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Database: UniProt
Entry: A0A452QVJ4_URSAM
LinkDB: A0A452QVJ4_URSAM
Original site: A0A452QVJ4_URSAM 
ID   A0A452QVJ4_URSAM        Unreviewed;      1134 AA.
AC   A0A452QVJ4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
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:ENSUAMP00000009708.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000009708.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000009708.1}
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   -!- 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   AlphaFoldDB; A0A452QVJ4; -.
DR   Ensembl; ENSUAMT00000010929.1; ENSUAMP00000009708.1; ENSUAMG00000008042.1.
DR   GeneTree; ENSGT00940000153838; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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: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: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:UP000291022};
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          64..124
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          130..220
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          245..496
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          524..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..604
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..663
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..775
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        873..897
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1134 AA;  123386 MW;  012DF3ACDA6D077B CRC64;
     IYSVNMKPVK CRTNFFPNSS CFLFPLCLPE ALQRPVASDF ETQGLSEAAR WNSKENLLAG
     PSENDPNLFV ALYDFVASGD NTLSITKGEK LRVLGYNHNG EWCEAQTKNG QGWVPSNYIT
     PVNSLEKHSW YHGPVSRNAA EYLLSSGING SFLVRESESS PGQRSISLRY EGRVYHYRIN
     TASDGKLYVS SESRFNTLAE LVHHHSTVAD GLITTLHYPA PKRNKPTVYG VSPNYDKWEM
     ERTDITMKHK LGGGQYGEVY EGVWKKYSLT VAVKTLKEDT MEVEEFLKEA AVMKEIKHPN
     LVQLLGVCTR EPPFYIITEF MTYGNLLDYL RECNRQEVNA VVLLYMATQI SSAMEYLEKK
     NFIHRDLAAR NCLVGENHLV KVADFGLSRL MTGDTYTAHA GAKFPIKWTA PESLAYNKFS
     IKSDVWAFGV LLWEIATYGM SPYPGIDLSQ VYELLEKDYR MERPEGCPEK VYELMRACWQ
     WNPSDRPSFA EIHQAFETMF QESSISDEVE KELGKKGVRG VASTLLQAPE LPTKTRTSRR
     AVEHKDPTDV PETPHSKGPG ETDPLDHEPP VSPLLPRKER GPQDGGLNED ERLLPKDKKT
     NLFSALIKKK KKTAPTPPKR SSSFREMDGQ PERKAASEEE GRETSNGGPA LTPSDTTEPA
     KSPKPSSGAG VPNGAFRETG GAGFRSPHLW KKSSTLTSSR LAASEEESGS SSSKRFLRSC
     SASCVPHGAR DTEWRSVTLP RDLQSTGRQF DSSTFGGHKS EKPALPRKRA SENRSDQVTR
     GTVTPPPRLV KKTEDAVDEV FRDTGESSPG SSPPSLTPKL LRRQVAGTPS SGLPHKDEAG
     KSGALGTPAT AEPVPPASRA GPGASGGASK ASTEEPRARR HKPSSESPGR DKAKLSKLKP
     VPPPPPPASV GKAGKPSQNL SQEAAGEAGT GGKAKATAVV GDAVNSDTIK PGPLGEGVKK
     PVLPSMPKPQ SSSKPAGTPT SPAPTPSTVP SASSALAGDQ PASTAFIPLI STRVSLRKTR
     QPPERIASGT ITKGVVLDGT EALCLAISKN SEQMASHSAV LEAGKNLCTF CVSYVDSIQQ
     MRNKFAFREA INKLENNLRE LQICPATAGS GPAATQDFSK LLSSVKEISD IVQR
//
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