Full text data of SH3GLB2
SH3GLB2
(KIAA1848)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Endophilin-B2 (SH3 domain-containing GRB2-like protein B2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Endophilin-B2 (SH3 domain-containing GRB2-like protein B2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NR46
ID SHLB2_HUMAN Reviewed; 395 AA.
AC Q9NR46; A6NC47; A8MPS4; Q8WY61; Q96JH9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=Endophilin-B2;
DE AltName: Full=SH3 domain-containing GRB2-like protein B2;
GN Name=SH3GLB2; Synonyms=KIAA1848; ORFNames=PP578;
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), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, HOMODIMERIZATION, AND INTERACTION WITH SH3GLB1.
RC TISSUE=Adipocyte, and Skeletal muscle;
RX PubMed=11161816; DOI=10.1006/geno.2000.6378;
RA Pierrat B., Simonen M., Cueto M., Mestan J., Ferrigno P., Heim J.;
RT "SH3GLB, a new endophilin-related protein family featuring an SH3
RT domain.";
RL Genomics 71:222-234(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- SUBUNIT: Homodimer, and heterodimer with SH3GLB1.
CC -!- INTERACTION:
CC Q9Y371:SH3GLB1; NbExp=5; IntAct=EBI-749607, EBI-2623095;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NR46-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NR46-2; Sequence=VSP_009278, VSP_009279;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle, adipocyte, brain,
CC lung, colon and mammary gland.
CC -!- SIMILARITY: Belongs to the endophilin family.
CC -!- SIMILARITY: Contains 1 BAR domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23792.1; Type=Frameshift; Positions=122, 128;
CC Sequence=BAB47477.2; Type=Erroneous initiation;
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; AF257319; AAF81226.1; -; mRNA.
DR EMBL; AB058751; BAB47477.2; ALT_INIT; mRNA.
DR EMBL; AF258589; AAG23792.1; ALT_FRAME; mRNA.
DR EMBL; AL592211; CAI12365.1; -; Genomic_DNA.
DR EMBL; AL592211; CAI12366.1; -; Genomic_DNA.
DR EMBL; BC014635; AAH14635.1; -; mRNA.
DR RefSeq; NP_064530.1; NM_020145.2.
DR RefSeq; XP_005252154.1; XM_005252097.1.
DR RefSeq; XP_005252156.1; XM_005252099.1.
DR RefSeq; XP_005252158.1; XM_005252101.1.
DR UniGene; Hs.460238; -.
DR ProteinModelPortal; Q9NR46; -.
DR SMR; Q9NR46; 18-232, 334-395.
DR IntAct; Q9NR46; 15.
DR MINT; MINT-1458485; -.
DR STRING; 9606.ENSP00000361640; -.
DR PhosphoSite; Q9NR46; -.
DR DMDM; 41018150; -.
DR PaxDb; Q9NR46; -.
DR PRIDE; Q9NR46; -.
DR DNASU; 56904; -.
DR Ensembl; ENST00000372554; ENSP00000361634; ENSG00000148341.
DR Ensembl; ENST00000372559; ENSP00000361640; ENSG00000148341.
DR Ensembl; ENST00000372564; ENSP00000361645; ENSG00000148341.
DR GeneID; 56904; -.
DR KEGG; hsa:56904; -.
DR UCSC; uc004bwv.3; human.
DR CTD; 56904; -.
DR GeneCards; GC09M131769; -.
DR H-InvDB; HIX0008444; -.
DR HGNC; HGNC:10834; SH3GLB2.
DR HPA; HPA021438; -.
DR HPA; HPA024734; -.
DR MIM; 609288; gene.
DR neXtProt; NX_Q9NR46; -.
DR PharmGKB; PA35740; -.
DR eggNOG; NOG309804; -.
DR HOGENOM; HOG000232056; -.
DR HOVERGEN; HBG054448; -.
DR KO; K11248; -.
DR OMA; HTASINF; -.
DR OrthoDB; EOG744T9N; -.
DR GeneWiki; SH3GLB2; -.
DR GenomeRNAi; 56904; -.
DR NextBio; 62367; -.
DR PRO; PR:Q9NR46; -.
DR ArrayExpress; Q9NR46; -.
DR Bgee; Q9NR46; -.
DR CleanEx; HS_SH3GLB2; -.
DR Genevestigator; Q9NR46; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR Gene3D; 1.20.1270.60; -; 2.
DR InterPro; IPR027267; AH/BAR-dom.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028500; SH3GLB2.
DR PANTHER; PTHR10661:SF14; PTHR10661:SF14; 1.
DR Pfam; PF03114; BAR; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Polymorphism; Reference proteome; SH3 domain.
FT CHAIN 1 395 Endophilin-B2.
FT /FTId=PRO_0000146755.
FT DOMAIN 24 287 BAR.
FT DOMAIN 335 395 SH3.
FT REGION 1 27 Membrane-binding amphipathic helix (By
FT similarity).
FT COILED 116 132 Potential.
FT COILED 206 240 Potential.
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 187 187 T -> TCEGD (in isoform 2).
FT /FTId=VSP_009278.
FT VAR_SEQ 280 280 R -> SSQGAI (in isoform 2).
FT /FTId=VSP_009279.
FT VARIANT 305 305 A -> V (in dbSNP:rs17455482).
FT /FTId=VAR_053078.
FT VARIANT 319 319 P -> L (in dbSNP:rs17455475).
FT /FTId=VAR_053079.
SQ SEQUENCE 395 AA; 43974 MW; 5549631DB2EB7CAA CRC64;
MDFNMKKLAS DAGIFFTRAV QFTEEKFGQA EKTELDAHFE NLLARADSTK NWTEKILRQT
EVLLQPNPSA RVEEFLYEKL DRKVPSRVTN GELLAQYMAD AASELGPTTP YGKTLIKVAE
AEKQLGAAER DFIHTASISF LTPLRNFLEG DWKTISKERR LLQNRRLDLD ACKARLKKAK
AAEAKATTVP DFQETRPRNY ILSASASALW NDEVDKAEQE LRVAQTEFDR QAEVTRLLLE
GISSTHVNHL RCLHEFVKSQ TTYYAQCYRH MLDLQKQLGR FPGTFVGTTE PASPPLSSTS
PTTAAATMPV VPSVASLAPP GEASLCLEEV APPASGTRKA RVLYDYEAAD SSELALLADE
LITVYSLPGM DPDWLIGERG NKKGKVPVTY LELLS
//
ID SHLB2_HUMAN Reviewed; 395 AA.
AC Q9NR46; A6NC47; A8MPS4; Q8WY61; Q96JH9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=Endophilin-B2;
DE AltName: Full=SH3 domain-containing GRB2-like protein B2;
GN Name=SH3GLB2; Synonyms=KIAA1848; ORFNames=PP578;
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), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, HOMODIMERIZATION, AND INTERACTION WITH SH3GLB1.
RC TISSUE=Adipocyte, and Skeletal muscle;
RX PubMed=11161816; DOI=10.1006/geno.2000.6378;
RA Pierrat B., Simonen M., Cueto M., Mestan J., Ferrigno P., Heim J.;
RT "SH3GLB, a new endophilin-related protein family featuring an SH3
RT domain.";
RL Genomics 71:222-234(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- SUBUNIT: Homodimer, and heterodimer with SH3GLB1.
CC -!- INTERACTION:
CC Q9Y371:SH3GLB1; NbExp=5; IntAct=EBI-749607, EBI-2623095;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NR46-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NR46-2; Sequence=VSP_009278, VSP_009279;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle, adipocyte, brain,
CC lung, colon and mammary gland.
CC -!- SIMILARITY: Belongs to the endophilin family.
CC -!- SIMILARITY: Contains 1 BAR domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23792.1; Type=Frameshift; Positions=122, 128;
CC Sequence=BAB47477.2; Type=Erroneous initiation;
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; AF257319; AAF81226.1; -; mRNA.
DR EMBL; AB058751; BAB47477.2; ALT_INIT; mRNA.
DR EMBL; AF258589; AAG23792.1; ALT_FRAME; mRNA.
DR EMBL; AL592211; CAI12365.1; -; Genomic_DNA.
DR EMBL; AL592211; CAI12366.1; -; Genomic_DNA.
DR EMBL; BC014635; AAH14635.1; -; mRNA.
DR RefSeq; NP_064530.1; NM_020145.2.
DR RefSeq; XP_005252154.1; XM_005252097.1.
DR RefSeq; XP_005252156.1; XM_005252099.1.
DR RefSeq; XP_005252158.1; XM_005252101.1.
DR UniGene; Hs.460238; -.
DR ProteinModelPortal; Q9NR46; -.
DR SMR; Q9NR46; 18-232, 334-395.
DR IntAct; Q9NR46; 15.
DR MINT; MINT-1458485; -.
DR STRING; 9606.ENSP00000361640; -.
DR PhosphoSite; Q9NR46; -.
DR DMDM; 41018150; -.
DR PaxDb; Q9NR46; -.
DR PRIDE; Q9NR46; -.
DR DNASU; 56904; -.
DR Ensembl; ENST00000372554; ENSP00000361634; ENSG00000148341.
DR Ensembl; ENST00000372559; ENSP00000361640; ENSG00000148341.
DR Ensembl; ENST00000372564; ENSP00000361645; ENSG00000148341.
DR GeneID; 56904; -.
DR KEGG; hsa:56904; -.
DR UCSC; uc004bwv.3; human.
DR CTD; 56904; -.
DR GeneCards; GC09M131769; -.
DR H-InvDB; HIX0008444; -.
DR HGNC; HGNC:10834; SH3GLB2.
DR HPA; HPA021438; -.
DR HPA; HPA024734; -.
DR MIM; 609288; gene.
DR neXtProt; NX_Q9NR46; -.
DR PharmGKB; PA35740; -.
DR eggNOG; NOG309804; -.
DR HOGENOM; HOG000232056; -.
DR HOVERGEN; HBG054448; -.
DR KO; K11248; -.
DR OMA; HTASINF; -.
DR OrthoDB; EOG744T9N; -.
DR GeneWiki; SH3GLB2; -.
DR GenomeRNAi; 56904; -.
DR NextBio; 62367; -.
DR PRO; PR:Q9NR46; -.
DR ArrayExpress; Q9NR46; -.
DR Bgee; Q9NR46; -.
DR CleanEx; HS_SH3GLB2; -.
DR Genevestigator; Q9NR46; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR Gene3D; 1.20.1270.60; -; 2.
DR InterPro; IPR027267; AH/BAR-dom.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028500; SH3GLB2.
DR PANTHER; PTHR10661:SF14; PTHR10661:SF14; 1.
DR Pfam; PF03114; BAR; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Polymorphism; Reference proteome; SH3 domain.
FT CHAIN 1 395 Endophilin-B2.
FT /FTId=PRO_0000146755.
FT DOMAIN 24 287 BAR.
FT DOMAIN 335 395 SH3.
FT REGION 1 27 Membrane-binding amphipathic helix (By
FT similarity).
FT COILED 116 132 Potential.
FT COILED 206 240 Potential.
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 187 187 T -> TCEGD (in isoform 2).
FT /FTId=VSP_009278.
FT VAR_SEQ 280 280 R -> SSQGAI (in isoform 2).
FT /FTId=VSP_009279.
FT VARIANT 305 305 A -> V (in dbSNP:rs17455482).
FT /FTId=VAR_053078.
FT VARIANT 319 319 P -> L (in dbSNP:rs17455475).
FT /FTId=VAR_053079.
SQ SEQUENCE 395 AA; 43974 MW; 5549631DB2EB7CAA CRC64;
MDFNMKKLAS DAGIFFTRAV QFTEEKFGQA EKTELDAHFE NLLARADSTK NWTEKILRQT
EVLLQPNPSA RVEEFLYEKL DRKVPSRVTN GELLAQYMAD AASELGPTTP YGKTLIKVAE
AEKQLGAAER DFIHTASISF LTPLRNFLEG DWKTISKERR LLQNRRLDLD ACKARLKKAK
AAEAKATTVP DFQETRPRNY ILSASASALW NDEVDKAEQE LRVAQTEFDR QAEVTRLLLE
GISSTHVNHL RCLHEFVKSQ TTYYAQCYRH MLDLQKQLGR FPGTFVGTTE PASPPLSSTS
PTTAAATMPV VPSVASLAPP GEASLCLEEV APPASGTRKA RVLYDYEAAD SSELALLADE
LITVYSLPGM DPDWLIGERG NKKGKVPVTY LELLS
//
MIM
609288
*RECORD*
*FIELD* NO
609288
*FIELD* TI
*609288 SH3 DOMAIN, GRB2-LIKE, ENDOPHILIN B2; SH3GLB2
;;ENDOPHILIN B2;;
KIAA1848
*FIELD* TX
read more
CLONING
Using SH3GLB1 (609287) as bait in a yeast 2-hybrid screen of skeletal
muscle and adipocyte cDNA libraries, Pierrat et al. (2001) cloned
SH3GLB2. The deduced 395-amino acid protein contains an N-terminal
domain, a central coiled-coil region, and a C-terminal SH3 domain.
SH3GLB2 shares 65% amino acid identity with SH3GLB1, but it has a
23-amino acid extension following the coiled-coil region that is not
present in SH3GLB1. RT-PCR and EST database analysis indicated that
SH3GLB2 is expressed in many tissues, including skeletal muscle,
adipocytes, brain, lung, colon, and mammary gland. SH3GLB2 was expressed
in the cytoplasm of transfected HeLa cells and was excluded from nuclei.
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Nagase et al. (2001) cloned SH3GLB2, which they designated
KIAA1848. The deduced protein contains 378 amino acids. RT-PCR ELISA
detected highest expression in adult and fetal brain, adult lung, ovary,
and spinal cord, and in all specific brain regions examined.
Intermediate expression was detected in all other tissues examined.
GENE FUNCTION
By Western blot analysis, Pierrat et al. (2001) confirmed that SH3GLB2
could form homodimers and heterodimers with SH3GLB1 in vitro. Mutation
analysis indicated that the core coiled-coil region was required for the
formation of SH3GLB homodimers and heterodimers, but the SH3 domain was
not.
MAPPING
By analysis of a human-rodent hybrid panel, Nagase et al. (2001) mapped
the SH3GLB2 gene to chromosome 9.
*FIELD* RF
1. Nagase, T.; Nakayama, M.; Nakajima, D.; Kikuno, R.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 8: 85-95, 2001.
2. Pierrat, B.; Simonen, M.; Cueto, M.; Mestan, J.; Ferrigno, P.;
Heim, J.: SH3GLB, a new endophilin-related protein family featuring
an SH3 domain. Genomics 71: 222-234, 2001.
*FIELD* CD
Patricia A. Hartz: 3/31/2005
*FIELD* ED
mgross: 03/31/2005
*RECORD*
*FIELD* NO
609288
*FIELD* TI
*609288 SH3 DOMAIN, GRB2-LIKE, ENDOPHILIN B2; SH3GLB2
;;ENDOPHILIN B2;;
KIAA1848
*FIELD* TX
read more
CLONING
Using SH3GLB1 (609287) as bait in a yeast 2-hybrid screen of skeletal
muscle and adipocyte cDNA libraries, Pierrat et al. (2001) cloned
SH3GLB2. The deduced 395-amino acid protein contains an N-terminal
domain, a central coiled-coil region, and a C-terminal SH3 domain.
SH3GLB2 shares 65% amino acid identity with SH3GLB1, but it has a
23-amino acid extension following the coiled-coil region that is not
present in SH3GLB1. RT-PCR and EST database analysis indicated that
SH3GLB2 is expressed in many tissues, including skeletal muscle,
adipocytes, brain, lung, colon, and mammary gland. SH3GLB2 was expressed
in the cytoplasm of transfected HeLa cells and was excluded from nuclei.
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Nagase et al. (2001) cloned SH3GLB2, which they designated
KIAA1848. The deduced protein contains 378 amino acids. RT-PCR ELISA
detected highest expression in adult and fetal brain, adult lung, ovary,
and spinal cord, and in all specific brain regions examined.
Intermediate expression was detected in all other tissues examined.
GENE FUNCTION
By Western blot analysis, Pierrat et al. (2001) confirmed that SH3GLB2
could form homodimers and heterodimers with SH3GLB1 in vitro. Mutation
analysis indicated that the core coiled-coil region was required for the
formation of SH3GLB homodimers and heterodimers, but the SH3 domain was
not.
MAPPING
By analysis of a human-rodent hybrid panel, Nagase et al. (2001) mapped
the SH3GLB2 gene to chromosome 9.
*FIELD* RF
1. Nagase, T.; Nakayama, M.; Nakajima, D.; Kikuno, R.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 8: 85-95, 2001.
2. Pierrat, B.; Simonen, M.; Cueto, M.; Mestan, J.; Ferrigno, P.;
Heim, J.: SH3GLB, a new endophilin-related protein family featuring
an SH3 domain. Genomics 71: 222-234, 2001.
*FIELD* CD
Patricia A. Hartz: 3/31/2005
*FIELD* ED
mgross: 03/31/2005