Skip Header

Contribute Send feedback
Read comments (?) or add your own

P54227 (STMN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Stathmin
Alternative name(s):
Leukemia-associated gene protein
Leukemia-associated phosphoprotein p18
Metablastin
Oncoprotein 18
Short name=Op18
Phosphoprotein p19
Short name=pp19
Prosolin
Protein Pr22
pp17
Gene names
Name:Stmn1
Synonyms:Lag, Lap18, Pr22
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Phosphorylation at Ser-16 may be required for axon formation during neurogenesis By similarity. Involved in the control of the learned and innate fear. Ref.8

Subunit structure

Binds to two alpha/beta-tubulin heterodimers. Interacts with KIST. Ref.7

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Highly expressed in the lateral nucleus of the amygdala. Ref.8

Post-translational modification

Many different phosphorylated forms are observed depending on specific combinations among the sites which can be phosphorylated. MAPK is responsible for the phosphorylation of stathmin in response to NGF Probable. Phosphorylation at Ser-16 seems to be required for neuron polarization By similarity. Ref.6 Ref.9 Ref.10 Ref.11 Ref.12

Disruption phenotype

Mice show deficits in spike-timing-dependent long-term potentiation, exhibit decreased memory in amygdala-dependent fear conditioning and fail to recognize danger in innately aversive environements. Ref.8

Sequence similarities

Belongs to the stathmin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cdkn1bP464142EBI-1006438,EBI-1005742

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 149148Stathmin
PRO_0000182390

Regions

Coiled coil41 – 140100 Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue91N6-acetyllysine By similarity
Modified residue161Phosphoserine; by PKA Ref.6 Ref.12
Modified residue251Phosphoserine; by CDK1, MAPK1 and MAPK3 Ref.6 Ref.9
Modified residue281Phosphoserine By similarity
Modified residue381Phosphoserine; by CDK1, MAPK1 and MAPK3 Ref.6 Ref.9 Ref.11
Modified residue461Phosphoserine Ref.9
Modified residue631Phosphoserine; by PKA Ref.6 Ref.10
Modified residue801N6-acetyllysine By similarity
Modified residue951N6-acetyllysine By similarity
Modified residue1001N6-acetyllysine By similarity
Modified residue1191N6-acetyllysine By similarity
Modified residue1281N6-acetyllysine By similarity
Modified residue1461Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
P54227 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 616526E0A6667BDA

FASTA14917,274
        10         20         30         40         50         60 
MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPDFPLSPP KKKDLSLEEI QKKLEAAEER 

        70         80         90        100        110        120 
RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL 

       130        140 
ERLREKDKHV EEVRKNKESK DPADETEAD 

« Hide

References

« Hide 'large scale' references
[1]"Molecular diversity of the SCG10/stathmin gene family in the mouse."
Okazaki T., Yoshida B.N., Avraham K.B., Wang H., Wuenschell C.W., Jenkins N.A., Copeland N.G., Anderson D.J., Mori N.
Genomics 18:360-373(1993) [PubMed: 8288240] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Erratum
Okazaki T., Yoshida B.N., Avraham K.B., Wang H., Wuenschell C.W., Jenkins N.A., Copeland N.G., Anderson D.J., Mori N.
Genomics 21:298-298(1994)
[3]"Transcriptional and post-transcriptional regulation of pr22 (Op18) with proliferation control."
Hosoya H., Ishikawa K., Dohi N., Marunouchi T.
Cell Struct. Funct. 21:237-243(1996) [PubMed: 8906359] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: 129.
Tissue: Mammary gland and Retina.
[5]Lubec G., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 15-27, MASS SPECTROMETRY.
Tissue: Brain and Hippocampus.
[6]"Multiple phosphorylation of stathmin. Identification of four sites phosphorylated in intact cells and in vitro by cyclic AMP-dependent protein kinase and p34cdc2."
Beretta L., Dobransky T., Sobel A.
J. Biol. Chem. 268:20076-20084(1993) [PubMed: 8376365] [Abstract]
Cited for: PHOSPHORYLATION AT SER-16; SER-25; SER-38 AND SER-63.
[7]"Stathmin interaction with a putative kinase and coiled-coil-forming protein domains."
Maucuer A., Camonis J.H., Sobel A.
Proc. Natl. Acad. Sci. U.S.A. 92:3100-3104(1995) [PubMed: 7724523] [Abstract]
Cited for: INTERACTION WITH KIST.
Tissue: Embryo.
[8]"Stathmin, a gene enriched in the amygdala, controls both learned and innate fear."
Shumyatsky G.P., Malleret G., Shin R.-M., Takizawa S., Tully K., Tsvetkov E., Zakharenko S.S., Joseph J., Vronskaya S., Yin D., Schubart U.K., Kandel E.R., Bolshakov V.Y.
Cell 123:697-709(2005) [PubMed: 16286011] [Abstract]
Cited for: FUNCTION IN CONTROL OF FEAR, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[9]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-38 AND SER-46, MASS SPECTROMETRY.
Tissue: Brain cortex.
[10]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, MASS SPECTROMETRY.
Tissue: Melanoma.
[11]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, MASS SPECTROMETRY.
Tissue: Macrophage.
[12]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L20256 Genomic DNA. No translation available.
L20257 Genomic DNA. No translation available.
L20258 Genomic DNA. No translation available.
X94915 mRNA. Translation: CAA64401.1.
BC010581 mRNA. Translation: AAH10581.1.
BC031831 mRNA. Translation: AAH31831.1.
BC054396 mRNA. Translation: AAH54396.1.
IPIIPI00551236.
PIRB48917.
RefSeqNP_062615.1. NM_019641.4.
UniGeneMm.378957.

3D structure databases

ProteinModelPortalP54227.
SMRP54227. Positions 6-141.
ModBaseSearch...

Protein-protein interaction databases

IntActP54227. 2 interactions.
STRINGP54227.

PTM databases

PhosphoSiteP54227.

2D gel databases

REPRODUCTION-2DPAGEP54227.
UCD-2DPAGEP54227.

Proteomic databases

PRIDEP54227.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030636; ENSMUSP00000030636; ENSMUSG00000028832.
ENSMUST00000105868; ENSMUSP00000101494; ENSMUSG00000028832.
GeneID16765.
KEGGmmu:16765.

Organism-specific databases

CTD3925.
MGIMGI:96739. Stmn1.

Phylogenomic databases

eggNOGroNOG12776.
HOGENOMHBG444413.
HOVERGENHBG054037.
InParanoidP54227.
OMAKEAVPEF.
OrthoDBEOG46MBKT.
PhylomeDBP54227.

Gene expression databases

ArrayExpressP54227.
BgeeP54227.
CleanExMM_STMN1.
GenevestigatorP54227.
GermOnlineENSMUSG00000028832. Mus musculus.

Family and domain databases

InterProIPR000956. Stathmin.
[Graphical view]
KOK04381.
PANTHERPTHR10104. Stathmin. 1 hit.
PfamPF00836. Stathmin. 1 hit.
[Graphical view]
PIRSFPIRSF002285. Stathmin. 1 hit.
PRINTSPR00345. STATHMIN.
SUPFAMSSF101494. Stathmin. 1 hit.
PROSITEPS00563. STATHMIN_1. 1 hit.
PS01041. STATHMIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio290586.
SOURCESearch...

Entry information

Entry nameSTMN1_MOUSE
AccessionPrimary (citable) accession number: P54227
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families