dbPTM

STMN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STMN1_HUMAN
UniProt AC	P16949
Protein Name	Stathmin
Gene Name	STMN1
Organism	Homo sapiens (Human).
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. Involved in the control of the learned and innate fear (By similarity)..
Protein Sequence	MASSDIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREKDKHIEEVRKNKESKDPADETEAD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASSDIQVK ------CCCCCCCHH	20.10	19413330
3	Phosphorylation	-----MASSDIQVKE -----CCCCCCCHHH	27.52	25159151
4	Phosphorylation	----MASSDIQVKEL ----CCCCCCCHHHH	29.24	25159151
9	Acetylation	ASSDIQVKELEKRAS CCCCCCHHHHHHHHC	39.96	19608861
9	Ubiquitination	ASSDIQVKELEKRAS CCCCCCHHHHHHHHC	39.96	21890473
9	Ubiquitination	ASSDIQVKELEKRAS CCCCCCHHHHHHHHC	39.96	21890473
9 (in isoform 2)	Ubiquitination	-	39.96	-
14	Methylation	QVKELEKRASGQAFE CHHHHHHHHCCCCCH	25.30	115917961
16	Phosphorylation	KELEKRASGQAFELI HHHHHHHCCCCCHHH	35.16	19664994
25	Phosphorylation	QAFELILSPRSKESV CCCHHHCCCCCCCCC	15.98	19664994
27	Methylation	FELILSPRSKESVPE CHHHCCCCCCCCCCC	57.91	115917965
28	Phosphorylation	ELILSPRSKESVPEF HHHCCCCCCCCCCCC	44.13	30266825
28	O-linked_Glycosylation	ELILSPRSKESVPEF HHHCCCCCCCCCCCC	44.13	28657654
29 (in isoform 2)	Ubiquitination	-	56.11	-
29	Ubiquitination	LILSPRSKESVPEFP HHCCCCCCCCCCCCC	56.11	21906983
29	Methylation	LILSPRSKESVPEFP HHCCCCCCCCCCCCC	56.11	24129315
29	Acetylation	LILSPRSKESVPEFP HHCCCCCCCCCCCCC	56.11	20167786
31	Phosphorylation	LSPRSKESVPEFPLS CCCCCCCCCCCCCCC	46.86	30266825
31	O-linked_Glycosylation	LSPRSKESVPEFPLS CCCCCCCCCCCCCCC	46.86	28657654
38	Phosphorylation	SVPEFPLSPPKKKDL CCCCCCCCCCCCCCC	39.12	19664994
41	Ubiquitination	EFPLSPPKKKDLSLE CCCCCCCCCCCCCHH	75.69	-
42 (in isoform 2)	Ubiquitination	-	58.24	-
43 (in isoform 2)	Ubiquitination	-	70.77	-
43	Ubiquitination	PLSPPKKKDLSLEEI CCCCCCCCCCCHHHH	70.77	-
46	Phosphorylation	PPKKKDLSLEEIQKK CCCCCCCCHHHHHHH	43.82	19664994
52	Ubiquitination	LSLEEIQKKLEAAEE CCHHHHHHHHHHHHH	66.06	-
52 (in isoform 2)	Ubiquitination	-	66.06	-
52	Succinylation	LSLEEIQKKLEAAEE CCHHHHHHHHHHHHH	66.06	23954790
52	Acetylation	LSLEEIQKKLEAAEE CCHHHHHHHHHHHHH	66.06	23954790
53	Acetylation	SLEEIQKKLEAAEER CHHHHHHHHHHHHHH	34.87	23749302
53 (in isoform 2)	Ubiquitination	-	34.87	-
53	Ubiquitination	SLEEIQKKLEAAEER CHHHHHHHHHHHHHH	34.87	-
62	Ubiquitination	EAAEERRKSHEAEVL HHHHHHHHHHHHHHH	63.49	-
63	Phosphorylation	AAEERRKSHEAEVLK HHHHHHHHHHHHHHH	25.42	29255136
70	Acetylation	SHEAEVLKQLAEKRE HHHHHHHHHHHHHHH	48.73	23236377
70 (in isoform 2)	Ubiquitination	-	48.73	-
70	Ubiquitination	SHEAEVLKQLAEKRE HHHHHHHHHHHHHHH	48.73	21890473
70	Ubiquitination	SHEAEVLKQLAEKRE HHHHHHHHHHHHHHH	48.73	21890473
75	Ubiquitination	VLKQLAEKREHEKEV HHHHHHHHHHHHHHH	58.44	-
80 (in isoform 2)	Ubiquitination	-	55.84	-
80	Ubiquitination	AEKREHEKEVLQKAI HHHHHHHHHHHHHHH	55.84	21890473
80	Ubiquitination	AEKREHEKEVLQKAI HHHHHHHHHHHHHHH	55.84	21890473
80	Acetylation	AEKREHEKEVLQKAI HHHHHHHHHHHHHHH	55.84	23749302
85 (in isoform 2)	Ubiquitination	-	47.36	-
85	Ubiquitination	HEKEVLQKAIEENNN HHHHHHHHHHHHCCC	47.36	21906983
94	Phosphorylation	IEENNNFSKMAEEKL HHHCCCHHHHHHHHH	24.52	20873877
95	Ubiquitination	EENNNFSKMAEEKLT HHCCCHHHHHHHHHH	37.68	19608861
95	Acetylation	EENNNFSKMAEEKLT HHCCCHHHHHHHHHH	37.68	19608861
100	Ubiquitination	FSKMAEEKLTHKMEA HHHHHHHHHHHHHHH	50.63	19608861
100	Acetylation	FSKMAEEKLTHKMEA HHHHHHHHHHHHHHH	50.63	19608861
100 (in isoform 2)	Ubiquitination	-	50.63	-
102	Phosphorylation	KMAEEKLTHKMEANK HHHHHHHHHHHHHCH	30.44	19664994
104	Ubiquitination	AEEKLTHKMEANKEN HHHHHHHHHHHCHHH	32.95	-
104	Acetylation	AEEKLTHKMEANKEN HHHHHHHHHHHCHHH	32.95	25953088
109	Acetylation	THKMEANKENREAQM HHHHHHCHHHHHHHH	64.51	30583515
119	Acetylation	REAQMAAKLERLREK HHHHHHHHHHHHHHH	41.15	19608861
119 (in isoform 2)	Ubiquitination	-	41.15	-
119	Ubiquitination	REAQMAAKLERLREK HHHHHHHHHHHHHHH	41.15	19608861
126	Acetylation	KLERLREKDKHIEEV HHHHHHHHHHHHHHH	66.69	25953088
128	Ubiquitination	ERLREKDKHIEEVRK HHHHHHHHHHHHHHH	58.51	-
128	Acetylation	ERLREKDKHIEEVRK HHHHHHHHHHHHHHH	58.51	23749302
134	Methylation	DKHIEEVRKNKESKD HHHHHHHHHCHHCCC	39.86	115917957
137	Ubiquitination	IEEVRKNKESKDPAD HHHHHHCHHCCCCCC	67.41	-
137	Acetylation	IEEVRKNKESKDPAD HHHHHHCHHCCCCCC	67.41	23749302
139	Phosphorylation	EVRKNKESKDPADET HHHHCHHCCCCCCCC	43.92	29496963
140	Acetylation	VRKNKESKDPADETE HHHCHHCCCCCCCCC	69.67	23749302
140	Ubiquitination	VRKNKESKDPADETE HHHCHHCCCCCCCCC	69.67	21906983
146	Phosphorylation	SKDPADETEAD---- CCCCCCCCCCC----	36.70	30576142

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	PAK1	Q13153	PSP
16	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
16	S	Phosphorylation	Kinase	PKACA	P17612	PSP
16	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
16	S	Phosphorylation	Kinase	CAMK2B	Q13554	PSP
16	S	Phosphorylation	Kinase	CAMK2G	Q13555	GPS
16	S	Phosphorylation	Kinase	CAMK4	Q16566	PSP
16	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
16	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
25	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
25	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
25	S	Phosphorylation	Kinase	MAPK13	O15264	GPS
25	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
25	S	Phosphorylation	Kinase	ERK1	P27361	PSP
25	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
25	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
25	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
25	S	Phosphorylation	Kinase	CDK2	P24941	PSP
38	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
38	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
38	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
38	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
38	S	Phosphorylation	Kinase	ERK1	P27361	PSP
38	S	Phosphorylation	Kinase	KIS	P97343	PSP
38	S	Phosphorylation	Kinase	UHMK1	Q8TAS1	GPS
38	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
38	S	Phosphorylation	Kinase	MAPK13	O15264	GPS
38	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
38	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
38	S	Phosphorylation	Kinase	CDK2	P24941	PSP
38	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
63	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
63	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
63	S	Phosphorylation	Kinase	PKA	-	Uniprot
63	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
63	S	Phosphorylation	Kinase	PKACA	P17612	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	RLIM	Q9NVW2	PMID:24686088

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
16	S	Phosphorylation	8245003
Phosphorylation at Ser-16 seems to be required for neuron polarization (By similarity).
63	S	Phosphorylation	11415983
Phosphorylation at Ser-63 reduces tubulin binding 10-fold and suppresses the MT polymerization inhibition activity.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRP78_MOUSE	Hspa5	physical	7724523
UHMK1_MOUSE	Uhmk1	physical	7724523
RBCC1_MOUSE	Rb1cc1	physical	7724523
HSP7C_HUMAN	HSPA8	physical	10197448
TPM2_HUMAN	TPM2	physical	22939629
CDN1B_HUMAN	CDKN1B	physical	15652749
RNF12_HUMAN	RLIM	physical	24686088
SESD1_HUMAN	SESTD1	physical	25416956
SIVA_HUMAN	SIVA1	physical	21768358
AHNK_HUMAN	AHNAK	physical	26344197
DUT_HUMAN	DUT	physical	26344197
JUPI1_HUMAN	HN1	physical	26344197
JUPI2_HUMAN	HN1L	physical	26344197
IMPA2_HUMAN	IMPA2	physical	26344197
MYO1E_HUMAN	MYO1E	physical	26344197
NUDC2_HUMAN	NUDCD2	physical	26344197
PFD2_HUMAN	PFDN2	physical	26344197
RAB1A_HUMAN	RAB1A	physical	26344197
TPM2_HUMAN	TPM2	physical	26344197
TPM3_HUMAN	TPM3	physical	26344197
TIF1B_HUMAN	TRIM28	physical	26344197
TYSY_HUMAN	TYMS	physical	26344197
UBQL1_HUMAN	UBQLN1	physical	26344197
PIWL1_HUMAN	PIWIL1	physical	26317901
RNF12_HUMAN	RLIM	physical	26317901
TBA1B_HUMAN	TUBA1B	physical	26317901
TBB3_HUMAN	TUBB3	physical	26317901
FANCC_HUMAN	FANCC	physical	26466335

Drug and Disease Associations

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

Regulatory Network of STMN1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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.	19413330 [Abstract]
"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.	1737801 [Abstract]
"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.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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.	19690332 [Abstract]
"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.	19413330 [Abstract]
"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.	18669648 [Abstract]
"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.	18220336 [Abstract]
"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.	18187866 [Abstract]
"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.	17287340 [Abstract]
"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.	17693683 [Abstract]
"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.	17924679 [Abstract]
"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.	16964243 [Abstract]
"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.	17081983 [Abstract]
"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.	16094384 [Abstract]
"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.	16083285 [Abstract]
"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.	11415983 [Abstract]
"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.	8125092 [Abstract]
"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.	8245003 [Abstract]
"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.	8325880 [Abstract]
"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.	1737801 [Abstract]

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