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P00520

- ABL1_MOUSE

UniProt

P00520 - ABL1_MOUSE

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Protein
Tyrosine-protein kinase ABL1
Gene
Abl1, Abl
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-191' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks.11 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.3 Publications

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 By similarity. Activated by RIN1 binding to the SH2 and SH3 domains. Also stimulated by cell death inducers and DNA-damage By similarity. Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant phosphoinositide known to regulate cytoskeletal and membrane proteins, inhibits also the tyrosine kinase activity. Inhibited by imatinib mesylate (Gleevec).6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei271 – 2711ATP By similarity
Active sitei363 – 3631Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi248 – 2569ATP Inferred
Nucleotide bindingi316 – 3227ATP Inferred

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. DNA binding Source: UniProtKB-KW
  3. kinase activity Source: MGI
  4. magnesium ion binding Source: UniProtKB
  5. manganese ion binding Source: UniProtKB
  6. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  7. proline-rich region binding Source: UniProtKB
  8. protein binding Source: IntAct
  9. protein domain specific binding Source: MGI
  10. protein kinase activity Source: MGI
  11. protein tyrosine kinase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. DNA damage induced protein phosphorylation Source: Ensembl
  2. DNA repair Source: UniProtKB-KW
  3. actin cytoskeleton organization Source: UniProtKB
  4. apoptotic process Source: UniProtKB-KW
  5. autophagy Source: UniProtKB-KW
  6. cell adhesion Source: UniProtKB-KW
  7. cellular response to DNA damage stimulus Source: UniProtKB
  8. endocytosis Source: UniProtKB-KW
  9. negative regulation of protein serine/threonine kinase activity Source: Ensembl
  10. peptidyl-tyrosine phosphorylation Source: UniProtKB
  11. platelet-derived growth factor receptor signaling pathway Source: MGI
  12. positive regulation of apoptotic process Source: Ensembl
  13. positive regulation of oxidoreductase activity Source: Ensembl
  14. positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  15. regulation of cell cycle Source: MGI
  16. regulation of response to DNA damage stimulus Source: Ensembl
  17. signal transduction in response to DNA damage Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Apoptosis, Autophagy, Cell adhesion, DNA damage, DNA repair, Endocytosis

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_198649. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase ABL1 (EC:2.7.10.2)
Alternative name(s):
Abelson murine leukemia viral oncogene homolog 1
Abelson tyrosine-protein kinase 1
Proto-oncogene c-Abl
p150
Gene namesi
Name:Abl1
Synonyms:Abl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:87859. Abl1.

Subcellular locationi

Cytoplasmcytoskeleton. Nucleus. Mitochondrion
Note: The myristoylated c-ABL protein is reported to be nuclear. Sequestered into the cytoplasm through interaction with 14-3-3 proteins By similarity. Localizes to mitochondria in response to oxidative stress.3 Publications

GO - Cellular componenti

  1. cell leading edge Source: MGI
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB-SubCell
  4. cytosol Source: MGI
  5. mitochondrion Source: UniProtKB-SubCell
  6. nucleolus Source: Ensembl
  7. nucleus Source: UniProtKB
  8. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutants are born with the expected Mendelian frequency, but fail to thrive and most die within three weeks after birth. Most mutants are runted, and have atrophied thymuses with severe thymocyte deficiency. Mutants that survive to weaning age are most often runted, and about half of them show lymphopenia. They display a major reduction in the number of pre-B and immature B-cell classes in bone marrow with a wide variation between individuals, but essentially normal mature B-cell levels. Mutants are highly susceptible to infections.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1121P → S: Strongly reduced inhibition by GNF-2. 1 Publication
Mutagenesisi128 – 1281Y → D: Strongly reduced inhibition by GNF-2. 1 Publication
Mutagenesisi139 – 1391Y → C: Strongly reduced inhibition by GNF-2. 1 Publication
Mutagenesisi226 – 2261Y → F: Minimal reduction in ability to autophosphorylate. 1 Publication
Mutagenesisi229 – 2291S → P: Strongly reduced inhibition by GNF-2. 1 Publication
Mutagenesisi271 – 2711K → M: Loss of kinase activity. 1 Publication
Mutagenesisi315 – 3151T → I: Loss of inhibition by imatinib. Loss of inhibition by GNF-2. 1 Publication
Mutagenesisi393 – 3931Y → F: Minimal reduction in ability to autophosphorylate. 1 Publication
Mutagenesisi446 – 4461S → A: No effect on basal activity, but abolishes ionizing radiation-induced activation. 1 Publication
Mutagenesisi464 – 4641C → Y: Loss of inhibition by GNF-2. 1 Publication
Mutagenesisi465 – 4651P → S: Loss of inhibition by GNF-2. 1 Publication
Mutagenesisi497 – 4971F → L: Strongly reduced inhibition by GNF-2. 1 Publication
Mutagenesisi505 – 5051E → K: Loss of inhibition by GNF-2. 1 Publication
Mutagenesisi506 – 5061V → L: Strongly reduced inhibition by GNF-2. 1 Publication
Mutagenesisi1083 – 10831L → A: Loss of nuclear export.

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11231123Tyrosine-protein kinase ABL1
PRO_0000088051Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501Phosphoserine By similarity
Modified residuei70 – 701Phosphotyrosine; by autocatalysis By similarity
Modified residuei185 – 1851Phosphotyrosine By similarity
Modified residuei226 – 2261Phosphotyrosine; by autocatalysis By similarity
Modified residuei253 – 2531Phosphotyrosine By similarity
Modified residuei257 – 2571Phosphotyrosine By similarity
Modified residuei264 – 2641Phosphotyrosine By similarity
Modified residuei392 – 3921Phosphothreonine By similarity
Modified residuei393 – 3931Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases2 Publications
Modified residuei394 – 3941Phosphothreonine By similarity
Modified residuei446 – 4461Phosphoserine1 Publication
Modified residuei469 – 4691Phosphotyrosine By similarity
Modified residuei547 – 5471Phosphothreonine1 Publication
Modified residuei569 – 5691Phosphoserine1 Publication
Modified residuei613 – 6131Phosphothreonine By similarity
Modified residuei618 – 6181Phosphoserine; by PAK2 By similarity
Modified residuei619 – 6191Phosphoserine; by PAK2 By similarity
Modified residuei620 – 6201Phosphoserine By similarity
Modified residuei658 – 6581Phosphoserine By similarity
Modified residuei682 – 6821Phosphoserine By similarity
Modified residuei710 – 7101N6-acetyllysine; by EP300 By similarity
Modified residuei717 – 7171Phosphoserine By similarity
Modified residuei734 – 7341Phosphothreonine By similarity
Modified residuei803 – 8031Phosphoserine By similarity
Modified residuei807 – 8071Phosphoserine By similarity
Modified residuei812 – 8121Phosphothreonine By similarity
Modified residuei844 – 8441Phosphothreonine By similarity
Modified residuei909 – 9091Phosphoserine By similarity
Modified residuei911 – 9111Phosphoserine By similarity
Modified residuei927 – 9271Phosphoserine By similarity
Modified residuei970 – 9701Phosphoserine By similarity

Post-translational modificationi

Acetylated at Lys-710 by EP300 which promotes the cytoplasmic translocation By similarity.
Phosphorylation at Tyr-70 by members of the SRC family of kinases disrupts SH3 domain-based autoinhibitory interactions and intermolecular associations, such as that with ABI1, and also enhances kinase activity By similarity. Phosphorylation at Tyr-226 and Tyr-393 correlate with increased activity By similarity. DNA damage-induced activation of ABL1 requires the function of ATM and Ser-446 phosphorylation. Phosphorylation at Thr-547 and Ser-569 has been attributed to a CDC2-associated kinase and is coupled to cell division. Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces binding to ABI1 By similarity. Phosphorylation on Thr-734 is required for binding 14-3-3 proteins for cytoplasmic translocation By similarity. Phosphorylated by PDGFRB and PRKDC.8 Publications
Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation By similarity.
Isoform IV is myristoylated on Gly-2.

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP00520.
PRIDEiP00520.

PTM databases

PhosphoSiteiP00520.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

ArrayExpressiP00520.
BgeeiP00520.
CleanExiMM_ABL1.
GenevestigatoriP00520.

Interactioni

Subunit structurei

Interacts with INPPL1/SHIP2. Interacts with SORBS1 following insulin stimulation. Found in a trimolecular complex containing CDK5 and CABLES1. Interacts with CABLES1 and PSTPIP1. Interacts with ZDHHC16. Interacts with the 14-3-3 proteins, YWHAB, YWHAE, YWHAG, YWHAH, SFN AND YWHAZ; the interaction with 14-3-3 proteins requires phosphorylation on Thr-734 and sequesters ABL1 into the cytoplasm. Interacts (via SH3 domain) with CASP9; the interaction is direct and increases in the response of cells to genotoxic stress and ABL1/c-Abl activation By similarity. Interacts with ABI1, ABI2, BCR, CRK, FYN, LYN, PSMA7 RAD9A, RAD51, RAD52, TP73 and WASF3. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Interacts with STX17; probably phosphorylates STX17 By similarity. Interacts with ITGB1, HCK and FGR.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1Q8IZP0-45EBI-8593082,EBI-8593095From a different organism.
CDKN1BP465272EBI-914519,EBI-519280From a different organism.
CdonQ32MD92EBI-914519,EBI-7017034
Dok1P974654EBI-914519,EBI-914917
EPHB2P28693-25EBI-914519,EBI-6725926From a different organism.
Nck1Q99M512EBI-914519,EBI-642202
Pstpip1P978145EBI-914519,EBI-7484574
Ptpn18P706022EBI-914519,EBI-7484661From a different organism.

Protein-protein interaction databases

BioGridi197906. 19 interactions.
IntActiP00520. 20 interactions.
MINTiMINT-85127.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi65 – 706
Beta strandi76 – 794
Beta strandi87 – 937
Beta strandi97 – 1037
Beta strandi108 – 1125
Helixi113 – 1153
Beta strandi116 – 1216
Helixi122 – 1243
Beta strandi128 – 1314
Helixi134 – 1407
Helixi141 – 1433
Beta strandi148 – 1536
Beta strandi155 – 1573
Beta strandi161 – 1677
Beta strandi170 – 1756
Beta strandi184 – 1874
Beta strandi192 – 1943
Helixi195 – 2028
Beta strandi209 – 2113
Beta strandi226 – 2283
Beta strandi230 – 2334
Helixi239 – 2413
Beta strandi242 – 2487
Helixi249 – 2513
Beta strandi255 – 2617
Helixi262 – 2643
Beta strandi266 – 2738
Beta strandi275 – 2784
Helixi280 – 29213
Beta strandi301 – 3055
Beta strandi307 – 31610
Helixi323 – 3297
Turni332 – 3343
Helixi337 – 35721
Beta strandi359 – 3624
Helixi366 – 3683
Beta strandi369 – 3713
Helixi373 – 3753
Beta strandi377 – 3793
Helixi384 – 3863
Beta strandi390 – 3967
Beta strandi399 – 4013
Helixi403 – 4053
Helixi408 – 4136
Helixi418 – 43316
Beta strandi439 – 4424
Helixi445 – 4473
Helixi448 – 4536
Helixi466 – 47510
Helixi480 – 4823
Helixi486 – 50924

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ABOX-ray2.00A/B61-121[»]
1ABQX-ray2.80A61-121[»]
1FPUX-ray2.40A/B229-515[»]
1IEPX-ray2.10A/B229-515[»]
1M52X-ray2.60A/B229-515[»]
1OPJX-ray1.75A/B229-515[»]
1OPKX-ray1.80A27-515[»]
2HZNX-ray2.70A229-515[»]
2QOHX-ray1.95A/B229-515[»]
2Z60X-ray1.95A229-515[»]
3DK3X-ray2.02A/B233-514[»]
3DK6X-ray2.02A/B233-514[»]
3DK7X-ray2.01A/B233-505[»]
3IK3X-ray1.90A/B229-513[»]
3K5VX-ray1.74A/B229-515[»]
3KF4X-ray1.90A/B229-515[»]
3KFAX-ray1.22A/B229-515[»]
3MS9X-ray1.80A/B229-515[»]
3MSSX-ray1.95A/B/C/D229-515[»]
3OXZX-ray2.20A229-511[»]
3OY3X-ray1.95A/B229-511[»]
ProteinModelPortaliP00520.
SMRiP00520. Positions 46-511, 1017-1123.

Miscellaneous databases

EvolutionaryTraceiP00520.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 12161SH3
Add
BLAST
Domaini127 – 21791SH2
Add
BLAST
Domaini242 – 493252Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6060CAP
Add
BLAST
Regioni863 – 96199DNA-binding
Add
BLAST
Regioni945 – 1123179F-actin-binding By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi381 – 40525Kinase activation loop
Add
BLAST
Motifi605 – 6095Nuclear localization signal 1 Reviewed prediction
Motifi708 – 7147Nuclear localization signal 2 Reviewed prediction
Motifi761 – 7688Nuclear localization signal 3 Reviewed prediction
Motifi1083 – 109311Nuclear export signal
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 225Poly-Ser
Compositional biasi605 – 6095Poly-Lys
Compositional biasi804 – 1012209Pro-rich
Add
BLAST
Compositional biasi891 – 8977Poly-Pro

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00640000091347.
HOVERGENiHBG004162.
KOiK06619.
OMAiGAFRESG.
OrthoDBiEOG7GTT2V.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform I (identifier: P00520-1) [UniParc]FASTAAdd to Basket

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

MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS     50
KENLLAGPSE NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC 100
EAQTKNGQGW VPSNYITPVN SLEKHSWYHG PVSRNAAEYL LSSGINGSFL 150
VRESESSPGQ RSISLRYEGR VYHYRINTAS DGKLYVSSES RFNTLAELVH 200
HHSTVADGLI TTLHYPAPKR NKPTIYGVSP NYDKWEMERT DITMKHKLGG 250
GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ 300
LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVSAVVL LYMATQISSA 350
MEYLEKKNFI HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK 400
FPIKWTAPES LAYNKFSIKS DVWAFGVLLW EIATYGMSPY PGIDLSQVYE 450
LLEKDYRMER PEGCPEKVYE LMRACWQWNP SDRPSFAEIH QAFETMFQES 500
SISDEVEKEL GKRGTRGGAG SMLQAPELPT KTRTCRRAAE QKDAPDTPEL 550
LHTKGLGESD ALDSEPAVSP LLPRKERGPP DGSLNEDERL LPRDRKTNLF 600
SALIKKKKKM APTPPKRSSS FREMDGQPDR RGASEDDSRE LCNGPPALTS 650
DAAEPTKSPK ASNGAGVPNG AFREPGNSGF RSPHMWKKSS TLTGSRLAAA 700
EEESGMSSSK RFLRSCSASC MPHGARDTEW RSVTLPRDLP SAGKQFDSST 750
FGGHKSEKPA LPRKRTSESR SEQVAKSTAM PPPRLVKKNE EAAEEGFKDT 800
ESSPGSSPPS LTPKLLRRQV TASPSSGLSH KEEATKGSAS GMGTPATAEP 850
APPSNKVGLS KASSEEMRVR RHKHSSESPG RDKGRLAKLK PAPPPPPACT 900
GKAGKPAQSP SQEAGEAGGP TKTKCTSLAM DAVNTDPTKA GPPGEGLRKP 950
VPPSVPKPQS TAKPPGTPTS PVSTPSTAPA PSPLAGDQQP SSAAFIPLIS 1000
TRVSLRKTRQ PPERIASGTI TKGVVLDSTE ALCLAISRNS EQMASHSAVL 1050
EAGKNLYTFC VSYVDSIQQM RNKFAFREAI NKLESNLREL QICPATASSG 1100
PAATQDFSKL LSSVKEISDI VRR 1123
Length:1,123
Mass (Da):122,673
Last modified:February 15, 2005 - v3
Checksum:iBD48ADE8557AE95C
GO
Isoform II (identifier: P00520-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MISFDLLSDELHLKLLVLDV

Show »
Length:1,117
Mass (Da):122,179
Checksum:i002F9D346307028A
GO
Isoform III (identifier: P00520-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MSQRWTYTKCRVQRDPALPFM

Show »
Length:1,118
Mass (Da):122,480
Checksum:iAB3B4510AE8C5C38
GO
Isoform IV (identifier: P00520-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MGQQPGKVLGDQRRPSLPALHFIKGAGKRDSSRHGGPHCNVFVEH

Show »
Length:1,142
Mass (Da):124,769
Checksum:i7A9DB9E772EAF05F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626MLEIC…SCYLE → MISFDLLSDELHLKLLVLDV in isoform II.
VSP_004959Add
BLAST
Alternative sequencei1 – 2626MLEIC…SCYLE → MSQRWTYTKCRVQRDPALPF M in isoform III.
VSP_004958Add
BLAST
Alternative sequencei1 – 2626MLEIC…SCYLE → MGQQPGKVLGDQRRPSLPAL HFIKGAGKRDSSRHGGPHCN VFVEH in isoform IV.
VSP_004960Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1874LYVS → VGDW in AAB60451. 1 Publication
Sequence conflicti184 – 1874LYVS → VGDW in AAB60450. 1 Publication
Sequence conflicti782 – 7865PPRLV → LPGWL in AAA88241. 1 Publication
Sequence conflicti987 – 9871D → G in BAC41088. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02995 mRNA. Translation: AAA88241.1.
AK090095 mRNA. Translation: BAC41088.1.
BC059260 mRNA. Translation: AAH59260.1.
U14721, U14720 Genomic DNA. Translation: AAB60451.1.
U14721, U14720 Genomic DNA. Translation: AAB60450.1.
U14721, U13835 Genomic DNA. Translation: AAB60448.1.
U14721, U13835 Genomic DNA. Translation: AAB60449.1.
X07539 Genomic DNA. Translation: CAA30411.1.
X07539 Genomic DNA. Translation: CAA30412.1.
X07540 Genomic DNA. Translation: CAA30413.1.
X07541 Genomic DNA. Translation: CAA30414.1.
M12263 mRNA. Translation: AAA37136.1.
M12264 mRNA. Translation: AAA37137.1.
M12265 mRNA. Translation: AAA37138.1.
M12266 Genomic DNA. Translation: AAA37134.1.
K03228 mRNA. Translation: AAA37135.1.
CCDSiCCDS15901.1. [P00520-1]
CCDS50563.1. [P00520-4]
PIRiA39962.
S00774.
RefSeqiNP_001106174.1. NM_001112703.2. [P00520-4]
NP_001269974.1. NM_001283045.1. [P00520-3]
NP_001269975.1. NM_001283046.1. [P00520-2]
NP_033724.2. NM_009594.4. [P00520-1]
UniGeneiMm.1318.

Genome annotation databases

EnsembliENSMUST00000028190; ENSMUSP00000028190; ENSMUSG00000026842. [P00520-1]
ENSMUST00000075759; ENSMUSP00000075167; ENSMUSG00000026842. [P00520-4]
GeneIDi11350.
KEGGimmu:11350.
UCSCiuc008jdz.2. mouse. [P00520-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02995 mRNA. Translation: AAA88241.1 .
AK090095 mRNA. Translation: BAC41088.1 .
BC059260 mRNA. Translation: AAH59260.1 .
U14721 , U14720 Genomic DNA. Translation: AAB60451.1 .
U14721 , U14720 Genomic DNA. Translation: AAB60450.1 .
U14721 , U13835 Genomic DNA. Translation: AAB60448.1 .
U14721 , U13835 Genomic DNA. Translation: AAB60449.1 .
X07539 Genomic DNA. Translation: CAA30411.1 .
X07539 Genomic DNA. Translation: CAA30412.1 .
X07540 Genomic DNA. Translation: CAA30413.1 .
X07541 Genomic DNA. Translation: CAA30414.1 .
M12263 mRNA. Translation: AAA37136.1 .
M12264 mRNA. Translation: AAA37137.1 .
M12265 mRNA. Translation: AAA37138.1 .
M12266 Genomic DNA. Translation: AAA37134.1 .
K03228 mRNA. Translation: AAA37135.1 .
CCDSi CCDS15901.1. [P00520-1 ]
CCDS50563.1. [P00520-4 ]
PIRi A39962.
S00774.
RefSeqi NP_001106174.1. NM_001112703.2. [P00520-4 ]
NP_001269974.1. NM_001283045.1. [P00520-3 ]
NP_001269975.1. NM_001283046.1. [P00520-2 ]
NP_033724.2. NM_009594.4. [P00520-1 ]
UniGenei Mm.1318.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ABO X-ray 2.00 A/B 61-121 [» ]
1ABQ X-ray 2.80 A 61-121 [» ]
1FPU X-ray 2.40 A/B 229-515 [» ]
1IEP X-ray 2.10 A/B 229-515 [» ]
1M52 X-ray 2.60 A/B 229-515 [» ]
1OPJ X-ray 1.75 A/B 229-515 [» ]
1OPK X-ray 1.80 A 27-515 [» ]
2HZN X-ray 2.70 A 229-515 [» ]
2QOH X-ray 1.95 A/B 229-515 [» ]
2Z60 X-ray 1.95 A 229-515 [» ]
3DK3 X-ray 2.02 A/B 233-514 [» ]
3DK6 X-ray 2.02 A/B 233-514 [» ]
3DK7 X-ray 2.01 A/B 233-505 [» ]
3IK3 X-ray 1.90 A/B 229-513 [» ]
3K5V X-ray 1.74 A/B 229-515 [» ]
3KF4 X-ray 1.90 A/B 229-515 [» ]
3KFA X-ray 1.22 A/B 229-515 [» ]
3MS9 X-ray 1.80 A/B 229-515 [» ]
3MSS X-ray 1.95 A/B/C/D 229-515 [» ]
3OXZ X-ray 2.20 A 229-511 [» ]
3OY3 X-ray 1.95 A/B 229-511 [» ]
ProteinModelPortali P00520.
SMRi P00520. Positions 46-511, 1017-1123.
ModBasei Search...

Protein-protein interaction databases

BioGridi 197906. 19 interactions.
IntActi P00520. 20 interactions.
MINTi MINT-85127.

Chemistry

BindingDBi P00520.
ChEMBLi CHEMBL3099.

PTM databases

PhosphoSitei P00520.

Proteomic databases

PaxDbi P00520.
PRIDEi P00520.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028190 ; ENSMUSP00000028190 ; ENSMUSG00000026842 . [P00520-1 ]
ENSMUST00000075759 ; ENSMUSP00000075167 ; ENSMUSG00000026842 . [P00520-4 ]
GeneIDi 11350.
KEGGi mmu:11350.
UCSCi uc008jdz.2. mouse. [P00520-1 ]

Organism-specific databases

CTDi 25.
MGIi MGI:87859. Abl1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00640000091347.
HOVERGENi HBG004162.
KOi K06619.
OMAi GAFRESG.
OrthoDBi EOG7GTT2V.
TreeFami TF105081.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_198649. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTracei P00520.
NextBioi 278620.
PROi P00520.
SOURCEi Search...

Gene expression databases

ArrayExpressi P00520.
Bgeei P00520.
CleanExi MM_ABL1.
Genevestigatori P00520.

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. "Nucleotide sequence of testis-derived c-abl cDNAs: implications for testis-specific transcription and abl oncogene activation."
    Oppi C., Shore S.K., Reddy E.P.
    Proc. Natl. Acad. Sci. U.S.A. 84:8200-8204(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
    Tissue: Testis.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
    Strain: ICR.
    Tissue: Embryo.
  3. "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 IV).
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Sequence and analysis of the human ABL gene, the BCR gene, and regions involved in the Philadelphia chromosomal translocation."
    Chissoe S.L., Bodenteich A., Wang Y.-F., Wang Y.-P., Burian D., Clifton S.W., Crabtree J., Freeman A., Iyer K., Jian L., Ma Y., McLaury H.-J., Pan H.-Q., Sarhan O.H., Toth S., Wang Z., Zhang G., Heisterkamp N., Groffen J., Roe B.A.
    Genomics 27:67-82(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-187 (ISOFORMS I; II; III AND IV).
  5. "The mouse c-abl locus: molecular cloning and characterization."
    Wang J.Y.J., Ledley F., Goff S., Lee R., Groner Y., Baltimore D.
    Cell 36:349-356(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-182.
  6. "Four murine c-abl mRNAs arise by usage of two transcriptional promoters and alternative splicing."
    Bernards A., Paskind M., Baltimore D.
    Oncogene 2:297-304(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  7. "Differential phosphorylation of c-Abl in cell cycle determined by cdc2 kinase and phosphatase activity."
    Kipreos E.T., Wang J.Y.
    Science 248:217-220(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-547 AND SER-569.
  8. "Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene."
    Tybulewicz V.L., Crawford C.E., Jackson P.K., Bronson R.T., Mulligan R.C.
    Cell 65:1153-1163(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "Mice homozygous for the ablm1 mutation show poor viability and depletion of selected B and T cell populations."
    Schwartzberg P.L., Stall A.M., Hardin J.D., Bowdish K.S., Humaran T., Boast S., Harbison M.L., Robertson E.J., Goff S.P.
    Cell 65:1165-1175(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. "Cell cycle-regulated binding of c-Abl tyrosine kinase to DNA."
    Kipreos E.T., Wang J.Y.
    Science 256:382-385(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, DOMAIN, PHOSPHORYLATION.
  11. "c-Abl kinase regulates the protein binding activity of c-Crk."
    Feller S.M., Knudsen B., Hanafusa H.
    EMBO J. 13:2341-2351(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases."
    Mayer B.J., Hirai H., Sakai R.
    Curr. Biol. 5:296-305(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Functional interaction between DNA-PK and c-Abl in response to DNA damage."
    Kharbanda S., Pandey P., Jin S., Inoue S., Bharti A., Yuan Z.-M., Weichselbaum R., Weaver D., Kufe D.
    Nature 386:732-735(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-446, MUTAGENESIS OF SER-446.
  14. Cited for: SUBCELLULAR LOCATION.
  15. "Cables links Cdk5 and c-Abl and facilitates Cdk5 tyrosine phosphorylation, kinase upregulation, and neurite outgrowth."
    Zukerberg L.R., Patrick G.N., Nikolic M., Humbert S., Wu C.-L., Lanier L.M., Gertler F.B., Vidal M., Van Etten R.A., Tsai L.-H.
    Neuron 26:633-646(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A TRIMOLECULAR COMPLEX WITH CDK5 AND CABLES1, INTERACTION WITH CABLES1.
    Tissue: Brain.
  16. "Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation."
    Cong F., Spencer S., Cote J.F., Wu Y., Tremblay M.L., Lasky L.A., Goff S.P.
    Mol. Cell 6:1413-1423(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSTPIP1.
  17. "Regulation of cell death by the Abl tyrosine kinase."
    Wang J.Y.
    Oncogene 19:5643-5650(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  18. "Inhibition of cell migration by Abl family tyrosine kinases through uncoupling of Crk-CAS complexes."
    Kain K.H., Klemke R.L.
    J. Biol. Chem. 276:16185-16192(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRK, FUNCTION.
  19. "Targeting of the c-Abl tyrosine kinase to mitochondria in the necrotic cell death response to oxidative stress."
    Kumar S., Bharti A., Mishra N.C., Raina D., Kharbanda S., Saxena S., Kufe D.
    J. Biol. Chem. 276:17281-17285(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  20. "The beta-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene."
    Zambrano N., Bruni P., Minopoli G., Mosca R., Molino D., Russo C., Schettini G., Sudol M., Russo T.
    J. Biol. Chem. 276:19787-19792(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has pro-apoptotic activity."
    Li B., Cong F., Tan C.P., Wang S.X., Goff S.P.
    J. Biol. Chem. 277:28870-28876(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZDHHC16.
  22. "Interaction between UV-damaged DNA binding activity proteins and the c-Abl tyrosine kinase."
    Cong F., Tang J., Hwang B.J., Vuong B.Q., Chu G., Goff S.P.
    J. Biol. Chem. 277:34870-34878(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "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.
  24. "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: FUNCTION, ENZYME REGULATION, INTERACTION WITH CRK, AUTOPHOSPHORYLATION AT TYR-226 AND TYR-393, MUTAGENESIS OF TYR-226; LYS-271 AND TYR-393.
  25. "Bidirectional signaling links the Abelson kinases to the platelet-derived growth factor receptor."
    Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M.
    Mol. Cell. Biol. 24:2573-2583(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION.
  26. "Role of c-Abl in the DNA damage stress response."
    Shaul Y., Ben-Yehoyada M.
    Cell Res. 15:33-35(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  27. "c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration."
    Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G., Berton G.
    FEBS Lett. 584:15-21(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF CELL MIGRATION, PHOSPHORYLATION, INTERACTION WITH ITGB1; HCK AND FGR.
  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. "High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides."
    Musacchio A., Saraste M., Wilmanns M.
    Nat. Struct. Biol. 1:546-551(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 61-121.
  30. "Structural mechanism for STI-571 inhibition of Abelson tyrosine kinase."
    Schindler T., Bornmann W., Pellicena P., Miller W.T., Clarkson B., Kuriyan J.
    Science 289:1938-1942(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 229-515 IN COMPLEX WITH INHIBITOR STI-571, CATALYTIC ACTIVITY, ENZYME REGULATION, PHOSPHORYLATION AT TYR-393, ACTIVATION LOOP.
  31. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 229-515, MYRISTOYLATION (ISOFORM IV), ENZYME REGULATION.
  32. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 229-515 OF WILD-TYPE AND MUTANT ILE-315 IN COMPLEX WITH INHIBITOR PPY-A.
  33. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 229-515 OF MUTANT ILE-315 IN COMPLEX WITH INHIBITOR AP24534, CATALYTIC ACTIVITY, FUNCTION.
  34. "Structural analysis of DFG-in and DFG-out dual Src-Abl inhibitors sharing a common vinyl purine template."
    Zhou T., Commodore L., Huang W.S., Wang Y., Sawyer T.K., Shakespeare W.C., Clackson T., Zhu X., Dalgarno D.C.
    Chem. Biol. Drug Des. 75:18-28(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 115-401 IN COMPLEXES WITH INHIBITORS AP24283 AND AP24163.
  35. Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 115-401 IN COMPLEX WITH INHIBITORS IMATINIB AND GNF-2, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF PRO-112; TYR-128; TYR-139; SER-229; THR-315; CYS-464; PRO-465; PHE-497; GLU-505 AND VAL-506.

Entry informationi

Entry nameiABL1_MOUSE
AccessioniPrimary (citable) accession number: P00520
Secondary accession number(s): P97896
, Q61252, Q61253, Q61254, Q61255, Q61256, Q61257, Q61258, Q61259, Q61260, Q61261, Q6PCM5, Q8C1X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 15, 2005
Last modified: September 3, 2014
This is version 190 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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