SSH1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SSH1_MOUSE
• UniProt AC: Q76I79
• Protein Name: Protein phosphatase Slingshot homolog 1
• Gene Name: Ssh1
• Organism: Mus musculus (Mouse).
• Sequence Length: 1042
• Subcellular Localization: Cytoplasm, cytoskeleton . Cleavage furrow. Midbody. Localized to the cleavage furrow and the midbody during cytokinesis (By similarity). Also colocalizes with F-actin in the cytoplasm and the cell periphery, which may allow local control of actin dyn
• Protein Description: Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein..
• Protein Sequence: MALVTLQRSPTPSAASSSASNSELEAGSDEERKLNLSLSESFFMVKGAALFLQQGNSPQGQRSLQHPHKHAGDLPQHLQVMINLLRCEDRIKLAVRLESVWTDRVRYMVVVYTSGRQDTEENILLGVDFSSKESKSCTIGMVLRLWSDTKIHLDGDGGFSVSTAGRMHIFKPVSVQAMWSALQVLHKACEVARRHNYFPGGVALIWATYYESCISSEQSCINEWNAMQDLESTRPDSPALFVDKPTEGERTERLIKAKLRSIMMSQDLENVTSKEIRNELEKQMNCNLKEFKEFIDNEMLLILGQMDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGILDASKQRHNKLWRQQPTDDTIAEPSEFLPETLDGALDAQLPCLDDTTHPGLPRSLAPGGPALPCCFRRLSDPLLLPHHDETGGLVHLEDLEKDALLEEEESQPVEVHKLVQHPQEGARLCEKDVKRKLEFGNSKPRSDSLPQVEELEKDGSPRTGRWRRASTQLDRSLLDQENLNNNNSKRSCPDDLERDAMFGILSKVKPPYTSCADCMYPTAGGTPEAYMERHEDPSSSAICTQPTFLPHVTSSPMAHASSRSRAPERPASGPANTSPFLLPAGSRKPDVSGSGAGAAPEPPASLLEPSRETSKALPKSLQLKNPHCDKNAANMEVSAKEEPSPKKDPKPAKDLRLLFSNEAEKPTTNSYLMQHQESIIQLQKAGLVRKHTKELERLKSLPSDSPAACRDSATCRLEASIPEEGSQEPAHPALCSQAGSEEQPVGGTLQKSPTSTLPRLDHTSNFSKDFLKTVCYTPTSSSISSNLTRSSSSDSIHSVRGKPGLVKQRAQEIETRLRLAGLTVSSPLKRSHSLAKLGSLNFSTEDLSSEADTSTIADSQDAKCGLSSSFLPEPQSAPRDPAATSKSSGKSAPEHLKSPSRVNKS

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
2	Acetylation	------MALVTLQRS ------CCEEEEECC	23.26	-
5	Phosphorylation	---MALVTLQRSPTP ---CCEEEEECCCCC	20.30	25619855
9	Phosphorylation	ALVTLQRSPTPSAAS CEEEEECCCCCCCCC	21.84	25619855
11	Phosphorylation	VTLQRSPTPSAASSS EEEECCCCCCCCCCC	30.99	25619855
13	Phosphorylation	LQRSPTPSAASSSAS EECCCCCCCCCCCCC	38.66	25619855
16	Phosphorylation	SPTPSAASSSASNSE CCCCCCCCCCCCCCC	25.25	25619855
17	Phosphorylation	PTPSAASSSASNSEL CCCCCCCCCCCCCCC	25.79	25619855
18	Phosphorylation	TPSAASSSASNSELE CCCCCCCCCCCCCCC	32.97	25619855
20	Phosphorylation	SAASSSASNSELEAG CCCCCCCCCCCCCCC	42.72	25619855
22	Phosphorylation	ASSSASNSELEAGSD CCCCCCCCCCCCCCH	40.85	25619855
28	Phosphorylation	NSELEAGSDEERKLN CCCCCCCCHHHHHHC	49.23	30635358
37	Phosphorylation	EERKLNLSLSESFFM HHHHHCCCHHHHHHH	28.86	-
57	Phosphorylation	LFLQQGNSPQGQRSL HHHHCCCCCHHHHCC	25.98	22817900
274	Acetylation	DLENVTSKEIRNELE CHHCCCHHHHHHHHH	48.04	15612579
325	Phosphorylation	LGSEWNASNLEELQG CCCCCCCCCHHHHCC	38.44	-
441	Phosphorylation	AGFMRQLSEYEGILD CCHHHHHHHHHCHHH	29.78	29514104
516	Phosphorylation	PCCFRRLSDPLLLPH CCCHHHCCCCCCCCC	35.06	25521595
579	Phosphorylation	RKLEFGNSKPRSDSL HHHHCCCCCCCCCCC	44.40	22817900
583	Phosphorylation	FGNSKPRSDSLPQVE CCCCCCCCCCCCCHH	39.83	25619855
585	Phosphorylation	NSKPRSDSLPQVEEL CCCCCCCCCCCHHHH	43.10	26824392
597	Phosphorylation	EELEKDGSPRTGRWR HHHHHCCCCCCCCHH	22.72	29895711
607	Phosphorylation	TGRWRRASTQLDRSL CCCHHHHHHHHHHHH	18.18	26824392
608	Phosphorylation	GRWRRASTQLDRSLL CCHHHHHHHHHHHHC	31.97	25266776
613	Phosphorylation	ASTQLDRSLLDQENL HHHHHHHHHCCHHHC	32.71	-
650	Phosphorylation	SKVKPPYTSCADCMY HCCCCCCCCCCCCCC	24.09	-
837	Phosphorylation	KELERLKSLPSDSPA HHHHHHHCCCCCCCH	50.53	28973931
857	Phosphorylation	ATCRLEASIPEEGSQ CEEEEEECCCCCCCC	29.33	25168779
863	Phosphorylation	ASIPEEGSQEPAHPA ECCCCCCCCCCCCHH	34.35	25168779
873	Phosphorylation	PAHPALCSQAGSEEQ CCCHHHCCCCCCCCC	24.74	25168779
877	Phosphorylation	ALCSQAGSEEQPVGG HHCCCCCCCCCCCCC	40.76	25168779
885	Phosphorylation	EEQPVGGTLQKSPTS CCCCCCCCCCCCCCC	21.78	25168779
889	Phosphorylation	VGGTLQKSPTSTLPR CCCCCCCCCCCCCCC	22.05	26824392
891	Phosphorylation	GTLQKSPTSTLPRLD CCCCCCCCCCCCCCC	41.24	27180971
892	Phosphorylation	TLQKSPTSTLPRLDH CCCCCCCCCCCCCCC	31.19	26643407
893	Phosphorylation	LQKSPTSTLPRLDHT CCCCCCCCCCCCCCC	43.17	26643407
927	Phosphorylation	ISSNLTRSSSSDSIH CCCCCCCCCCCCCHH	29.36	27087446
928	Phosphorylation	SSNLTRSSSSDSIHS CCCCCCCCCCCCHHH	30.48	30635358
929	Phosphorylation	SNLTRSSSSDSIHSV CCCCCCCCCCCHHHC	39.14	27087446
930	Phosphorylation	NLTRSSSSDSIHSVR CCCCCCCCCCHHHCC	37.01	27087446
932	Phosphorylation	TRSSSSDSIHSVRGK CCCCCCCCHHHCCCC	24.93	23684622
935	Phosphorylation	SSSDSIHSVRGKPGL CCCCCHHHCCCCCCH	16.31	27717184
962	Phosphorylation	RLAGLTVSSPLKRSH HHCCCCCCCCCCCCC	22.47	29895711
963	Phosphorylation	LAGLTVSSPLKRSHS HCCCCCCCCCCCCCC	29.89	26824392
970	Phosphorylation	SPLKRSHSLAKLGSL CCCCCCCCHHHHCCC	31.13	27149854
976	Phosphorylation	HSLAKLGSLNFSTED CCHHHHCCCCCCHHH	30.49	26643407
980	Phosphorylation	KLGSLNFSTEDLSSE HHCCCCCCHHHCCCC	29.79	30352176
981	Phosphorylation	LGSLNFSTEDLSSEA HCCCCCCHHHCCCCC	29.40	30352176
985	Phosphorylation	NFSTEDLSSEADTST CCCHHHCCCCCCCCC	38.15	29899451
986	Phosphorylation	FSTEDLSSEADTSTI CCHHHCCCCCCCCCC	44.06	23984901
990	Phosphorylation	DLSSEADTSTIADSQ HCCCCCCCCCCCCCC	34.51	30635358
991	Phosphorylation	LSSEADTSTIADSQD CCCCCCCCCCCCCCC	20.54	30635358
992	Phosphorylation	SSEADTSTIADSQDA CCCCCCCCCCCCCCC	23.44	30635358
996	Phosphorylation	DTSTIADSQDAKCGL CCCCCCCCCCCCCCC	22.42	30635358
1035	Phosphorylation	SAPEHLKSPSRVNKS CCCCHHCCCCCCCCC	34.17	26824392
1037	Phosphorylation	PEHLKSPSRVNKS-- CCHHCCCCCCCCC--	56.82	28066266

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

Oops, there are no upstream regulatory protein records of SSH1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
970	S	Phosphorylation	Phosphorylation at Ser-970 is decreased by stimuli which promote actin reorganization and lamellipodia formation.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SSH1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of SSH1_MOUSE !!

Drug and Disease Associations

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