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Reviewed, UniProtKB/Swiss-Prot P00520 (ABL1_MOUSE)

Last modified June 16, 2009. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Proto-oncogene tyrosine-protein kinase ABL1
    EC=2.7.10.2
Alternative name(s):
    Abelson murine leukemia viral oncogene homolog 1
    c-ABL
    p150
Gene names
Name: Abl1
Synonyms: Abl
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length1123 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Regulates cytoskeleton remodeling during cell differentiation, cell division and cell adhesion. Localizes to dynamic actin structures, and phosphorylates CRK and CRKL, DOK1, and other proteins controlling cytoskeleton dynamics. Regulates DNA repair potentially by activating the proapoptotic pathway when the DNA damage is too severe to be repaired. Ref.7 Ref.11 Ref.13

Catalytic activity

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

Cofactor

Magnesium or manganese.

Enzyme regulation

Stabilized in the inactive form by an association between the SH3 domain and the SH2-TK linker region, interactions of the amino-terminal cap, and contributions from an amino-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). Ref.7 Ref.13

Subunit structure

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-735' and, sequesters ABL1 into the cytoplasm By similarity.

Subcellular location

Cytoplasmcytoskeleton. Nucleus. Note: The myristoylated c-ABL protein is reported to be nuclear. Sequestered into the cytoplasm through interaction with 14-3-3 proteins By similarity.

Tissue specificity

Widely expressed.

Post-translational modification

DNA damage-induced activation of c-Abl requires the function of ATM and Ser-446 phosphorylation. Phosphorylated by PRKDC. Isoform IV is myristoylated on Gly-2 By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDKN1BP465271EBI-914519,EBI-519280From a different organism.
Dok1P974653EBI-914519,EBI-914917
Nck1Q99M511EBI-914519,EBI-642202

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform I (identifier: P00520-1)

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.
Isoform II (identifier: P00520-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MISFDLLSDELHLKLLVLDV
Isoform III (identifier: P00520-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MSQRWTYTKCRVQRDPALPFM
Isoform IV (identifier: P00520-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11231123Proto-oncogene tyrosine-protein kinase ABL1
PRO_0000088051

Regions

Domain61 – 12161SH3
Domain127 – 21791SH2
Domain242 – 493252Protein kinase
Nucleotide binding248 – 2569ATP By similarity
Region1 – 6060CAP
Motif605 – 6095Nuclear localization signal Potential
Compositional bias18 – 225Poly-Ser
Compositional bias605 – 6095Poly-Lys
Compositional bias804 – 1012209Pro-rich
Compositional bias891 – 8977Poly-Pro

Sites

Active site3631Proton acceptor By similarity
Binding site2711ATP

Amino acid modifications

Modified residue501Phosphoserine By similarity
Modified residue1851Phosphotyrosine By similarity
Modified residue2261Phosphotyrosine By similarity
Modified residue2531Phosphotyrosine By similarity
Modified residue2571Phosphotyrosine By similarity
Modified residue2641Phosphotyrosine By similarity
Modified residue3931Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases Ref.13
Modified residue3941Phosphothreonine By similarity
Modified residue4461Phosphoserine Ref.7
Modified residue4691Phosphotyrosine By similarity
Modified residue5691Phosphoserine By similarity
Modified residue6131Phosphothreonine By similarity
Modified residue6201Phosphoserine By similarity
Modified residue6581Phosphoserine By similarity
Modified residue6821Phosphoserine By similarity
Modified residue7171Phosphoserine By similarity
Modified residue8031Phosphoserine By similarity
Modified residue8071Phosphoserine By similarity
Modified residue8121Phosphothreonine By similarity
Modified residue8441Phosphothreonine By similarity
Modified residue9091Phosphoserine By similarity
Modified residue9111Phosphoserine By similarity
Modified residue9271Phosphoserine By similarity
Modified residue9701Phosphoserine By similarity

Natural variations

Alternative sequence1 – 2626MLEIC…SCYLE → MISFDLLSDELHLKLLVLDV in isoform II.
VSP_004959
Alternative sequence1 – 2626MLEIC…SCYLE → MSQRWTYTKCRVQRDPALPF M in isoform III.
VSP_004958
Alternative sequence1 – 2626MLEIC…SCYLE → MGQQPGKVLGDQRRPSLPAL HFIKGAGKRDSSRHGGPHCN VFVEH in isoform IV.
VSP_004960

Experimental info

Mutagenesis2261Y → F: Minimal reduction in ability to autophosphorylate. Ref.13
Mutagenesis2711K → M: Loss of kinase activity. Ref.13
Mutagenesis3931Y → F: Minimal reduction in ability to autophosphorylate. Ref.13
Mutagenesis4461S → A: No effect on basal activity, but abolishes ionizing radiation-induced activation. Ref.7
Mutagenesis10831L → A: Loss of nuclear export.
Sequence conflict184 – 1874LYVS → VGDW in AAB60451. Ref.4
Sequence conflict184 – 1874LYVS → VGDW in AAB60450. Ref.4
Sequence conflict782 – 7865PPRLV → LPGWL in AAA88241. Ref.1
Sequence conflict9871D → G in BAC41088. Ref.2

Secondary structure

...................................................................................... 1123
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform I [UniParc].

Last modified February 15, 2005. Version 3.
Checksum: BD48ADE8557AE95C

FASTA1,123122,673
        10         20         30         40         50         60 
MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS KENLLAGPSE 

        70         80         90        100        110        120 
NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC EAQTKNGQGW VPSNYITPVN 

       130        140        150        160        170        180 
SLEKHSWYHG PVSRNAAEYL LSSGINGSFL VRESESSPGQ RSISLRYEGR VYHYRINTAS 

       190        200        210        220        230        240 
DGKLYVSSES RFNTLAELVH HHSTVADGLI TTLHYPAPKR NKPTIYGVSP NYDKWEMERT 

       250        260        270        280        290        300 
DITMKHKLGG GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ 

       310        320        330        340        350        360 
LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVSAVVL LYMATQISSA MEYLEKKNFI 

       370        380        390        400        410        420 
HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK FPIKWTAPES LAYNKFSIKS 

       430        440        450        460        470        480 
DVWAFGVLLW EIATYGMSPY PGIDLSQVYE LLEKDYRMER PEGCPEKVYE LMRACWQWNP 

       490        500        510        520        530        540 
SDRPSFAEIH QAFETMFQES SISDEVEKEL GKRGTRGGAG SMLQAPELPT KTRTCRRAAE 

       550        560        570        580        590        600 
QKDAPDTPEL LHTKGLGESD ALDSEPAVSP LLPRKERGPP DGSLNEDERL LPRDRKTNLF 

       610        620        630        640        650        660 
SALIKKKKKM APTPPKRSSS FREMDGQPDR RGASEDDSRE LCNGPPALTS DAAEPTKSPK 

       670        680        690        700        710        720 
ASNGAGVPNG AFREPGNSGF RSPHMWKKSS TLTGSRLAAA EEESGMSSSK RFLRSCSASC 

       730        740        750        760        770        780 
MPHGARDTEW RSVTLPRDLP SAGKQFDSST FGGHKSEKPA LPRKRTSESR SEQVAKSTAM 

       790        800        810        820        830        840 
PPPRLVKKNE EAAEEGFKDT ESSPGSSPPS LTPKLLRRQV TASPSSGLSH KEEATKGSAS 

       850        860        870        880        890        900 
GMGTPATAEP APPSNKVGLS KASSEEMRVR RHKHSSESPG RDKGRLAKLK PAPPPPPACT 

       910        920        930        940        950        960 
GKAGKPAQSP SQEAGEAGGP TKTKCTSLAM DAVNTDPTKA GPPGEGLRKP VPPSVPKPQS 

       970        980        990       1000       1010       1020 
TAKPPGTPTS PVSTPSTAPA PSPLAGDQQP SSAAFIPLIS TRVSLRKTRQ PPERIASGTI 

      1030       1040       1050       1060       1070       1080 
TKGVVLDSTE ALCLAISRNS EQMASHSAVL EAGKNLYTFC VSYVDSIQQM RNKFAFREAI 

      1090       1100       1110       1120 
NKLESNLREL QICPATASSG PAATQDFSKL LSSVKEISDI VRR 

« Hide

Isoform II.

Checksum: 002F9D346307028A
Show »

FASTA1,117122,179
Isoform III.

Checksum: AB3B4510AE8C5C38
Show »

FASTA1,118122,480
Isoform IV.

Checksum: 7A9DB9E772EAF05F
Show »

FASTA1,142124,769

References

« Hide 'large scale' references
[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: 3317402] [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. expand/collapse author list , 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: 16141072] [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: 15489334] [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: 7665185] [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: 6319018] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE 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: 3283651] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[7]"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: 9109492] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCALIZATION, PHOSPHORYLATION AT SER-446, MUTAGENESIS OF SER-446.
[8]"Nuclear-cytoplasmic shuttling of C-ABL tyrosine kinase."
Taagepera S., McDonald D., Loeb J.E., Whitaker L.L., McElroy A.K., Wang J.Y., Hope T.J.
Proc. Natl. Acad. Sci. U.S.A. 95:7457-7462(1998) [PubMed: 9636171] [Abstract]
Cited for: SUBCELLULAR LOCALIZATION.
[9]"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: 10896159] [Abstract]
Cited for: IDENTIFICATION IN A TRIMOLECULAR COMPLEX WITH CDK5 AND CABLES1, INTERACTION WITH CABLES1.
Tissue: Brain.
[10]"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: 11163214] [Abstract]
Cited for: INTERACTION WITH PSTPIP1.
[11]"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: 11279004] [Abstract]
Cited for: INTERACTION WITH CRK, FUNCTION.
[12]"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: 12021275] [Abstract]
Cited for: INTERACTION WITH ZDHHC16.
[13]"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: 12748290] [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.
[14]"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: 7664083] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 61-121.
[15]"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: 10988075] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 229-515.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00227806.
IPI00227807.
IPI00314762.
IPI00453940.
PIRA39962.
S00774.
RefSeqNP_033724.2.
UniGeneMm.1318

3D structure databases

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[»]
SMRP00520. Positions 1017-1123.
ModBaseSearch...

Protein-protein interaction databases

IntActP00520. 5 interactions.

PTM databases

PhosphoSiteP00520.

Genome annotation databases

EnsemblENSMUSG00000026842. Mus musculus. [Contig view]
GeneID11350.

Organism-specific databases

MGIMGI:87859. Abl1.

Phylogenomic databases

HOVERGENP00520.
OMAP00520. GAFRESG.

Enzyme and pathway databases

BRENDA2.7.10.2. 244.

Gene expression databases

ArrayExpressP00520.
BgeeP00520.
CleanExMM_ABL1.
GermOnlineENSMUSG00000026842. Mus musculus.

Family and domain databases

InterProIPR015015. F-actin_binding.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
[Graphical view]
Gene3DG3DSA:3.30.505.10. SH2. 1 hit.
PfamPF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
ProDomPD000001. Prot_kinase. 1 hit.
PD000093. SH2. 1 hit.
PD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS00107. 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]
ProtoNetSearch...

Other Resources

NextBio278620.
SOURCESearch...

Entry information

Entry nameABL1_MOUSE
AccessionPrimary (citable) accession number: P00520
Secondary accession number(s): P97896 expand/collapse secondary AC list , Q61252, Q61253, Q61254, Q61255, Q61256, Q61257, Q61258, Q61259, Q61260, Q61261, Q6PCM5, Q8C1X4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 15, 2005
Last modified: June 16, 2009
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents