dbPTM

STMN1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STMN1_MOUSE
UniProt AC	P54227
Protein Name	Stathmin
Gene Name	Stmn1
Organism	Mus musculus (Mouse).
Sequence Length	149
Subcellular Localization	Cytoplasm, cytoskeleton.
Protein Description	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	MASSDIQVKELEKRASGQAFELILSPRSKESVPDFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREKDKHVEEVRKNKESKDPADETEAD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASSDIQVK ------CCCCCCCHH	20.10	-
3	Phosphorylation	-----MASSDIQVKE -----CCCCCCCHHH	27.52	22006019
4	Phosphorylation	----MASSDIQVKEL ----CCCCCCCHHHH	29.24	27180971
9	Acetylation	ASSDIQVKELEKRAS CCCCCCHHHHHHHHC	39.96	22826441
16	Phosphorylation	KELEKRASGQAFELI HHHHHHHCCCCEEHH	35.16	20630875
25	Phosphorylation	QAFELILSPRSKESV CCEEHHCCCCCCCCC	15.98	20630875
28	Phosphorylation	ELILSPRSKESVPDF EHHCCCCCCCCCCCC	44.13	23527152
29	Methylation	LILSPRSKESVPDFP HHCCCCCCCCCCCCC	56.11	-
29	Ubiquitination	LILSPRSKESVPDFP HHCCCCCCCCCCCCC	56.11	22790023
31	Phosphorylation	LSPRSKESVPDFPLS CCCCCCCCCCCCCCC	42.56	24925903
38	Phosphorylation	SVPDFPLSPPKKKDL CCCCCCCCCCCCCCC	39.12	20630875
46	Phosphorylation	PPKKKDLSLEEIQKK CCCCCCCCHHHHHHH	43.82	25521595
52	Ubiquitination	LSLEEIQKKLEAAEE CCHHHHHHHHHHHHH	66.06	22790023
53	Acetylation	SLEEIQKKLEAAEER CHHHHHHHHHHHHHH	34.87	22826441
63	Phosphorylation	AAEERRKSHEAEVLK HHHHHHHHHHHHHHH	25.42	25521595
70	Acetylation	SHEAEVLKQLAEKRE HHHHHHHHHHHHHHH	48.73	22826441
85	Acetylation	HEKEVLQKAIEENNN HHHHHHHHHHHHCCC	47.36	22826441
95	Acetylation	EENNNFSKMAEEKLT HHCCCHHHHHHHHHH	37.68	22826441
95	Ubiquitination	EENNNFSKMAEEKLT HHCCCHHHHHHHHHH	37.68	-
100	Acetylation	FSKMAEEKLTHKMEA HHHHHHHHHHHHHHH	50.63	22826441
104	Ubiquitination	AEEKLTHKMEANKEN HHHHHHHHHHHCHHH	32.95	-
119	Ubiquitination	REAQMAAKLERLREK HHHHHHHHHHHHHHH	41.15	-
119	Acetylation	REAQMAAKLERLREK HHHHHHHHHHHHHHH	41.15	23806337
126	Ubiquitination	KLERLREKDKHVEEV HHHHHHHHHHHHHHH	66.69	-
128	Acetylation	ERLREKDKHVEEVRK HHHHHHHHHHHHHHH	61.69	23806337
139	Phosphorylation	EVRKNKESKDPADET HHHHCCCCCCCCCCC	43.92	25266776
140	Ubiquitination	VRKNKESKDPADETE HHHCCCCCCCCCCCC	69.67	-
146	Phosphorylation	SKDPADETEAD---- CCCCCCCCCCC----	36.70	29899451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
16	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
16	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
16	S	Phosphorylation	Kinase	CAMK2A	P11798	PSP
16	S	Phosphorylation	Kinase	PKA	-	Uniprot
16	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
25	S	Phosphorylation	Kinase	ERK2	P63085	PSP
25	S	Phosphorylation	Kinase	MAPK10	P53779	GPS
25	S	Phosphorylation	Kinase	MAPK9	P45984	GPS
25	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
25	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
25	S	Phosphorylation	Kinase	ERK1	Q63844	PSP
25	S	Phosphorylation	Kinase	ERK1	P27361	PSP
25	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
25	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
25	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot
38	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot
38	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
38	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
38	S	Phosphorylation	Kinase	MAPK10	P53779	GPS
38	S	Phosphorylation	Kinase	MAPK9	P45984	GPS
38	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
38	S	Phosphorylation	Kinase	MAPK3	Q63844	Uniprot
38	S	Phosphorylation	Kinase	ERK2	P63085	PSP
38	S	Phosphorylation	Kinase	CDK5	P49615	PSP
38	S	Phosphorylation	Kinase	CDK2	P97377	PSP
63	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
63	S	Phosphorylation	Kinase	PKA	-	Uniprot
63	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
63	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
16	S	Phosphorylation		8376365
Phosphorylation at Ser-16 seems to be required for neuron polarization (By similarity).

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of STMN1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDN1B_MOUSE	Cdkn1b	physical	15652749
APOB_HUMAN	APOB	physical	26496610
FMR1_HUMAN	FMR1	physical	26496610
TRIO_HUMAN	TRIO	physical	26496610
UPP1_HUMAN	UPP1	physical	26496610
TERA_HUMAN	VCP	physical	26496610
FXR1_HUMAN	FXR1	physical	26496610
CPSF5_HUMAN	NUDT21	physical	26496610
ERI3_HUMAN	ERI3	physical	26496610

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of STMN1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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.	19131326 [Abstract]
"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.	19144319 [Abstract]
"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.	19367708 [Abstract]
"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.	17114649 [Abstract]
"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.	8376365 [Abstract]

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