ID I6TRR8_HUMAN Unreviewed; 979 AA. AC I6TRR8; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 27-MAR-2024, entry version 48. DE SubName: Full=SND1-BRAF fusion {ECO:0000313|EMBL:AFN01665.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AFN01665.1}; RN [1] {ECO:0000313|EMBL:AFN01665.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=22745804; DOI=10.1371/journal.pone.0039653; RA Lee N.V., Lira M.E., Pavlicek A., Ye J., Buckman D., Bagrodia S., RA Srinivasa S.P., Zhao Y., Aparicio S., Rejto P.A., Christensen J.G., RA Ching K.A.; RT "A Novel SND1-BRAF Fusion Confers Resistance to c-Met Inhibitor PF-04217903 RT in GTL16 Cells though MAPK Activation."; RL PLoS ONE 7:e39653-e39653(2012). CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JX013981; AFN01665.1; -; mRNA. DR AlphaFoldDB; I6TRR8; -. DR PeptideAtlas; I6TRR8; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR CDD; cd00175; SNc; 3. DR CDD; cd14062; STKc_Raf; 1. DR Gene3D; 2.40.50.90; -; 4. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR035437; SNase_OB-fold_sf. DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold. DR InterPro; IPR002071; Thermonucl_AS. DR PANTHER; PTHR12302; EBNA2 BINDING PROTEIN P100; 1. DR PANTHER; PTHR12302:SF28; STAPHYLOCOCCAL NUCLEASE DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF00565; SNase; 3. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00318; SNc; 4. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF50199; Staphylococcal nuclease; 4. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS01284; TNASE_2; 1. DR PROSITE; PS50830; TNASE_3; 3. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Isopeptide bond {ECO:0000256|ARBA:ARBA00022499}; KW Kinase {ECO:0000256|ARBA:ARBA00022527}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527}; KW Transferase {ECO:0000256|ARBA:ARBA00022527}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}. FT DOMAIN 18..166 FT /note="TNase-like" FT /evidence="ECO:0000259|PROSITE:PS50830" FT DOMAIN 193..328 FT /note="TNase-like" FT /evidence="ECO:0000259|PROSITE:PS50830" FT DOMAIN 341..496 FT /note="TNase-like" FT /evidence="ECO:0000259|PROSITE:PS50830" FT DOMAIN 670..930 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 599..667 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 605..639 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 640..664 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 696 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 979 AA; 109147 MW; 8B4B073875C717F1 CRC64; MASSAQSGGS SGGPAVPTVQ RGIIKMVLSG CAIIVRGQPR GGPPPERQIN LSNIRAGNLA RRAAATQPDA KDTPDEPWAF PAREFLRKKL IGKEVCFTIE NKTPQGREYG MIYLGKDTNG ENIAESLVAE GLATRREGMR ANNPEQNRLS ECEEQAKAAK KGMWSEGNGS HTIRDLKYTI ENPRHFVDSH HQKPVNAIIE HVRDGSVVRA LLLPDYYLVT VMLSGIKCPT FRREADGSET PEPFAAEAKF FTESRLLQRD VQIILESCHN QNILGTILHP NGNITELLLK EGFARCVDWS IAVYTRGAEK LRAAERFAKE RRLRIWRDYV APTANLDQKD KQFVAKVMQV LNADAIVVKL NSGDYKTIHL SSIRPPRLEG ENTQDKNKKL RPLYDIPYMF EAREFLRKKL IGKKVNVTVD YIRPASPATE TVPAFSERTC ATVTIGGINI AEALVSKGLA TVIRYRQDDD QRSSHYDELL AAEARAIKNG KGLHSKKEVP IHRVADISGD TQKAKQFLPF LQRAGRSEAV VEYVFSGSRL KLYLPKETCL ITFLLAGIEC PRGARNLPGL VQEGEPFSEE ATLFTKELVL QREDLIRDQG FRGDGGSTTG LSATPPASLP GSLTNVKALQ KSPGPQRERK SSSSSEDRNR MKTLGRRDSS DDWEIPDGQI TVGQRIGSGS FGTVYKGKWH GDVAVKMLNV TAPTPQQLQA FKNEVGVLRK TRHVNILLFM GYSTKPQLAI VTQWCEGSSL YHHLHIIETK FEMIKLIDIA RQTAQGMDYL HAKSIIHRDL KSNNIFLHED LTVKIGDFGL ATVKSRWSGS HQFEQLSGSI LWMAPEVIRM QDKNPYSFQS DVYAFGIVLY ELMTGQLPYS NINNRDQIIF MVGRGYLSPD LSKVRSNCPK AMKRLMAECL KKKRDERPLF PQILASIELL ARSLPKIHRS ASEPSLNRAG FQTEDFSLYA CASPKTPIQA GGYGAFPVH //