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   30-MAY-2000 (Rel. 39, Last annotation update)
DE   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.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 91232862.
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.
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.
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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      857    892       LEUCINE-ZIPPER.
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
//