SSH2_MOUSE - dbPTM
SSH2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSH2_MOUSE
UniProt AC Q5SW75
Protein Name Protein phosphatase Slingshot homolog 2
Gene Name Ssh2
Organism Mus musculus (Mouse).
Sequence Length 1423
Subcellular Localization Cytoplasm, cytoskeleton . Cell junction, focal adhesion . Colocalizes with filamentous actin in the cytoplasm and the cell periphery. Also localizes to focal adhesions.
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 MALVTVQRSPTPSTTSSPCASEADSGEEECRSQPRSISESFLTVKGAALFLPRGNGSSTPRVSHRRNKHAGDLQQHLQAMFILLRPEDNIRLAVRLESTYQNRTRYMVVVSTNGRQDTEESIVLGMDFSSNDSSTCTMGLVLPLWSDTLIHLDGDGGFSVSTDNRVHIFKPVSVQAMWSALQSLHKACEVARMHNYYPGSLFLTWVSYYESHINSDQSSVNEWNAMQDVQSHRPDSPALFTDIPTERERTERLIKTKLREIMMQKDLENITSKEIRTELEMQMVCNLREFKEFIDNEMIVILGQMDSPTQIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREIDNFFPGVFEYHNIRVYDEEATDLLAYWNDTYKFISKAKKHGSKCLVHCKMGVSRSASTVIAYAMKEYGWNLDRAYDYVKERRTVTKPNPSFMRQLEEYQGILLASKQRHNKLWRSHSDSDLSDHHEPICKPGLELNKKEMTTSADQIAEVKTVENLAAMPTVFMEHVVPQDANQKGLHTKERVICLEFSSQEFRAGQIEDELNLNDINGCSSGCCLSESKLPLDNCHASKALLQPGQAPDIANKFPDLAVEDLETDALKADMNVHLLPMEELTSRLKDLPMSPDLESPSPQASCQAAISDFSTDRIDFFSALEKFVELSQETRSRSFSHSRIEELGGGRSEGCRLSVIEVAASEMAADDQRSSSLSNTPHASEESSVDEDQSKAITELVSPDIIMQSHSENAISVKEIVTEIESISQGVGQVQLKGDILSNPCHTPKKSTIHELPLERVPAPESKPGHWEQDESFCSVQPELARDSGKCAPEEGCLTTHSSTADLEEEEPVEGEHDWGPGMHSGAKWCPGSVRRATLEFEERLRQEQENHGTASAGPTLSNRKNSKNDSSVADLMPKWKSDETTPEHSFFLKEAEPSKGKGKCSGSEAGSLSHCERNPTMPDCELLEHHSLPAPQDCLGSDSRSKKQEGDLKKQRAVVPNQECDTQAILLPLPKKIEIIEYTPTVTSLGHTEPGGEATPSKEGEKQGLRKVKMEQSITMFCALDENLNRTLEPSQVSLHPQVLPLPHSSSECDRPADPNPMLSSPQDKGDCPSTPFKTAAPFVSCSTQGASFSLDYLLPHSVVHLEGCTEQSSATDNELSPEQASWEDSRGHFLSSGSGMAHTSSPLTNEDLSLINKLGDSVGVLQKKLDPSPEACRIPHSSSSENIRDLSHSRGVVKEHAKEIESRVIFQAGFSKTSQMKRSASLAKLGYLDLCKDYLPDRELVSSESPHLKLLQPFLRTDSGMHALMAHEPSESAGAQQNPQPTKYSVEQLKTSECIVQSKPVERPSVQYAKEFGYSQQCLLPKARPELTSSEGGLPLLQTQGLQYTGPSPGLAVAPRQQHGRTHPLRRLKRANDKKRTTNPFYNTM
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
5Phosphorylation---MALVTVQRSPTP
---CCEEEEECCCCC		16.2725293948
9PhosphorylationALVTVQRSPTPSTTS
CEEEEECCCCCCCCC		18.9419060867
11PhosphorylationVTVQRSPTPSTTSSP
EEEECCCCCCCCCCC		30.9925293948
13PhosphorylationVQRSPTPSTTSSPCA
EECCCCCCCCCCCCC		46.9625293948
14PhosphorylationQRSPTPSTTSSPCAS
ECCCCCCCCCCCCCC		31.7225293948
15PhosphorylationRSPTPSTTSSPCASE
CCCCCCCCCCCCCCC		31.3825293948
16PhosphorylationSPTPSTTSSPCASEA
CCCCCCCCCCCCCCC		32.1625293948
17PhosphorylationPTPSTTSSPCASEAD
CCCCCCCCCCCCCCC		23.1619060867
21PhosphorylationTTSSPCASEADSGEE
CCCCCCCCCCCCCCH		39.7822172670
25PhosphorylationPCASEADSGEEECRS
CCCCCCCCCCHHHHC		55.9725521595
32PhosphorylationSGEEECRSQPRSISE
CCCHHHHCCCCCCCH		57.0822172670
36PhosphorylationECRSQPRSISESFLT
HHHCCCCCCCHHHHE		36.8322942356
38PhosphorylationRSQPRSISESFLTVK
HCCCCCCCHHHHEEC		28.5628833060
40PhosphorylationQPRSISESFLTVKGA
CCCCCCHHHHEECEE		20.8328833060
43PhosphorylationSISESFLTVKGAALF
CCCHHHHEECEEEEE		20.4028833060
133PhosphorylationMDFSSNDSSTCTMGL
EECCCCCCCCCEEEE		31.62-
134PhosphorylationDFSSNDSSTCTMGLV
ECCCCCCCCCEEEEE		30.30-
173PhosphorylationVHIFKPVSVQAMWSA
EEEECCCCHHHHHHH		19.62-
179PhosphorylationVSVQAMWSALQSLHK
CCHHHHHHHHHHHHH		13.1525338131
183PhosphorylationAMWSALQSLHKACEV
HHHHHHHHHHHHHHH		33.0425338131
374PhosphorylationLLAYWNDTYKFISKA
HHHHHHHHHHHHHHH		25.9528576409
429PhosphorylationVKERRTVTKPNPSFM
HHHCCCCCCCCHHHH		39.9228059163
459PhosphorylationRHNKLWRSHSDSDLS
HCCCHHHCCCCCCCC		18.7627742792
461PhosphorylationNKLWRSHSDSDLSDH
CCHHHCCCCCCCCCC		39.8027742792
463PhosphorylationLWRSHSDSDLSDHHE
HHHCCCCCCCCCCCC		43.3927742792
466PhosphorylationSHSDSDLSDHHEPIC
CCCCCCCCCCCCCCC		39.6327742792
485PhosphorylationELNKKEMTTSADQIA
CCCHHHCCCCHHHHH		20.7724925903
486PhosphorylationLNKKEMTTSADQIAE
CCHHHCCCCHHHHHH		22.1724925903
487PhosphorylationNKKEMTTSADQIAEV
CHHHCCCCHHHHHHH		22.2325521595
534PhosphorylationVICLEFSSQEFRAGQ
EEEEEECCCCHHCCC		38.7619060867
626PhosphorylationRLKDLPMSPDLESPS
HHHCCCCCCCCCCCC		17.2125293948
631PhosphorylationPMSPDLESPSPQASC
CCCCCCCCCCCCHHH		37.6719060867
633PhosphorylationSPDLESPSPQASCQA
CCCCCCCCCCHHHHH		38.6319060867
637PhosphorylationESPSPQASCQAAISD
CCCCCCHHHHHHHHC		11.0825293948
670PhosphorylationSQETRSRSFSHSRIE
CHHHHHCCCCHHHHH		32.1426643407
672PhosphorylationETRSRSFSHSRIEEL
HHHHCCCCHHHHHHH		23.0725266776
674PhosphorylationRSRSFSHSRIEELGG
HHCCCCHHHHHHHCC		33.4826643407
708PhosphorylationADDQRSSSLSNTPHA
CCCCHHHCCCCCCCC		36.7419060867
712PhosphorylationRSSSLSNTPHASEES
HHHCCCCCCCCCCCC		17.0519060867
716PhosphorylationLSNTPHASEESSVDE
CCCCCCCCCCCCCCH		38.5721082442
779PhosphorylationILSNPCHTPKKSTIH
CCCCCCCCCCCCCCC		43.4519060867
870PhosphorylationPGSVRRATLEFEERL
CCCHHHHHHHHHHHH		25.6326239621
899PhosphorylationTLSNRKNSKNDSSVA
CCCCCCCCCCCCCHH		35.5529899451
903PhosphorylationRKNSKNDSSVADLMP
CCCCCCCCCHHHHCC		35.7825266776
999PhosphorylationVPNQECDTQAILLPL
CCCCCCCCEEEEEEC		31.4021454597
1108PhosphorylationDKGDCPSTPFKTAAP
CCCCCCCCCCCCCCC		20.2123384938
1206PhosphorylationLQKKLDPSPEACRIP
HHHCCCCCHHHHCCC		34.7319060867
1215PhosphorylationEACRIPHSSSSENIR
HHHCCCCCCCCCCHH		26.9328833060
1216PhosphorylationACRIPHSSSSENIRD
HHCCCCCCCCCCHHH		34.5423684622
1217PhosphorylationCRIPHSSSSENIRDL
HCCCCCCCCCCHHHH		44.6926824392
1218PhosphorylationRIPHSSSSENIRDLS
CCCCCCCCCCHHHHH		36.2926824392
1227PhosphorylationNIRDLSHSRGVVKEH
CHHHHHHCCCHHHHH		27.6129899451
1259PhosphorylationSQMKRSASLAKLGYL
HHHHHHHHHHHHCHH		30.0626745281
1280PhosphorylationLPDRELVSSESPHLK
CCCHHHCCCCCCCHH		40.8025338131
1415PhosphorylationRANDKKRTTNPFYNT
HHCCCCCCCCCCCCC		39.5425619855
1422PhosphorylationTTNPFYNTM------
CCCCCCCCC------		16.9325521595
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
21SPhosphorylationKinaseGSK3BP49841
PSP
32SPhosphorylationKinaseGSK3BP49841
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSH2_MOUSE !!
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 SSH2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SSH2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SSH2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1422, AND MASSSPECTROMETRY.

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