ID CBL_HUMAN STANDARD; PRT; 906 AA. AC P22681; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE SIGNAL TRANSDUCTION PROTEIN CBL (PROTO-ONCOGENE C-CBL). GN CBL OR CBL2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91232862; PubMed=2030914; RA Blake T.J., Shapiro M., Morse H.C. III, Langdon W.Y.; RT "The sequences of the human and mouse c-cbl proto-oncogenes show RT v-cbl was generated by a large truncation encompassing a proline-rich RT domain and a leucine zipper-like motif."; RL Oncogene 6:653-657(1991). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 47-350. RX MEDLINE=99176421; PubMed=10078535; RA Meng W., Sawasdikosol S., Burakoff S.J., Eck M.J.; RT "Structure of the amino-terminal domain of Cbl complexed to its RT binding site on ZAP-70 kinase."; RL Nature 398:84-90(1999). CC -!- FUNCTION: PARTICIPATES IN SIGNAL TRANSDUCTION IN HEMATOPOIETIC CC CELLS. ADAPTOR PROTEIN THAT FUNCTIONS AS A NEGATIVE REGULATOR OF CC MANY SIGNALLING PATHWAYS THAT START FROM RECEPTORS AT THE CELL CC SURFACE. CC -!- SUBUNIT: ASSOCIATES WITH NCK VIA ITS SH3 DOMAIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- PTM: PHOSPHORYLATED ON TYROSINE. CC -!- SIMILARITY: CONTAINS A C3HC4-CLASS ZINC FINGER. CC -!- SIMILARITY: CONTAINS 1 UBA DOMAIN. 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; X57110; CAA40393.1; -. DR PIR; A43817; A43817. DR PDB; 1B47; 27-APR-99. DR MIM; 165360; -. DR InterPro; IPR000449; -. DR InterPro; IPR001841; -. DR Pfam; PF00627; UBA; 1. DR Pfam; PF00097; zf-C3HC4; 1. DR PROSITE; PS00518; ZINC_FINGER_C3HC4; 1. KW Proto-oncogene; Nuclear protein; Zinc-finger; Phosphorylation; KW 3D-structure. FT DOMAIN 124 127 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT ZN_FING 381 419 C3HC4-TYPE. FT DOMAIN 357 476 ASP/GLU-RICH (ACIDIC). FT DOMAIN 477 688 PRO-RICH. FT DOMAIN 689 834 ASP/GLU-RICH (ACIDIC). FT DOMAIN 856 895 UBA. FT MOD_RES 700 700 PHOSPHORYLATION. FT MOD_RES 774 774 PHOSPHORYLATION. SQ SEQUENCE 906 AA; 99646 MW; 7D686B050204AD8F CRC64; MAGNVKKSSG AGGGTGSGGS GSGGLIGLMK DAFQPHHHHH HHLSPHPPGT VDKKMVEKCW KLMDKVVRLC QNPKLALKNS PPYILDLLPD TYQHLRTILS RYEGKMETLG ENEYFRVFME NLMKKTKQTI SLFKEGKERM YEENSQPRRN LTKLSLIFSH MLAELKGIFP SGLFQGDTFR ITKADAAEFW RKAFGEKTIV PWKSFRQALH EVHPISSGLE AMALKSTIDL TCNDYISVFE FDIFTRLFQP WSSLLRNWNS LAVTHPGYMA FLTYDEVKAR LQKFIHKPGS YIFRLSCTRL GQWAIGYVTA DGNILQTIPH NKPLFQALID GFREGFYLFP DGRNQNPDLT GLCEPTPQDH IKVTQEQYEL YCEMGSTFQL CKICAENDKD VKIEPCGHLM CTSCLTSWQE SEGQGCPFCR CEIKGTEPIV VDPFDPRGSG SLLRQGAEGA PSPNYDDDDD ERADDTLFMM KELAGAKVER PPSPFSMAPQ ASLPPVPPRL DLLPQRVCVP SSASALGTAS KAASGSLHKD KPLPVPPTLR DLPPPPPPDR PYSVGAESRP QRRPLPCTPG DCPSRDKLPP VPSSRLGDSW LPRPIPKVPV SAPSSSDPWT GRELTNRHSL PFSLPSQMEP RPDVPRLGST FSLDTSMSMN SSPLVGPECD HPKIKPSSSA NAIYSLAARP LPVPKLPPGE QCEGEEDTEY MTPSSRPLRP LDTSQSSRAC DCDQQIDSCT YEAMYNIQSQ APSITESSTF GEGNLAAAHA NTGPEESENE DDGYDVPKPP VPAVLARRTL SDISNASSSF GWLSLDGDPT TNVTEGSQVP ERPPKPFPRR INSERKAGSC QQGSGPAASA ATASPQLSSE IENLMSQGYS YQDIQKALVI AQNNIEMAKN ILREFVSISS PAHVAT //