ID DTNB_MOUSE Reviewed; 659 AA. AC O70585; E9Q0F2; O70563; Q9CTZ1; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 3. DT 24-JAN-2024, entry version 167. DE RecName: Full=Dystrobrevin beta {ECO:0000305}; DE Short=DTN-B {ECO:0000303|PubMed:9540997}; DE Short=mDTN-BDTN-B; DE AltName: Full=Beta-dystrobrevin {ECO:0000303|PubMed:9419360}; GN Name=Dtnb {ECO:0000312|MGI:MGI:1203728}; 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). 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=9419360; DOI=10.1073/pnas.95.1.241; RA Blake D.J., Nawrotzki R., Loh N.Y., Gorecki D.C., Davies K.E.; RT "Beta-dystrobrevin, a member of the dystrophin-related protein family."; RL Proc. Natl. Acad. Sci. U.S.A. 95:241-246(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2). RX PubMed=9799833; DOI=10.1007/s003359900883; RA Loh N.Y., Ambrose H.J., Guay-Woodford L.M., Dasgupta S., Nawrotzki R.A., RA Blake D.J., Davies K.E.; RT "Genomic organization and refined mapping of the mouse beta-dystrobrevin RT gene."; RL Mamm. Genome 9:857-862(1998). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 590-608 (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Stomach; 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 [6] RP INTERACTION WITH SNTB2 AND SNTA1. RX PubMed=10545507; DOI=10.1083/jcb.147.3.645; RA Blake D.J., Hawkes R., Benson M.A., Beesley P.W.; RT "Different dystrophin-like complexes are expressed in neurons and glia."; RL J. Cell Biol. 147:645-658(1999). RN [7] RP TISSUE SPECIFICITY, AND INTERACTION WITH UTRN; DMD; SNTB1; SNTB2 AND SNTA1. RX PubMed=10893187; DOI=10.1242/jcs.113.15.2715; RA Loh N.Y., Newey S.E., Davies K.E., Blake D.J.; RT "Assembly of multiple dystrobrevin-containing complexes in the kidney."; RL J. Cell Sci. 113:2715-2724(2000). RN [8] RP INTERACTION WITH DTNBP1. RX PubMed=11316798; DOI=10.1074/jbc.m010418200; RA Benson M.A., Newey S.E., Martin-Rendon E., Hawkes R., Blake D.J.; RT "Dysbindin, a novel coiled-coil-containing protein that interacts with the RT dystrobrevins in muscle and brain."; RL J. Biol. Chem. 276:24232-24241(2001). RN [9] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=11585924; DOI=10.1128/mcb.21.21.7442-7448.2001; RA Loh N.Y., Nebenius-Oosthuizen D., Blake D.J., Smith A.J., Davies K.E.; RT "Role of beta-dystrobrevin in nonmuscle dystrophin-associated protein RT complex-like complexes in kidney and liver."; RL Mol. Cell. Biol. 21:7442-7448(2001). RN [10] RP INTERACTION WITH KIF5A. RX PubMed=14600269; DOI=10.1242/jcs.00805; RA Macioce P., Gambara G., Bernassola M., Gaddini L., Torreri P., Macchia G., RA Ramoni C., Ceccarini M., Petrucci T.C.; RT "Beta-dystrobrevin interacts directly with kinesin heavy chain in brain."; RL J. Cell Sci. 116:4847-4856(2003). RN [11] RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION. RX PubMed=16540561; DOI=10.1523/jneurosci.4823-05.2006; RA Grady R.M., Wozniak D.F., Ohlemiller K.K., Sanes J.R.; RT "Cerebellar synaptic defects and abnormal motor behavior in mice lacking RT alpha- and beta-dystrobrevin."; RL J. Neurosci. 26:2841-2851(2006). RN [12] RP PHOSPHORYLATION, AND INTERACTION WITH PRKAR2B AND PRKAR1A. RX PubMed=17610895; DOI=10.1016/j.jmb.2007.06.019; RA Ceccarini M., Grasso M., Veroni C., Gambara G., Artegiani B., Macchia G., RA Ramoni C., Torreri P., Mallozzi C., Petrucci T.C., Macioce P.; RT "Association of dystrobrevin and regulatory subunit of protein kinase A: a RT new role for dystrobrevin as a scaffold for signaling proteins."; RL J. Mol. Biol. 371:1174-1187(2007). RN [13] RP INTERACTION WITH OLFM1. RX PubMed=17265465; DOI=10.1002/jnr.21186; RA Veroni C., Grasso M., Macchia G., Ramoni C., Ceccarini M., Petrucci T.C., RA Macioce P.; RT "beta-dystrobrevin, a kinesin-binding receptor, interacts with the RT extracellular matrix components pancortins."; RL J. Neurosci. Res. 85:2631-2639(2007). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver, 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). RN [15] RP INTERACTION WITH HMG20A AND HMG20B, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=20530487; DOI=10.1074/jbc.m109.090654; RA Artegiani B., Labbaye C., Sferra A., Quaranta M.T., Torreri P., Macchia G., RA Ceccarini M., Petrucci T.C., Macioce P.; RT "The interaction with HMG20a/b proteins suggests a potential role for beta- RT dystrobrevin in neuronal differentiation."; RL J. Biol. Chem. 285:24740-24750(2010). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-11; THR-69; RP THR-179; THR-212 AND THR-424, MUTAGENESIS OF THR-11, AND INTERACTION WITH RP KIF5A. RX PubMed=22978324; DOI=10.1111/febs.12006; RA Fratini F., Macchia G., Torreri P., Matteucci A., Salzano A.M., RA Crescenzi M., Macioce P., Petrucci T.C., Ceccarini M.; RT "Phosphorylation on threonine 11 of beta-dystrobrevin alters its RT interaction with kinesin heavy chain."; RL FEBS J. 279:4131-4144(2012). CC -!- FUNCTION: Scaffolding protein that assembles DMD and SNTA1 molecules to CC the basal membrane of kidney cells and liver sinusoids CC (PubMed:11585924). May function as a repressor of the SYN1 promoter CC through the binding of repressor element-1 (RE-1), in turn regulates CC SYN1 expression and may be involved in cell proliferation regulation CC during the early phase of neural differentiation (PubMed:20530487). May CC be required for proper maturation and function of a subset of CC inhibitory synapses (PubMed:16540561). {ECO:0000269|PubMed:11585924, CC ECO:0000269|PubMed:16540561, ECO:0000269|PubMed:20530487}. CC -!- SUBUNIT: Interacts with dystrophin short form DP71 and syntrophins CC SNTG1 and SNTG2 (By similarity). Binds DTNBP1 (PubMed:11316798). Forms CC a specific complex composed of DMD, SNTB2 and SNTA1 in neuron; the CC interaction with SNTB2 and SNTA1 is DMD independent (PubMed:10545507). CC Interacts with UTRN and dystrophin short form DP71 in the kidney and CC liver (PubMed:10893187). Interacts with SNTB1, SNTB2 and SNTA1 in CC kidney and liver (PubMed:10893187). Interacts with KIF5A CC (PubMed:14600269, PubMed:22978324). Interacts with HMG20A and HMG20B CC (PubMed:20530487). Interacts with OLFM1 (PubMed:17265465). Interacts CC with PRKAR2B and PRKAR1A (PubMed:17610895). CC {ECO:0000250|UniProtKB:O60941, ECO:0000269|PubMed:10545507, CC ECO:0000269|PubMed:10893187, ECO:0000269|PubMed:11316798, CC ECO:0000269|PubMed:14600269, ECO:0000269|PubMed:17265465, CC ECO:0000269|PubMed:17610895, ECO:0000269|PubMed:20530487, CC ECO:0000269|PubMed:22978324}. CC -!- INTERACTION: CC O70585; P33175: Kif5a; NbExp=4; IntAct=EBI-349714, EBI-349710; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20530487}. CC Postsynaptic density {ECO:0000250|UniProtKB:P84060}. Cell projection, CC dendrite {ECO:0000269|PubMed:11585924, ECO:0000269|PubMed:16540561}. CC Basal cell membrane {ECO:0000269|PubMed:10893187}. Postsynapse CC {ECO:0000269|PubMed:16540561}. Nucleus {ECO:0000269|PubMed:20530487}. CC Note=Localized at inhibitory synapses on the dendrites of cerebellar CC Purkinje cells. {ECO:0000269|PubMed:16540561}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=O70585-1; Sequence=Displayed; CC Name=2; CC IsoId=O70585-2; Sequence=VSP_004227, VSP_004228, VSP_004229; CC -!- TISSUE SPECIFICITY: Expressed mainly in liver and lung. Expressed in CC brain, namely in neurons of the cortex and hippocampus and in the CC dendrites, soma, and nuclei of pyramidal neurons of the hippocampus CC region CA1 (PubMed:11585924). Expressed in kidney, namely in epithelial CC cells of renal tubules, collecting ducts, Bowman's capsules and CC glomeruli (PubMed:10893187). Expressed in blood vessels and pia CC (PubMed:16540561). {ECO:0000269|PubMed:10893187, CC ECO:0000269|PubMed:11585924, ECO:0000269|PubMed:16540561}. CC -!- DOMAIN: The coiled coil domain may mediate the interaction with CC dystrophin. CC -!- PTM: Phosphorylated by PKA (PubMed:17610895). Phosphorylation at Thr-11 CC alters the interaction with KIF5A (PubMed:22978324). CC {ECO:0000269|PubMed:17610895, ECO:0000269|PubMed:22978324}. CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice for Dtnb are viable and CC fertile, and are normal in appearance (PubMed:11585924, CC PubMed:16540561). Double knockout mice for DTNA and DTNB genes have a CC mild myopathy plus synaptic defects and abnormal motor behavior CC (PubMed:16540561). {ECO:0000269|PubMed:11585924, CC ECO:0000269|PubMed:16540561}. CC -!- MISCELLANEOUS: [Isoform 2]: 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 -!- SEQUENCE CAUTION: CC Sequence=CAA75752.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA75752.1; Type=Frameshift; Evidence={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; Y15742; CAA75752.1; ALT_SEQ; mRNA. DR EMBL; AJ003007; CAA05796.1; -; mRNA. DR EMBL; AJ010204; CAA09038.1; -; Genomic_DNA. DR EMBL; AJ010205; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010206; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010207; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010208; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010209; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010210; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010211; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010212; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010213; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010214; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010215; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010216; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010217; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010218; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010219; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010220; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AJ010221; CAA09038.1; JOINED; Genomic_DNA. DR EMBL; AC155273; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR974568; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK019068; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS49015.1; -. [O70585-1] DR RefSeq; NP_001155937.1; NM_001162465.1. [O70585-1] DR AlphaFoldDB; O70585; -. DR SMR; O70585; -. DR BioGRID; 199335; 9. DR CORUM; O70585; -. DR IntAct; O70585; 7. DR MINT; O70585; -. DR STRING; 10090.ENSMUSP00000126194; -. DR GlyGen; O70585; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O70585; -. DR PhosphoSitePlus; O70585; -. DR SwissPalm; O70585; -. DR jPOST; O70585; -. DR MaxQB; O70585; -. DR PaxDb; 10090-ENSMUSP00000126194; -. DR ProteomicsDB; 277522; -. [O70585-1] DR ProteomicsDB; 277523; -. [O70585-2] DR Pumba; O70585; -. DR DNASU; 13528; -. DR Ensembl; ENSMUST00000101637.11; ENSMUSP00000099161.5; ENSMUSG00000071454.14. [O70585-2] DR Ensembl; ENSMUST00000164578.9; ENSMUSP00000126194.3; ENSMUSG00000071454.14. [O70585-1] DR GeneID; 13528; -. DR KEGG; mmu:13528; -. DR UCSC; uc007mww.2; mouse. [O70585-2] DR UCSC; uc007mwy.2; mouse. [O70585-1] DR AGR; MGI:1203728; -. DR CTD; 1838; -. DR MGI; MGI:1203728; Dtnb. DR VEuPathDB; HostDB:ENSMUSG00000071454; -. DR eggNOG; KOG4301; Eukaryota. DR GeneTree; ENSGT00940000153897; -. DR InParanoid; O70585; -. DR OrthoDB; 5405762at2759; -. DR PhylomeDB; O70585; -. DR TreeFam; TF343849; -. DR BioGRID-ORCS; 13528; 0 hits in 76 CRISPR screens. DR ChiTaRS; Dtnb; mouse. DR PRO; PR:O70585; -. DR Proteomes; UP000000589; Chromosome 12. DR RNAct; O70585; Protein. DR Bgee; ENSMUSG00000071454; Expressed in superior frontal gyrus and 210 other cell types or tissues. DR ExpressionAtlas; O70585; baseline and differential. 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; IDA: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; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0019902; F:phosphatase binding; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030182; P:neuron differentiation; ISO:MGI. DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central. DR CDD; cd16244; EFh_DTN; 1. DR CDD; cd02334; ZZ_dystrophin; 1. DR Gene3D; 3.30.60.90; -; 1. DR Gene3D; 1.10.238.10; EF-hand; 2. 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 PANTHER; PTHR12268:SF22; DYSTROBREVIN BETA; 1. DR PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1. 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; EF-hand; 2. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS01357; ZF_ZZ_1; 1. DR PROSITE; PS50135; ZF_ZZ_2; 1. DR Genevisible; O70585; MM. 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..659 FT /note="Dystrobrevin beta" FT /id="PRO_0000086879" FT ZN_FING 238..294 FT /note="ZZ-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT REGION 369..418 FT /note="Syntrophin-binding region" FT REGION 520..562 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 599..620 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 429..519 FT /evidence="ECO:0000255" FT COMPBIAS 542..556 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 600..614 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:0000250|UniProtKB:O60941" FT MOD_RES 11 FT /note="Phosphothreonine; by PKA and PKC" FT /evidence="ECO:0000269|PubMed:22978324" FT MOD_RES 69 FT /note="Phosphothreonine; by PKC" FT /evidence="ECO:0000269|PubMed:22978324" FT MOD_RES 179 FT /note="Phosphothreonine; by PKC" FT /evidence="ECO:0000269|PubMed:22978324" FT MOD_RES 212 FT /note="Phosphothreonine; by PKC" FT /evidence="ECO:0000269|PubMed:22978324" FT MOD_RES 394 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O60941" FT MOD_RES 424 FT /note="Phosphothreonine; by PKA" FT /evidence="ECO:0000269|PubMed:22978324" FT VAR_SEQ 518 FT /note="K -> KEEEQKQA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:9419360" FT /id="VSP_004227" FT VAR_SEQ 603..608 FT /note="AEAEEQ -> EVTPVS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:9419360" FT /id="VSP_004228" FT VAR_SEQ 609..659 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:9419360" FT /id="VSP_004229" FT MUTAGEN 11 FT /note="T->A: Does not affect interaction with Kif5A." FT /evidence="ECO:0000269|PubMed:22978324" FT MUTAGEN 11 FT /note="T->D: Reduces interaction with Kif5A." FT /evidence="ECO:0000269|PubMed:22978324" FT CONFLICT 412 FT /note="L -> P (in Ref. 1; CAA75752)" FT /evidence="ECO:0000305" FT CONFLICT 465 FT /note="S -> F (in Ref. 2; CAA05796 and 3; CAA09038)" FT /evidence="ECO:0000305" SQ SEQUENCE 659 AA; 74399 MW; 27AB3141A65797A8 CRC64; MIEEGGNKRK TMAEKRQLFI EMRAQNFDVI RLSTYRTACK LRFVQKRCNL HLVDIWNMIE AFRDNGLNTL DHSTEISVSR LETVISSIYY QLNKRLPSTH QISVEQSISL LLNFMVAAYD SEGRGKLTVF SVKAMLATMC GGKMLDKLRY IFSQMSDSNG LMMFGKLDQF LKEALKLPTA VFEGPSFGYT EHAVRTCFPQ QKKIMLNMFL DTMMADPPPQ CLVWLPLMHR LAHVENVFHP VECSYCHCES MMGFRYRCQQ CHNYQLCQNC FWRGHASGAH SNQHQMKEHS SWKSPAKKLS HAISKSLGCV PSREPPHPVF PEQPEKPLDL AHLVPPRPLT NMNDTVVSHM SSGVPTPTKR LQYSQDMPNL LADEHALIAS YVARLQHCTR VLDSPSRLDE EHRLIARYAA RLAAEAGNMT RPPTDASFNF DANKQQRQLI AELENKNREI LQEIQRLRLE HEQASQPTPE KAQQNPMLLA ELRLLRQRKD ELEQRMSALQ ESRRELMVQL EGLMKLLKAQ ATGSPHTSPT HGGGRPMPMP VRSTSAGSTP THGPQDSLSG VGGDVQEAFA QGTRRNLRND LLVAADSITN TMSSLVKELH SGAEAEEQAG TEKTREGLPP RGTFLSVFLL HTWTKLAGCQ THSTSRERSQ AYGKWGGTA //