STMN2_MOUSE
ID STMN2_MOUSE Reviewed; 179 AA.
AC P55821;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Stathmin-2;
DE AltName: Full=Superior cervical ganglion-10 protein;
DE Short=Protein SCG10;
GN Name=Stmn2; Synonyms=Scg10, Scgn10, Stmb2;
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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16618812; DOI=10.1083/jcb.200511055;
RA Tararuk T., Ostman N., Li W., Bjorkblom B., Padzik A., Zdrojewska J.,
RA Hongisto V., Herdegen T., Konopka W., Courtney M.J., Coffey E.T.;
RT "JNK1 phosphorylation of SCG10 determines microtubule dynamics and
RT axodendritic length.";
RL J. Cell Biol. 173:265-277(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-62, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [6]
RP FUNCTION.
RX PubMed=21297631; DOI=10.1038/nn.2755;
RA Westerlund N., Zdrojewska J., Padzik A., Komulainen E., Bjorkblom B.,
RA Rannikko E., Tararuk T., Garcia-Frigola C., Sandholm J., Nguyen L.,
RA Kallunki T., Courtney M.J., Coffey E.T.;
RT "Phosphorylation of SCG10/stathmin-2 determines multipolar stage exit and
RT neuronal migration rate.";
RL Nat. Neurosci. 14:305-313(2011).
CC -!- FUNCTION: Regulator of microtubule stability. When phosphorylated by
CC MAPK8, stabilizes microtubules and consequently controls neurite length
CC in cortical neurons. In the developing brain, negatively regulates the
CC rate of exit from multipolar stage and retards radial migration from
CC the ventricular zone. {ECO:0000269|PubMed:21297631}.
CC -!- SUBUNIT: Interacts with ITM2C. Interacts with MAPK8. Interacts with
CC KIFBP. Interacts (via the N-terminal region) with CIB1 (via C-terminal
CC region); the interaction is direct, occurs in a calcium-dependent
CC manner and attenuates the neurite outgrowth inhibition of STMN2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16618812}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:16618812}. Cell
CC projection, growth cone {ECO:0000269|PubMed:16618812}. Cell projection,
CC axon {ECO:0000269|PubMed:16618812}. Membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC Endosome {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell projection,
CC lamellipodium {ECO:0000250}. Note=Colocalized with CIB1 in neurites of
CC developing hippocampal primary neurons. Colocalized with CIB1 in the
CC cell body, neuritis, growth cones of neurons and in neurites of
CC developing hippocampal primary neurons. Colocalized with CIB1 to the
CC leading edge of lamellipodia (By similarity). Associated with punctate
CC structures in the perinuclear cytoplasm, axons, and growth cones of
CC developing neurons. Exists in both soluble and membrane-bound forms. In
CC the developing brain, mostly cytosolic. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Neuron specific.
CC -!- DEVELOPMENTAL STAGE: At 15.5 dpc, mid to low expression throughout the
CC midbrain, with more prominent levels in the telencephalon, especially
CC in the intermediate zone, the midbrain roof, the olfactory epithelium,
CC the inferior colliculus, and the medulla oblongata. telencephalon
CC revealed concentrated (at protein level).
CC {ECO:0000269|PubMed:16618812}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated mostly by MAPK8, but also by MAPK9 and MAPK10 in
CC the developing brain cortex. {ECO:0000269|PubMed:16618812}.
CC -!- PTM: N-terminal palmitoylation promotes specific anchoring to the
CC cytosolic leaflet of Golgi membranes and subsequent vesicular
CC trafficking along dendrites and axons. Neuronal Stathmins are
CC substrates for palmitoyltransferases ZDHHC3, ZDHHC7 and ZDHHC15 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the stathmin family. {ECO:0000305}.
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DR EMBL; L20259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L20260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L20261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L20262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L20263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026538; AAH26538.1; -; mRNA.
DR CCDS; CCDS17231.1; -.
DR PIR; A48917; A48917.
DR RefSeq; NP_079561.1; NM_025285.2.
DR AlphaFoldDB; P55821; -.
DR SMR; P55821; -.
DR BioGRID; 203093; 6.
DR IntAct; P55821; 1.
DR MINT; P55821; -.
DR STRING; 10090.ENSMUSP00000029002; -.
DR iPTMnet; P55821; -.
DR PhosphoSitePlus; P55821; -.
DR EPD; P55821; -.
DR jPOST; P55821; -.
DR PaxDb; P55821; -.
DR PeptideAtlas; P55821; -.
DR PRIDE; P55821; -.
DR ProteomicsDB; 258641; -.
DR ABCD; P55821; 1 sequenced antibody.
DR Antibodypedia; 6337; 462 antibodies from 40 providers.
DR Ensembl; ENSMUST00000029002; ENSMUSP00000029002; ENSMUSG00000027500.
DR GeneID; 20257; -.
DR KEGG; mmu:20257; -.
DR UCSC; uc008oon.1; mouse.
DR CTD; 11075; -.
DR MGI; MGI:98241; Stmn2.
DR VEuPathDB; HostDB:ENSMUSG00000027500; -.
DR eggNOG; ENOG502RENQ; Eukaryota.
DR GeneTree; ENSGT01030000234597; -.
DR HOGENOM; CLU_102026_0_0_1; -.
DR InParanoid; P55821; -.
DR OMA; HMAAMME; -.
DR OrthoDB; 1381987at2759; -.
DR PhylomeDB; P55821; -.
DR TreeFam; TF326935; -.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 20257; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Stmn2; mouse.
DR PRO; PR:P55821; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P55821; protein.
DR Bgee; ENSMUSG00000027500; Expressed in embryonic brain and 255 other tissues.
DR ExpressionAtlas; P55821; baseline and differential.
DR Genevisible; P55821; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISO:MGI.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central.
DR InterPro; IPR026729; Stathmin-2.
DR InterPro; IPR030514; Stathmin_CS.
DR InterPro; IPR000956; Stathmin_fam.
DR InterPro; IPR036002; Stathmin_sf.
DR PANTHER; PTHR10104; PTHR10104; 1.
DR PANTHER; PTHR10104:SF18; PTHR10104:SF18; 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 Cell projection; Coiled coil; Cytoplasm; Endosome; Golgi apparatus;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..179
FT /note="Stathmin-2"
FT /id="PRO_0000182397"
FT DOMAIN 38..179
FT /note="SLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00998"
FT REGION 1..26
FT /note="Membrane attachment"
FT /evidence="ECO:0000255"
FT REGION 39..96
FT /note="Regulatory/phosphorylation domain"
FT /evidence="ECO:0000255"
FT COILED 75..179
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21818"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHU6, ECO:0000255"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16949, ECO:0000255"
FT LIPID 22
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 24
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 179 AA; 20828 MW; F9A258A1B57E620D CRC64;
MAKTAMAYKE KMKELSMLSL ICSCFYPEPR NINIYTYDDM EVKQINKRAS GQAFELILKP
PSPISEAPRT LASPKKKDLS LEEIQKKLEA AEERRKSQEA QVLKQLAEKR EHEREVLQKA
LEENNNFSKM AEEKLILKME QIKENREANL AAIIERLQEK ERHAAEVRRN KELQVELSG
