Overview
| Uniprot ID | P42684 |
| Protein Name | Tyrosine-protein kinase ABL2 |
| Gene Name | ABL2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 578 |
RLPILPSKTRTLKKQ |
| 809 |
PRNCQRSKLQLERTV |
Function
Non-receptor tyrosine-protein kinase that plays an ABL1-overlapping role in key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion and receptor endocytosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and regulates actin cytoskeletal structure through its F-actin-bundling activity. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL, DOK1 or ARHGAP35. Adhesion-dependent phosphorylation of ARHGAP35 promotes its association with RASA1, resulting in recruitment of ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other substrates which are involved in endocytosis regulation such as RIN1. In brain, may regulate neurotransmission by phosphorylating proteins at the synapse. ABL2 also acts 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. Positively regulates chemokine-mediated T-cell migration, polarization, and homing to lymph nodes and immune-challenged tissues, potentially via activation of NEDD9/HEF1 and RAP1 (By similarity)
Protein Sequence
10
MGQQVGRVGE
20
APGLQQPQPR
30
GIRGSSAARP
40
SGRRRDPAGR
50
TTETGFNIFT
60
QHDHFASCVE
70
DGFEGDKTGG
80
SSPEALHRPY
90
GCDVEPQALN
100
EAIRWSSKEN
110
LLGATESDPN
120
LFVALYDFVA
130
SGDNTLSITK
140
GEKLRVLGYN
150
QNGEWSEVRS
160
KNGQGWVPSN
170
YITPVNSLEK
180
HSWYHGPVSR
190
SAAEYLLSSL
200
INGSFLVRES
210
ESSPGQLSIS
220
LRYEGRVYHY
230
RINTTADGKV
240
YVTAESRFST
250
LAELVHHHST
260
VADGLVTTLH
270
YPAPKCNKPT
280
VYGVSPIHDK
290
WEMERTDITM
300
KHKLGGGQYG
310
EVYVGVWKKY
320
SLTVAVKTLK
330
EDTMEVEEFL
340
KEAAVMKEIK
350
HPNLVQLLGV
360
CTLEPPFYIV
370
TEYMPYGNLL
380
DYLRECNREE
390
VTAVVLLYMA
400
TQISSAMEYL
410
EKKNFIHRDL
420
AARNCLVGEN
430
HVVKVADFGL
440
SRLMTGDTYT
450
AHAGAKFPIK
460
WTAPESLAYN
470
TFSIKSDVWA
480
FGVLLWEIAT
490
YGMSPYPGID
500
LSQVYDLLEK
510
GYRMEQPEGC
520
PPKVYELMRA
530
CWKWSPADRP
540
SFAETHQAFE
550
TMFHDSSISE
560
EVAEELGRAA
570
SSSSVVPYLP
580
RLPILPSKTR
590
TLKKQVENKE
600
NIEGAQDATE
610
NSASSLAPGF
620
IRGAQASSGS
630
PALPRKQRDK
640
SPSSLLEDAK
650
ETCFTRDRKG
660
GFFSSFMKKR
670
NAPTPPKRSS
680
SFREMENQPH
690
KKYELTGNFS
700
SVASLQHADG
710
FSFTPAQQEA
720
NLVPPKCYGG
730
SFAQRNLCND
740
DGGGGGGSGT
750
AGGGWSGITG
760
FFTPRLIKKT
770
LGLRAGKPTA
780
SDDTSKPFPR
790
SNSTSSMSSG
800
LPEQDRMAMT
810
LPRNCQRSKL
820
QLERTVSTSS
830
QPEENVDRAN
840
DMLPKKSEES
850
AAPSRERPKA
860
KLLPRGATAL
870
PLRTPSGDLA
880
ITEKDPPGVG
890
VAGVAAAPKG
900
KEKNGGARLG
910
MAGVPEDGEQ
920
PGWPSPAKAA
930
PVLPTTHNHK
940
VPVLISPTLK
950
HTPADVQLIG
960
TDSQGNKFKL
970
LSEHQVTSSG
980
DKDRPRRVKP
990
KCAPPPPPVM
1000
RLLQHPSICS
1010
DPTEEPTALT
1020
AGQSTSETQE
1030
GGKKAALGAV
1040
PISGKAGRPV
1050
MPPPQVPLPT
1060
SSISPAKMAN
1070
GTAGTKVALR
1080
KTKQAAEKIS
1090
ADKISKEALL
1100
ECADLLSSAL
1110
TEPVPNSQLV
1120
DTGHQLLDYC
1130
SGYVDCIPQT
1140
RNKFAFREAV
1150
SKLELSLQEL
1160
QVSSAAAGVP
1170
GTNPVLNNLL
1180
SCVQEISDVV
QR
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0015629 |
actin cytoskeleton |
| Biological Process |
GO:0010976 |
positive regulation of neuron projection development |
| Biological Process |
GO:2000406 |
positive regulation of T cell migration |
| Biological Process |
GO:0036211 |
protein modification process |
| Biological Process |
GO:0032956 |
regulation of actin cytoskeleton organization |
| Biological Process |
GO:0010506 |
regulation of autophagy |
| Biological Process |
GO:0030155 |
regulation of cell adhesion |
| Biological Process |
GO:2000145 |
regulation of cell motility |
| Biological Process |
GO:0030100 |
regulation of endocytosis |
| Biological Process |
GO:0007165 |
signal transduction |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Molecular Function |
GO:0051015 |
actin filament binding |
| Molecular Function |
GO:0003785 |
actin monomer binding |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0008047 |
enzyme activator activity |
| Molecular Function |
GO:0019899 |
enzyme binding |
| Molecular Function |
GO:0000287 |
magnesium ion binding |
| Molecular Function |
GO:0030145 |
manganese ion binding |
| Molecular Function |
GO:0004715 |
non-membrane spanning protein tyrosine kinase activity |
| Molecular Function |
GO:0001784 |
phosphotyrosine residue binding |
| Molecular Function |
GO:0004672 |
protein kinase activity |
| Molecular Function |
GO:0004713 |
protein tyrosine kinase activity |
| Biological Process |
GO:0007155 |
cell adhesion |
| Biological Process |
GO:0034599 |
cellular response to oxidative stress |
| Biological Process |
GO:0071300 |
cellular response to retinoic acid |
| Biological Process |
GO:0007173 |
epidermal growth factor receptor signaling pathway |
| Biological Process |
GO:0035640 |
exploration behavior |
| Biological Process |
GO:0035024 |
negative regulation of Rho protein signal transduction |
| Biological Process |
GO:0018108 |
peptidyl-tyrosine phosphorylation |
| Biological Process |
GO:0007200 |
phospholipase C-activating G protein-coupled receptor signaling pathway |
| Biological Process |
GO:0007204 |
positive regulation of cytosolic calcium ion concentration |
| Biological Process |
GO:1903905 |
positive regulation of establishment of T cell polarity |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.