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_HUMAN

Gene Name (Synonyms) : 
STMN1, C1orf215, LAP18, OP18  

Species :  Homo sapiens (Human). 

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. Involved in the control of the learned and innate fear (By similarity). 

Protein Sequence MASSDIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLK...
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
Predicted 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
2N-acetylalanine.---MASSDI
---CCCCCH
20.10UniProtKB
Link-
9Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DIQVKELEK
CHHHHHHHH
39.96Phosphositeplus
Link-
9N6-acetyllysineDIQVKELEK
CHHHHHHHH
39.96HPRD
Link-
9N6-acetyllysineDIQVKELEK
CHHHHHHHH
39.96Phosphositeplus
Link-
9N6-acetyllysine.DIQVKELEK
CHHHHHHHH
39.96UniProtKB
Link-
16PhosphoserineEKRASGQAF
HHHCCCCEE
35.16HPRD
Link-
16PhosphoserineEKRASGQAF
HHHCCCCEE
35.16Phosphositeplus
Link-
16PhosphoserineEKRASGQAF
HHHCCCCEE
35.16SysPTM
Link-
16Phosphoserine (CSNK2A1)EKRASGQAF
HHHCCCCEE
35.16HPRD
Link-
16Phosphoserine (PAK1)EKRASGQAF
HHHCCCCEE
35.16PhosphoELM
Link-
16Phosphoserine (PRKACA)EKRASGQAF
HHHCCCCEE
35.16HPRD
Link-
16Phosphoserine.EKRASGQAF
HHHCCCCEE
35.16UniProtKB
Link-
25PhosphoserineELILSPRSK
EEEECCCCC
15.98HPRD
Link-
25PhosphoserineELILSPRSK
EEEECCCCC
15.98HPRD
Link-
25PhosphoserineELILSPRSK
EEEECCCCC
15.98Phosphositeplus
Link-
25PhosphoserineELILSPRSK
EEEECCCCC
15.98SysPTM
Link-
25Phosphoserine (CDK1)ELILSPRSK
EEEECCCCC
15.98HPRD
Link-
25Phosphoserine (CDK1)ELILSPRSK
EEEECCCCC
15.98HPRD
Link-
25Phosphoserine (MAPK3)ELILSPRSK
EEEECCCCC
15.98HPRD
Link-
25Phosphoserine (MAPK3)ELILSPRSK
EEEECCCCC
15.98HPRD
Link-
25Phosphoserine (MAPK_group;MAPK_group;MAPK_group;MAPK13)ELILSPRSK
EEEECCCCC
15.98PhosphoELM
Link-
25Phosphoserine; by CDK1, MAPK1 and MAPK3.ELILSPRSK
EEEECCCCC
15.98UniProtKB
Link-
28PhosphoserineLSPRSKESV
ECCCCCCCC
44.13HPRD
Link-
28PhosphoserineLSPRSKESV
ECCCCCCCC
44.13PhosphoELM
Link-
28PhosphoserineLSPRSKESV
ECCCCCCCC
44.13Phosphositeplus
Link-
28Phosphoserine.LSPRSKESV
ECCCCCCCC
44.13UniProtKB
Link-
29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SPRSKESVP
CCCCCCCCC
56.11Phosphositeplus
Link-
29N6-acetyllysineSPRSKESVP
CCCCCCCCC
56.11Phosphositeplus
Link-
31PhosphoserineRSKESVPEF
CCCCCCCCC
46.86HPRD
Link-
31PhosphoserineRSKESVPEF
CCCCCCCCC
46.86Phosphositeplus
Link-
38PhosphoserineEFPLSPPKK
CCCCCCCCC
39.12HPRD
Link-
38PhosphoserineEFPLSPPKK
CCCCCCCCC
39.12HPRD
Link-
38PhosphoserineEFPLSPPKK
CCCCCCCCC
39.12Phosphositeplus
Link-
38PhosphoserineEFPLSPPKK
CCCCCCCCC
39.12SysPTM
Link-
38Phosphoserine (CDK1)EFPLSPPKK
CCCCCCCCC
39.12HPRD
Link-
38Phosphoserine (CDK1)EFPLSPPKK
CCCCCCCCC
39.12HPRD
Link-
38Phosphoserine (CDK_group;MAPK_group;MAPK_group;MAPK13)EFPLSPPKK
CCCCCCCCC
39.12PhosphoELM
Link-
38Phosphoserine; by CDK1, MAPK1 and MAPK3.EFPLSPPKK
CCCCCCCCC
39.12UniProtKB
Link-
46PhosphoserineKKDLSLEEI
CCCCCHHHH
43.82HPRD
Link-
46PhosphoserineKKDLSLEEI
CCCCCHHHH
43.82Phosphositeplus
Link-
52Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EEIQKKLEA
HHHHHHHHH
66.06Phosphositeplus
Link-
63PhosphoserineERRKSHEAE
HHHHHHHHH
25.42HPRD
Link-
63PhosphoserineERRKSHEAE
HHHHHHHHH
25.42Phosphositeplus
Link-
63Phosphoserine (CSNK2A1)ERRKSHEAE
HHHHHHHHH
25.42HPRD
Link-
63Phosphoserine (PKA_group;PKA_group)ERRKSHEAE
HHHHHHHHH
25.42PhosphoELM
Link-
63Phosphoserine (PRKACA)ERRKSHEAE
HHHHHHHHH
25.42HPRD
Link-
63Phosphoserine; by PKA.ERRKSHEAE
HHHHHHHHH
25.42UniProtKB
Link-
70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AEVLKQLAE
HHHHHHHHH
48.73Phosphositeplus
Link-
80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)REHEKEVLQ
HHHHHHHHH
55.84Phosphositeplus
Link-
80N6-acetyllysineREHEKEVLQ
HHHHHHHHH
55.84HPRD
Link-
80N6-acetyllysineREHEKEVLQ
HHHHHHHHH
55.84Phosphositeplus
Link-
80N6-acetyllysine.REHEKEVLQ
HHHHHHHHH
55.84UniProtKB
Link-
85Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EVLQKAIEE
HHHHHHHHC
47.36Phosphositeplus
Link-
95Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NNFSKMAEE
CCHHHHHHH
37.68Phosphositeplus
Link-
95N6-acetyllysineNNFSKMAEE
CCHHHHHHH
37.68HPRD
Link-
95N6-acetyllysineNNFSKMAEE
CCHHHHHHH
37.68Phosphositeplus
Link-
95N6-acetyllysine.NNFSKMAEE
CCHHHHHHH
37.68UniProtKB
Link-
100N6-acetyllysineMAEEKLTHK
HHHHHHHHH
50.63HPRD
Link-
100N6-acetyllysineMAEEKLTHK
HHHHHHHHH
50.63Phosphositeplus
Link-
100N6-acetyllysine.MAEEKLTHK
HHHHHHHHH
50.63UniProtKB
Link-
102PhosphothreonineEEKLTHKME
HHHHHHHHH
30.44HPRD
Link-
102PhosphothreonineEEKLTHKME
HHHHHHHHH
30.44Phosphositeplus
Link-
119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QMAAKLERL
HHHHHHHHH
41.15Phosphositeplus
Link-
119N6-acetyllysineQMAAKLERL
HHHHHHHHH
41.15HPRD
Link-
119N6-acetyllysineQMAAKLERL
HHHHHHHHH
41.15Phosphositeplus
Link-
119N6-acetyllysine.QMAAKLERL
HHHHHHHHH
41.15UniProtKB
Link-
128N6-acetyllysineREKDKHIEE
HHHHHHHHH
58.51HPRD
Link-
128N6-acetyllysineREKDKHIEE
HHHHHHHHH
58.51Phosphositeplus
Link-
128N6-acetyllysine.REKDKHIEE
HHHHHHHHH
58.51UniProtKB
Link-
140Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NKESKDPAD
CCCCCCCCC
69.67Phosphositeplus
Link-
146PhosphothreoninePADETEAD
CCCCCCCC
36.70HPRD
Link-
146PhosphothreoninePADETEAD
CCCCCCCC
36.70PhosphoELM
Link-
146PhosphothreoninePADETEAD
CCCCCCCC
36.70Phosphositeplus
Link-
146Phosphothreonine.PADETEAD
CCCCCCCC
36.70UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
UBQL4_HUMANphysical interactionMINT-2860477MINT16713569
CDN1B_HUMANphysical interactionEBI-1006412
intact15652749
GRP78_HUMANin vitro
yeast 2-hybrid
HPRD:01047HPRD10197448
7724523
UBQL4_HUMANyeast 2-hybridHPRD:01047HPRD16713569
STAT3_HUMANin vitro
in vivo
HPRD:01047HPRD16401721
MK03_HUMANENSP00000236291STRING
MK03_HUMANENSP00000236291STRING
CDC2_HUMANENSP00000236291STRING
CDC2_HUMANENSP00000236291STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Analysis of phosphoprotein p19 by liquid chromatography/massspectrometry. Identification of two proline-directed serinephosphorylation sites and a blocked amino terminus.";
Labdon J.E., Nieves E., Schubart U.K.;
J. Biol. Chem. 267:3506-3513(1992).
Cited for: ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-25 AND SER-38, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-16; SER-25 AND SER-38, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-80; LYS-95; LYS-100;LYS-119 AND LYS-128, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Analysis of phosphoprotein p19 by liquid chromatography/massspectrometry. Identification of two proline-directed serinephosphorylation sites and a blocked amino terminus.";
Labdon J.E., Nieves E., Schubart U.K.;
J. Biol. Chem. 267:3506-3513(1992).
Cited for: ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-25 AND SER-38, AND MASSSPECTROMETRY.
"Serine 25 of oncoprotein 18 is a major cytosolic target for themitogen-activated protein kinase.";
Marklund U., Brattsand G., Shingler V., Gullberg M.;
J. Biol. Chem. 268:15039-15047(1993).
Cited for: PHOSPHORYLATION AT SER-25 AND SER-38.
"Multiple signal transduction pathways induce phosphorylation ofserines 16, 25, and 38 of oncoprotein 18 in T lymphocytes.";
Marklund U., Brattsand G., Osterman O., Ohlsson P.-I., Gullberg M.;
J. Biol. Chem. 268:25671-25680(1993).
Cited for: PHOSPHORYLATION AT SER-16; SER-25 AND SER-38.
"Cell-cycle-regulated phosphorylation of oncoprotein 18 on Ser16,Ser25 and Ser38.";
Brattsand G., Marklund U., Nylander K., Roos G., Gullberg M.;
Eur. J. Biochem. 220:359-368(1994).
Cited for: PHOSPHORYLATION AT SER-16; SER-25 AND SER-38.
"Phosphorylation disrupts the central helix in Op18/stathmin andsuppresses binding to tubulin.";
Steinmetz M.O., Jahnke W., Towbin H., Garcia-Echeverria C., Voshol H.,Mueller D., van Oostrum J.;
EMBO Rep. 2:505-510(2001).
Cited for: EFFECT OF PHOSPHORYLATION AT SER-63 ON TUBULIN BINDING.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-38 ANDSER-63, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-38,AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-38 ANDSER-63, AND MASS SPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-38,AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-28;SER-38; SER-63 AND THR-146, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-25, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-38 ANDSER-63, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-16; SER-25 AND SER-38, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-38,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