UniProt: M3YMM7

Database: UniProt
Entry: M3YMM7_MUSPF

LinkDB:  M3YMM7_MUSPF 
Original site:  M3YMM7_MUSPF

All links

Ontology (98)   
   GO (98)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (9)   
   EMBL (9)   
Protein domain (25)   
   InterPro (12)   
   Pfam (4)   
   PROSITE (5)   
   SMART (4)   
All databases (139)   

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ID   M3YMM7_MUSPF            Unreviewed;      1150 AA.
AC   M3YMM7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN   Name=ABL1 {ECO:0000313|Ensembl:ENSMPUP00000012584.1,
GN   ECO:0000313|RefSeq:XP_004757162.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000012584.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000012584.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_004757162.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_004757162.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001149,
CC         ECO:0000256|RuleBase:RU362096};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000256|RuleBase:RU362096}.
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DR   EMBL; AEYP01042476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01042477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01042478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01042479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01042480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01042481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01042482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01042483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01042484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004757162.1; XM_004757105.3.
DR   STRING; 9669.ENSMPUP00000012584; -.
DR   Ensembl; ENSMPUT00000012787.1; ENSMPUP00000012584.1; ENSMPUG00000012678.1.
DR   GeneID; 101689921; -.
DR   KEGG; mpuf:101689921; -.
DR   CTD; 25; -.
DR   eggNOG; KOG4278; Eukaryota.
DR   GeneTree; ENSGT00940000153838; -.
DR   HOGENOM; CLU_002795_0_0_1; -.
DR   OMA; KCKSSNI; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000000715; Unplaced.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000405; F:bubble DNA binding; IEA:Ensembl.
DR   GO; GO:0046875; F:ephrin receptor binding; IEA:Ensembl.
DR   GO; GO:0000400; F:four-way junction DNA binding; IEA:Ensembl.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR   GO; GO:0030145; F:manganese ion binding; IEA:Ensembl.
DR   GO; GO:0051019; F:mitogen-activated protein kinase binding; IEA:Ensembl.
DR   GO; GO:0038191; F:neuropilin binding; IEA:Ensembl.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl.
DR   GO; GO:0070064; F:proline-rich region binding; IEA:Ensembl.
DR   GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR   GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:Ensembl.
DR   GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR   GO; GO:0019905; F:syntaxin binding; IEA:Ensembl.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl.
DR   GO; GO:0046632; P:alpha-beta T cell differentiation; IEA:Ensembl.
DR   GO; GO:0002322; P:B cell proliferation involved in immune response; IEA:Ensembl.
DR   GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0001922; P:B-1 B cell homeostasis; IEA:Ensembl.
DR   GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
DR   GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0007249; P:canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
DR   GO; GO:0021587; P:cerebellum morphogenesis; IEA:Ensembl.
DR   GO; GO:0072359; P:circulatory system development; IEA:Ensembl.
DR   GO; GO:1904157; P:DN4 thymocyte differentiation; IEA:Ensembl.
DR   GO; GO:0071103; P:DNA conformation change; IEA:Ensembl.
DR   GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0030035; P:microspike assembly; IEA:Ensembl.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:2000773; P:negative regulation of cellular senescence; IEA:Ensembl.
DR   GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR   GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR   GO; GO:0060563; P:neuroepithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR   GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   GO; GO:0038189; P:neuropilin signaling pathway; IEA:Ensembl.
DR   GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; IEA:Ensembl.
DR   GO; GO:1905555; P:positive regulation of blood vessel branching; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:1903905; P:positive regulation of establishment of T cell polarity; IEA:Ensembl.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:2000406; P:positive regulation of T cell migration; IEA:Ensembl.
DR   GO; GO:0032729; P:positive regulation of type II interferon production; IEA:Ensembl.
DR   GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:1904518; P:protein localization to cytoplasmic microtubule plus-end; IEA:Ensembl.
DR   GO; GO:0030516; P:regulation of axon extension; IEA:Ensembl.
DR   GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IEA:Ensembl.
DR   GO; GO:1903053; P:regulation of extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0031113; P:regulation of microtubule polymerization; IEA:Ensembl.
DR   GO; GO:1905244; P:regulation of modification of synaptic structure; IEA:Ensembl.
DR   GO; GO:0045580; P:regulation of T cell differentiation; IEA:Ensembl.
DR   GO; GO:0042770; P:signal transduction in response to DNA damage; IEA:Ensembl.
DR   GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR   GO; GO:0002333; P:transitional one stage B cell differentiation; IEA:Ensembl.
DR   CDD; cd05052; PTKc_Abl; 1.
DR   CDD; cd09935; SH2_ABL; 1.
DR   CDD; cd11850; SH3_Abl; 1.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR035837; ABL_SH2.
DR   InterPro; IPR015015; F-actin-binding.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF438; TYROSINE-PROTEIN KINASE ABL1; 1.
DR   Pfam; PF08919; F_actin_bind; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00808; FABD; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW   ECO:0000256|RuleBase:RU362096}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|RuleBase:RU362096}.
FT   DOMAIN          80..140
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          146..236
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          261..512
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          537..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..568
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..620
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..657
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..734
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..772
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..791
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        889..913
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         290
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1150 AA;  124651 MW;  6126C97011BA1BDD CRC64;
     MGQQPGKVVG DQRRPSLPAL HFIKGAGKKE SSRHGGPHCN VFVEHEALQR PVASDFEPQG
     LSEAARWNSK ENLLAGPSEN DPNLFVALYD FVASGDNTLS ITKGEKLRVL GYNHNGEWCE
     AQTKNGQGWV PSNYITPVNS LEKHSWYHGP VSRNAAEYLL SSGINGSFLV RESESSPGQR
     SISLRYEGRV YHYRINTASD GKLYVSSESR FNALAELVHH HSTVADGLIT TLHYPAPKRN
     KPTIYGVSPN YDKWEMERTD ITMKHKLGGG QYGEVYEGVW KKYSLTVAVK TLKEDTMEVE
     EFLKEAAVMK EIKHPNLVQL LGVCTREPPF YIITEFMTYG NLLDYLRECN RQEVNAVVLL
     YMATQISSAM EYLEKKNFIH RDLAARNCLV GENHLVKVAD FGLSRLMTGD TYTAHAGAKF
     PIKWTAPESL AYNKFSIKSD VWAFGVLLWE IATYGMSPYP GIDLSQVYEL LEKDYRMERP
     EGCPEKVHGL MRACWQWNPS DRPSFAEIHQ AFETMFQESS ISDEVEKELG KQGVRGVAST
     LLQAPELPTK TRTSRRAAEH KDPTEVPETP HSKGPGETEP LDHEPPVSPL LPRKERGPQY
     GGLNEDERLL PKDKKTNLFS ALIKKKKKTA PTPPKRSSSF REMDGQPERK ATSEEEGRET
     SNGAPVLTPS DAAEPAKSPK PSSRAGVPNG AFRESGGAGF RSPHLWKKSS TLTSGRLAAS
     EEESGSSASK RFLRSCSASC VPHGAKDTEW RSVTLPRDLQ STGRQFDSST FGGHKSEKPA
     LPRKRASENR SDQVTRGTVT PPPRLVKKTE DAADEVFRDA GEASPGSSPP SLTPKLLRRQ
     VAGASSSGLP HKDEVGKSGA LGTIVAAEPV PATSRAGPGA SGGAGKAPTE EPRARRHKPS
     SESPGRDKGK LSKLKPVPPP PPPASAGKAG KPSQSQSQEA AGEAGAGGKA KAAAMVVDAV
     NSDTVKPGPL GEGVKKPGLP SMPKPQSSSK PAGTPTSPAP APSASPSASS ALAGDQPAST
     AFIPLISTRV SLRKTRQPPE RIASGTITKG VVLDGTEALC LAISKNSEQM ASHSAVLEAG
     KNLYTFCVSY VDSIQQMRNK FAFREAINKL ENNLRELQIC PATAGSGPAA TQDFSKLLSS
     VKEISDIVQR
//

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