DTNB_HUMAN
ID DTNB_HUMAN Reviewed; 627 AA.
AC O60941; B7Z733; F5GZG4; G5E9F6; O43782; O60881; O75538; Q86VR4; Q96AW0;
AC Q9UE14; Q9UE15; Q9UE16;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Dystrobrevin beta {ECO:0000305};
DE Short=DTN-B {ECO:0000303|PubMed:9540997};
DE AltName: Full=Beta-dystrobrevin {ECO:0000303|PubMed:9395493};
GN Name=DTNB {ECO:0000312|HGNC:HGNC:3058};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9395493; DOI=10.1074/jbc.272.50.31561;
RA Peters M.F., O'Brien K.F., Sadoulet-Puccio H.M., Kunkel L.M., Adams M.E.,
RA Froehner S.C.;
RT "Beta-dystrobrevin, a new member of the dystrophin family. Identification,
RT cloning, and protein associations.";
RL J. Biol. Chem. 272:31561-31569(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Skeletal muscle;
RX PubMed=9540997; DOI=10.1016/s0014-5793(98)00097-0;
RA Puca A.A., Piluso V.N.G., Belsito A., Sampaolo S., Quaderi N., Rossi E.,
RA Di Iorio G., Ballabio A., Franco B.;
RT "Identification and characterization of a novel member of the dystrobrevin
RT gene family.";
RL FEBS Lett. 425:7-13(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Synovium;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7), AND VARIANTS
RP HIS-97 AND THR-116.
RC TISSUE=Brain, and Eye;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 200-627 (ISOFORM 4).
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP INTERACTION WITH SNTG1 AND SNTG2.
RX PubMed=10747910; DOI=10.1074/jbc.m000439200;
RA Piluso G., Mirabella M., Ricci E., Belsito A., Abbondanza C., Servidei S.,
RA Puca A.A., Tonali P., Puca G.A., Nigro V.;
RT "Gamma1- and gamma2-syntrophins, two novel dystrophin-binding proteins
RT localized in neuronal cells.";
RL J. Biol. Chem. 275:15851-15860(2000).
RN [10]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP ACETYLATION AT MET-1.
RX PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
RA Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I.,
RA Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S.,
RA Ziegler M., Niere M., Gevaert K., Arnesen T.;
RT "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
RT termini of transmembrane proteins and maintains Golgi integrity.";
RL Cell Rep. 10:1362-1374(2015).
RN [16]
RP INDUCTION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27223470; DOI=10.1371/journal.pone.0156325;
RA Quaranta M.T., Spinello I., Paolillo R., Macchia G., Boe A., Ceccarini M.,
RA Labbaye C., Macioce P.;
RT "Identification of beta-Dystrobrevin as a Direct Target of miR-143:
RT Involvement in Early Stages of Neural Differentiation.";
RL PLoS ONE 11:e0156325-e0156325(2016).
CC -!- FUNCTION: Scaffolding protein that assembles DMD and SNTA1 molecules to
CC the basal membrane of kidney cells and liver sinusoids (By similarity).
CC May function as a repressor of the SYN1 promoter through the binding of
CC repressor element-1 (RE-1), in turn regulates SYN1 expression and may
CC be involved in cell proliferation regulation during the early phase of
CC neural differentiation (PubMed:27223470). May be required for proper
CC maturation and function of a subset of inhibitory synapses (By
CC similarity). {ECO:0000250|UniProtKB:O70585,
CC ECO:0000269|PubMed:27223470}.
CC -!- SUBUNIT: Interacts with dystrophin short form DP71 and syntrophins
CC SNTG1 and SNTG2 (PubMed:10747910). Binds DTNBP1. Forms a specific
CC complex composed of DMD, SNTB2 and SNTA1 in neuron; the interaction
CC with SNTB2 and SNTA1 is DMD independent. Interacts with UTRN and
CC dystrophin short form DP71 in the kidney and liver. Interacts with
CC SNTB1, SNTB2 and SNTA1 in kidney and liver. Interacts with KIF5A.
CC Interacts with HMG20A and HMG20B. Interacts with OLFM1. Interacts with
CC PRKAR2B and PRKAR1A (By similarity). {ECO:0000250|UniProtKB:O70585,
CC ECO:0000269|PubMed:10747910}.
CC -!- INTERACTION:
CC O60941; Q9NYB9: ABI2; NbExp=6; IntAct=EBI-740402, EBI-743598;
CC O60941; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-740402, EBI-742038;
CC O60941; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-740402, EBI-747776;
CC O60941; Q96MT8: CEP63; NbExp=5; IntAct=EBI-740402, EBI-741977;
CC O60941; Q9UBT7: CTNNAL1; NbExp=2; IntAct=EBI-740402, EBI-514206;
CC O60941; P11532: DMD; NbExp=4; IntAct=EBI-740402, EBI-295827;
CC O60941; Q96EV8: DTNBP1; NbExp=3; IntAct=EBI-740402, EBI-465804;
CC O60941; Q9UJY5: GGA1; NbExp=4; IntAct=EBI-740402, EBI-447141;
CC O60941; V9HW80: HEL-S-70; NbExp=3; IntAct=EBI-740402, EBI-10175326;
CC O60941; Q9NP66: HMG20A; NbExp=4; IntAct=EBI-740402, EBI-740641;
CC O60941; Q15323: KRT31; NbExp=3; IntAct=EBI-740402, EBI-948001;
CC O60941; Q6A162: KRT40; NbExp=3; IntAct=EBI-740402, EBI-10171697;
CC O60941; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-740402, EBI-742948;
CC O60941; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-740402, EBI-928842;
CC O60941; P37198: NUP62; NbExp=5; IntAct=EBI-740402, EBI-347978;
CC O60941; Q13136: PPFIA1; NbExp=6; IntAct=EBI-740402, EBI-745426;
CC O60941; Q9BXG8: SPZ1; NbExp=4; IntAct=EBI-740402, EBI-8483734;
CC O60941; Q12933: TRAF2; NbExp=5; IntAct=EBI-740402, EBI-355744;
CC O60941; P40222: TXLNA; NbExp=5; IntAct=EBI-740402, EBI-359793;
CC O60941; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-740402, EBI-739895;
CC O60941; Q96C00: ZBTB9; NbExp=5; IntAct=EBI-740402, EBI-395708;
CC O60941-5; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-11984733, EBI-11743294;
CC O60941-5; Q9NYB9-2: ABI2; NbExp=5; IntAct=EBI-11984733, EBI-11096309;
CC O60941-5; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-11984733, EBI-746752;
CC O60941-5; Q9BUH8: BEGAIN; NbExp=3; IntAct=EBI-11984733, EBI-742722;
CC O60941-5; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-11984733, EBI-11524851;
CC O60941-5; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-11984733, EBI-10181422;
CC O60941-5; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-11984733, EBI-347573;
CC O60941-5; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-11984733, EBI-10175300;
CC O60941-5; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-11984733, EBI-747776;
CC O60941-5; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-11984733, EBI-11522539;
CC O60941-5; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-11984733, EBI-3866319;
CC O60941-5; P56545-3: CTBP2; NbExp=5; IntAct=EBI-11984733, EBI-10171902;
CC O60941-5; Q05D60: DEUP1; NbExp=3; IntAct=EBI-11984733, EBI-748597;
CC O60941-5; P11532: DMD; NbExp=3; IntAct=EBI-11984733, EBI-295827;
CC O60941-5; Q96KS9: FAM167A; NbExp=3; IntAct=EBI-11984733, EBI-10290462;
CC O60941-5; A1L4K1: FSD2; NbExp=3; IntAct=EBI-11984733, EBI-5661036;
CC O60941-5; Q9UJY5-4: GGA1; NbExp=3; IntAct=EBI-11984733, EBI-12108696;
CC O60941-5; Q9NP66: HMG20A; NbExp=4; IntAct=EBI-11984733, EBI-740641;
CC O60941-5; Q2T9L4: INSYN1; NbExp=3; IntAct=EBI-11984733, EBI-4311436;
CC O60941-5; P19012: KRT15; NbExp=3; IntAct=EBI-11984733, EBI-739566;
CC O60941-5; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-11984733, EBI-3044087;
CC O60941-5; Q15323: KRT31; NbExp=3; IntAct=EBI-11984733, EBI-948001;
CC O60941-5; Q14525: KRT33B; NbExp=3; IntAct=EBI-11984733, EBI-1049638;
CC O60941-5; Q92764: KRT35; NbExp=3; IntAct=EBI-11984733, EBI-1058674;
CC O60941-5; O76015: KRT38; NbExp=3; IntAct=EBI-11984733, EBI-1047263;
CC O60941-5; Q96LR2: LURAP1; NbExp=5; IntAct=EBI-11984733, EBI-741355;
CC O60941-5; Q8IYB1: MB21D2; NbExp=3; IntAct=EBI-11984733, EBI-11323212;
CC O60941-5; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-11984733, EBI-11522433;
CC O60941-5; P37198: NUP62; NbExp=3; IntAct=EBI-11984733, EBI-347978;
CC O60941-5; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-11984733, EBI-79165;
CC O60941-5; P78424: POU6F2; NbExp=3; IntAct=EBI-11984733, EBI-12029004;
CC O60941-5; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-11984733, EBI-1105153;
CC O60941-5; P31321: PRKAR1B; NbExp=3; IntAct=EBI-11984733, EBI-2805516;
CC O60941-5; Q9NY99-2: SNTG2; NbExp=3; IntAct=EBI-11984733, EBI-18173613;
CC O60941-5; Q9BXG8: SPZ1; NbExp=5; IntAct=EBI-11984733, EBI-8483734;
CC O60941-5; Q9BWW4: SSBP3; NbExp=3; IntAct=EBI-11984733, EBI-2902395;
CC O60941-5; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-11984733, EBI-1105213;
CC O60941-5; Q12933: TRAF2; NbExp=3; IntAct=EBI-11984733, EBI-355744;
CC O60941-5; P14373: TRIM27; NbExp=3; IntAct=EBI-11984733, EBI-719493;
CC O60941-5; O94972: TRIM37; NbExp=3; IntAct=EBI-11984733, EBI-741602;
CC O60941-5; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-11984733, EBI-2130429;
CC O60941-5; P40222: TXLNA; NbExp=3; IntAct=EBI-11984733, EBI-359793;
CC O60941-5; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-11984733, EBI-739895;
CC O60941-5; P55072: VCP; NbExp=3; IntAct=EBI-11984733, EBI-355164;
CC O60941-5; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-11984733, EBI-2799833;
CC O60941-5; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-11984733, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27223470}.
CC Postsynaptic density {ECO:0000250|UniProtKB:P84060}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:O70585}. Basal cell membrane
CC {ECO:0000250|UniProtKB:O70585}. Postsynapse
CC {ECO:0000250|UniProtKB:O70585}. Nucleus {ECO:0000269|PubMed:27223470}.
CC Note=Localized at inhibitory synapses on the dendrites of cerebellar
CC Purkinje cells. {ECO:0000250|UniProtKB:O70585}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=DTN-B1;
CC IsoId=O60941-1; Sequence=Displayed;
CC Name=2; Synonyms=Dystrophin-associated protein A0;
CC IsoId=O60941-2; Sequence=VSP_004223, VSP_004226;
CC Name=3; Synonyms=DTN-B2;
CC IsoId=O60941-3; Sequence=VSP_004224, VSP_004225;
CC Name=4;
CC IsoId=O60941-4; Sequence=VSP_004226;
CC Name=5;
CC IsoId=O60941-5; Sequence=VSP_004223, VSP_043445, VSP_004226;
CC Name=6;
CC IsoId=O60941-6; Sequence=VSP_045534, VSP_043445, VSP_045535;
CC Name=7;
CC IsoId=O60941-7; Sequence=VSP_045535;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, kidney and pancreas.
CC -!- INDUCTION: Post-transcriptionally repressed by microRNA miR-143 during
CC neural differentiation. {ECO:0000269|PubMed:27223470}.
CC -!- DOMAIN: The coiled coil domain may mediate the interaction with
CC dystrophin.
CC -!- PTM: Phosphorylated by PKA. Phosphorylation at Thr-11 alters the
CC interaction with KIF5A. {ECO:0000250|UniProtKB:O70585}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the dystrophin family. Dystrobrevin subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF022728; AAC05082.1; -; mRNA.
DR EMBL; Y15722; CAA75737.1; -; mRNA.
DR EMBL; Y12712; CAA73249.1; -; mRNA.
DR EMBL; Y15718; CAA75733.1; -; mRNA.
DR EMBL; Y15719; CAA75734.1; -; mRNA.
DR EMBL; Y15720; CAA75735.1; -; mRNA.
DR EMBL; Y15721; CAA75736.1; -; mRNA.
DR EMBL; BT009805; AAP88807.1; -; mRNA.
DR EMBL; AK301386; BAH13469.1; -; mRNA.
DR EMBL; AC010150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC019144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00719.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00722.1; -; Genomic_DNA.
DR EMBL; BC016655; AAH16655.1; -; mRNA.
DR EMBL; BC049366; AAH49366.1; -; mRNA.
DR EMBL; AF070567; AAC28643.1; -; mRNA.
DR CCDS; CCDS46233.1; -. [O60941-5]
DR CCDS; CCDS46234.1; -. [O60941-2]
DR CCDS; CCDS46235.1; -. [O60941-4]
DR CCDS; CCDS46236.1; -. [O60941-7]
DR CCDS; CCDS46237.1; -. [O60941-1]
DR CCDS; CCDS58702.1; -. [O60941-6]
DR RefSeq; NP_001243232.1; NM_001256303.1.
DR RefSeq; NP_001243237.1; NM_001256308.2. [O60941-6]
DR RefSeq; NP_001307861.1; NM_001320932.1.
DR RefSeq; NP_001307862.1; NM_001320933.1.
DR RefSeq; NP_001307863.1; NM_001320934.1.
DR RefSeq; NP_001307864.1; NM_001320935.1.
DR RefSeq; NP_001307865.1; NM_001320936.1.
DR RefSeq; NP_068707.1; NM_021907.4. [O60941-1]
DR RefSeq; NP_149159.2; NM_033147.3. [O60941-4]
DR RefSeq; NP_149160.1; NM_033148.3. [O60941-2]
DR RefSeq; NP_899204.1; NM_183360.2. [O60941-7]
DR RefSeq; NP_899205.1; NM_183361.2. [O60941-5]
DR AlphaFoldDB; O60941; -.
DR SMR; O60941; -.
DR BioGRID; 108171; 109.
DR IntAct; O60941; 84.
DR MINT; O60941; -.
DR STRING; 9606.ENSP00000384084; -.
DR iPTMnet; O60941; -.
DR PhosphoSitePlus; O60941; -.
DR BioMuta; DTNB; -.
DR EPD; O60941; -.
DR jPOST; O60941; -.
DR MassIVE; O60941; -.
DR MaxQB; O60941; -.
DR PaxDb; O60941; -.
DR PeptideAtlas; O60941; -.
DR PRIDE; O60941; -.
DR ProteomicsDB; 25023; -.
DR ProteomicsDB; 33923; -.
DR ProteomicsDB; 49683; -. [O60941-1]
DR ProteomicsDB; 49684; -. [O60941-2]
DR ProteomicsDB; 49685; -. [O60941-3]
DR ProteomicsDB; 49686; -. [O60941-4]
DR ProteomicsDB; 49687; -. [O60941-5]
DR Antibodypedia; 27711; 289 antibodies from 24 providers.
DR DNASU; 1838; -.
DR Ensembl; ENST00000404103.7; ENSP00000385482.3; ENSG00000138101.20. [O60941-4]
DR Ensembl; ENST00000405222.5; ENSP00000384787.1; ENSG00000138101.20. [O60941-5]
DR Ensembl; ENST00000406818.8; ENSP00000384084.3; ENSG00000138101.20. [O60941-1]
DR Ensembl; ENST00000407038.7; ENSP00000384767.3; ENSG00000138101.20. [O60941-2]
DR Ensembl; ENST00000407661.7; ENSP00000385193.3; ENSG00000138101.20. [O60941-7]
DR GeneID; 1838; -.
DR KEGG; hsa:1838; -.
DR MANE-Select; ENST00000406818.8; ENSP00000384084.3; NM_021907.5; NP_068707.1.
DR UCSC; uc002rgh.5; human. [O60941-1]
DR CTD; 1838; -.
DR DisGeNET; 1838; -.
DR GeneCards; DTNB; -.
DR HGNC; HGNC:3058; DTNB.
DR HPA; ENSG00000138101; Tissue enhanced (salivary).
DR MIM; 602415; gene.
DR neXtProt; NX_O60941; -.
DR OpenTargets; ENSG00000138101; -.
DR PharmGKB; PA27511; -.
DR VEuPathDB; HostDB:ENSG00000138101; -.
DR eggNOG; KOG4301; Eukaryota.
DR GeneTree; ENSGT00940000164272; -.
DR InParanoid; O60941; -.
DR OMA; HSAGCSM; -.
DR OrthoDB; 699158at2759; -.
DR PhylomeDB; O60941; -.
DR TreeFam; TF343849; -.
DR PathwayCommons; O60941; -.
DR SignaLink; O60941; -.
DR SIGNOR; O60941; -.
DR BioGRID-ORCS; 1838; 9 hits in 1071 CRISPR screens.
DR ChiTaRS; DTNB; human.
DR GeneWiki; DTNB; -.
DR GenomeRNAi; 1838; -.
DR Pharos; O60941; Tbio.
DR PRO; PR:O60941; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O60941; protein.
DR Bgee; ENSG00000138101; Expressed in C1 segment of cervical spinal cord and 127 other tissues.
DR ExpressionAtlas; O60941; baseline and differential.
DR Genevisible; O60941; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0060077; C:inhibitory synapse; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030182; P:neuron differentiation; IMP:UniProtKB.
DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR017432; Distrobrevin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF038204; Distrobrevin; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..627
FT /note="Dystrobrevin beta"
FT /id="PRO_0000086878"
FT ZN_FING 238..294
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 399..448
FT /note="Syntrophin-binding region"
FT REGION 520..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 428..529
FT /evidence="ECO:0000255"
FT COMPBIAS 549..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:25732826"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70585"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70585"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70585"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70585"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 424
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70585"
FT VAR_SEQ 1..57
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045534"
FT VAR_SEQ 360..390
FT /note="RLQYSQDIPSHLADEHALIASYVARLQHCAR -> S (in isoform 2
FT and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9540997, ECO:0000303|Ref.3"
FT /id="VSP_004223"
FT VAR_SEQ 519..525
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_043445"
FT VAR_SEQ 526..558
FT /note="AQATGSPHTSPTHGGGRPMPMPVRSTSAGSTPT -> VSELRNFPPDSRSFA
FT RSSFPHINVSPLLPAHHL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9540997"
FT /id="VSP_004224"
FT VAR_SEQ 559..627
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9540997"
FT /id="VSP_004225"
FT VAR_SEQ 579..608
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9540997, ECO:0000303|Ref.3,
FT ECO:0000303|Ref.8"
FT /id="VSP_004226"
FT VAR_SEQ 609..626
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_045535"
FT VARIANT 97
FT /note="P -> H (in dbSNP:rs17854576)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_069146"
FT VARIANT 116
FT /note="I -> T (in dbSNP:rs17854577)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_069147"
FT CONFLICT 102
FT /note="I -> T (in Ref. 4; BAH13469)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="K -> T (in Ref. 4; BAH13469)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 71356 MW; 6927EC0BD86D375C CRC64;
MIEESGNKRK TMAEKRQLFI EMRAQNFDVI RLSTYRTACK LRFVQKRCNL HLVDIWNMIE
AFRDNGLNTL DHTTEISVSR LETVISSIYY QLNKRLPSTH QISVEQSISL LLNFMIAAYD
SEGRGKLTVF SVKAMLATMC GGKMLDKLRY VFSQMSDSNG LMIFSKFDQF LKEVLKLPTA
VFEGPSFGYT EHSVRTCFPQ QRKIMLNMFL DTMMADPPPQ CLVWLPLMHR LAHVENVFHP
VECSYCRCES MMGFRYRCQQ CHNYQLCQNC FWRGHAGGPH SNQHQMKEHS SWKSPAKKLS
HAISKSLGCV PTREPPHPVF PEQPEKPLDL AHIVPPRPLT NMNDTMVSHM SSGVPTPTKR
LQYSQDIPSH LADEHALIAS YVARLQHCAR VLDSPSRLDE EHRLIARYAA RLAAEAGNVT
RPPTDLSFNF DANKQQRQLI AELENKNREI LQEIQRLRLE HEQASQPTPE KAQQNPTLLA
ELRLLRQRKD ELEQRMSALQ ESRRELMVQL EELMKLLKEE EQKQAAQATG SPHTSPTHGG
GRPMPMPVRS TSAGSTPTHC PQDSLSGVGG DVQEAFAQGT RRNLRNDLLV AADSITNTMS
SLVKELHSAE EGAEEEEEKM QNGKDRG
