Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Stathmin  

UniProtKB / Swiss-Prot ID :  STMN1_MOUSE

Gene Name (Synonyms) : 
Stmn1, Lag, Lap18, Pr22  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasm, cytoskeleton. 

Protein 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. 

Protein Sequence MASSDIQVKELEKRASGQAFELILSPRSKESVPDFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLK...
Predicted Secondary Structure CCCCCHHHHHHHHHCCCCEEEEEECCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
4Phosphoserine-MASSDIQV
-CCCCCHHH
29.24Phosphositeplus
Link-
16PhosphoserineEKRASGQAF
HHHCCCCEE
35.16Phosphositeplus
Link-
16PhosphoserineEKRASGQAF
HHHCCCCEE
35.16SysPTM
Link-
16Phosphoserine (PKA_group)EKRASGQAF
HHHCCCCEE
35.16PhosphoELM
Link-
16Phosphoserine; by PKA.EKRASGQAF
HHHCCCCEE
35.16UniProtKB
Link-
25PhosphoserineELILSPRSK
EEEECCCCC
15.98Phosphositeplus
Link-
25PhosphoserineELILSPRSK
EEEECCCCC
15.98SysPTM
Link-
25Phosphoserine (CDK_group)ELILSPRSK
EEEECCCCC
15.98PhosphoELM
Link-
25Phosphoserine; by CDK1, MAPK1 and MAPK3.ELILSPRSK
EEEECCCCC
15.98UniProtKB
Link-
28PhosphoserineLSPRSKESV
ECCCCCCCC
44.13Phosphositeplus
Link-
31PhosphoserineRSKESVPDF
CCCCCCCCC
42.56Phosphositeplus
Link-
34Caspase cleavage aspartic acidESVPDFPLS
CCCCCCCCC
56.49Phosphositeplus
Link-
38PhosphoserineDFPLSPPKK
CCCCCCCCC
39.12Phosphositeplus
Link-
38PhosphoserineDFPLSPPKK
CCCCCCCCC
39.12SysPTM
Link-
38Phosphoserine (CDK_group)DFPLSPPKK
CCCCCCCCC
39.12PhosphoELM
Link-
38Phosphoserine; by CDK1, MAPK1 and MAPK3.DFPLSPPKK
CCCCCCCCC
39.12UniProtKB
Link-
46PhosphoserineKKDLSLEEI
CCCCCHHHH
43.82PhosphoELM
Link-
46PhosphoserineKKDLSLEEI
CCCCCHHHH
43.82Phosphositeplus
Link-
46Phosphoserine.KKDLSLEEI
CCCCCHHHH
43.82UniProtKB
Link-
63PhosphoserineERRKSHEAE
HHHHHHHHH
25.42Phosphositeplus
Link-
63PhosphoserineERRKSHEAE
HHHHHHHHH
25.42SysPTM
Link-
63Phosphoserine (PKA_group)ERRKSHEAE
HHHHHHHHH
25.42PhosphoELM
Link-
63Phosphoserine; by PKA.ERRKSHEAE
HHHHHHHHH
25.42UniProtKB
Link-
139PhosphoserineKNKESKDPA
CCCCCCCCC
43.92Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASSSPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASSSPECTROMETRY.
"Multiple phosphorylation of stathmin. Identification of four sitesphosphorylated in intact cells and in vitro by cyclic AMP-dependentprotein kinase and p34cdc2.";
Beretta L., Dobransky T., Sobel A.;
J. Biol. Chem. 268:20076-20084(1993).
Cited for: PHOSPHORYLATION AT SER-16; SER-25; SER-38 AND SER-63.
"Qualitative and quantitative analyses of protein phosphorylation innaive 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-38 AND SER-46,AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures