beta strandi347 – 3515
    Beta strandi353 – 3564
    Beta strandi358 – 3625
    Helixi369 – 3757
    Turni378 – 3803
    Helixi383 – 40220
    Helixi412 – 4143
    Beta strandi415 – 4173
    Helixi419 – 4213
    Beta strandi423 – 4253
    Beta strandi435 – 4373
    Beta strandi438 – 4403
    Helixi449 – 4513
    Helixi454 – 4596
    Helixi464 – 47916
    Helixi491 – 4933
    Helixi494 – 4996
    Helixi512 – 52110
    Helixi526 – 5283
    Helixi532 – 54514
    Helixi1069 – 10713
    Turni1076 – 10783
    Helixi1080 – 10834
    Helixi1086 – 109914
    Helixi1106 – 112318
    Helixi1124 – 11263
    Helixi1130 – 115223
    Beta strandi1155 – 11584
    Helixi1165 – 118117

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP42684.
    SMRiP42684. Positions 108-558, 1058-1182.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42684.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini107 – 16761SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini173 – 26391SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini288 – 539252Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 106105CAPAdd
    BLAST
    Regioni694 – 930237F-actin-bindingBy similarityAdd
    BLAST
    Regioni1020 – 1182163F-actin-bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi427 – 45125Kinase activation loopBy similarityAdd
    BLAST
    Motifi658 – 6603Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi561 – 5644Poly-Ser
    Compositional biasi732 – 7398Poly-Gly
    Compositional biasi843 – 1055213Pro-richAdd
    BLAST
    Compositional biasi984 – 9885Poly-Pro

    Domaini

    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).By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG004162.
    InParanoidiP42684.
    KOiK08887.
    OMAiPPKCYGG.
    OrthoDBiEOG7GTT2V.
    PhylomeDBiP42684.
    TreeFamiTF105081.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR015015. 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]
    PfamiPF08919. F_actin_bind. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00808. FABD. 1 hit.
    SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. 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]

    Sequences (9)i

    Sequence statusi: Complete.

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

    This entry describes 9 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P42684-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TTETGFNIFT     50
    QHDHFASCVE DGFEGDKTGG SSPEALHRPY GCDVEPQALN EAIRWSSKEN 100
    LLGATESDPN LFVALYDFVA SGDNTLSITK GEKLRVLGYN QNGEWSEVRS 150
    KNGQGWVPSN YITPVNSLEK HSWYHGPVSR SAAEYLLSSL INGSFLVRES 200
    ESSPGQLSIS LRYEGRVYHY RINTTADGKV YVTAESRFST LAELVHHHST 250
    VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG 300
    EVYVGVWKKY SLTVAVKTLK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV 350
    CTLEPPFYIV TEYMPYGNLL DYLRECNREE VTAVVLLYMA TQISSAMEYL 400
    EKKNFIHRDL AARNCLVGEN HVVKVADFGL SRLMTGDTYT AHAGAKFPIK 450
    WTAPESLAYN TFSIKSDVWA FGVLLWEIAT YGMSPYPGID LSQVYDLLEK 500
    GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE TMFHDSSISE 550
    EVAEELGRAA SSSSVVPYLP RLPILPSKTR TLKKQVENKE NIEGAQDATE 600
    NSASSLAPGF IRGAQASSGS PALPRKQRDK SPSSLLEDAK ETCFTRDRKG 650
    GFFSSFMKKR NAPTPPKRSS SFREMENQPH KKYELTGNFS SVASLQHADG 700
    FSFTPAQQEA NLVPPKCYGG SFAQRNLCND DGGGGGGSGT AGGGWSGITG 750
    FFTPRLIKKT LGLRAGKPTA SDDTSKPFPR SNSTSSMSSG LPEQDRMAMT 800
    LPRNCQRSKL QLERTVSTSS QPEENVDRAN DMLPKKSEES AAPSRERPKA 850
    KLLPRGATAL PLRTPSGDLA ITEKDPPGVG VAGVAAAPKG KEKNGGARLG 900
    MAGVPEDGEQ PGWPSPAKAA PVLPTTHNHK VPVLISPTLK HTPADVQLIG 950
    TDSQGNKFKL LSEHQVTSSG DKDRPRRVKP KCAPPPPPVM RLLQHPSICS 1000
    DPTEEPTALT AGQSTSETQE GGKKAALGAV PISGKAGRPV MPPPQVPLPT 1050
    SSISPAKMAN GTAGTKVALR KTKQAAEKIS ADKISKEALL ECADLLSSAL 1100
    TEPVPNSQLV DTGHQLLDYC SGYVDCIPQT RNKFAFREAV SKLELSLQEL 1150
    QVSSAAAGVP GTNPVLNNLL SCVQEISDVV QR 1182
    Length:1,182
    Mass (Da):128,343
    Last modified:November 1, 1995 - v1
    Checksum:iED93869BC2B14FAA
    GO
    Isoform 2 (identifier: P42684-2) [UniParc]FASTAAdd to Basket

    Also known as: IA, 1ASCTL

    The sequence of this isoform differs from the canonical sequence as follows:
         2-73: GQQVGRVGEA...EGDKTGGSSP → MVLGTVLLPP...ASESALPDLT

    Show »
    Length:1,147
    Mass (Da):124,691
    Checksum:i8A3D812B95967973
    GO
    Isoform 3 (identifier: P42684-3) [UniParc]FASTAAdd to Basket

    Also known as: IC, 1ALCTL

    The sequence of this isoform differs from the canonical sequence as follows:
         2-52: GQQVGRVGEA...ETGFNIFTQH → MVLGTVLLPP...ASESALPDLT

    Show »
    Length:1,168
    Mass (Da):126,815
    Checksum:i5D5DD889471CAF96
    GO
    Isoform 4 (identifier: P42684-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,044
    Mass (Da):114,290
    Checksum:iD7A147578C36CBA0
    GO
    Isoform 5 (identifier: P42684-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,079
    Mass (Da):117,942
    Checksum:i9916652E5DB8F74D
    GO
    Isoform 6 (identifier: P42684-6) [UniParc]FASTAAdd to Basket

    Also known as: 1BSCTL

    The sequence of this isoform differs from the canonical sequence as follows:
         53-73: Missing.

    Show »
    Length:1,161
    Mass (Da):126,219
    Checksum:iA54046CDF6770B1C
    GO
    Isoform 7 (identifier: P42684-7) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,058
    Mass (Da):115,817
    Checksum:i28DCB354F9917898
    GO
    Isoform 10 (identifier: P42684-10) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,065
    Mass (Da):116,414
    Checksum:iABED958129E9D74E
    GO
    Isoform 8 (identifier: P42684-8) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:542
    Mass (Da):60,864
    Checksum:i89E988F0EFF2ABCF
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti343 – 3442NL → TI no nucleotide entry (PubMed:3787260)Curated
    Sequence conflicti435 – 4351T → I in AK311045. (PubMed:14702039)Curated
    Sequence conflicti981 – 9811K → R in CAD98092. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti78 – 781R → H.1 Publication
    Corresponds to variant rs55655202 [ dbSNP | Ensembl ].
    VAR_055411
    Natural varianti99 – 991E → Q Somatic mutation in a breast cancer sample. 1 Publication
    VAR_055412
    Natural varianti519 – 5191R → I Somatic mutation in a lung squamous cell carcinoma. 1 Publication
    VAR_055413
    Natural varianti769 – 7691T → S.1 Publication
    Corresponds to variant rs55892721 [ dbSNP | Ensembl ].
    VAR_055414
    Natural varianti930 – 9301K → R.2 Publications
    Corresponds to variant rs17277288 [ dbSNP | Ensembl ].
    VAR_029232
    Natural varianti946 – 9461V → M.1 Publication
    Corresponds to variant rs28913889 [ dbSNP | Ensembl ].
    VAR_029233
    Natural varianti996 – 9961P → R.2 Publications
    Corresponds to variant rs28913890 [ dbSNP | Ensembl ].
    VAR_029234
    Natural varianti1085 – 10851S → N.1 Publication
    Corresponds to variant rs28913891 [ dbSNP | Ensembl ].
    VAR_029235
    Natural varianti1101 – 11011T → A.1 Publication
    Corresponds to variant rs28913892 [ dbSNP | Ensembl ].
    VAR_029236
    Isoform 4 (identifier: P42684-4)
    Natural varianti12 – 121N → T.
    Corresponds to variant rs1318056 [ dbSNP | Ensembl ].

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 7372GQQVG…GGSSP → MVLGTVLLPPNSYGRDQDTS LCCLCTEASESALPDLT in isoform 2 and isoform 4. 2 PublicationsVSP_004961Add
    BLAST
    Alternative sequencei2 – 5251GQQVG…IFTQH → MVLGTVLLPPNSYGRDQDTS LCCLCTEASESALPDLT in isoform 3 and isoform 10. 1 PublicationVSP_017112Add
    BLAST
    Alternative sequencei53 – 7321Missing in isoform 6, isoform 7 and isoform 8. 2 PublicationsVSP_041772Add
    BLAST
    Alternative sequencei550 – 56415EEVAE…ASSSS → EVLLHCANQTCITL in isoform 8. 1 PublicationVSP_041773Add
    BLAST
    Alternative sequencei565 – 1182618Missing in isoform 8. 1 PublicationVSP_041774Add
    BLAST
    Alternative sequencei688 – 790103Missing in isoform 4, isoform 5, isoform 7 and isoform 10. 2 PublicationsVSP_021308Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS30947.1. [P42684-1]
    CCDS44283.1. [P42684-8]
    CCDS53436.1. [P42684-6]
    CCDS53437.1. [P42684-7]
    CCDS53438.1. [P42684-5]
    PIRiA35962.
    B35962.
    RefSeqiNP_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]
    UniGeneiHs.159472.

    Genome annotation databases

    EnsembliENST00000367623; ENSP00000356595; ENSG00000143322. [P42684-6]
    ENST00000392043; ENSP00000375897; ENSG00000143322. [P42684-8]
    ENST00000502732; ENSP00000427562; ENSG00000143322. [P42684-1]
    ENST00000507173; ENSP00000423413; ENSG00000143322. [P42684-7]
    ENST00000511413; ENSP00000424697; ENSG00000143322. [P42684-5]
    ENST00000512653; ENSP00000423578; ENSG00000143322. [P42684-3]
    GeneIDi27.
    KEGGihsa:27.
    UCSCiuc001gmg.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]

    Polymorphism databases

    DMDMi1168268.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs
    CGP resequencing studies

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS30947.1. [P42684-1 ]
    CCDS44283.1. [P42684-8 ]
    CCDS53436.1. [P42684-6 ]
    CCDS53437.1. [P42684-7 ]
    CCDS53438.1. [P42684-5 ]
    PIRi A35962.
    B35962.
    RefSeqi NP_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 ]
    UniGenei Hs.159472.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ECD NMR - A 163-268 [» ]
    2KK1 NMR - A 1058-1182 [» ]
    2XYN X-ray 2.81 A/B/C 279-546 [» ]
    3GVU X-ray 2.05 A 279-546 [» ]
    3HMI X-ray 1.65 A 279-546 [» ]
    3ULR X-ray 1.65 C 563-579 [» ]
    4EIH X-ray 1.20 A 165-273 [» ]
    ProteinModelPortali P42684.
    SMRi P42684. Positions 108-558, 1058-1182.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106545. 25 interactions.
    DIPi DIP-91N.
    IntActi P42684. 37 interactions.
    MINTi MINT-1347081.
    STRINGi 9606.ENSP00000356595.

    Chemistry

    BindingDBi P42684.
    ChEMBLi CHEMBL4014.
    DrugBanki DB00171. Adenosine triphosphate.
    DB01254. Dasatinib.
    GuidetoPHARMACOLOGYi 1924.

    PTM databases

    PhosphoSitei P42684.

    Polymorphism databases

    DMDMi 1168268.

    Proteomic databases

    MaxQBi P42684.
    PaxDbi P42684.
    PRIDEi P42684.

    Protocols and materials databases

    DNASUi 27.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367623 ; ENSP00000356595 ; ENSG00000143322 . [P42684-6 ]
    ENST00000392043 ; ENSP00000375897 ; ENSG00000143322 . [P42684-8 ]
    ENST00000502732 ; ENSP00000427562 ; ENSG00000143322 . [P42684-1 ]
    ENST00000507173 ; ENSP00000423413 ; ENSG00000143322 . [P42684-7 ]
    ENST00000511413 ; ENSP00000424697 ; ENSG00000143322 . [P42684-5 ]
    ENST00000512653 ; ENSP00000423578 ; ENSG00000143322 . [P42684-3 ]
    GeneIDi 27.
    KEGGi hsa:27.
    UCSCi uc001gmg.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

    CTDi 27.
    GeneCardsi GC01M179068.
    HGNCi HGNC:77. ABL2.
    HPAi CAB017106.
    HPA001866.
    MIMi 164690. gene.
    neXtProti NX_P42684.
    PharmGKBi PA24414.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG004162.
    InParanoidi P42684.
    KOi K08887.
    OMAi PPKCYGG.
    OrthoDBi EOG7GTT2V.
    PhylomeDBi P42684.
    TreeFami TF105081.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_19230. Role of Abl in Robo-Slit signaling.
    SignaLinki P42684.

    Miscellaneous databases

    ChiTaRSi ABL2. human.
    EvolutionaryTracei P42684.
    GeneWikii ABL2.
    GenomeRNAii 27.
    NextBioi 89.
    PROi P42684.
    SOURCEi Search...

    Gene expression databases

    Bgeei P42684.
    CleanExi HS_ABL2.
    Genevestigatori P42684.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR015015. 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 ]
    Pfami PF08919. F_actin_bind. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00808. FABD. 1 hit.
    SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.
      , 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. 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. 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: PHOSPHORYLATION 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. 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. 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. 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. "Unc119 protects from Shigella infection by inhibiting the Abl family kinases."
      Vepachedu R., Karim Z., Patel O., Goplen N., Alam R.
      PLoS ONE 4:E5211-E5211(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH UNC119: ABL1 AND CRK.
    26. "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.
    27. "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.
    28. "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.
    29. "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].
    30. "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.
    31. "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.
    32. "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.
    33. "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.
      , 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).

    Entry informationi

    Entry nameiABL2_HUMAN
    AccessioniPrimary (citable) accession number: P42684
    Secondary accession number(s): A0M8X0
    , B7UEF2, B7UEF3, B7UEF4, B7UEF5, Q5T0X6, Q5W0C5, Q6NZY6, Q7Z301
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 170 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3