Full text data of SH3GL1
SH3GL1
(CNSA1, SH3D2B)
[Confidence: low (only semi-automatic identification from reviews)]
Endophilin-A2 (EEN fusion partner of MLL; Endophilin-2; Extra eleven-nineteen leukemia fusion gene protein; EEN; SH3 domain protein 2B; SH3 domain-containing GRB2-like protein 1)
Endophilin-A2 (EEN fusion partner of MLL; Endophilin-2; Extra eleven-nineteen leukemia fusion gene protein; EEN; SH3 domain protein 2B; SH3 domain-containing GRB2-like protein 1)
UniProt
Q99961
ID SH3G1_HUMAN Reviewed; 368 AA.
AC Q99961; B4DRA1; E7EVZ4; M0QZV5; Q99668;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Endophilin-A2;
DE AltName: Full=EEN fusion partner of MLL;
DE AltName: Full=Endophilin-2;
DE AltName: Full=Extra eleven-nineteen leukemia fusion gene protein;
DE Short=EEN;
DE AltName: Full=SH3 domain protein 2B;
DE AltName: Full=SH3 domain-containing GRB2-like protein 1;
GN Name=SH3GL1; Synonyms=CNSA1, SH3D2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=9169142; DOI=10.1006/geno.1997.4645;
RA Giachino C., Lantelme E., Lanzetti L., Saccone S., Della Valle G.,
RA Migone N.;
RT "A novel SH3-containing human gene family preferentially expressed in
RT the central nervous system.";
RL Genomics 41:427-434(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION.
RC TISSUE=Fetal brain;
RX PubMed=9122235; DOI=10.1073/pnas.94.6.2563;
RA So C.W., Caldas C., Liu M.-M., Chen S.-J., Huang Q.-H., Gu L.-J.,
RA Sham M.H., Wiedemann L.M., Chan L.C.;
RT "EEN encodes for a member of a new family of proteins containing an
RT Src homology 3 domain and is the third gene located on chromosome
RT 19p13 that fuses to MLL in human leukemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2563-2568(1997).
RN [3]
RP SEQUENCE REVISION.
RA So C.W., Caldas C., Liu M.-M., Chen S.-J., Huang Q.-H., Gu L.-J.,
RA Sham M.H., Wiedemann L.M., Chan L.C.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chen S., Xiong H., Dong H., Lin W., Zhang C., Fu G., Qi Z.,
RA Huang G.M.;
RT "Homo sapiens SH3-containing protein EEN gene.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH SYNJ1.
RX PubMed=10542231; DOI=10.1074/jbc.274.45.32001;
RA Cestra G., Castagnoli L., Dente L., Minenkova O., Petrelli A.,
RA Migone N., Hoffmueller U., Schneider-Mergener J., Cesareni G.;
RT "The SH3 domains of endophilin and amphiphysin bind to the proline-
RT rich region of synaptojanin 1 at distinct sites that display an
RT unconventional binding specificity.";
RL J. Biol. Chem. 274:32001-32007(1999).
RN [9]
RP INTERACTION WITH PDCD6IP.
RX PubMed=17350572; DOI=10.1016/j.cell.2007.01.035;
RA Fisher R.D., Chung H.Y., Zhai Q., Robinson H., Sundquist W.I.,
RA Hill C.P.;
RT "Structural and biochemical studies of ALIX/AIP1 and its role in
RT retrovirus budding.";
RL Cell 128:841-852(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP INTERACTION WITH BIN2, AND SUBCELLULAR LOCATION.
RX PubMed=23285027; DOI=10.1371/journal.pone.0052401;
RA Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J.,
RA Veprintsev D.B., Evans P.R., McMahon H.T.;
RT "Bin2 is a membrane sculpting N-BAR protein that influences leucocyte
RT podosomes, motility and phagocytosis.";
RL PLoS ONE 7:E52401-E52401(2012).
CC -!- FUNCTION: Implicated in endocytosis. May recruit other proteins to
CC membranes with high curvature (By similarity).
CC -!- SUBUNIT: Interacts with ARC (By similarity). Interacts with SYNJ1
CC and DNM1. Interacts with PDCD6IP. Interacts with BIN2.
CC -!- INTERACTION:
CC Self; NbExp=3; IntAct=EBI-697911, EBI-697911;
CC Q7L190:DPPA4; NbExp=5; IntAct=EBI-697911, EBI-710457;
CC Q9H788:SH2D4A; NbExp=3; IntAct=EBI-697911, EBI-747035;
CC Q99962:SH3GL2; NbExp=3; IntAct=EBI-697911, EBI-77938;
CC Q99963:SH3GL3; NbExp=4; IntAct=EBI-697911, EBI-473910;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Early endosome
CC membrane; Peripheral membrane protein (By similarity). Cell
CC projection, podosome. Note=Associated with postsynaptic endosomes
CC in hippocampal neurons (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99961-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99961-2; Sequence=VSP_045837;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q99961-3; Sequence=VSP_047037;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Higher expression in pancreas,
CC placenta, prostate, testis and uterus.
CC -!- DOMAIN: An N-terminal amphipathic helix, the BAR domain and a
CC second amphipathic helix inserted into helix 1 of the BAR domain
CC (N-BAR domain) induce membrane curvature and bind curved membranes
CC (By similarity).
CC -!- DISEASE: Note=In some cases of acute leukemia, a translocation
CC results in the formation of a KMT2A/MLL1-EEN fusion gene.
CC -!- SIMILARITY: Belongs to the endophilin family.
CC -!- SIMILARITY: Contains 1 BAR domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EEN.html";
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DR EMBL; X99656; CAA67970.1; -; mRNA.
DR EMBL; U65999; AAB86800.1; -; mRNA.
DR EMBL; AF190465; AAF04290.1; -; Genomic_DNA.
DR EMBL; AK299166; BAG61213.1; -; mRNA.
DR EMBL; AK097616; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC007292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001270; AAH01270.1; -; mRNA.
DR RefSeq; NP_001186872.1; NM_001199943.1.
DR RefSeq; NP_001186873.1; NM_001199944.1.
DR RefSeq; NP_003016.1; NM_003025.3.
DR UniGene; Hs.97616; -.
DR ProteinModelPortal; Q99961; -.
DR SMR; Q99961; 26-247, 305-368.
DR IntAct; Q99961; 23.
DR MINT; MINT-128645; -.
DR STRING; 9606.ENSP00000269886; -.
DR PhosphoSite; Q99961; -.
DR DMDM; 12643797; -.
DR OGP; Q99961; -.
DR PaxDb; Q99961; -.
DR PeptideAtlas; Q99961; -.
DR PRIDE; Q99961; -.
DR DNASU; 6455; -.
DR Ensembl; ENST00000269886; ENSP00000269886; ENSG00000141985.
DR Ensembl; ENST00000417295; ENSP00000404568; ENSG00000141985.
DR Ensembl; ENST00000598564; ENSP00000470792; ENSG00000141985.
DR GeneID; 6455; -.
DR KEGG; hsa:6455; -.
DR UCSC; uc010xig.2; human.
DR CTD; 6455; -.
DR GeneCards; GC19M004360; -.
DR HGNC; HGNC:10830; SH3GL1.
DR HPA; HPA021485; -.
DR MIM; 601768; gene.
DR neXtProt; NX_Q99961; -.
DR PharmGKB; PA35736; -.
DR eggNOG; NOG307129; -.
DR HOGENOM; HOG000231641; -.
DR HOVERGEN; HBG052866; -.
DR InParanoid; Q99961; -.
DR KO; K11247; -.
DR OMA; FRDLERK; -.
DR OrthoDB; EOG7G1V6H; -.
DR PhylomeDB; Q99961; -.
DR GeneWiki; SH3GL1; -.
DR GenomeRNAi; 6455; -.
DR NextBio; 25089; -.
DR PRO; PR:Q99961; -.
DR ArrayExpress; Q99961; -.
DR Bgee; Q99961; -.
DR CleanEx; HS_SH3GL1; -.
DR Genevestigator; Q99961; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR-dom.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell projection;
KW Chromosomal rearrangement; Coiled coil; Complete proteome; Cytoplasm;
KW Endocytosis; Endosome; Lipid-binding; Membrane; Phosphoprotein;
KW Proto-oncogene; Reference proteome; SH3 domain.
FT CHAIN 1 368 Endophilin-A2.
FT /FTId=PRO_0000146744.
FT DOMAIN 18 249 BAR.
FT DOMAIN 306 365 SH3.
FT REGION 1 21 Membrane-binding amphipathic helix (By
FT similarity).
FT REGION 60 87 Required for dimerization upon membrane
FT association (By similarity).
FT REGION 218 254 Interaction with ARC (By similarity).
FT COILED 145 250 Potential.
FT SITE 15 16 Breakpoint for translocation to form
FT KMT2A/MLL1-EEN oncogene.
FT MOD_RES 288 288 Phosphoserine.
FT MOD_RES 315 315 Phosphotyrosine (By similarity).
FT VAR_SEQ 63 110 Missing (in isoform 2).
FT /FTId=VSP_045837.
FT VAR_SEQ 80 143 Missing (in isoform 3).
FT /FTId=VSP_047037.
FT CONFLICT 316 316 D -> G (in Ref. 5; BAG61213).
SQ SEQUENCE 368 AA; 41490 MW; 6E5BE978BC955077 CRC64;
MSVAGLKKQF YKASQLVSEK VGGAEGTKLD DDFKEMEKKV DVTSKAVTEV LARTIEYLQP
NPASRAKLTM LNTVSKIRGQ VKNPGYPQSE GLLGECMIRH GKELGGESNF GDALLDAGES
MKRLAEVKDS LDIEVKQNFI DPLQNLCEKD LKEIQHHLKK LEGRRLDFDY KKKRQGKIPD
EELRQALEKF EESKEVAETS MHNLLETDIE QVSQLSALVD AQLDYHRQAV QILDELAEKL
KRRMREASSR PKREYKPKPR EPFDLGEPEQ SNGGFPCTTA PKIAASSSFR SSDKPIRTPS
RSMPPLDQPS CKALYDFEPE NDGELGFHEG DVITLTNQID ENWYEGMLDG QSGFFPLSYV
EVLVPLPQ
//
ID SH3G1_HUMAN Reviewed; 368 AA.
AC Q99961; B4DRA1; E7EVZ4; M0QZV5; Q99668;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Endophilin-A2;
DE AltName: Full=EEN fusion partner of MLL;
DE AltName: Full=Endophilin-2;
DE AltName: Full=Extra eleven-nineteen leukemia fusion gene protein;
DE Short=EEN;
DE AltName: Full=SH3 domain protein 2B;
DE AltName: Full=SH3 domain-containing GRB2-like protein 1;
GN Name=SH3GL1; Synonyms=CNSA1, SH3D2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=9169142; DOI=10.1006/geno.1997.4645;
RA Giachino C., Lantelme E., Lanzetti L., Saccone S., Della Valle G.,
RA Migone N.;
RT "A novel SH3-containing human gene family preferentially expressed in
RT the central nervous system.";
RL Genomics 41:427-434(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION.
RC TISSUE=Fetal brain;
RX PubMed=9122235; DOI=10.1073/pnas.94.6.2563;
RA So C.W., Caldas C., Liu M.-M., Chen S.-J., Huang Q.-H., Gu L.-J.,
RA Sham M.H., Wiedemann L.M., Chan L.C.;
RT "EEN encodes for a member of a new family of proteins containing an
RT Src homology 3 domain and is the third gene located on chromosome
RT 19p13 that fuses to MLL in human leukemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2563-2568(1997).
RN [3]
RP SEQUENCE REVISION.
RA So C.W., Caldas C., Liu M.-M., Chen S.-J., Huang Q.-H., Gu L.-J.,
RA Sham M.H., Wiedemann L.M., Chan L.C.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chen S., Xiong H., Dong H., Lin W., Zhang C., Fu G., Qi Z.,
RA Huang G.M.;
RT "Homo sapiens SH3-containing protein EEN gene.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH SYNJ1.
RX PubMed=10542231; DOI=10.1074/jbc.274.45.32001;
RA Cestra G., Castagnoli L., Dente L., Minenkova O., Petrelli A.,
RA Migone N., Hoffmueller U., Schneider-Mergener J., Cesareni G.;
RT "The SH3 domains of endophilin and amphiphysin bind to the proline-
RT rich region of synaptojanin 1 at distinct sites that display an
RT unconventional binding specificity.";
RL J. Biol. Chem. 274:32001-32007(1999).
RN [9]
RP INTERACTION WITH PDCD6IP.
RX PubMed=17350572; DOI=10.1016/j.cell.2007.01.035;
RA Fisher R.D., Chung H.Y., Zhai Q., Robinson H., Sundquist W.I.,
RA Hill C.P.;
RT "Structural and biochemical studies of ALIX/AIP1 and its role in
RT retrovirus budding.";
RL Cell 128:841-852(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP INTERACTION WITH BIN2, AND SUBCELLULAR LOCATION.
RX PubMed=23285027; DOI=10.1371/journal.pone.0052401;
RA Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J.,
RA Veprintsev D.B., Evans P.R., McMahon H.T.;
RT "Bin2 is a membrane sculpting N-BAR protein that influences leucocyte
RT podosomes, motility and phagocytosis.";
RL PLoS ONE 7:E52401-E52401(2012).
CC -!- FUNCTION: Implicated in endocytosis. May recruit other proteins to
CC membranes with high curvature (By similarity).
CC -!- SUBUNIT: Interacts with ARC (By similarity). Interacts with SYNJ1
CC and DNM1. Interacts with PDCD6IP. Interacts with BIN2.
CC -!- INTERACTION:
CC Self; NbExp=3; IntAct=EBI-697911, EBI-697911;
CC Q7L190:DPPA4; NbExp=5; IntAct=EBI-697911, EBI-710457;
CC Q9H788:SH2D4A; NbExp=3; IntAct=EBI-697911, EBI-747035;
CC Q99962:SH3GL2; NbExp=3; IntAct=EBI-697911, EBI-77938;
CC Q99963:SH3GL3; NbExp=4; IntAct=EBI-697911, EBI-473910;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Early endosome
CC membrane; Peripheral membrane protein (By similarity). Cell
CC projection, podosome. Note=Associated with postsynaptic endosomes
CC in hippocampal neurons (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99961-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99961-2; Sequence=VSP_045837;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q99961-3; Sequence=VSP_047037;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Higher expression in pancreas,
CC placenta, prostate, testis and uterus.
CC -!- DOMAIN: An N-terminal amphipathic helix, the BAR domain and a
CC second amphipathic helix inserted into helix 1 of the BAR domain
CC (N-BAR domain) induce membrane curvature and bind curved membranes
CC (By similarity).
CC -!- DISEASE: Note=In some cases of acute leukemia, a translocation
CC results in the formation of a KMT2A/MLL1-EEN fusion gene.
CC -!- SIMILARITY: Belongs to the endophilin family.
CC -!- SIMILARITY: Contains 1 BAR domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EEN.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X99656; CAA67970.1; -; mRNA.
DR EMBL; U65999; AAB86800.1; -; mRNA.
DR EMBL; AF190465; AAF04290.1; -; Genomic_DNA.
DR EMBL; AK299166; BAG61213.1; -; mRNA.
DR EMBL; AK097616; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC007292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001270; AAH01270.1; -; mRNA.
DR RefSeq; NP_001186872.1; NM_001199943.1.
DR RefSeq; NP_001186873.1; NM_001199944.1.
DR RefSeq; NP_003016.1; NM_003025.3.
DR UniGene; Hs.97616; -.
DR ProteinModelPortal; Q99961; -.
DR SMR; Q99961; 26-247, 305-368.
DR IntAct; Q99961; 23.
DR MINT; MINT-128645; -.
DR STRING; 9606.ENSP00000269886; -.
DR PhosphoSite; Q99961; -.
DR DMDM; 12643797; -.
DR OGP; Q99961; -.
DR PaxDb; Q99961; -.
DR PeptideAtlas; Q99961; -.
DR PRIDE; Q99961; -.
DR DNASU; 6455; -.
DR Ensembl; ENST00000269886; ENSP00000269886; ENSG00000141985.
DR Ensembl; ENST00000417295; ENSP00000404568; ENSG00000141985.
DR Ensembl; ENST00000598564; ENSP00000470792; ENSG00000141985.
DR GeneID; 6455; -.
DR KEGG; hsa:6455; -.
DR UCSC; uc010xig.2; human.
DR CTD; 6455; -.
DR GeneCards; GC19M004360; -.
DR HGNC; HGNC:10830; SH3GL1.
DR HPA; HPA021485; -.
DR MIM; 601768; gene.
DR neXtProt; NX_Q99961; -.
DR PharmGKB; PA35736; -.
DR eggNOG; NOG307129; -.
DR HOGENOM; HOG000231641; -.
DR HOVERGEN; HBG052866; -.
DR InParanoid; Q99961; -.
DR KO; K11247; -.
DR OMA; FRDLERK; -.
DR OrthoDB; EOG7G1V6H; -.
DR PhylomeDB; Q99961; -.
DR GeneWiki; SH3GL1; -.
DR GenomeRNAi; 6455; -.
DR NextBio; 25089; -.
DR PRO; PR:Q99961; -.
DR ArrayExpress; Q99961; -.
DR Bgee; Q99961; -.
DR CleanEx; HS_SH3GL1; -.
DR Genevestigator; Q99961; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR-dom.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell projection;
KW Chromosomal rearrangement; Coiled coil; Complete proteome; Cytoplasm;
KW Endocytosis; Endosome; Lipid-binding; Membrane; Phosphoprotein;
KW Proto-oncogene; Reference proteome; SH3 domain.
FT CHAIN 1 368 Endophilin-A2.
FT /FTId=PRO_0000146744.
FT DOMAIN 18 249 BAR.
FT DOMAIN 306 365 SH3.
FT REGION 1 21 Membrane-binding amphipathic helix (By
FT similarity).
FT REGION 60 87 Required for dimerization upon membrane
FT association (By similarity).
FT REGION 218 254 Interaction with ARC (By similarity).
FT COILED 145 250 Potential.
FT SITE 15 16 Breakpoint for translocation to form
FT KMT2A/MLL1-EEN oncogene.
FT MOD_RES 288 288 Phosphoserine.
FT MOD_RES 315 315 Phosphotyrosine (By similarity).
FT VAR_SEQ 63 110 Missing (in isoform 2).
FT /FTId=VSP_045837.
FT VAR_SEQ 80 143 Missing (in isoform 3).
FT /FTId=VSP_047037.
FT CONFLICT 316 316 D -> G (in Ref. 5; BAG61213).
SQ SEQUENCE 368 AA; 41490 MW; 6E5BE978BC955077 CRC64;
MSVAGLKKQF YKASQLVSEK VGGAEGTKLD DDFKEMEKKV DVTSKAVTEV LARTIEYLQP
NPASRAKLTM LNTVSKIRGQ VKNPGYPQSE GLLGECMIRH GKELGGESNF GDALLDAGES
MKRLAEVKDS LDIEVKQNFI DPLQNLCEKD LKEIQHHLKK LEGRRLDFDY KKKRQGKIPD
EELRQALEKF EESKEVAETS MHNLLETDIE QVSQLSALVD AQLDYHRQAV QILDELAEKL
KRRMREASSR PKREYKPKPR EPFDLGEPEQ SNGGFPCTTA PKIAASSSFR SSDKPIRTPS
RSMPPLDQPS CKALYDFEPE NDGELGFHEG DVITLTNQID ENWYEGMLDG QSGFFPLSYV
EVLVPLPQ
//
MIM
601768
*RECORD*
*FIELD* NO
601768
*FIELD* TI
*601768 SH3 DOMAIN, GRB2-LIKE, 1; SH3GL1
;;SH3p8;;
EXTRA ELEVEN-NINETEEN LEUKEMIA FUSION GENE; EEN;;
read moreEEN FUSION PARTNER OF MLL;;
ENDOPHILIN 2
EEN/MLL FUSION GENE, INCLUDED
*FIELD* TX
CLONING
The MLL gene (159555), the closest human homolog of the Drosophila
trithorax gene, undergoes chromosomal translocation with a large number
of different partner genes in both acute lymphoid and acute myeloid
leukemias. So et al. (1997) identified a novel partner gene, designated
EEN by them, that was fused to MLL in a case of acute myeloid leukemia.
Since no PCR products were amplified from the patient's DNA when
specific primers for 4 common MLL fusion partners were used, So et al.
(1997) inferred that MLL in this patient was fused to a novel partner
gene sequence. As all characterized MLL fusion genes previously
identified had been shown to retain the derivative chromosome 11, the
3-prime RACE (rapid amplification of cDNA ends) method was chosen to
isolate the fusion partner of MLL in the patient's leukemic cells. The
deduced EEN protein of 368 amino acids contains a central alpha-helical
region and a C-terminal Src homology 3 (SH3) domain most similar to the
C-terminal SH3 domain found in the GRB2 (108355) family of genes. EEN
was expressed in a variety of tissue types and encoded a protein of
approximately 46 kD. The EEN protein is the human homolog of a member of
a recently described murine SH3 domain-containing protein family. It is
also highly related to a putative gene identified in C. elegans.
GENE FUNCTION
By yeast 2-hybrid screening of a rat brain cDNA library using the C
termini of 3 different Ca(2+) channel subunits as bait, Chen et al.
(2003) found that the C terminus of CACNA1B (601012) interacted with
endophilin-2 in a calcium-dependent manner. Ca(2+) bound primarily to
endophilin-2. Introduction of a dominant-negative endophilin-2 construct
into hippocampal neurons significantly reduced endocytosis-mediated dye
uptake without abolishing exocytosis. Chen et al. (2003) proposed that
calcium channels play an important role in synaptic vesicle recycling by
directly coupling to both exocytotic and endocytic machinery.
MAPPING
Using a panel of somatic cell hybrids, Giachino et al. (1997) mapped the
SH3GL1 gene to chromosome 19. By radiation hybrid mapping and FISH, they
localized the gene to 19p13.3. By fluorescence in situ hybridization, So
et al. (1997) mapped the EEN gene to chromosome 19p13.
CYTOGENETICS
So et al. (1997) identified EEN as the fusion partner of MLL in a case
of acute myeloid leukemia. The patient was a 22-month-old female in whom
the diagnosis had been made on morphologic and cytochemical criteria.
Sequence analysis of the fusion MLL/EEN transcript revealed that exon 6
of MLL was fused to the N-terminal sequence of EEN, resulting in a
predicted chimeric protein that includes the major functional domain of
EEN.
*FIELD* RF
1. Chen, Y.; Deng, L.; Maeno-Hikichi, Y.; Lai, M.; Chang, S.; Chen,
G.; Zhang, J.: Formation of an endophilin-Ca(2+) channel complex
is critical for clathrin-mediated synaptic vesicle endocytosis. Cell 115:
37-48, 2003.
2. Giachino, C.; Lantelme, E.; Lanzetti, L.; Saccone, S.; Della Valle,
G.; Migone, N.: A novel SH3-containing human gene family preferentially
expressed in the central nervous system. Genomics 41: 427-434, 1997.
3. So, C. W.; Caldas, C.; Liu, M.-M.; Chen, S.-J.; Huang, Q.-H.; Gu,
L.-J.; Sham, M. H.; Wiedemann, L. M.; Chan, L. C.: EEN encodes for
a member of a new family of proteins containing an Src homology 3
domain and is the third gene located on chromosome 19p13 that fuses
to MLL in human leukemia. Proc. Nat. Acad. Sci. 94: 2563-2568, 1997.
*FIELD* CN
Paul J. Converse - updated: 06/20/2006
Patti M. Sherman - updated: 1/26/2000
*FIELD* CD
Victor A. McKusick: 4/21/1997
*FIELD* ED
mgross: 06/20/2006
mgross: 9/4/2003
mgross: 1/27/2000
psherman: 1/26/2000
carol: 9/20/1999
carol: 7/15/1999
carol: 12/16/1998
mark: 4/21/1997
*RECORD*
*FIELD* NO
601768
*FIELD* TI
*601768 SH3 DOMAIN, GRB2-LIKE, 1; SH3GL1
;;SH3p8;;
EXTRA ELEVEN-NINETEEN LEUKEMIA FUSION GENE; EEN;;
read moreEEN FUSION PARTNER OF MLL;;
ENDOPHILIN 2
EEN/MLL FUSION GENE, INCLUDED
*FIELD* TX
CLONING
The MLL gene (159555), the closest human homolog of the Drosophila
trithorax gene, undergoes chromosomal translocation with a large number
of different partner genes in both acute lymphoid and acute myeloid
leukemias. So et al. (1997) identified a novel partner gene, designated
EEN by them, that was fused to MLL in a case of acute myeloid leukemia.
Since no PCR products were amplified from the patient's DNA when
specific primers for 4 common MLL fusion partners were used, So et al.
(1997) inferred that MLL in this patient was fused to a novel partner
gene sequence. As all characterized MLL fusion genes previously
identified had been shown to retain the derivative chromosome 11, the
3-prime RACE (rapid amplification of cDNA ends) method was chosen to
isolate the fusion partner of MLL in the patient's leukemic cells. The
deduced EEN protein of 368 amino acids contains a central alpha-helical
region and a C-terminal Src homology 3 (SH3) domain most similar to the
C-terminal SH3 domain found in the GRB2 (108355) family of genes. EEN
was expressed in a variety of tissue types and encoded a protein of
approximately 46 kD. The EEN protein is the human homolog of a member of
a recently described murine SH3 domain-containing protein family. It is
also highly related to a putative gene identified in C. elegans.
GENE FUNCTION
By yeast 2-hybrid screening of a rat brain cDNA library using the C
termini of 3 different Ca(2+) channel subunits as bait, Chen et al.
(2003) found that the C terminus of CACNA1B (601012) interacted with
endophilin-2 in a calcium-dependent manner. Ca(2+) bound primarily to
endophilin-2. Introduction of a dominant-negative endophilin-2 construct
into hippocampal neurons significantly reduced endocytosis-mediated dye
uptake without abolishing exocytosis. Chen et al. (2003) proposed that
calcium channels play an important role in synaptic vesicle recycling by
directly coupling to both exocytotic and endocytic machinery.
MAPPING
Using a panel of somatic cell hybrids, Giachino et al. (1997) mapped the
SH3GL1 gene to chromosome 19. By radiation hybrid mapping and FISH, they
localized the gene to 19p13.3. By fluorescence in situ hybridization, So
et al. (1997) mapped the EEN gene to chromosome 19p13.
CYTOGENETICS
So et al. (1997) identified EEN as the fusion partner of MLL in a case
of acute myeloid leukemia. The patient was a 22-month-old female in whom
the diagnosis had been made on morphologic and cytochemical criteria.
Sequence analysis of the fusion MLL/EEN transcript revealed that exon 6
of MLL was fused to the N-terminal sequence of EEN, resulting in a
predicted chimeric protein that includes the major functional domain of
EEN.
*FIELD* RF
1. Chen, Y.; Deng, L.; Maeno-Hikichi, Y.; Lai, M.; Chang, S.; Chen,
G.; Zhang, J.: Formation of an endophilin-Ca(2+) channel complex
is critical for clathrin-mediated synaptic vesicle endocytosis. Cell 115:
37-48, 2003.
2. Giachino, C.; Lantelme, E.; Lanzetti, L.; Saccone, S.; Della Valle,
G.; Migone, N.: A novel SH3-containing human gene family preferentially
expressed in the central nervous system. Genomics 41: 427-434, 1997.
3. So, C. W.; Caldas, C.; Liu, M.-M.; Chen, S.-J.; Huang, Q.-H.; Gu,
L.-J.; Sham, M. H.; Wiedemann, L. M.; Chan, L. C.: EEN encodes for
a member of a new family of proteins containing an Src homology 3
domain and is the third gene located on chromosome 19p13 that fuses
to MLL in human leukemia. Proc. Nat. Acad. Sci. 94: 2563-2568, 1997.
*FIELD* CN
Paul J. Converse - updated: 06/20/2006
Patti M. Sherman - updated: 1/26/2000
*FIELD* CD
Victor A. McKusick: 4/21/1997
*FIELD* ED
mgross: 06/20/2006
mgross: 9/4/2003
mgross: 1/27/2000
psherman: 1/26/2000
carol: 9/20/1999
carol: 7/15/1999
carol: 12/16/1998
mark: 4/21/1997