SSH3_HUMAN - dbPTM
SSH3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSH3_HUMAN
UniProt AC Q8TE77
Protein Name Protein phosphatase Slingshot homolog 3
Gene Name SSH3
Organism Homo sapiens (Human).
Sequence Length 659
Subcellular Localization Cytoplasm, cytoskeleton. Nucleus.
Protein Description Protein phosphatase which may play a role in the regulation of actin filament dynamics. Can dephosphorylate and activate the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly (By similarity)..
Protein Sequence MALVTVSRSPPGSGASTPVGPWDQAVQRRSRLQRRQSFAVLRGAVLGLQDGGDNDDAAEASSEPTEKAPSEEELHGDQTDFGQGSQSPQKQEEQRQHLHLMVQLLRPQDDIRLAAQLEAPRPPRLRYLLVVSTREGEGLSQDETVLLGVDFPDSSSPSCTLGLVLPLWSDTQVYLDGDGGFSVTSGGQSRIFKPISIQTMWATLQVLHQACEAALGSGLVPGGSALTWASHYQERLNSEQSCLNEWTAMADLESLRPPSAEPGGSSEQEQMEQAIRAELWKVLDVSDLESVTSKEIRQALELRLGLPLQQYRDFIDNQMLLLVAQRDRASRIFPHLYLGSEWNAANLEELQRNRVTHILNMAREIDNFYPERFTYHNVRLWDEESAQLLPHWKETHRFIEAARAQGTHVLVHCKMGVSRSAATVLAYAMKQYECSLEQALRHVQELRPIARPNPGFLRQLQIYQGILTASRQSHVWEQKVGGVSPEEHPAPEVSTPFPPLPPEPEGGGEEKVVGMEESQAAPKEEPGPRPRINLRGVMRSISLLEPSLELESTSETSDMPEVFSSHESSHEEPLQPFPQLARTKGGQQVDRGPQPALKSRQSVVTLQGSAVVANRTQAFQEQEQGQGQGQGEPCISSTPRFRKVVRQASVHDSGEEGEA
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 Orthologous
Protein Cluster
2Acetylation------MALVTVSRS
------CCEEEECCC		15.67-
5Phosphorylation---MALVTVSRSPPG
---CCEEEECCCCCC		17.3922617229
7Phosphorylation-MALVTVSRSPPGSG
-CCEEEECCCCCCCC		20.0623401153
9PhosphorylationALVTVSRSPPGSGAS
CEEEECCCCCCCCCC		28.1322167270
13PhosphorylationVSRSPPGSGASTPVG
ECCCCCCCCCCCCCC		36.6423401153
16PhosphorylationSPPGSGASTPVGPWD
CCCCCCCCCCCCHHH		36.4522167270
17PhosphorylationPPGSGASTPVGPWDQ
CCCCCCCCCCCHHHH		22.8122167270
37PhosphorylationSRLQRRQSFAVLRGA
HHHHHHHHHHHHHHH		17.2322167270
61PhosphorylationNDDAAEASSEPTEKA
CCHHHHHCCCCCCCC		27.0920873877
62PhosphorylationDDAAEASSEPTEKAP
CHHHHHCCCCCCCCC		55.4320873877
65PhosphorylationAEASSEPTEKAPSEE
HHHCCCCCCCCCCHH		46.1730278072
67AcetylationASSEPTEKAPSEEEL
HCCCCCCCCCCHHHH		68.997667063
70PhosphorylationEPTEKAPSEEELHGD
CCCCCCCCHHHHCCC		63.6029255136
79PhosphorylationEELHGDQTDFGQGSQ
HHHCCCCCCCCCCCC		37.7329255136
85PhosphorylationQTDFGQGSQSPQKQE
CCCCCCCCCCHHHHH		21.4323401153
87PhosphorylationDFGQGSQSPQKQEEQ
CCCCCCCCHHHHHHH		30.8829255136
90 (in isoform 1)Ubiquitination-64.1621906983
90UbiquitinationQGSQSPQKQEEQRQH
CCCCCHHHHHHHHHH		64.1621906983
90 (in isoform 2)Ubiquitination-64.1621906983
90 (in isoform 4)Ubiquitination-64.1621906983
135 (in isoform 3)Ubiquitination-62.7821906983
148 (in isoform 3)Ubiquitination-16.8821906983
259PhosphorylationLESLRPPSAEPGGSS
HHHCCCCCCCCCCCC		48.2028348404
281 (in isoform 2)Ubiquitination-45.6121906983
281 (in isoform 1)Ubiquitination-45.6121906983
281UbiquitinationAIRAELWKVLDVSDL
HHHHHHHHHCCHHHH		45.6121906983
290PhosphorylationLDVSDLESVTSKEIR
CCHHHHHCCCHHHHH		37.68-
292PhosphorylationVSDLESVTSKEIRQA
HHHHHCCCHHHHHHH		43.28-
293PhosphorylationSDLESVTSKEIRQAL
HHHHCCCHHHHHHHH		26.57-
294 (in isoform 2)Ubiquitination-48.0421906983
294 (in isoform 1)Ubiquitination-48.0421906983
294UbiquitinationDLESVTSKEIRQALE
HHHCCCHHHHHHHHH		48.042190698
375PhosphorylationFYPERFTYHNVRLWD
CCCCCCCEECEECCC		6.6727642862
385PhosphorylationVRLWDEESAQLLPHW
EECCCHHHHHHCHHH		21.1927251275
418PhosphorylationVHCKMGVSRSAATVL
EECCCCCCHHHHHHH		18.1322210691
420PhosphorylationCKMGVSRSAATVLAY
CCCCCCHHHHHHHHH		18.1022210691
423PhosphorylationGVSRSAATVLAYAMK
CCCHHHHHHHHHHHH		18.7722210691
463PhosphorylationFLRQLQIYQGILTAS
HHHHHHHHHHHHHHH		6.4227642862
468PhosphorylationQIYQGILTASRQSHV
HHHHHHHHHHCCCCC		22.2127251275
470PhosphorylationYQGILTASRQSHVWE
HHHHHHHHCCCCCEE		26.1427251275
473PhosphorylationILTASRQSHVWEQKV
HHHHHCCCCCEEECC		20.9227251275
484PhosphorylationEQKVGGVSPEEHPAP
EECCCCCCCCCCCCC		29.8429255136
494PhosphorylationEHPAPEVSTPFPPLP
CCCCCCCCCCCCCCC		28.8029255136
495PhosphorylationHPAPEVSTPFPPLPP
CCCCCCCCCCCCCCC		33.8429255136
518PhosphorylationKVVGMEESQAAPKEE
CCCCCHHHHCCCCCC		16.2928555341
523SumoylationEESQAAPKEEPGPRP
HHHHCCCCCCCCCCC		70.73-
523SumoylationEESQAAPKEEPGPRP
HHHHCCCCCCCCCCC		70.73-
540PhosphorylationNLRGVMRSISLLEPS
CHHHHHHHHHHHCCC		9.8324247654
542PhosphorylationRGVMRSISLLEPSLE
HHHHHHHHHHCCCEE		28.3129802988
547PhosphorylationSISLLEPSLELESTS
HHHHHCCCEECEECC		25.7127251275
552PhosphorylationEPSLELESTSETSDM
CCCEECEECCCCCCC		50.2728348404
553PhosphorylationPSLELESTSETSDMP
CCEECEECCCCCCCC		22.6228348404
554PhosphorylationSLELESTSETSDMPE
CEECEECCCCCCCCH		48.4328348404
598MethylationRGPQPALKSRQSVVT
CCCCCCCCCCCEEEE		45.78100332089
599PhosphorylationGPQPALKSRQSVVTL
CCCCCCCCCCEEEEE		36.0826699800
602PhosphorylationPALKSRQSVVTLQGS
CCCCCCCEEEEEECC		19.9025849741
605PhosphorylationKSRQSVVTLQGSAVV
CCCCEEEEEECCEEE		15.9426699800
609PhosphorylationSVVTLQGSAVVANRT
EEEEEECCEEEECCC		12.6228857561
636PhosphorylationGQGEPCISSTPRFRK
CCCCCCCCCCHHHHH		34.5724719451
637PhosphorylationQGEPCISSTPRFRKV
CCCCCCCCCHHHHHH		23.6321712546
638PhosphorylationGEPCISSTPRFRKVV
CCCCCCCCHHHHHHH		16.2221815630
649PhosphorylationRKVVRQASVHDSGEE
HHHHHHHCCCCCCCC		16.2028355574
653PhosphorylationRQASVHDSGEEGEA-
HHHCCCCCCCCCCC-		32.9728355574
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
37SPhosphorylationKinaseAURKBQ96GD4
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSH3_HUMAN !!
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 SSH3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
NADAP_HUMANSLC4A1APphysical
27880917
ZN330_HUMANZNF330physical
27880917
HERC1_HUMANHERC1physical
27880917
TF65_HUMANRELAphysical
27880917
CRBG3_HUMANCRYBG3physical
27880917
NBR1_HUMANNBR1physical
27880917
CK5P2_HUMANCDK5RAP2physical
27880917
PUR4_HUMANPFASphysical
27880917
BIRC6_HUMANBIRC6physical
27880917
KDM5C_HUMANKDM5Cphysical
28514442
HERC1_HUMANHERC1physical
28514442
FMC1_HUMANC7orf55physical
28514442
K0232_HUMANKIAA0232physical
28514442
JMJD4_HUMANJMJD4physical
28514442
PSME3_HUMANPSME3physical
28514442
MKS1_HUMANMKS1physical
28514442
DPOA2_HUMANPOLA2physical
28514442
YBEY_HUMANYBEYphysical
28514442
HSP7C_HUMANHSPA8physical
28514442
ANGE1_HUMANANGEL1physical
28514442
SSH3_HUMANSSH3physical
27432908
PIMT_HUMANPCMT1physical
27432908
KEAP1_HUMANKEAP1physical
27432908
PSME3_HUMANPSME3physical
27432908
CALU_HUMANCALUphysical
27432908
STIP1_HUMANSTIP1physical
27432908
SPA5L_HUMANSPATA5L1physical
27432908
HDHD5_HUMANCECR5physical
27432908
MAIP1_HUMANC2orf47physical
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 SSH3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-37; SER-649 AND SER-653,AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-87, AND MASSSPECTROMETRY.
"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-609, AND MASSSPECTROMETRY.
"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-649, AND MASSSPECTROMETRY.

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