DNMBP_MOUSE
ID DNMBP_MOUSE Reviewed; 1580 AA.
AC Q6TXD4; Q6ZQ05; Q8CEW8; Q8R0Y2;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Dynamin-binding protein {ECO:0000250|UniProtKB:Q6XZF7};
DE AltName: Full=Scaffold protein Tuba {ECO:0000305|PubMed:14506234};
GN Name=Dnmbp {ECO:0000312|MGI:MGI:1917352};
GN Synonyms=Kiaa1010 {ECO:0000303|PubMed:14621295},
GN Tuba {ECO:0000303|PubMed:14506234};
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), FUNCTION, ALTERNATIVE SPLICING,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ACTIN; TUBULIN; HSP70; DNM1 AND
RP A COMPLEX OF ACTIN-REGULATORY PROTEINS.
RC TISSUE=Embryo;
RX PubMed=14506234; DOI=10.1074/jbc.m308104200;
RA Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
RA Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.;
RT "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
RT domains, links dynamin to regulation of the actin cytoskeleton.";
RL J. Biol. Chem. 278:49031-49043(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 954-1318 (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 975-1580 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Testis;
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 -!- FUNCTION: Plays a critical role as a guanine nucleotide exchange factor
CC (GEF) for CDC42 in several intracellular processes associated with the
CC actin and microtubule cytoskeleton. Regulates the structure of apical
CC junctions in epithelial cells (By similarity). Participates in the
CC normal lumenogenesis of epithelial cell cysts by regulating spindle
CC orientation (By similarity). Plays a role in ciliogenesis (By
CC similarity). May play a role in membrane trafficking between the cell
CC surface and the Golgi (PubMed:14506234). {ECO:0000250|UniProtKB:E2RP94,
CC ECO:0000250|UniProtKB:Q6XZF7, ECO:0000269|PubMed:14506234}.
CC -!- SUBUNIT: Binds DNM1 via its N-terminal SH3 domains (PubMed:14506234).
CC The C-terminal SH3 domain binds a complex containing actin, tubulin,
CC Hsp70 and actin-regulatory proteins, such as ENAH, EVL, WIRE, CR16,
CC WAVE1 and NAP1L1 (PubMed:14506234). Interacts with FASLG (By
CC similarity). Interacts (via SH3 domain 6) with WASL (By similarity).
CC Interacts (via SH3 domain 6) interacts with ENAH (By similarity).
CC Interacts (via C-terminal domain) with TJP1; required for the apical
CC cell-cell junction localization of DNMBP (By similarity).
CC {ECO:0000250|UniProtKB:Q6XZF7, ECO:0000269|PubMed:14506234}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14506234}. Golgi
CC apparatus, Golgi stack {ECO:0000269|PubMed:14506234}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:14506234}. Synapse
CC {ECO:0000250|UniProtKB:M0R4F8}. Cell junction
CC {ECO:0000250|UniProtKB:Q6XZF7}. Note=Localizes to the apical junction,
CC colocalizes with TJP1. {ECO:0000250|UniProtKB:Q6XZF7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6TXD4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6TXD4-2; Sequence=VSP_012081, VSP_012082, VSP_012083;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25293.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC98071.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY383729; AAQ81299.1; -; mRNA.
DR EMBL; AK129261; BAC98071.1; ALT_INIT; mRNA.
DR EMBL; AK010367; BAC25293.1; ALT_FRAME; mRNA.
DR EMBL; BC025944; AAH25944.1; -; mRNA.
DR CCDS; CCDS29839.1; -. [Q6TXD4-1]
DR CCDS; CCDS84442.1; -. [Q6TXD4-2]
DR RefSeq; NP_001293017.1; NM_001306088.1.
DR RefSeq; NP_082305.1; NM_028029.4.
DR AlphaFoldDB; Q6TXD4; -.
DR SMR; Q6TXD4; -.
DR BioGRID; 215065; 13.
DR STRING; 10090.ENSMUSP00000026209; -.
DR iPTMnet; Q6TXD4; -.
DR PhosphoSitePlus; Q6TXD4; -.
DR jPOST; Q6TXD4; -.
DR MaxQB; Q6TXD4; -.
DR PaxDb; Q6TXD4; -.
DR PeptideAtlas; Q6TXD4; -.
DR PRIDE; Q6TXD4; -.
DR ProteomicsDB; 279747; -. [Q6TXD4-1]
DR ProteomicsDB; 279748; -. [Q6TXD4-2]
DR DNASU; 71972; -.
DR GeneID; 71972; -.
DR KEGG; mmu:71972; -.
DR UCSC; uc008hox.2; mouse. [Q6TXD4-2]
DR UCSC; uc033hkq.1; mouse. [Q6TXD4-1]
DR CTD; 23268; -.
DR MGI; MGI:1917352; Dnmbp.
DR eggNOG; KOG3519; Eukaryota.
DR eggNOG; KOG4225; Eukaryota.
DR InParanoid; Q6TXD4; -.
DR OrthoDB; 207472at2759; -.
DR PhylomeDB; Q6TXD4; -.
DR TreeFam; TF330015; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR BioGRID-ORCS; 71972; 1 hit in 57 CRISPR screens.
DR ChiTaRS; Dnmbp; mouse.
DR PRO; PR:Q6TXD4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6TXD4; protein.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11798; SH3_DNMBP_C1; 1.
DR CDD; cd11794; SH3_DNMBP_N1; 1.
DR CDD; cd11795; SH3_DNMBP_N2; 1.
DR CDD; cd11796; SH3_DNMBP_N3; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR035469; DNMBP.
DR InterPro; IPR035820; DNMBP_SH3_C1.
DR InterPro; IPR035817; DNMBP_SH3_N1.
DR InterPro; IPR035818; DNMBP_SH3_N2.
DR InterPro; IPR035819; DNMBP_SH3_N3.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR22834:SF19; PTHR22834:SF19; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 2.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 6.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 6.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50002; SH3; 6.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell junction; Coiled coil; Cytoplasm;
KW Cytoskeleton; Golgi apparatus; Guanine-nucleotide releasing factor;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Synapse.
FT CHAIN 1..1580
FT /note="Dynamin-binding protein"
FT /id="PRO_0000079960"
FT DOMAIN 2..61
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 66..127
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 146..205
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 244..303
FT /note="SH3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 783..970
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1011..1220
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 1288..1351
FT /note="SH3 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1516..1579
FT /note="SH3 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 211..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 694..755
FT /evidence="ECO:0000255"
FT COMPBIAS 304..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..654
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6XZF7"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6XZF7"
FT VAR_SEQ 1..753
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_012081"
FT VAR_SEQ 851..860
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_012082"
FT VAR_SEQ 910
FT /note="K -> KSLYHEW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_012083"
FT CONFLICT 1471
FT /note="S -> G (in Ref. 1; AAQ81299)"
FT /evidence="ECO:0000305"
FT CONFLICT 1485
FT /note="R -> Q (in Ref. 1; AAQ81299)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1580 AA; 177277 MW; CEB70B6459341C1F CRC64;
MEPGSMVRAI FDFCPSVSEE LPLFVGDVIE VLAVVDEFWL LGKKEDVTGQ FPSSFVEIVT
IPSLKEGERL FVCICEFVSR ELNSLSLHRG DLVILDDSAP TAGWLQGRSC WGAWGFFPSS
CVQELCLSSR SRRWHAQSAL LQAPEYSLGQ ARALMGLSAQ LDEELDFREG DLITIIGVPE
PGWFEGELEG RRGIFPEGFV ELLGPLRTVD ESVNSRSGDD SAVNGEVDVP PEEAESGGDE
DDQQSGTYGI ALYRFQALET NELDFEVGDR IQILGTLEDG WLEGCLKGKT GVFPHRFVKL
CPSNRTEETT AQPQESSFPK DSESSVGKSG DSVVEEARQE PWECEEERPD YDLPGQASVP
QDHVAPEWTG DTISGQDKDA SGSSPDVDLE RPLAKDLSTP DPSEEVNGVS SQPQVPIHPK
VQKSQHYLTA GGSHQTSDPF SELVPLEART RDYSSLPPRR TYAQGWSFQK PASHLQRASS
LTASRLDRPS HFCHPAMASY AQKHQTSTEN TASLHDPPER PERRPGLQDR GPATDITTAS
QGDSLDLDSK LTQQLIEFEK SLSGPSTEPE TIVRRFSIMD FYSEKDIVRG SSNSLPSQAF
PERRKTLRPP PPRPRTPTPI SSHLLVDQSP KPVPTLVVRP SRPAPLPPPA QQRMNTASPK
PTSCAHPGWE APEKEDSEHM EKSPAQTFPC PSMLARIRDV EQDLDTCTRA QEELNLLLEE
KQDDPSRAET LETLRSYEST IQSLTLELQQ LRDMTLLSSQ SSSLAAPFGS VSTENPEQRM
LEKRAKVVAE LLQTERDYIR DLEMCIERVM VPLQQAQVPN VDFEGLFGNM QTVIKVSKQL
LAALEISDAV GMSSCDCLVP GPVFLDHRDE LEGTYRVYCQ NHDEAISLLE MYEKDEKTQK
HLQDYLADLK GCTNYINLGS FLIKPVQRIM RYPLLLMELL NSTPESHPDK VPLTNAVLAV
KEINVNINEY KRRKDLVLKY RKGDEDSLME KISKLNIHSI IKKSSRVSSH LKHLTGFAPQ
LKDEVFEETE KNFRMQERLI KSFIRDLSLY LQHIRESACV KVVAAMSIWD LCMERGHHDL
EQFEKVHRYI SDQLFTRFKE RTERLVINPL NQLLNMFTGP YKLVQKRFDK LLDFYNCTER
AEKLKDKKTL EELQSARNNY EALNSQLLDE LPKFQQYAQS LFTNCIHGYA EAHCDFVQQA
LEQLQPLLSL LKATDREGNL IAIFLEEHSR VLQQLQVFTF FPESLPAPRK PFERKTTDRQ
SSRKTLLGMP SYMLQSEELR SSLLARYPPE KLFHVQRNFN AAQDLDVSLL EGDLVGVIKK
KDPMGSQNRW LVDNGVTKGF VYSSFLKPYN PRCSHSDASV ASHSSTESEH SGSSPGCHRQ
NSHSALTFNS NNMTVSFTSG LALTQPQDAS PLKDCAHETL AVSWNTGHPE TGPSTCSSDP
GFSCQRRLGN PADGARDISQ PASTLRGCQR SSPHSEVVGY SVPGRNDQGS DSIKGSARVC
QAPEDRDRGV GSSETEGNQV YFAIYTFKAR NPNELSVLAN QRLRIHEFKD VTGNTEWWLA
EVNGRKGYVP SNYIRKTEYT
