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Database: UniProt
Entry: A2JNH2_HUMAN
LinkDB: A2JNH2_HUMAN
Original site: A2JNH2_HUMAN 
ID   A2JNH2_HUMAN            Unreviewed;       390 AA.
AC   A2JNH2;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   SubName: Full=MLL/GAS7 fusion protein {ECO:0000313|EMBL:AAG26331.2};
DE   Flags: Fragment;
GN   Name=MLL/GAS7 {ECO:0000313|EMBL:AAG26331.2};
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:AAG26331.2};
RN   [1] {ECO:0000313|EMBL:AAG26331.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=10706619; DOI=10.1073/pnas.050397097;
RA   Megonigal M.D., Cheung N.-K.V., Rappaport E.F., Nowell P.C., Wilson R.B.,
RA   Jones D.H., Addya K., Leonard D.G.B., Kushner B.H., Williams T.M.,
RA   Lange B.J., Felix C.A.;
RT   "Detection of leukemia-associated MLL-GAS7 translocation early during
RT   chemotherapy with DNA topoisomerase II inhibitors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:2814-2819(2000).
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DR   EMBL; AF231997; AAG26331.2; -; mRNA.
DR   AlphaFoldDB; A2JNH2; -.
DR   PeptideAtlas; A2JNH2; -.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR23065:SF57; GROWTH ARREST-SPECIFIC PROTEIN 7; 1.
DR   PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00397; WW; 1.
DR   Pfam; PF16623; WW_FCH_linker; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils}.
FT   DOMAIN          112..145
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          231..390
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   REGION          1..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          361..388
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        61..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAG26331.2"
FT   NON_TER         390
FT                   /evidence="ECO:0000313|EMBL:AAG26331.2"
SQ   SEQUENCE   390 AA;  43590 MW;  2903456795042886 CRC64;
     TTGPPRKEVP KTTPSEPKKK QPPPPESGPE QSKQKKVAPR PSIPVKQKPK EKEKPPPVNK
     QENAGTLNIL STLSNGNSSK QKIPADGVHR IRVDFKKPGM VPPPPGEESQ TVILPPGWQS
     YLSPQGRRYY VNTTTNETTW ERPSSSPGIP ASPGSHRSSL PPTVNGYHAS GTPAHPPETA
     HMSVRKSTGD SQNLGSSSPS KKQSKENTIT INCVTFPHPD TMPEQQLLKP TEWSYCDYFW
     ADKKDPQGNG TVAGFELLLQ KQLKGKQMQK EMSEFIRERI KIEEDYAKNL AKLSQNSLAS
     QEEGSLGEAW AQVKKSLADE AEVHLKFSAK LHSEVEKPLM NFRENFKKDM KKCDHHIADL
     RKQLASRYAS VEKARKALTE RQRDLEMKTR
//
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