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P42684

- ABL2_HUMAN

UniProt

P42684 - ABL2_HUMAN

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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

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 kinase activity Source: ProtInc
  8. 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 cytosolic calcium ion concentration Source: MGI
  8. positive regulation of neuron projection development Source: BHF-UCL
  9. positive regulation of oxidoreductase activity Source: BHF-UCL
  10. positive regulation of phospholipase C activity Source: MGI
  11. regulation of actin cytoskeleton reorganization Source: UniProtKB
  12. regulation of autophagy Source: UniProtKB
  13. regulation of cell adhesion Source: UniProtKB
  14. regulation of cell motility Source: UniProtKB
  15. regulation of endocytosis Source: UniProtKB
  16. signal transduction Source: ProtInc
Complete GO annotation...

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
Complete GO annotation...

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
EGFRP005338EBI-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. 28 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.
GeneTreeiENSGT00760000118938.
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

        10         20         30         40         50
MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TTETGFNIFT
60 70 80 90 100
QHDHFASCVE DGFEGDKTGG SSPEALHRPY GCDVEPQALN EAIRWSSKEN
110 120 130 140 150
LLGATESDPN LFVALYDFVA SGDNTLSITK GEKLRVLGYN QNGEWSEVRS
160 170 180 190 200
KNGQGWVPSN YITPVNSLEK HSWYHGPVSR SAAEYLLSSL INGSFLVRES
210 220 230 240 250
ESSPGQLSIS LRYEGRVYHY RINTTADGKV YVTAESRFST LAELVHHHST
260 270 280 290 300
VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG
310 320 330 340 350
EVYVGVWKKY SLTVAVKTLK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV
360 370 380 390 400
CTLEPPFYIV TEYMPYGNLL DYLRECNREE VTAVVLLYMA TQISSAMEYL
410 420 430 440 450
EKKNFIHRDL AARNCLVGEN HVVKVADFGL SRLMTGDTYT AHAGAKFPIK
460 470 480 490 500
WTAPESLAYN TFSIKSDVWA FGVLLWEIAT YGMSPYPGID LSQVYDLLEK
510 520 530 540 550
GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE TMFHDSSISE
560 570 580 590 600
EVAEELGRAA SSSSVVPYLP RLPILPSKTR TLKKQVENKE NIEGAQDATE
610 620 630 640 650
NSASSLAPGF IRGAQASSGS PALPRKQRDK SPSSLLEDAK ETCFTRDRKG
660 670 680 690 700
GFFSSFMKKR NAPTPPKRSS SFREMENQPH KKYELTGNFS SVASLQHADG
710 720 730 740 750
FSFTPAQQEA NLVPPKCYGG SFAQRNLCND DGGGGGGSGT AGGGWSGITG
760 770 780 790 800
FFTPRLIKKT LGLRAGKPTA SDDTSKPFPR SNSTSSMSSG LPEQDRMAMT
810 820 830 840 850
LPRNCQRSKL QLERTVSTSS QPEENVDRAN DMLPKKSEES AAPSRERPKA
860 870 880 890 900
KLLPRGATAL PLRTPSGDLA ITEKDPPGVG VAGVAAAPKG KEKNGGARLG
910 920 930 940 950
MAGVPEDGEQ PGWPSPAKAA PVLPTTHNHK VPVLISPTLK HTPADVQLIG
960 970 980 990 1000
TDSQGNKFKL LSEHQVTSSG DKDRPRRVKP KCAPPPPPVM RLLQHPSICS
1010 1020 1030 1040 1050
DPTEEPTALT AGQSTSETQE GGKKAALGAV PISGKAGRPV MPPPQVPLPT
1060 1070 1080 1090 1100
SSISPAKMAN GTAGTKVALR KTKQAAEKIS ADKISKEALL ECADLLSSAL
1110 1120 1130 1140 1150
TEPVPNSQLV DTGHQLLDYC SGYVDCIPQT RNKFAFREAV SKLELSLQEL
1160 1170 1180
QVSSAAAGVP GTNPVLNNLL SCVQEISDVV QR
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.
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. 28 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 .
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.
GeneTreei ENSGT00760000118938.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 171 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