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Protein

Abelson tyrosine-protein kinase 2

Gene

ABL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

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)DescriptionActionsGraphical viewLength
Binding sitei317ATPPROSITE-ProRule annotation1
Active sitei409Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi294 – 302ATPPROSITE-ProRule annotation9
Nucleotide bindingi362 – 368ATPPROSITE-ProRule annotation7

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • actin monomer binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • magnesium ion binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  • protein kinase activity Source: ProtInc
  • protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: InterPro
  • cell adhesion Source: UniProtKB-KW
  • cell migration Source: InterPro
  • cellular protein modification process Source: ProtInc
  • cellular response to retinoic acid Source: BHF-UCL
  • innate immune response Source: GO_Central
  • peptidyl-tyrosine autophosphorylation Source: GO_Central
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of cytosolic calcium ion concentration Source: MGI
  • positive regulation of neuron projection development Source: BHF-UCL
  • positive regulation of oxidoreductase activity Source: BHF-UCL
  • positive regulation of phospholipase C activity Source: MGI
  • regulation of actin cytoskeleton reorganization Source: UniProtKB
  • regulation of autophagy Source: UniProtKB
  • regulation of cell adhesion Source: UniProtKB
  • regulation of cell motility Source: UniProtKB
  • regulation of cell proliferation Source: GO_Central
  • regulation of endocytosis Source: UniProtKB
  • signal transduction Source: ProtInc
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
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

BioCyciZFISH:HS07027-MONOMER.
BRENDAi2.7.10.2. 2681.
ReactomeiR-HSA-428890. Role of Abl in Robo-Slit signaling.
SignaLinkiP42684.
SIGNORiP42684.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:77. ABL2.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • cytosol Source: Reactome
  • extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

DisGeNETi27.
OpenTargetsiENSG00000143322.
PharmGKBiPA24414.

Chemistry databases

ChEMBLiCHEMBL4014.
DrugBankiDB00171. Adenosine triphosphate.
DB01254. Dasatinib.
GuidetoPHARMACOLOGYi1924.

Polymorphism and mutation databases

BioMutaiABL2.
DMDMi1168268.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000880522 – 1182Abelson tyrosine-protein kinase 2Add BLAST1181

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineBy similarity1
Modified residuei97PhosphoserineBy similarity1
Modified residuei116PhosphotyrosineBy similarity1
Modified residuei161PhosphotyrosineBy similarity1
Modified residuei174PhosphotyrosineBy similarity1
Modified residuei185PhosphotyrosineBy similarity1
Modified residuei218PhosphotyrosineBy similarity1
Modified residuei231PhosphotyrosineBy similarity1
Modified residuei261Phosphotyrosine; by ABL1 and autocatalysis1 Publication1
Modified residuei272Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei275PhosphoserineCombined sources1
Modified residuei299PhosphotyrosineBy similarity1
Modified residuei303PhosphotyrosineBy similarity1
Modified residuei439Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases1 Publication1
Modified residuei459PhosphotyrosineBy similarity1
Modified residuei492PhosphoserineBy similarity1
Modified residuei568Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei620PhosphoserineCombined sources1
Modified residuei631PhosphoserineCombined sources1
Modified residuei633PhosphoserineCombined sources1
Modified residuei655PhosphoserineCombined sources1
Modified residuei669PhosphoserineBy similarity1
Modified residuei670PhosphoserineBy similarity1
Modified residuei671PhosphoserineCombined sources1
Modified residuei683Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei718PhosphotyrosineCombined sources1
Modified residuei776N6-acetyllysineBy similarity1
Modified residuei783PhosphoserineCombined sources1
Modified residuei800PhosphothreonineBy similarity1
Modified residuei817PhosphoserineCombined sources1
Modified residuei820PhosphoserineCombined sources1
Modified residuei915PhosphoserineCombined sources1
Modified residuei936PhosphoserineCombined sources1
Isoform 4 (identifier: P42684-4)
Modified residuei647PhosphotyrosineCombined sources1
Isoform 7 (identifier: P42684-7)
Modified residuei662PhosphotyrosineCombined sources1
Isoform 10 (identifier: P42684-10)
Modified residuei668PhosphotyrosineCombined sources1
Isoform 5 (identifier: P42684-5)
Modified residuei683PhosphotyrosineCombined sources1

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

Acetylation, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP42684.
MaxQBiP42684.
PaxDbiP42684.
PeptideAtlasiP42684.
PRIDEiP42684.

PTM databases

iPTMnetiP42684.
PhosphoSitePlusiP42684.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiENSG00000143322.
CleanExiHS_ABL2.
GenevisibleiP42684. HS.

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
SF1Q156373EBI-1102694,EBI-744603
SRCP129312EBI-1102694,EBI-621482

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • actin monomer binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106545. 41 interactors.
DIPiDIP-91N.
IntActiP42684. 42 interactors.
MINTiMINT-1347081.
STRINGi9606.ENSP00000427562.

Chemistry databases

BindingDBiP42684.

Structurei

Secondary structure

11182
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi168 – 170Combined sources3
Beta strandi174 – 177Combined sources4
Helixi180 – 187Combined sources8
Beta strandi194 – 199Combined sources6
Beta strandi207 – 213Combined sources7
Beta strandi216 – 221Combined sources6
Beta strandi226 – 228Combined sources3
Beta strandi230 – 233Combined sources4
Beta strandi236 – 240Combined sources5
Helixi241 – 248Combined sources8
Beta strandi255 – 257Combined sources3
Beta strandi280 – 282Combined sources3
Helixi285 – 287Combined sources3
Beta strandi288 – 293Combined sources6
Helixi294 – 297Combined sources4
Beta strandi300 – 307Combined sources8
Helixi308 – 310Combined sources3
Beta strandi312 – 318Combined sources7
Helixi326 – 337Combined sources12
Beta strandi347 – 351Combined sources5
Beta strandi353 – 356Combined sources4
Beta strandi358 – 362Combined sources5
Helixi369 – 375Combined sources7
Turni378 – 380Combined sources3
Helixi383 – 402Combined sources20
Helixi412 – 414Combined sources3
Beta strandi415 – 417Combined sources3
Helixi419 – 421Combined sources3
Beta strandi423 – 425Combined sources3
Beta strandi435 – 437Combined sources3
Beta strandi438 – 440Combined sources3
Helixi449 – 451Combined sources3
Helixi454 – 459Combined sources6
Helixi464 – 479Combined sources16
Helixi491 – 493Combined sources3
Helixi494 – 499Combined sources6
Helixi512 – 521Combined sources10
Helixi526 – 528Combined sources3
Helixi532 – 545Combined sources14
Helixi1069 – 1071Combined sources3
Turni1076 – 1078Combined sources3
Helixi1080 – 1083Combined sources4
Helixi1086 – 1099Combined sources14
Helixi1106 – 1123Combined sources18
Helixi1124 – 1126Combined sources3
Helixi1130 – 1152Combined sources23
Beta strandi1155 – 1158Combined sources4
Helixi1165 – 1181Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42684.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini107 – 167SH3PROSITE-ProRule annotationAdd BLAST61
Domaini173 – 263SH2PROSITE-ProRule annotationAdd BLAST91
Domaini288 – 539Protein kinasePROSITE-ProRule annotationAdd BLAST252

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 106CAPAdd BLAST105
Regioni694 – 930F-actin-bindingBy similarityAdd BLAST237
Regioni1020 – 1182F-actin-bindingBy similarityAdd BLAST163

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi427 – 451Kinase activation loopBy similarityAdd BLAST25
Motifi658 – 660Nuclear localization signalSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi561 – 564Poly-Ser4
Compositional biasi732 – 739Poly-Gly8
Compositional biasi843 – 1055Pro-richAdd BLAST213
Compositional biasi984 – 988Poly-Pro5

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

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOVERGENiHBG004162.
InParanoidiP42684.
KOiK08887.
OMAiVDTGHQL.
OrthoDBiEOG091G0D46.
PhylomeDBiP42684.
TreeFamiTF105081.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR033217. ABL2.
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]
PANTHERiPTHR24418:SF87. PTHR24418:SF87. 1 hit.
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. AlignAdd to basket

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:
     1-73: MGQQVGRVGE...EGDKTGGSSP → MVLGTVLLPP...ASESALPDLT

Show »
Length:1,146
Mass (Da):124,560
Checksum:iEB47F5DE7CFDAE67
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:
     1-52: MGQQVGRVGE...ETGFNIFTQH → MVLGTVLLPP...ASESALPDLT

Show »
Length:1,167
Mass (Da):126,684
Checksum:i0E3923FE9EEEAFEC
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:
     1-73: MGQQVGRVGE...EGDKTGGSSP → MVLGTVLLPP...ASESALPDLT
     688-790: Missing.

Show »
Length:1,043
Mass (Da):114,159
Checksum:i973C4751FD7E13F9
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.

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.

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:
     1-52: MGQQVGRVGE...ETGFNIFTQH → MVLGTVLLPP...ASESALPDLT
     688-790: Missing.

Show »
Length:1,064
Mass (Da):116,283
Checksum:iAF67137EC553DFE7
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti343 – 344NL → TI no nucleotide entry (PubMed:3787260).Curated2
Sequence conflicti435T → I in AK311045 (PubMed:14702039).Curated1
Sequence conflicti981K → R in CAD98092 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05541178R → H.1 PublicationCorresponds to variant rs55655202dbSNPEnsembl.1
Natural variantiVAR_05541299E → Q Somatic mutation in a breast cancer sample. 1 Publication1
Natural variantiVAR_055413519R → I Somatic mutation in a lung squamous cell carcinoma. 1 Publication1
Natural variantiVAR_055414769T → S.1 PublicationCorresponds to variant rs55892721dbSNPEnsembl.1
Natural variantiVAR_029232930K → R.2 PublicationsCorresponds to variant rs17277288dbSNPEnsembl.1
Natural variantiVAR_029233946V → M.1 PublicationCorresponds to variant rs28913889dbSNPEnsembl.1
Natural variantiVAR_029234996P → R.2 PublicationsCorresponds to variant rs28913890dbSNPEnsembl.1
Natural variantiVAR_0292351085S → N.1 PublicationCorresponds to variant rs28913891dbSNPEnsembl.1
Natural variantiVAR_0292361101T → A.1 PublicationCorresponds to variant rs28913892dbSNPEnsembl.1
Isoform 4 (identifier: P42684-4)
Natural varianti12S → T.Combined sourcesCorresponds to variant rs1318056dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0049611 – 73MGQQV…GGSSP → MVLGTVLLPPNSYGRDQDTS LCCLCTEASESALPDLT in isoform 2 and isoform 4. 2 PublicationsAdd BLAST73
Alternative sequenceiVSP_0171121 – 52MGQQV…IFTQH → MVLGTVLLPPNSYGRDQDTS LCCLCTEASESALPDLT in isoform 3 and isoform 10. 1 PublicationAdd BLAST52
Alternative sequenceiVSP_04177253 – 73Missing in isoform 6, isoform 7 and isoform 8. 2 PublicationsAdd BLAST21
Alternative sequenceiVSP_041773550 – 564EEVAE…ASSSS → EVLLHCANQTCITL in isoform 8. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_041774565 – 1182Missing in isoform 8. 1 PublicationAdd BLAST618
Alternative sequenceiVSP_021308688 – 790Missing in isoform 4, isoform 5, isoform 7 and isoform 10. 2 PublicationsAdd BLAST103

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
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]
PIRiA35962.
B35962.
RefSeqiNP_001129472.1. NM_001136000.2. [P42684-10]
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. [P42684-4]
NP_005149.4. NM_005158.4. [P42684-3]
NP_009298.1. NM_007314.3. [P42684-1]
XP_005245145.1. XM_005245088.2. [P42684-2]
UniGeneiHs.159472.

Genome annotation databases

EnsembliENST00000344730; ENSP00000339209; ENSG00000143322. [P42684-10]
ENST00000367623; ENSP00000356595; ENSG00000143322. [P42684-6]
ENST00000392043; ENSP00000375897; ENSG00000143322. [P42684-8]
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]
GeneIDi27.
KEGGihsa:27.
UCSCiuc001gmg.5. human. [P42684-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
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]
PIRiA35962.
B35962.
RefSeqiNP_001129472.1. NM_001136000.2. [P42684-10]
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. [P42684-4]
NP_005149.4. NM_005158.4. [P42684-3]
NP_009298.1. NM_007314.3. [P42684-1]
XP_005245145.1. XM_005245088.2. [P42684-2]
UniGeneiHs.159472.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106545. 41 interactors.
DIPiDIP-91N.
IntActiP42684. 42 interactors.
MINTiMINT-1347081.
STRINGi9606.ENSP00000427562.

Chemistry databases

BindingDBiP42684.
ChEMBLiCHEMBL4014.
DrugBankiDB00171. Adenosine triphosphate.
DB01254. Dasatinib.
GuidetoPHARMACOLOGYi1924.

PTM databases

iPTMnetiP42684.
PhosphoSitePlusiP42684.

Polymorphism and mutation databases

BioMutaiABL2.
DMDMi1168268.

Proteomic databases

EPDiP42684.
MaxQBiP42684.
PaxDbiP42684.
PeptideAtlasiP42684.
PRIDEiP42684.

Protocols and materials databases

DNASUi27.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344730; ENSP00000339209; ENSG00000143322. [P42684-10]
ENST00000367623; ENSP00000356595; ENSG00000143322. [P42684-6]
ENST00000392043; ENSP00000375897; ENSG00000143322. [P42684-8]
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]
GeneIDi27.
KEGGihsa:27.
UCSCiuc001gmg.5. human. [P42684-1]

Organism-specific databases

CTDi27.
DisGeNETi27.
GeneCardsiABL2.
HGNCiHGNC:77. ABL2.
HPAiCAB017106.
HPA001866.
MIMi164690. gene.
neXtProtiNX_P42684.
OpenTargetsiENSG00000143322.
PharmGKBiPA24414.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOVERGENiHBG004162.
InParanoidiP42684.
KOiK08887.
OMAiVDTGHQL.
OrthoDBiEOG091G0D46.
PhylomeDBiP42684.
TreeFamiTF105081.

Enzyme and pathway databases

BioCyciZFISH:HS07027-MONOMER.
BRENDAi2.7.10.2. 2681.
ReactomeiR-HSA-428890. Role of Abl in Robo-Slit signaling.
SignaLinkiP42684.
SIGNORiP42684.

Miscellaneous databases

ChiTaRSiABL2. human.
EvolutionaryTraceiP42684.
GeneWikiiABL2.
GenomeRNAii27.
PROiP42684.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143322.
CleanExiHS_ABL2.
GenevisibleiP42684. HS.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR033217. ABL2.
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]
PANTHERiPTHR24418:SF87. PTHR24418:SF87. 1 hit.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 193 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.