ID STMN1_MOUSE Reviewed; 149 AA. AC P54227; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 196. DE RecName: Full=Stathmin; DE AltName: Full=Leukemia-associated gene protein; DE AltName: Full=Leukemia-associated phosphoprotein p18; DE AltName: Full=Metablastin; DE AltName: Full=Oncoprotein 18; DE Short=Op18; DE AltName: Full=Phosphoprotein p19; DE Short=pp19; DE AltName: Full=Prosolin; DE AltName: Full=Protein Pr22; DE AltName: Full=pp17; GN Name=Stmn1; Synonyms=Lag, Lap18, Pr22; 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 [GENOMIC DNA]. RX PubMed=8288240; DOI=10.1006/geno.1993.1477; RA Okazaki T., Yoshida B.N., Avraham K.B., Wang H., Wuenschell C.W., RA Jenkins N.A., Copeland N.G., Anderson D.J., Mori N.; RT "Molecular diversity of the SCG10/stathmin gene family in the mouse."; RL Genomics 18:360-373(1993). RN [2] RP ERRATUM OF PUBMED:8288240. RA Okazaki T., Yoshida B.N., Avraham K.B., Wang H., Wuenschell C.W., RA Jenkins N.A., Copeland N.G., Anderson D.J., Mori N.; RL Genomics 21:298-298(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RX PubMed=8906359; DOI=10.1247/csf.21.237; RA Hosoya H., Ishikawa K., Dohi N., Marunouchi T.; RT "Transcriptional and post-transcriptional regulation of pr22 (Op18) with RT proliferation control."; RL Cell Struct. Funct. 21:237-243(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=129; TISSUE=Mammary gland, and Retina; 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 PROTEIN SEQUENCE OF 15-27, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [6] RP PHOSPHORYLATION AT SER-16; SER-25; SER-38 AND SER-63. RX PubMed=8376365; DOI=10.1016/s0021-9258(20)80696-6; RA Beretta L., Dobransky T., Sobel A.; RT "Multiple phosphorylation of stathmin. Identification of four sites RT phosphorylated in intact cells and in vitro by cyclic AMP-dependent protein RT kinase and p34cdc2."; RL J. Biol. Chem. 268:20076-20084(1993). RN [7] RP INTERACTION WITH KIST. RC TISSUE=Embryo; RX PubMed=7724523; DOI=10.1073/pnas.92.8.3100; RA Maucuer A., Camonis J.H., Sobel A.; RT "Stathmin interaction with a putative kinase and coiled-coil-forming RT protein domains."; RL Proc. Natl. Acad. Sci. U.S.A. 92:3100-3104(1995). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-38, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [9] RP FUNCTION IN CONTROL OF FEAR, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=16286011; DOI=10.1016/j.cell.2005.08.038; RA Shumyatsky G.P., Malleret G., Shin R.-M., Takizawa S., Tully K., RA Tsvetkov E., Zakharenko S.S., Joseph J., Vronskaya S., Yin D., RA Schubart U.K., Kandel E.R., Bolshakov V.Y.; RT "Stathmin, a gene enriched in the amygdala, controls both learned and RT innate fear."; RL Cell 123:697-709(2005). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., RA Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in naive RT and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-38, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, 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). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-119, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Involved in the regulation of the microtubule (MT) filament CC system by destabilizing microtubules. Prevents assembly and promotes CC disassembly of microtubules. Phosphorylation at Ser-16 may be required CC for axon formation during neurogenesis (By similarity). Involved in the CC control of the learned and innate fear. {ECO:0000250, CC ECO:0000269|PubMed:16286011}. CC -!- SUBUNIT: Binds to two alpha/beta-tubulin heterodimers. Interacts with CC KIST. {ECO:0000269|PubMed:7724523}. CC -!- INTERACTION: CC P54227; P46414: Cdkn1b; NbExp=2; IntAct=EBI-1006438, EBI-1005742; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- TISSUE SPECIFICITY: Highly expressed in the lateral nucleus of the CC amygdala. {ECO:0000269|PubMed:16286011}. CC -!- PTM: Many different phosphorylated forms are observed depending on CC specific combinations among the sites which can be phosphorylated. MAPK CC is responsible for the phosphorylation of stathmin in response to NGF CC (Probable). Phosphorylation at Ser-16 seems to be required for neuron CC polarization (By similarity). {ECO:0000250, ECO:0000305}. CC -!- DISRUPTION PHENOTYPE: Mice show deficits in spike-timing-dependent CC long-term potentiation, exhibit decreased memory in amygdala-dependent CC fear conditioning and fail to recognize danger in innately aversive CC environments. {ECO:0000269|PubMed:16286011}. CC -!- SIMILARITY: Belongs to the stathmin family. {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; L20256; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L20257; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L20258; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X94915; CAA64401.1; -; mRNA. DR EMBL; BC010581; AAH10581.1; -; mRNA. DR EMBL; BC031831; AAH31831.1; -; mRNA. DR EMBL; BC054396; AAH54396.1; -; mRNA. DR CCDS; CCDS18772.1; -. DR PIR; B48917; B48917. DR RefSeq; NP_001416805.1; NM_001429876.1. DR RefSeq; NP_062615.1; NM_019641.5. DR AlphaFoldDB; P54227; -. DR SMR; P54227; -. DR BioGRID; 201092; 27. DR FunCoup; P54227; 1281. DR IntAct; P54227; 10. DR STRING; 10090.ENSMUSP00000030636; -. DR GlyGen; P54227; 3 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (2 sites). DR iPTMnet; P54227; -. DR PhosphoSitePlus; P54227; -. DR SwissPalm; P54227; -. DR REPRODUCTION-2DPAGE; P54227; -. DR jPOST; P54227; -. DR PaxDb; 10090-ENSMUSP00000030636; -. DR PeptideAtlas; P54227; -. DR ProteomicsDB; 257456; -. DR Pumba; P54227; -. DR Antibodypedia; 4112; 1515 antibodies from 48 providers. DR DNASU; 16765; -. DR Ensembl; ENSMUST00000030636.11; ENSMUSP00000030636.5; ENSMUSG00000028832.12. DR Ensembl; ENSMUST00000105868.2; ENSMUSP00000101494.2; ENSMUSG00000028832.12. DR GeneID; 16765; -. DR KEGG; mmu:16765; -. DR UCSC; uc008vfc.2; mouse. DR AGR; MGI:96739; -. DR CTD; 3925; -. DR MGI; MGI:96739; Stmn1. DR VEuPathDB; HostDB:ENSMUSG00000028832; -. DR eggNOG; KOG1280; Eukaryota. DR GeneTree; ENSGT01030000234597; -. DR InParanoid; P54227; -. DR OMA; RKSHEAM; -. DR OrthoDB; 5986631at2759; -. DR PhylomeDB; P54227; -. DR BioGRID-ORCS; 16765; 6 hits in 79 CRISPR screens. DR PRO; PR:P54227; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; P54227; protein. DR Bgee; ENSMUSG00000028832; Expressed in cortical plate and 93 other cell types or tissues. DR ExpressionAtlas; P54227; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0015631; F:tubulin binding; ISO:MGI. DR GO; GO:0007409; P:axonogenesis; IMP:MGI. DR GO; GO:0061436; P:establishment of skin barrier; ISO:GO_Central. DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISO:GO_Central. DR GO; GO:0007019; P:microtubule depolymerization; ISO:MGI. DR GO; GO:0000281; P:mitotic cytokinesis; IGI:MGI. DR GO; GO:0007052; P:mitotic spindle organization; ISO:MGI. DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:MGI. DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISO:GO_Central. DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:GO_Central. DR GO; GO:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; ISO:GO_Central. DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central. DR GO; GO:0030334; P:regulation of cell migration; IGI:MGI. DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISO:GO_Central. DR GO; GO:0009615; P:response to virus; IEA:Ensembl. DR Gene3D; 6.10.280.30; -; 1. DR InterPro; IPR030514; Stathmin_CS. DR InterPro; IPR000956; Stathmin_fam. DR InterPro; IPR036002; Stathmin_sf. DR PANTHER; PTHR10104; STATHMIN; 1. DR PANTHER; PTHR10104:SF5; STATHMIN; 1. DR Pfam; PF00836; Stathmin; 1. DR PIRSF; PIRSF002285; Stathmin; 1. DR PRINTS; PR00345; STATHMIN. DR SUPFAM; SSF101494; Stathmin; 1. DR PROSITE; PS00563; STATHMIN_1; 1. DR PROSITE; PS01041; STATHMIN_2; 1. DR PROSITE; PS51663; STATHMIN_3; 1. PE 1: Evidence at protein level; KW Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein; KW Differentiation; Direct protein sequencing; Methylation; Microtubule; KW Neurogenesis; Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P16949" FT CHAIN 2..149 FT /note="Stathmin" FT /id="PRO_0000182390" FT DOMAIN 4..145 FT /note="SLD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00998" FT REGION 27..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 104..149 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 41..140 FT /evidence="ECO:0000255" FT COMPBIAS 104..143 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P16949" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P16949" FT MOD_RES 9 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P16949" FT MOD_RES 16 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:8376365, FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:21183079" FT MOD_RES 25 FT /note="Phosphoserine; by CDK1, MAPK1 and MAPK3" FT /evidence="ECO:0000269|PubMed:8376365, FT ECO:0007744|PubMed:15345747, ECO:0007744|PubMed:21183079" FT MOD_RES 29 FT /note="N6-methyllysine" FT /evidence="ECO:0000250|UniProtKB:P16949" FT MOD_RES 31 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P16949" FT MOD_RES 38 FT /note="Phosphoserine; by CDK1, MAPK1 and MAPK3" FT /evidence="ECO:0000269|PubMed:8376365, FT ECO:0007744|PubMed:15345747, ECO:0007744|PubMed:21183079" FT MOD_RES 63 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:8376365" FT MOD_RES 100 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P16949" FT MOD_RES 119 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" SQ SEQUENCE 149 AA; 17274 MW; 616526E0A6667BDA CRC64; MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPDFPLSPP KKKDLSLEEI QKKLEAAEER RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL ERLREKDKHV EEVRKNKESK DPADETEAD //