SHLB2_MOUSE
ID SHLB2_MOUSE Reviewed; 400 AA.
AC Q8R3V5; Q3TIQ1; Q3U2J4; Q3U824; Q8K140; Q91ZI7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Endophilin-B2;
DE AltName: Full=SH3 domain-containing GRB2-like protein B2;
GN Name=Sh3glb2; Synonyms=Kiaa1848;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Heart;
RA Chang N.-S., Doherty J., Schultz L.;
RT "TIAF1 physically interacts with SH3GLB2.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, DBA/2J, and NOD; TISSUE=Bone marrow, and Dendritic cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary gland;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBUNIT: Homodimer, and heterodimer with SH3GLB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2;
CC IsoId=Q8R3V5-4; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8R3V5-1; Sequence=VSP_028795;
CC Name=3;
CC IsoId=Q8R3V5-3; Sequence=VSP_009280;
CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH28859.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC98265.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF426314; AAL24820.1; -; mRNA.
DR EMBL; AK129455; BAC98265.2; ALT_INIT; Transcribed_RNA.
DR EMBL; AK152409; BAE31195.1; -; mRNA.
DR EMBL; AK155248; BAE33146.1; -; mRNA.
DR EMBL; AK167762; BAE39795.1; -; mRNA.
DR EMBL; AL954388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024477; AAH24477.1; -; mRNA.
DR EMBL; BC028859; AAH28859.1; ALT_SEQ; mRNA.
DR CCDS; CCDS15879.1; -. [Q8R3V5-1]
DR CCDS; CCDS71020.1; -. [Q8R3V5-4]
DR RefSeq; NP_001276638.1; NM_001289709.1. [Q8R3V5-4]
DR RefSeq; NP_647463.1; NM_139302.2. [Q8R3V5-1]
DR RefSeq; XP_006498002.1; XM_006497939.1. [Q8R3V5-3]
DR AlphaFoldDB; Q8R3V5; -.
DR SMR; Q8R3V5; -.
DR BioGRID; 230668; 23.
DR IntAct; Q8R3V5; 1.
DR STRING; 10090.ENSMUSP00000028214; -.
DR iPTMnet; Q8R3V5; -.
DR PhosphoSitePlus; Q8R3V5; -.
DR REPRODUCTION-2DPAGE; Q8R3V5; -.
DR MaxQB; Q8R3V5; -.
DR PaxDb; Q8R3V5; -.
DR PeptideAtlas; Q8R3V5; -.
DR PRIDE; Q8R3V5; -.
DR ProteomicsDB; 255411; -. [Q8R3V5-4]
DR ProteomicsDB; 255412; -. [Q8R3V5-1]
DR ProteomicsDB; 255413; -. [Q8R3V5-3]
DR Antibodypedia; 17774; 149 antibodies from 24 providers.
DR DNASU; 227700; -.
DR Ensembl; ENSMUST00000028214; ENSMUSP00000028214; ENSMUSG00000026860. [Q8R3V5-1]
DR Ensembl; ENSMUST00000100215; ENSMUSP00000097788; ENSMUSG00000026860. [Q8R3V5-4]
DR Ensembl; ENSMUST00000163668; ENSMUSP00000131545; ENSMUSG00000026860. [Q8R3V5-3]
DR GeneID; 227700; -.
DR KEGG; mmu:227700; -.
DR UCSC; uc008jcc.2; mouse. [Q8R3V5-1]
DR UCSC; uc008jcd.2; mouse. [Q8R3V5-4]
DR CTD; 56904; -.
DR MGI; MGI:2385131; Sh3glb2.
DR VEuPathDB; HostDB:ENSMUSG00000026860; -.
DR eggNOG; KOG3725; Eukaryota.
DR GeneTree; ENSGT00940000155841; -.
DR HOGENOM; CLU_043817_1_1_1; -.
DR InParanoid; Q8R3V5; -.
DR OMA; TMSFRGS; -.
DR PhylomeDB; Q8R3V5; -.
DR TreeFam; TF313281; -.
DR BioGRID-ORCS; 227700; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Sh3glb2; mouse.
DR PRO; PR:Q8R3V5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8R3V5; protein.
DR Bgee; ENSMUSG00000026860; Expressed in superior frontal gyrus and 258 other tissues.
DR ExpressionAtlas; Q8R3V5; baseline and differential.
DR Genevisible; Q8R3V5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR CDD; cd11944; SH3_Endophilin_B2; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR035640; Endophilin_B2_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..400
FT /note="Endophilin-B2"
FT /id="PRO_0000146756"
FT DOMAIN 24..287
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 340..400
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..27
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000250"
FT COILED 205..234
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR46"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR46"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PPJ9"
FT VAR_SEQ 188..208
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009280"
FT VAR_SEQ 280..285
FT /note="SSQGAI -> R (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|Ref.1"
FT /id="VSP_028795"
FT CONFLICT 7
FT /note="K -> N (in Ref. 1; AAL24820)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="L -> M (in Ref. 4; BAE31195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 44503 MW; 0614F451F4B4370F CRC64;
MDFNMKKLAS DAGIFFTRAV QFTEEKFGQA EKTELDAHFE NLLARADSTK NWTERILRQT
EVLLQPNPSA RVEEFLYEKL DRKVPSRVTN GELLAQYMAE AASELGPSTP YGKTLIKVSE
AEKRLGAAER DFIHTASLSF LTPLRNFLEG DWKTISKERR LLQNRRLDLD ACKARLKKAK
AAEAKATTVP DFQETRPRNY ILSASASALW NDEVDKAEQE LRVAQTEFDR QAEVTRLLLE
GISSTHVNHL RCLHEFVKSQ TTYYAQCYRH MLDLQKQLGS SQGAIFPGTF VGTTEPASPP
LSSTSPTTTA ATMPVVPTGA VLAPPEEAAL CLEEVAPPAS GTRKARVLYD YEAADSSELA
LLADELITVY SLPGMDPDWL IGERGNKKGK VPVTYLELLS
