STMN1_HUMAN
ID STMN1_HUMAN Reviewed; 149 AA.
AC P16949; A2A2D1; B2R4E7; B7Z8N4; D3DPJ5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Stathmin;
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=C1orf215, LAP18, OP18;
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), AND PROTEIN SEQUENCE OF 45-61.
RX PubMed=2760073; DOI=10.1016/s0021-9258(18)71714-6;
RA Zhu X.-X., Kozarsky K., Strahler J.R., Eckerskorn C., Lottspeich F.,
RA Melhem R., Lowe J., Fox D.A., Hanash S.M., Atweh G.F.;
RT "Molecular cloning of a novel human leukemia-associated gene. Evidence of
RT conservation in animal species.";
RL J. Biol. Chem. 264:14556-14560(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2358074; DOI=10.1016/0014-5793(90)80266-l;
RA Maucuer A., Doye V., Sobel A.;
RT "A single amino acid difference distinguishes the human and the rat
RT sequences of stathmin, a ubiquitous intracellular phosphoprotein associated
RT with cell regulations.";
RL FEBS Lett. 264:275-278(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=1917919; DOI=10.1016/s0021-9258(18)55189-9;
RA Melhem R.F., Zhu X., Hailat N., Strahler J.R., Hanash S.M.;
RT "Characterization of the gene for a proliferation-related phosphoprotein
RT (oncoprotein 18) expressed in high amounts in acute leukemia.";
RL J. Biol. Chem. 266:17747-17753(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [9]
RP PROTEIN SEQUENCE OF 14-41 AND 44-52, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 87-96.
RX PubMed=2546936; DOI=10.1016/s0021-9258(18)51559-3;
RA Hanash S.M., Strahler J.R., Kuick R., Chu E.H.Y., Nichols D.;
RT "Ca2+-dependent and cAMP-dependent control of nicotinic acetylcholine
RT receptor phosphorylation in muscle cells.";
RL J. Biol. Chem. 264:12813-12819(1989).
RN [11]
RP ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-25 AND SER-38, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=1737801; DOI=10.1016/s0021-9258(19)50759-1;
RA Labdon J.E., Nieves E., Schubart U.K.;
RT "Analysis of phosphoprotein p19 by liquid chromatography/mass spectrometry.
RT Identification of two proline-directed serine phosphorylation sites and a
RT blocked amino terminus.";
RL J. Biol. Chem. 267:3506-3513(1992).
RN [12]
RP PHOSPHORYLATION AT SER-25 AND SER-38.
RX PubMed=8325880; DOI=10.1016/s0021-9258(18)82435-8;
RA Marklund U., Brattsand G., Shingler V., Gullberg M.;
RT "Serine 25 of oncoprotein 18 is a major cytosolic target for the mitogen-
RT activated protein kinase.";
RL J. Biol. Chem. 268:15039-15047(1993).
RN [13]
RP PHOSPHORYLATION AT SER-16; SER-25 AND SER-38.
RX PubMed=8245003; DOI=10.1016/s0021-9258(19)74442-1;
RA Marklund U., Brattsand G., Osterman O., Ohlsson P.-I., Gullberg M.;
RT "Multiple signal transduction pathways induce phosphorylation of serines
RT 16, 25, and 38 of oncoprotein 18 in T lymphocytes.";
RL J. Biol. Chem. 268:25671-25680(1993).
RN [14]
RP PHOSPHORYLATION AT SER-16; SER-25 AND SER-38.
RX PubMed=8125092; DOI=10.1111/j.1432-1033.1994.tb18632.x;
RA Brattsand G., Marklund U., Nylander K., Roos G., Gullberg M.;
RT "Cell-cycle-regulated phosphorylation of oncoprotein 18 on Ser16, Ser25 and
RT Ser38.";
RL Eur. J. Biochem. 220:359-368(1994).
RN [15]
RP INTERACTION WITH TUBULIN.
RX PubMed=10675326; DOI=10.1093/emboj/19.4.572;
RA Steinmetz M.O., Kammerer R.A., Jahnke W., Goldie K.N., Lustig A.,
RA van Oostrum J.;
RT "Op18/stathmin caps a kinked protofilament-like tubulin tetramer.";
RL EMBO J. 19:572-580(2000).
RN [16]
RP INTERACTION WITH TUBULIN.
RX PubMed=10702243; DOI=10.1074/jbc.275.10.6841;
RA Redeker V., Lachkar S., Siavoshian S., Charbaut E., Rossier J., Sobel A.,
RA Curmi P.A.;
RT "Probing the native structure of stathmin and its interaction domains with
RT tubulin. Combined use of limited proteolysis, size exclusion
RT chromatography, and mass spectrometry.";
RL J. Biol. Chem. 275:6841-6849(2000).
RN [17]
RP EFFECT OF PHOSPHORYLATION AT SER-63 ON TUBULIN BINDING.
RX PubMed=11415983; DOI=10.1093/embo-reports/kve105;
RA Steinmetz M.O., Jahnke W., Towbin H., Garcia-Echeverria C., Voshol H.,
RA Mueller D., van Oostrum J.;
RT "Phosphorylation disrupts the central helix in Op18/stathmin and suppresses
RT binding to tubulin.";
RL EMBO Rep. 2:505-510(2001).
RN [18]
RP TISSUE SPECIFICITY.
RX PubMed=12676564; DOI=10.1016/s0888-7543(03)00031-4;
RA Bieche I., Maucuer A., Laurendeau I., Lachkar S., Spano A.J.,
RA Frankfurter A., Levy P., Manceau V., Sobel A., Vidaud M., Curmi P.A.;
RT "Expression of stathmin family genes in human tissues: non-neural-
RT restricted expression for SCLIP.";
RL Genomics 81:400-410(2003).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-63, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [20]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
RT differential cellular gene expression in response to enterovirus 71
RT infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-38, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-38 AND
RP SER-63, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-38, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-25, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP 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 [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-38, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-100 AND LYS-119, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-38 AND
RP SER-63, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-31; SER-38
RP AND SER-63, AND 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 [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-16; SER-25; SER-31;
RP SER-38 AND SER-63, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [36]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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. Involved in the control of the
CC learned and innate fear (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to two alpha/beta-tubulin heterodimers. Interacts with
CC KIST. {ECO:0000269|PubMed:10675326, ECO:0000269|PubMed:10702243}.
CC -!- INTERACTION:
CC P16949; P46527: CDKN1B; NbExp=3; IntAct=EBI-445909, EBI-519280;
CC P16949; Q86VW0: SESTD1; NbExp=3; IntAct=EBI-445909, EBI-6117072;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P16949-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P16949-2; Sequence=VSP_041377;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expression is strongest in fetal and
CC adult brain, spinal cord, and cerebellum, followed by thymus, bone
CC marrow, testis, and fetal liver. Expression is intermediate in colon,
CC ovary, placenta, uterus, and trachea, and is readily detected at
CC substantially lower levels in all other tissues examined. Lowest
CC expression is found in adult liver. Present in much greater abundance
CC in cells from patients with acute leukemia of different subtypes than
CC in normal peripheral blood lymphocytes, non-leukemic proliferating
CC lymphoid cells, bone marrow cells, or cells from patients with chronic
CC lymphoid or myeloid leukemia. {ECO:0000269|PubMed:12676564,
CC ECO:0000269|PubMed:1917919}.
CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
CC infection (at protein level). {ECO:0000269|PubMed:16548883}.
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 Phosphorylation at Ser-16 seems to be required for neuron polarization
CC (By similarity). Phosphorylation at Ser-63 reduces tubulin binding 10-
CC fold and suppresses the MT polymerization inhibition activity.
CC {ECO:0000250, ECO:0000269|PubMed:1737801, ECO:0000269|PubMed:8125092,
CC ECO:0000269|PubMed:8245003, ECO:0000269|PubMed:8325880}.
CC -!- SIMILARITY: Belongs to the stathmin family. {ECO:0000305}.
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DR EMBL; J04991; AAA59980.1; -; mRNA.
DR EMBL; M31303; AAA59971.1; -; Genomic_DNA.
DR EMBL; X53305; CAA37391.1; -; mRNA.
DR EMBL; Z11566; CAA77660.1; -; mRNA.
DR EMBL; X94912; CAA64398.1; -; Genomic_DNA.
DR EMBL; AK303692; BAH14020.1; -; mRNA.
DR EMBL; AK311801; BAG34744.1; -; mRNA.
DR EMBL; AL033528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07854.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07855.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07856.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07857.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07858.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07859.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07860.1; -; Genomic_DNA.
DR EMBL; BC082228; AAH82228.1; -; mRNA.
DR CCDS; CCDS269.1; -. [P16949-1]
DR CCDS; CCDS44090.1; -. [P16949-2]
DR PIR; A40936; A40936.
DR RefSeq; NP_001138926.1; NM_001145454.2. [P16949-2]
DR RefSeq; NP_005554.1; NM_005563.3. [P16949-1]
DR RefSeq; NP_981944.1; NM_203399.1. [P16949-1]
DR RefSeq; NP_981946.1; NM_203401.1. [P16949-1]
DR AlphaFoldDB; P16949; -.
DR SMR; P16949; -.
DR BioGRID; 110119; 130.
DR IntAct; P16949; 30.
DR MINT; P16949; -.
DR STRING; 9606.ENSP00000410452; -.
DR ChEMBL; CHEMBL3879843; -.
DR GlyGen; P16949; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P16949; -.
DR PhosphoSitePlus; P16949; -.
DR SwissPalm; P16949; -.
DR BioMuta; STMN1; -.
DR DMDM; 134973; -.
DR DOSAC-COBS-2DPAGE; P16949; -.
DR REPRODUCTION-2DPAGE; IPI00479997; -.
DR SWISS-2DPAGE; P16949; -.
DR UCD-2DPAGE; P16949; -.
DR CPTAC; CPTAC-1009; -.
DR CPTAC; CPTAC-1010; -.
DR CPTAC; CPTAC-1368; -.
DR EPD; P16949; -.
DR jPOST; P16949; -.
DR MassIVE; P16949; -.
DR MaxQB; P16949; -.
DR PaxDb; P16949; -.
DR PeptideAtlas; P16949; -.
DR PRIDE; P16949; -.
DR ProteomicsDB; 53402; -. [P16949-1]
DR ProteomicsDB; 53403; -. [P16949-2]
DR TopDownProteomics; P16949-1; -. [P16949-1]
DR TopDownProteomics; P16949-2; -. [P16949-2]
DR Antibodypedia; 4112; 1482 antibodies from 46 providers.
DR DNASU; 3925; -.
DR Ensembl; ENST00000357865.6; ENSP00000350531.2; ENSG00000117632.23. [P16949-1]
DR Ensembl; ENST00000374291.5; ENSP00000363409.1; ENSG00000117632.23. [P16949-1]
DR Ensembl; ENST00000399728.5; ENSP00000382633.1; ENSG00000117632.23. [P16949-1]
DR Ensembl; ENST00000426559.6; ENSP00000410452.2; ENSG00000117632.23. [P16949-2]
DR Ensembl; ENST00000455785.7; ENSP00000387858.2; ENSG00000117632.23. [P16949-1]
DR GeneID; 3925; -.
DR KEGG; hsa:3925; -.
DR MANE-Select; ENST00000455785.7; ENSP00000387858.2; NM_005563.4; NP_005554.1.
DR UCSC; uc001bkz.4; human. [P16949-1]
DR CTD; 3925; -.
DR DisGeNET; 3925; -.
DR GeneCards; STMN1; -.
DR HGNC; HGNC:6510; STMN1.
DR HPA; ENSG00000117632; Tissue enhanced (brain, lymphoid tissue).
DR MIM; 151442; gene.
DR neXtProt; NX_P16949; -.
DR OpenTargets; ENSG00000117632; -.
DR PharmGKB; PA35491; -.
DR VEuPathDB; HostDB:ENSG00000117632; -.
DR eggNOG; KOG1280; Eukaryota.
DR GeneTree; ENSGT01030000234597; -.
DR HOGENOM; CLU_1562320_0_0_1; -.
DR InParanoid; P16949; -.
DR OMA; MAFELVF; -.
DR OrthoDB; 1381987at2759; -.
DR PhylomeDB; P16949; -.
DR TreeFam; TF326935; -.
DR PathwayCommons; P16949; -.
DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
DR SignaLink; P16949; -.
DR SIGNOR; P16949; -.
DR BioGRID-ORCS; 3925; 23 hits in 1090 CRISPR screens.
DR ChiTaRS; STMN1; human.
DR GeneWiki; Stathmin; -.
DR GenomeRNAi; 3925; -.
DR Pharos; P16949; Tbio.
DR PRO; PR:P16949; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P16949; protein.
DR Bgee; ENSG00000117632; Expressed in cortical plate and 177 other tissues.
DR ExpressionAtlas; P16949; baseline and differential.
DR Genevisible; P16949; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0015631; F:tubulin binding; IDA:MGI.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0061436; P:establishment of skin barrier; IMP:CAFA.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IMP:CAFA.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0007019; P:microtubule depolymerization; IDA:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IDA:MGI.
DR GO; GO:1905098; P:negative regulation of guanyl-nucleotide exchange factor activity; IMP:CAFA.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IMP:CAFA.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:CAFA.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:CAFA.
DR GO; GO:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; IMP:CAFA.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IMP:CAFA.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR DisProt; DP00174; -.
DR InterPro; IPR030514; Stathmin_CS.
DR InterPro; IPR000956; Stathmin_fam.
DR InterPro; IPR036002; Stathmin_sf.
DR PANTHER; PTHR10104; PTHR10104; 1.
DR Pfam; PF00836; Stathmin; 1.
DR PIRSF; PIRSF002285; Stathmin; 1.
DR PRINTS; PR00345; STATHMIN.
DR SUPFAM; SSF101494; SSF101494; 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; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Methylation; Microtubule; Neurogenesis; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1737801,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..149
FT /note="Stathmin"
FT /id="PRO_0000182389"
FT DOMAIN 4..145
FT /note="SLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00998"
FT REGION 121..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 41..140
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:1737801,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8125092,
FT ECO:0000269|PubMed:8245003, ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 25
FT /note="Phosphoserine; by CDK1, MAPK1 and MAPK3"
FT /evidence="ECO:0000269|PubMed:1737801,
FT ECO:0000269|PubMed:8125092, ECO:0000269|PubMed:8245003,
FT ECO:0000269|PubMed:8325880, ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17693683,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 29
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 38
FT /note="Phosphoserine; by CDK1, MAPK1 and MAPK3"
FT /evidence="ECO:0000269|PubMed:1737801,
FT ECO:0000269|PubMed:8125092, ECO:0000269|PubMed:8245003,
FT ECO:0000269|PubMed:8325880, ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 63
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 127..149
FT /note="DKHIEEVRKNKESKDPADETEAD -> MYFWTHGPGAHPAQISAEQSCLHSV
FT PALCPALGLQSALITWSDLSHHH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041377"
SQ SEQUENCE 149 AA; 17303 MW; 316426F60DABCD01 CRC64;
MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER
RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL
ERLREKDKHI EEVRKNKESK DPADETEAD
