STMN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: STMN2_HUMAN
• UniProt AC: Q93045
• Protein Name: Stathmin-2
• Gene Name: STMN2
• Organism: Homo sapiens (Human).
• Sequence Length: 179
• Subcellular Localization: Cytoplasm. Cytoplasm, perinuclear region. Cell projection, growth cone. Membrane ; Peripheral membrane protein ; Cytoplasmic side . Cell projection, axon. Golgi apparatus. Endosome. Cell projection, lamellipodium. Associated with punctate structures
• Protein Description: Regulator of microtubule stability. When phosphorylated by MAPK8, stabilizes microtubules and consequently controls neurite length in cortical neurons. In the developing brain, negatively regulates the rate of exit from multipolar stage and retards radial migration from the ventricular zone (By similarity)..
• Protein Sequence: MAKTAMAYKEKMKELSMLSLICSCFYPEPRNINIYTYDDMEVKQINKRASGQAFELILKPPSPISEAPRTLASPKKKDLSLEEIQKKLEAAEERRKSQEAQVLKQLAEKREHEREVLQKALEENNNFSKMAEEKLILKMEQIKENREANLAAIIERLQEKERHAAEVRRNKELQVELSG

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Ubiquitination	AKTAMAYKEKMKELS CHHHHHHHHHHHHHH	41.12	32142685
16	Phosphorylation	KEKMKELSMLSLICS HHHHHHHHHHHHHHH	20.83	20068231
19	Phosphorylation	MKELSMLSLICSCFY HHHHHHHHHHHHHHC	13.67	20068231
22	S-palmitoylation	LSMLSLICSCFYPEP HHHHHHHHHHHCCCC	3.34	21471001
23	Phosphorylation	SMLSLICSCFYPEPR HHHHHHHHHHCCCCC	10.56	20068231
24	S-palmitoylation	MLSLICSCFYPEPRN HHHHHHHHHCCCCCC	3.08	21471001
35	Phosphorylation	EPRNINIYTYDDMEV CCCCCEEEEECCCCH	8.51	25884760
43	Ubiquitination	TYDDMEVKQINKRAS EECCCCHHHHHHHCC	31.96	32142685
50	Phosphorylation	KQINKRASGQAFELI HHHHHHCCCCEEEEE	35.16	9525956
54	Ubiquitination	KRASGQAFELILKPP HHCCCCEEEEEECCC	6.36	23503661
59	Ubiquitination	QAFELILKPPSPISE CEEEEEECCCCCCCC	48.14	32142685
62	Phosphorylation	ELILKPPSPISEAPR EEEECCCCCCCCCCC	43.31	30177828
65	Phosphorylation	LKPPSPISEAPRTLA ECCCCCCCCCCCCCC	30.96	20068231
73	Phosphorylation	EAPRTLASPKKKDLS CCCCCCCCCCCCCCC	40.12	9525956
76	Ubiquitination	RTLASPKKKDLSLEE CCCCCCCCCCCCHHH	55.70	29967540
77	Ubiquitination	TLASPKKKDLSLEEI CCCCCCCCCCCHHHH	70.77	-
80	Phosphorylation	SPKKKDLSLEEIQKK CCCCCCCCHHHHHHH	43.82	19664994
81	Ubiquitination	PKKKDLSLEEIQKKL CCCCCCCHHHHHHHH	9.96	22053931
82	Ubiquitination	KKKDLSLEEIQKKLE CCCCCCHHHHHHHHH	50.07	22817900
86	Acetylation	LSLEEIQKKLEAAEE CCHHHHHHHHHHHHH	66.06	66726425
86	Ubiquitination	LSLEEIQKKLEAAEE CCHHHHHHHHHHHHH	66.06	21906983
87	Acetylation	SLEEIQKKLEAAEER CHHHHHHHHHHHHHH	34.87	133901
87	Ubiquitination	SLEEIQKKLEAAEER CHHHHHHHHHHHHHH	34.87	22817900
97	Phosphorylation	AAEERRKSQEAQVLK HHHHHHHHHHHHHHH	31.29	9525956
114	Ubiquitination	AEKREHEREVLQKAL HHHHHHHHHHHHHHH	41.03	21890473
119	Ubiquitination	HEREVLQKALEENNN HHHHHHHHHHHHCCC	51.26	23000965
119	Acetylation	HEREVLQKALEENNN HHHHHHHHHHHHCCC	51.26	23236377
124	Ubiquitination	LQKALEENNNFSKMA HHHHHHHCCCHHHHH	39.09	21890473
128	Phosphorylation	LEENNNFSKMAEEKL HHHCCCHHHHHHHHH	24.52	25159151
129	Ubiquitination	EENNNFSKMAEEKLI HHCCCHHHHHHHHHH	37.68	22817900
129	Acetylation	EENNNFSKMAEEKLI HHCCCHHHHHHHHHH	37.68	23954790
129	2-Hydroxyisobutyrylation	EENNNFSKMAEEKLI HHCCCHHHHHHHHHH	37.68	-
134	Ubiquitination	FSKMAEEKLILKMEQ HHHHHHHHHHHHHHH	32.12	22817900

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
50	S	Phosphorylation	Kinase	PAK4	O96013	PSP
62	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
62	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
73	S	Phosphorylation	Kinase	JNK1	P45983	PSP
73	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
73	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of STMN2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of STMN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TEX11_HUMAN	TEX11	physical	16189514
GASP1_HUMAN	GPRASP1	physical	16169070
EF1A1_HUMAN	EEF1A1	physical	16169070
RGS20_HUMAN	RGS20	physical	11882662
RGS6_HUMAN	RGS6	physical	12140291
CC85A_HUMAN	CCDC85A	physical	21900206
CEP70_HUMAN	CEP70	physical	21900206
GASP2_HUMAN	GPRASP2	physical	21900206
TNR16_HUMAN	NGFR	physical	21900206
TEX11_HUMAN	TEX11	physical	25416956
TXLNA_HUMAN	TXLNA	physical	25416956
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.

Related Literatures of Post-Translational Modification

Palmitoylation

"Subcellular Golgi localization of stathmin family proteins ispromoted by a specific set of DHHC palmitoyl transferases.";
Levy A.D., Devignot V., Fukata Y., Fukata M., Sobel A., Chauvin S.;
Mol. Biol. Cell 22:1930-1942(2011).
Cited for: PALMITOYLATION AT CYS-22 AND CYS-24 BY ZDHHC3; ZDHHC7 AND ZDHHC15, ANDSUBCELLULAR LOCATION.
PubMed: 21471001

Phosphorylation

"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-80, AND MASSSPECTROMETRY.
PubMed: 18669648