STMN1_RAT
ID STMN1_RAT Reviewed; 149 AA.
AC P13668;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 158.
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=Pr22 protein;
DE AltName: Full=Prosolin;
DE AltName: Full=pp17;
GN Name=Stmn1; Synonyms=Lap18;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2745432; DOI=10.1016/s0021-9258(18)63830-x;
RA Doye V., Soubrier F., Bauw G., Boutterin M.-C., Beretta L., Koppel J.,
RA Vandekerckhove J., Sobel A.;
RT "A single cDNA encodes two isoforms of stathmin, a developmentally
RT regulated neuron-enriched phosphoprotein.";
RL J. Biol. Chem. 264:12134-12137(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2776625; DOI=10.1089/dna.1.1989.8.389;
RA Schubart U.K., Das Banerjee M., Eng J.;
RT "Homology between the cDNAs encoding phosphoprotein p19 and SCG10 reveals a
RT novel mammalian gene family preferentially expressed in developing brain.";
RL DNA 8:389-398(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hosoya H.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 15-28 AND 30-41, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP FUNCTION, AND PHOSPHORYLATION AT SER-16.
RX PubMed=16982419; DOI=10.1016/j.neuron.2006.07.020;
RA Watabe-Uchida M., John K.A., Janas J.A., Newey S.E., Van Aelst L.;
RT "The Rac activator DOCK7 regulates neuronal polarity through local
RT phosphorylation of stathmin/Op18.";
RL Neuron 51:727-739(2006).
RN [7]
RP ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-25 AND SER-38, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-38 AND
RP SER-63, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in the regulation of the microtubule (MT) filament
CC system by destabilizing microtubules. Prevents assembly and promotes
CC disassembly of microtubules (By similarity). Its phosphorylation at
CC Ser-16 may be required for axon formation during neurogenesis. Involved
CC in the control of the learned and innate fear (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:16982419}.
CC -!- SUBUNIT: Binds to two alpha/beta-tubulin heterodimers. Interacts with
CC KIST (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
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 (By similarity). Phosphorylation at Ser-16 is higher in the developing
CC axons from hippocampal neurons and seems to be required for neuron
CC polarization. {ECO:0000250, ECO:0000269|PubMed:16982419,
CC ECO:0000269|Ref.7}.
CC -!- SIMILARITY: Belongs to the stathmin family. {ECO:0000305}.
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DR EMBL; J04979; AAA42184.1; -; mRNA.
DR EMBL; M27876; AAA81570.1; -; mRNA.
DR EMBL; X94914; CAA64400.1; -; mRNA.
DR EMBL; BC062234; AAH62234.1; -; mRNA.
DR PIR; A34294; A34294.
DR RefSeq; NP_058862.1; NM_017166.1.
DR RefSeq; XP_006239185.1; XM_006239123.3.
DR RefSeq; XP_017448691.1; XM_017593202.1.
DR AlphaFoldDB; P13668; -.
DR SMR; P13668; -.
DR BioGRID; 247991; 1.
DR IntAct; P13668; 2.
DR STRING; 10116.ENSRNOP00000022574; -.
DR iPTMnet; P13668; -.
DR PhosphoSitePlus; P13668; -.
DR World-2DPAGE; 0004:P13668; -.
DR jPOST; P13668; -.
DR PaxDb; P13668; -.
DR PRIDE; P13668; -.
DR GeneID; 29332; -.
DR KEGG; rno:29332; -.
DR UCSC; RGD:2992; rat.
DR CTD; 3925; -.
DR RGD; 2992; Stmn1.
DR VEuPathDB; HostDB:ENSRNOG00000016810; -.
DR eggNOG; KOG1280; Eukaryota.
DR InParanoid; P13668; -.
DR OMA; MAFELVF; -.
DR OrthoDB; 1381987at2759; -.
DR PhylomeDB; P13668; -.
DR TreeFam; TF326935; -.
DR PRO; PR:P13668; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000016810; Expressed in cerebellum and 19 other tissues.
DR ExpressionAtlas; P13668; baseline and differential.
DR Genevisible; P13668; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0061436; P:establishment of skin barrier; ISO:RGD.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:RGD.
DR GO; GO:0007019; P:microtubule depolymerization; ISO:RGD.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:RGD.
DR GO; GO:0007052; P:mitotic spindle organization; ISO:RGD.
DR GO; GO:1905098; P:negative regulation of guanyl-nucleotide exchange factor activity; ISO:RGD.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISO:RGD.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISO:RGD.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISO:RGD.
DR GO; GO:0009615; P:response to virus; ISO:RGD.
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; 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:0000269|Ref.7"
FT CHAIN 2..149
FT /note="Stathmin"
FT /id="PRO_0000182392"
FT DOMAIN 4..145
FT /note="SLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00998"
FT REGION 104..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|Ref.7"
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"
FT /evidence="ECO:0000269|PubMed:16982419,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 25
FT /note="Phosphoserine; by CDK1, MAPK1 and MAPK3"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22673903"
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|Ref.7, ECO:0007744|PubMed:22673903"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0000250|UniProtKB:P16949"
SQ SEQUENCE 149 AA; 17288 MW; 316426E0617BCD01 CRC64;
MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER
RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL
ERLREKDKHV EEVRKNKESK DPADETEAD
