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Database: UniProt
Entry: A0A3Q7SR65_VULVU
LinkDB: A0A3Q7SR65_VULVU
Original site: A0A3Q7SR65_VULVU 
ID   A0A3Q7SR65_VULVU        Unreviewed;      1150 AA.
AC   A0A3Q7SR65;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
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|RefSeq:XP_025865314.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025865314.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025865314.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025865314.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025865314.1};
RG   RefSeq;
RL   Submitted (SEP-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   RefSeq; XP_025865314.1; XM_026009529.1.
DR   AlphaFoldDB; A0A3Q7SR65; -.
DR   STRING; 9627.ENSVVUP00000038805; -.
DR   Ensembl; ENSVVUT00000050858; ENSVVUP00000038805; ENSVVUG00000027674.
DR   KEGG; vvp:112927987; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000286640; 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:0043124; P:negative regulation of canonical NF-kappaB signal transduction; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; 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:UP000286640};
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          536..952
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          965..1010
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        598..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..735
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        824..847
FT                   /note="Polar 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   COMPBIAS        987..1010
FT                   /note="Polar 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;  125153 MW;  DCF5CFD01D424199 CRC64;
     MGQQPGKVLG DQRRPSLPAL HFIKGAGKKE SSRHGGPHCN VFVEHEALQR PVASDFEPQG
     LSEAARWNSK ENLLAGPSEN DPNLFVALYD FVASGDNTLS ITKGEKLRVL GYNHNGEWCE
     AQTKNGQGWV PSNYITPVNS LEKHSWYHGP VSRNAAEYLL SSGINGSFLV RESESSPGQR
     SISLRYEGRV YHYRINTASD GKLYVSSESR FNTLAELVHH HSTVADGLIT TLHYPAPKRN
     KPTVYGVSPN YDKWEMERTD ITMKHKLGGG QYGEVYEGVW KKYSLTVAVK TLKEDTMEVE
     EFLKEAAVMK EIKHPNLVQL LGVCTREPPF YIITEFMTYG NLLDYLRECN RQEVNAVVLL
     YMATQISSAM EYLEKKNFIH RDLAARNCLV GENHLVKVAD FGLSRLMTGD TYTAHAGAKF
     PIKWTAPESL AYNKFSIKSD VWAFGVLLWE IATYGMSPYP GIDLSQVYEL LEKDYRMERP
     EGCPEKVYEL MRACWQWNPS DRPSFAEIHQ AFETMFQESS ISDEVEKELG KKGVRGVAST
     LLQAPELPTK TRTSRRAAEH KDPTDVPETP HTKGPGETDP LDHEPPVSPL LPRKERGPQD
     SSLNEDERLL PKDKKTNLFS ALIKKKKKTA PTPPKRSSSF REMDGQPERK AAVEEEGRET
     SNGVPALTTL DAAEPAKSPK PSSGAGVPNG AFRESGGPGF RSPHLWKKSS TLTSSRLTAN
     EEESGGSSSK RFLRSCSASC VPHGAKDTEW RSVTLPRDLQ STGRQFDSST FGGHKSEKPA
     LPRKRASENR SDQVTRGTVT PPPRLVKKTE DAADEVFRDM GESSPGSSPP SLTPKLLRKQ
     VSGAPSSSLP HKDEAGKSSA LGTPTTAELG TPASRGGPGM SGGASKAPTE EPRARRHKPS
     SESPGRDKGK LSKLKPVPPP PLPASIGKAG KPSQSLSQEA AGEASTGGKA KAAAVVVDAV
     NSDTVKPGLL GEGIKKPVLP SMPKPQSSGK PAGTPASPAS TPSTLSSASS ALAVDQPAST
     AFIPLISTRV SLRKTRQPPE RIASGTITKG VVLDGTEALC LAISKNSEQM ASHSAVLEAG
     KNLYTFCVSY VDSIQQMRNK FAFREAINKL ENNLRELQIC PATAGSGPAA TQDFSKLLSS
     VKEISDIVQR
//
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