ID A0A2K6KIL7_RHIBE Unreviewed; 1040 AA.
AC A0A2K6KIL7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN Name=ABL2 {ECO:0000313|Ensembl:ENSRBIP00000011107.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000011107.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000011107.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000011107.1}
RP IDENTIFICATION.
RG Ensembl;
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000256|RuleBase:RU362096}.
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DR RefSeq; XP_017747157.1; XM_017891668.1.
DR AlphaFoldDB; A0A2K6KIL7; -.
DR Ensembl; ENSRBIT00000034750.1; ENSRBIP00000011107.1; ENSRBIG00000029397.1.
DR GeneID; 108541908; -.
DR CTD; 27; -.
DR GeneTree; ENSGT00940000153838; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
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:SF87; TYROSINE-PROTEIN KINASE ABL2; 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:UP000233180};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW 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 71..131
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 137..227
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 252..503
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 551..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1040 AA; 113923 MW; DDFFC42E62C9D8C5 CRC64;
MVLGTVLLPP NSYGRDQDTS LCCLCTEASE SALPDMTEAL HRPYGCDVEP QALNEAIRWS
SKENLLGATE SDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNQNGEWS EVRSKNGQGW
VPSNYITPVN SLEKHSWYHG PVSRSAAEYL LSSLINGSFL VRESESSPGQ LSISLRYEGR
VYHYRINTTA DGKVYVTAES RFSTLAELVH HHSTVADGLV TTLHYPAPKC NKPTVYGVSP
IHDKWEMERT DITMKHKLGG GQYGEVYVGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM
KEIKHPNLVQ LLGVCTLEPP FYIVTEYMPY GNLLDYLREC NREEVTAVVL LYMATQISSA
MEYLEKKNFI HRDLAARNCL VGENHVVKVA DFGLSRLMTG DTYTAHAGAK FPIKWTAPES
LAYNTFSIKS DVWAFGVLLW EIATYGMSPY PGIDLSQVYD LLEKGYRMEQ PEGCPPKVYE
LMRACWKWSP ADRPSFAETH QAFETMFHDS SISEEVAEEL GRAASSSSVV PYLPRLPILP
SKTRTLKKQV ENKENIEGAQ DATENSASSL TPGFIRGAQA SSGSPALPRK QRDKSPSSLL
EDAKETCFTR DRKGGFFSSF MKKRNAPTPP KRSSSFREME NQPHKKYELT GLPEQDRMAM
TLPRNCQRSK LQLERTVSTS SQPEENVDRA NDMLPKKSEE GAAPSRERPK AKLLPRGATA
LPLRTPSGDL AITEKDPPGV GVAGVAAAPK GKEKNGGTRL GMAGVLEDGE QPGWPSPAKA
APVLPTTHNH KVPVLISPTL KHTPADVQLI GTDSQGNKFK LLSEHQVTSS GDKDRPRRVK
PKCAPPPPPV MRLLQHPSIC SDPTEEPTAG QSTSETQEGG KKAALGAVPV SGKAGRPVMP
PPQVPLPTSS ISPAKMANGT AGTKVALRKT KQATEKISAD KISKEALLEC ADLLSSAITE
PVPNSQLVDT GHQLLDYCSG YVDCIPQTRN KFAFREAVSK LELSLQELQV SSAAAGVPGA
NPVLNNLLSC VQEISDVVQR
//
