dbPTM

SSH1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SSH1_HUMAN
UniProt AC	Q8WYL5
Protein Name	Protein phosphatase Slingshot homolog 1
Gene Name	SSH1
Organism	Homo sapiens (Human).
Sequence Length	1049
Subcellular Localization	Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cleavage furrow. Midbody. Also recruited to actin rich membrane protrusions such as lamellipodia, which may allow local control of actin dynamics at sites of cell locomotion. Also localized to
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	MALVTLQRSPTPSAASSSASNSELEAGSEEDRKLNLSLSESFFMVKGAALFLQQGSSPQGQRSLQHPHKHAGDLPQHLQVMINLLRCEDRIKLAVRLESAWADRVRYMVVVYSSGRQDTEENILLGVDFSSKESKSCTIGMVLRLWSDTKIHLDGDGGFSVSTAGRMHIFKPVSVQAMWSALQVLHKACEVARRHNYFPGGVALIWATYYESCISSEQSCINEWNAMQDLESTRPDSPALFVDKPTEGERTERLIKAKLRSIMMSQDLENVTSKEIRNELEKQMNCNLKELKEFIDNEMLLILGQMDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGILDASKQRHNKLWRQQTDSSLQQPVDDPAGPGDFLPETPDGTPESQLPFLDDAAQPGLGPPLPCCFRRLSDPLLPSPEDETGSLVHLEDPEREALLEEAAPPAEVHRPARQPQQGSGLCEKDVKKKLEFGSPKGRSGSLLQVEETEREEGLGAGRWGQLPTQLDQNLLNSENLNNNSKRSCPNGMEDDAIFGILNKVKPSYKSCADCMYPTASGAPEASRERCEDPNAPAICTQPAFLPHITSSPVAHLASRSRVPEKPASGPTEPPPFLPPAGSRRADTSGPGAGAALEPPASLLEPSRETPKVLPKSLLLKNSHCDKNPPSTEVVIKEESSPKKDMKPAKDLRLLFSNESEKPTTNSYLMQHQESIIQLQKAGLVRKHTKELERLKSVPADPAPPSRDGPASRLEASIPEESQDPAALHELGPLVMPSQAGSDEKSEAAPASLEGGSLKSPPPFFYRLDHTSSFSKDFLKTICYTPTSSSMSSNLTRSSSSDSIHSVRGKPGLVKQRTQEIETRLRLAGLTVSSPLKRSHSLAKLGSLTFSTEDLSSEADPSTVADSQDTTLSESSFLHEPQGTPRDPAATSKPSGKPAPENLKSPSWMSKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MALVTLQRS ------CCEEEEECC	23.26	19413330
5	Phosphorylation	---MALVTLQRSPTP ---CCEEEEECCCCC	20.30	22199227
9	Phosphorylation	ALVTLQRSPTPSAAS CEEEEECCCCCCCCC	21.84	29255136
11	Phosphorylation	VTLQRSPTPSAASSS EEEECCCCCCCCCCC	30.99	29255136
13	Phosphorylation	LQRSPTPSAASSSAS EECCCCCCCCCCCCC	38.66	22199227
16	Phosphorylation	SPTPSAASSSASNSE CCCCCCCCCCCCCCH	25.25	22468782
17	Phosphorylation	PTPSAASSSASNSEL CCCCCCCCCCCCCHH	25.79	26852163
20	Phosphorylation	SAASSSASNSELEAG CCCCCCCCCCHHCCC	42.72	22468782
37	Phosphorylation	EDRKLNLSLSESFFM HHHHHCCCHHHHHHH	28.86	22199227
39	Phosphorylation	RKLNLSLSESFFMVK HHHCCCHHHHHHHHH	28.02	29396449
41	Phosphorylation	LNLSLSESFFMVKGA HCCCHHHHHHHHHHH	22.02	29396449
56	Phosphorylation	ALFLQQGSSPQGQRS HHHHHCCCCCHHHHH	34.21	24732914
57	Phosphorylation	LFLQQGSSPQGQRSL HHHHCCCCCHHHHHC	28.24	25159151
112	Phosphorylation	VRYMVVVYSSGRQDT EEEEEEEEECCCCCC	5.87	20068231
113	Phosphorylation	RYMVVVYSSGRQDTE EEEEEEEECCCCCCC	18.08	20068231
114	Phosphorylation	YMVVVYSSGRQDTEE EEEEEEECCCCCCCC	21.95	20068231
232	Phosphorylation	NAMQDLESTRPDSPA HHHHHHHHCCCCCCC	36.69	26074081
233	Phosphorylation	AMQDLESTRPDSPAL HHHHHHHCCCCCCCE	36.52	26074081
237	Phosphorylation	LESTRPDSPALFVDK HHHCCCCCCCEEECC	18.11	26074081
261	Phosphorylation	LIKAKLRSIMMSQDL HHHHHHHHHHCCCCH	25.85	22199227
366	Phosphorylation	RVYDEETTDLLAHWN EEECHHHHHHHHHHH	28.12	24719451
376	Phosphorylation	LAHWNEAYHFINKAK HHHHHHHHHHHHHHH	7.35	24719451
400	Phosphorylation	CKMGVSRSASTVIAY CCCCCCCCHHHHHHH	21.04	27251275
402	Phosphorylation	MGVSRSASTVIAYAM CCCCCCHHHHHHHHH	25.18	21525957
403	Phosphorylation	GVSRSASTVIAYAMK CCCCCHHHHHHHHHH	18.69	-
407	Phosphorylation	SASTVIAYAMKEFGW CHHHHHHHHHHHHCC	8.98	-
428	Phosphorylation	NYVKQKRSITRPNAG HHHHHCCCCCCCCCC	35.03	-
430	Phosphorylation	VKQKRSITRPNAGFM HHHCCCCCCCCCCHH	41.12	-
441	Phosphorylation	AGFMRQLSEYEGILD CCHHHHHHHHHCHHH	29.78	29978859
443	Phosphorylation	FMRQLSEYEGILDAS HHHHHHHHHCHHHHH	18.97	29978859
456	Ubiquitination	ASKQRHNKLWRQQTD HHHHHHHHHHHHHCC	43.21	-
462	Phosphorylation	NKLWRQQTDSSLQQP HHHHHHHCCCCCCCC	29.52	28655764
464	Phosphorylation	LWRQQTDSSLQQPVD HHHHHCCCCCCCCCC	36.01	-
465	Phosphorylation	WRQQTDSSLQQPVDD HHHHCCCCCCCCCCC	32.76	-
515	Phosphorylation	PCCFRRLSDPLLPSP CCCHHCCCCCCCCCC	35.06	30266825
521	Phosphorylation	LSDPLLPSPEDETGS CCCCCCCCCCCCCCC	40.67	30266825
526	Phosphorylation	LPSPEDETGSLVHLE CCCCCCCCCCCEECC	44.38	30266825
528	Phosphorylation	SPEDETGSLVHLEDP CCCCCCCCCEECCCH	34.34	30266825
576	Phosphorylation	KKKLEFGSPKGRSGS HHHHCCCCCCCCCCC	28.85	23401153
581	Phosphorylation	FGSPKGRSGSLLQVE CCCCCCCCCCEEEEE	41.21	29255136
583	Phosphorylation	SPKGRSGSLLQVEET CCCCCCCCEEEEEEC	27.44	29255136
590	Phosphorylation	SLLQVEETEREEGLG CEEEEEECCCCCCCC	27.17	23403867
644 (in isoform 2)	Phosphorylation	-	45.97	-
645	Phosphorylation	ILNKVKPSYKSCADC HHHCCCCCCCCHHHH	39.20	-
646	Phosphorylation	LNKVKPSYKSCADCM HHCCCCCCCCHHHHC	18.56	-
655 (in isoform 5)	Phosphorylation	-	8.46	-
687	Phosphorylation	PAFLPHITSSPVAHL CCCCCCCCCCHHHHH	21.81	23898821
688	Phosphorylation	AFLPHITSSPVAHLA CCCCCCCCCHHHHHH	31.85	25627689
689	Phosphorylation	FLPHITSSPVAHLAS CCCCCCCCHHHHHHH	18.10	28348404
696	Phosphorylation	SPVAHLASRSRVPEK CHHHHHHHCCCCCCC	36.83	27050516
739	Phosphorylation	AALEPPASLLEPSRE CCCCCCHHHCCCCCC	38.98	25850435
744	Phosphorylation	PASLLEPSRETPKVL CHHHCCCCCCCCCCC	33.11	25850435
747	Phosphorylation	LLEPSRETPKVLPKS HCCCCCCCCCCCCHH	27.57	25850435
758	Methylation	LPKSLLLKNSHCDKN CCHHHHHCCCCCCCC	57.27	115980465
768	Phosphorylation	HCDKNPPSTEVVIKE CCCCCCCCCCEEEEC	38.16	23312004
769	Phosphorylation	CDKNPPSTEVVIKEE CCCCCCCCCEEEECC	38.28	30108239
777	Phosphorylation	EVVIKEESSPKKDMK CEEEECCCCCCCCCC	53.70	29255136
778	Phosphorylation	VVIKEESSPKKDMKP EEEECCCCCCCCCCC	43.98	29255136
802	Phosphorylation	NESEKPTTNSYLMQH CCCCCCCCHHHHHHH	30.60	28555341
805	Phosphorylation	EKPTTNSYLMQHQES CCCCCHHHHHHHHHH	14.30	26657352
812	Phosphorylation	YLMQHQESIIQLQKA HHHHHHHHHHHHHHH	20.58	26657352
826	Phosphorylation	AGLVRKHTKELERLK HHHHHHHHHHHHHHH	29.29	29514088
834	Phosphorylation	KELERLKSVPADPAP HHHHHHHCCCCCCCC	37.61	25159151
854	Phosphorylation	PASRLEASIPEESQD CHHHCCCCCCHHHCC	29.33	-
883	Phosphorylation	QAGSDEKSEAAPASL HCCCCCCCCCCCCCC	30.35	26699800
889	Phosphorylation	KSEAAPASLEGGSLK CCCCCCCCCCCCCCC	26.37	29255136
894	Phosphorylation	PASLEGGSLKSPPPF CCCCCCCCCCCCCCC	43.40	25159151
897	Phosphorylation	LEGGSLKSPPPFFYR CCCCCCCCCCCCEEC	48.18	30266825
903	Phosphorylation	KSPPPFFYRLDHTSS CCCCCCEECCCCCCC	15.62	30266825
908	Phosphorylation	FFYRLDHTSSFSKDF CEECCCCCCCCCHHH	26.23	25159151
909	Phosphorylation	FYRLDHTSSFSKDFL EECCCCCCCCCHHHH	26.43	25159151
910	Phosphorylation	YRLDHTSSFSKDFLK ECCCCCCCCCHHHHH	34.39	25159151
912	Phosphorylation	LDHTSSFSKDFLKTI CCCCCCCCHHHHHHH	33.01	25159151
922	Phosphorylation	FLKTICYTPTSSSMS HHHHHEECCCCCCCC	18.71	28985074
924	Phosphorylation	KTICYTPTSSSMSSN HHHEECCCCCCCCCC	33.18	28857561
925	Phosphorylation	TICYTPTSSSMSSNL HHEECCCCCCCCCCC	22.94	28348404
933	Phosphorylation	SSMSSNLTRSSSSDS CCCCCCCCCCCCCCC	32.52	-
935	Phosphorylation	MSSNLTRSSSSDSIH CCCCCCCCCCCCCHH	29.36	23927012
936	Phosphorylation	SSNLTRSSSSDSIHS CCCCCCCCCCCCHHH	30.48	29255136
937	Phosphorylation	SNLTRSSSSDSIHSV CCCCCCCCCCCHHHC	39.14	23401153
938	Phosphorylation	NLTRSSSSDSIHSVR CCCCCCCCCCHHHCC	37.01	23927012
940	Phosphorylation	TRSSSSDSIHSVRGK CCCCCCCCHHHCCCC	24.93	23927012
943	Phosphorylation	SSSDSIHSVRGKPGL CCCCCHHHCCCCCCC	16.31	23927012
952	Acetylation	RGKPGLVKQRTQEIE CCCCCCHHHHHHHHH	38.82	19817433
968	Phosphorylation	RLRLAGLTVSSPLKR HHHHCCCCCCCCCCC	19.88	29255136
970	Phosphorylation	RLAGLTVSSPLKRSH HHCCCCCCCCCCCCC	22.47	29255136
971	Phosphorylation	LAGLTVSSPLKRSHS HCCCCCCCCCCCCCC	29.89	29255136
976	Phosphorylation	VSSPLKRSHSLAKLG CCCCCCCCCCHHHHC	18.81	20068231
978	Phosphorylation	SPLKRSHSLAKLGSL CCCCCCCCHHHHCCE	31.13	16230460
984	Phosphorylation	HSLAKLGSLTFSTED CCHHHHCCEEEEHHH	34.37	30108239
986	Phosphorylation	LAKLGSLTFSTEDLS HHHHCCEEEEHHHCC	19.76	30108239
988	Phosphorylation	KLGSLTFSTEDLSSE HHCCEEEEHHHCCCC	26.17	30108239
989	Phosphorylation	LGSLTFSTEDLSSEA HCCEEEEHHHCCCCC	29.36	30108239
993	Phosphorylation	TFSTEDLSSEADPST EEEHHHCCCCCCHHH	38.15	30108239
994	Phosphorylation	FSTEDLSSEADPSTV EEHHHCCCCCCHHHC	44.06	30108239
999	Phosphorylation	LSSEADPSTVADSQD CCCCCCHHHCCCCCC	35.74	25002506
1000	Phosphorylation	SSEADPSTVADSQDT CCCCCHHHCCCCCCC	25.71	25002506
1004	Phosphorylation	DPSTVADSQDTTLSE CHHHCCCCCCCCCCH	21.88	25002506
1007	Phosphorylation	TVADSQDTTLSESSF HCCCCCCCCCCHHHC	23.23	25002506
1008	Phosphorylation	VADSQDTTLSESSFL CCCCCCCCCCHHHCC	36.25	25002506
1010	Phosphorylation	DSQDTTLSESSFLHE CCCCCCCCHHHCCCC	33.08	25002506
1021	Phosphorylation	FLHEPQGTPRDPAAT CCCCCCCCCCCCCCC	15.20	-
1029	Phosphorylation	PRDPAATSKPSGKPA CCCCCCCCCCCCCCC	37.53	30108239
1032	Phosphorylation	PAATSKPSGKPAPEN CCCCCCCCCCCCCCC	64.28	30108239
1041	Methylation	KPAPENLKSPSWMSK CCCCCCCCCCCHHCC	72.42	115980457
1042	Phosphorylation	PAPENLKSPSWMSKS CCCCCCCCCCHHCCC	27.60	19276368
1044	Phosphorylation	PENLKSPSWMSKS-- CCCCCCCCHHCCC--	42.37	28857561
1047	Phosphorylation	LKSPSWMSKS----- CCCCCHHCCC-----	24.40	22199227
1049	Phosphorylation	SPSWMSKS------- CCCHHCCC-------	37.84	22199227

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
402	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
826	T	Phosphorylation	Kinase	AKT1	P31749	PSP
937	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
937	S	Phosphorylation	Kinase	PRKD2	Q9BZL6	PSP
978	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
978	S	Phosphorylation	Kinase	PRKD2	Q9BZL6	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
978	S	Phosphorylation		15159416
Phosphorylation at Ser-978 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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of SSH1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LIMK1_DROME	LIMK1	genetic	11832213
COF1_MOUSE	Cfl1	physical	11832213
DEST_HUMAN	DSTN	physical	11832213
MYO5A_HUMAN	MYO5A	physical	27880917
ADSV_HUMAN	SCIN	physical	27880917
1433E_HUMAN	YWHAE	physical	27880917
MYO5B_HUMAN	MYO5B	physical	27880917
SVIL_HUMAN	SVIL	physical	27880917
MYH10_HUMAN	MYH10	physical	27880917
ACTN4_HUMAN	ACTN4	physical	27880917
MYO1D_HUMAN	MYO1D	physical	27880917
K1671_HUMAN	KIAA1671	physical	27880917
ACTBL_HUMAN	ACTBL2	physical	28514442
GELS_HUMAN	GSN	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
TMOD2_HUMAN	TMOD2	physical	28514442
ACTB_HUMAN	ACTB	physical	28514442
1433Z_HUMAN	YWHAZ	physical	28514442
TMOD3_HUMAN	TMOD3	physical	28514442
1433G_HUMAN	YWHAG	physical	28514442
SSH1_HUMAN	SSH1	physical	27432908
1433F_HUMAN	YWHAH	physical	27432908
COR1C_HUMAN	CORO1C	physical	27432908
ATF1_HUMAN	ATF1	physical	27432908
1433G_HUMAN	YWHAG	physical	27432908
1433B_HUMAN	YWHAB	physical	27432908
1433T_HUMAN	YWHAQ	physical	27432908
1433Z_HUMAN	YWHAZ	physical	27432908

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 SSH1_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, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"A pathway of neuregulin-induced activation of cofilin-phosphataseSlingshot and cofilin in lamellipodia."; Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M.,Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.; J. Cell Biol. 165:465-471(2004). Cited for: FUNCTION, INTERACTION WITH YWHAB; YWHAG; YWHAQ AND YWHAZ, SUBCELLULARLOCATION, PHOSPHORYLATION AT SER-978, AND MUTAGENESIS OF CYS-393;SER-937 AND SER-978.	15159416 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1042, AND MASSSPECTROMETRY.	15302935 [Abstract]

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