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   28-FEB-2003 (Rel. 41, 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 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -!- DATABASE: NAME=Atlas Genet. Cytogenet. Oncol. Haematol.;
CC       WWW="http://www.infobiogen.fr/services/chromcancer/Genes/CBLID171.html".
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DR   EMBL; X57110; CAA40393.1; -.
DR   PIR; A43817; A43817.
DR   PDB; 1B47; 27-APR-99.
DR   Genew; HGNC:1541; CBL.
DR   MIM; 165360; -.
DR   GO; GO:0003700; F:transcription factor activity; TAS.
DR   GO; GO:0007048; P:oncogenesis; TAS.
DR   InterPro; IPR003153; Cbl_N.
DR   InterPro; IPR000449; UBA_domain.
DR   InterPro; IPR001841; Znf_ring.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF00627; UBA; 1.
DR   Pfam; PF02262; Cbl_N; 1.
DR   Pfam; PF02761; Cbl_N2; 1.
DR   Pfam; PF02762; Cbl_N3; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00165; UBA; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
KW   Proto-oncogene; Nuclear protein; Zinc-finger; Phosphorylation;
KW   3D-structure.
FT   DOMAIN      124    127       NUCLEAR LOCALIZATION SIGNAL (POTENTIAL).
FT   ZN_FING     381    420       RING-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.
FT   HELIX        53     70
FT   TURN         71     71
FT   HELIX        73     75
FT   HELIX        84    101
FT   TURN        102    102
FT   HELIX       106    110
FT   TURN        111    111
FT   HELIX       113    136
FT   HELIX       137    141
FT   TURN        143    144
FT   HELIX       146    168
FT   HELIX       170    172
FT   HELIX       176    178
FT   HELIX       184    194
FT   TURN        195    196
FT   STRAND      199    201
FT   HELIX       202    212
FT   HELIX       218    228
FT   TURN        230    231
FT   STRAND      235    237
FT   HELIX       238    248
FT   HELIX       251    253
FT   HELIX       254    262
FT   TURN        263    263
FT   TURN        266    267
FT   STRAND      268    271
FT   HELIX       274    281
FT   HELIX       282    284
FT   TURN        285    286
FT   TURN        288    289
FT   STRAND      290    295
FT   TURN        297    298
FT   TURN        300    301
FT   STRAND      303    308
FT   TURN        310    311
FT   STRAND      314    317
FT   TURN        320    321
FT   HELIX       324    333
FT   TURN        334    335
FT   STRAND      339    340
FT   TURN        341    342
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
//