SSH2_HUMAN - dbPTM
SSH2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSH2_HUMAN
UniProt AC Q76I76
Protein Name Protein phosphatase Slingshot homolog 2
Gene Name SSH2
Organism Homo sapiens (Human).
Sequence Length 1423
Subcellular Localization Cytoplasm, cytoskeleton.
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 MALVTVQRSPTPSTTSSPCASEADSGEEECRSQPRSISESFLTVKGAALFLPRGNGSSTPRISHRRNKHAGDLQQHLQAMFILLRPEDNIRLAVRLESTYQNRTRYMVVVSTNGRQDTEESIVLGMDFSSNDSSTCTMGLVLPLWSDTLIHLDGDGGFSVSTDNRVHIFKPVSVQAMWSALQSLHKACEVARAHNYYPGSLFLTWVSYYESHINSDQSSVNEWNAMQDVQSHRPDSPALFTDIPTERERTERLIKTKLREIMMQKDLENITSKEIRTELEMQMVCNLREFKEFIDNEMIVILGQMDSPTQIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREIDNFFPGVFEYHNIRVYDEEATDLLAYWNDTYKFISKAKKHGSKCLVHCKMGVSRSASTVIAYAMKEYGWNLDRAYDYVKERRTVTKPNPSFMRQLEEYQGILLASKQRHNKLWRSHSDSDLSDHHEPICKPGLELNKKDITTSADQIAEVKTMESHPPIPPVFVEHMVPQDANQKGLCTKERMICLEFTSREFHAGQIEDELNLNDINGCSSGCCLNESKFPLDNCHASKALIQPGHVPEMANKFPDLTVEDLETDALKADMNVHLLPMEELTSPLKDPPMSPDPESPSPQPSCQTEISDFSTDRIDFFSALEKFVELSQETRSRSFSHSRMEELGGGRNESCRLSVVEVAPSKVTADDQRSSSLSNTPHASEESSMDEEQSKAISELVSPDIFMQSHSENAISVKEIVTEIESISQGVGQIQLKGDILPNPCHTPKKNSIHELLLERAQTPENKPGHMEQDEDSCTAQPELAKDSGMCNPEGCLTTHSSIADLEEGEPAEGEQELQGSGMHPGAKWYPGSVRRATLEFEERLRQEQEHHGAAPTCTSLSTRKNSKNDSSVADLAPKGKSDEAPPEHSFVLKEPEMSKGKGKYSGSEAGSLSHSEQNATVPAPRVLEFDHLPDPQEGPGSDTGTQQEGVLKDLRTVIPYQESETQAVPLPLPKRVEIIEYTHIVTSPNHTGPGSEIATSEKSGEQGLRKVNMEKSVTVLCTLDENLNRTLDPNQVSLHPQVLPLPHSSSPEHNRPTDHPTSILSSPEDRGSSLSTALETAAPFVSHTTHLLSASLDYLHPQTMVHLEGFTEQSSTTDEPSAEQVSWEESQESPLSSGSEVPYKDSQLSSADLSLISKLGDNTGELQEKMDPLPVACRLPHSSSSENIKSLSHSPGVVKERAKEIESRVVFQAGLTKPSQMRRSASLAKLGYLDLCKDCLPEREPASCESPHLKLLQPFLRTDSGMHAMEDQESLENPGAPHNPEPTKSFVEQLTTTECIVQSKPVERPLVQYAKEFGSSQQYLLPRAGLELTSSEGGLPVLQTQGLQCACPAPGLAVAPRQQHGRTHPLRRLKKANDKKRTTNPFYNTM
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
13PhosphorylationVQRSPTPSTTSSPCA
EECCCCCCCCCCCCC
46.9628450419
14PhosphorylationQRSPTPSTTSSPCAS
ECCCCCCCCCCCCCC
31.7228450419
15PhosphorylationRSPTPSTTSSPCASE
CCCCCCCCCCCCCCC
31.3828450419
16PhosphorylationSPTPSTTSSPCASEA
CCCCCCCCCCCCCCC
32.1628450419
17PhosphorylationPTPSTTSSPCASEAD
CCCCCCCCCCCCCCC
23.1628450419
21PhosphorylationTTSSPCASEADSGEE
CCCCCCCCCCCCCCH
39.7828450419
25PhosphorylationPCASEADSGEEECRS
CCCCCCCCCCHHHHC
55.9728450419
32PhosphorylationSGEEECRSQPRSISE
CCCHHHHCCCCCCCH
57.0828450419
36PhosphorylationECRSQPRSISESFLT
HHHCCCCCCCHHHHE
36.8330266825
38PhosphorylationRSQPRSISESFLTVK
HCCCCCCCHHHHEEC
28.5630266825
40PhosphorylationQPRSISESFLTVKGA
CCCCCCHHHHEECEE
20.8323927012
43PhosphorylationSISESFLTVKGAALF
CCCHHHHEECEEEEE
20.4023927012
63PhosphorylationGSSTPRISHRRNKHA
CCCCCCCCCCCCCCC
16.54-
134PhosphorylationDFSSNDSSTCTMGLV
ECCCCCCCCCEEEEE
30.3025332170
135PhosphorylationFSSNDSSTCTMGLVL
CCCCCCCCCEEEEEE
18.8925332170
148PhosphorylationVLPLWSDTLIHLDGD
EEEEECCEEEEECCC
23.3025332170
231PhosphorylationNAMQDVQSHRPDSPA
HHHHHHHHCCCCCCC
22.7026074081
236PhosphorylationVQSHRPDSPALFTDI
HHHCCCCCCCCCCCC
18.1126074081
241PhosphorylationPDSPALFTDIPTERE
CCCCCCCCCCCCHHH
33.5926074081
245PhosphorylationALFTDIPTERERTER
CCCCCCCCHHHHHHH
48.2726074081
255AcetylationERTERLIKTKLREIM
HHHHHHHHHHHHHHH
44.1725953088
265UbiquitinationLREIMMQKDLENITS
HHHHHCHHCHHCCCC
46.51-
273UbiquitinationDLENITSKEIRTELE
CHHCCCCHHHHHHHH
48.81-
399PhosphorylationCKMGVSRSASTVIAY
CCCCCCCCHHHHHHH
21.0427251275
401PhosphorylationMGVSRSASTVIAYAM
CCCCCCHHHHHHHHH
25.18-
402PhosphorylationGVSRSASTVIAYAMK
CCCCCHHHHHHHHHH
18.69-
406PhosphorylationSASTVIAYAMKEYGW
CHHHHHHHHHHHHCC
8.98-
411PhosphorylationIAYAMKEYGWNLDRA
HHHHHHHHCCCHHHH
23.1722817900
419PhosphorylationGWNLDRAYDYVKERR
CCCHHHHHHHHHHCC
14.5422817900
421PhosphorylationNLDRAYDYVKERRTV
CHHHHHHHHHHCCCC
10.7622817900
423UbiquitinationDRAYDYVKERRTVTK
HHHHHHHHHCCCCCC
39.00-
430UbiquitinationKERRTVTKPNPSFMR
HHCCCCCCCCHHHHH
38.16-
450UbiquitinationQGILLASKQRHNKLW
HHHHHHHHHHCCCHH
45.82-
455UbiquitinationASKQRHNKLWRSHSD
HHHHHCCCHHHCCCC
43.21-
459PhosphorylationRHNKLWRSHSDSDLS
HCCCHHHCCCCCCCC
18.7623927012
461PhosphorylationNKLWRSHSDSDLSDH
CCHHHCCCCCCCCCC
39.8023927012
463PhosphorylationLWRSHSDSDLSDHHE
HHHCCCCCCCCCCCC
43.3923927012
466PhosphorylationSHSDSDLSDHHEPIC
CCCCCCCCCCCCCCC
39.6323927012
482UbiquitinationPGLELNKKDITTSAD
CCCCCCHHHCCCCHH
53.97-
485PhosphorylationELNKKDITTSADQIA
CCCHHHCCCCHHHHH
25.4930266825
486PhosphorylationLNKKDITTSADQIAE
CCHHHCCCCHHHHHH
23.4230266825
487PhosphorylationNKKDITTSADQIAEV
CHHHCCCCHHHHHHH
22.6219664994
534PhosphorylationMICLEFTSREFHAGQ
EEEEEECCCCCCCCC
34.82-
588UbiquitinationHVPEMANKFPDLTVE
CCHHHHHHCCCCCHH
49.05-
617PhosphorylationLLPMEELTSPLKDPP
ECCHHHCCCCCCCCC
31.4228634298
618PhosphorylationLPMEELTSPLKDPPM
CCHHHCCCCCCCCCC
40.6424719451
626PhosphorylationPLKDPPMSPDPESPS
CCCCCCCCCCCCCCC
31.7428348404
631PhosphorylationPMSPDPESPSPQPSC
CCCCCCCCCCCCCCC
35.7528348404
633PhosphorylationSPDPESPSPQPSCQT
CCCCCCCCCCCCCCC
45.5028348404
654PhosphorylationTDRIDFFSALEKFVE
CCCHHHHHHHHHHHH
31.75-
666PhosphorylationFVELSQETRSRSFSH
HHHHCHHHHHCCCCH
26.72-
668PhosphorylationELSQETRSRSFSHSR
HHCHHHHHCCCCHHH
39.4328348404
670PhosphorylationSQETRSRSFSHSRME
CHHHHHCCCCHHHHH
32.1428348404
672PhosphorylationETRSRSFSHSRMEEL
HHHHCCCCHHHHHHH
23.0728122231
674PhosphorylationRSRSFSHSRMEELGG
HHCCCCHHHHHHHCC
31.9328122231
686PhosphorylationLGGGRNESCRLSVVE
HCCCCCCCCCEEEEE
14.2128122231
690O-linked_GlycosylationRNESCRLSVVEVAPS
CCCCCCEEEEEECCC
12.5530379171
690PhosphorylationRNESCRLSVVEVAPS
CCCCCCEEEEEECCC
12.5528111955
698AcetylationVVEVAPSKVTADDQR
EEEECCCCCCCCCCC
42.4125953088
706PhosphorylationVTADDQRSSSLSNTP
CCCCCCCCCCCCCCC
20.7429978859
707PhosphorylationTADDQRSSSLSNTPH
CCCCCCCCCCCCCCC
37.1729978859
708PhosphorylationADDQRSSSLSNTPHA
CCCCCCCCCCCCCCC
36.7429978859
710PhosphorylationDQRSSSLSNTPHASE
CCCCCCCCCCCCCCC
40.3729978859
712PhosphorylationRSSSLSNTPHASEES
CCCCCCCCCCCCCCC
17.0529978859
716PhosphorylationLSNTPHASEESSMDE
CCCCCCCCCCCCCCH
38.5723312004
719PhosphorylationTPHASEESSMDEEQS
CCCCCCCCCCCHHHH
27.2323312004
720PhosphorylationPHASEESSMDEEQSK
CCCCCCCCCCHHHHH
33.2723312004
730PhosphorylationEEQSKAISELVSPDI
HHHHHHHHHHHCHHH
29.7220068231
734PhosphorylationKAISELVSPDIFMQS
HHHHHHHCHHHHHCC
29.4920068231
741PhosphorylationSPDIFMQSHSENAIS
CHHHHHCCCCCCCCC
19.7220068231
743PhosphorylationDIFMQSHSENAISVK
HHHHCCCCCCCCCHH
37.4820068231
754PhosphorylationISVKEIVTEIESISQ
CCHHHHHHHHHHHHC
36.59-
758PhosphorylationEIVTEIESISQGVGQ
HHHHHHHHHHCCCCE
32.95-
760PhosphorylationVTEIESISQGVGQIQ
HHHHHHHHCCCCEEE
30.11-
779PhosphorylationILPNPCHTPKKNSIH
CCCCCCCCCCCCCHH
43.4530266825
782UbiquitinationNPCHTPKKNSIHELL
CCCCCCCCCCHHHHH
58.07-
784PhosphorylationCHTPKKNSIHELLLE
CCCCCCCCHHHHHHH
33.9123401153
795PhosphorylationLLLERAQTPENKPGH
HHHHHCCCCCCCCCC
31.4223401153
809PhosphorylationHMEQDEDSCTAQPEL
CCCCCCCCCCCCHHH
16.0023403867
811PhosphorylationEQDEDSCTAQPELAK
CCCCCCCCCCHHHHH
32.0723403867
870PhosphorylationPGSVRRATLEFEERL
CCCCCHHHHHHHHHH
25.6328985074
894PhosphorylationAPTCTSLSTRKNSKN
CCCCCCCCCCCCCCC
26.4028555341
899PhosphorylationSLSTRKNSKNDSSVA
CCCCCCCCCCCCCHH
35.5523403867
903PhosphorylationRKNSKNDSSVADLAP
CCCCCCCCCHHHHCC
35.7823403867
904PhosphorylationKNSKNDSSVADLAPK
CCCCCCCCHHHHCCC
24.9623403867
931PhosphorylationVLKEPEMSKGKGKYS
EECCCCCCCCCCCCC
36.2728258704
936AcetylationEMSKGKGKYSGSEAG
CCCCCCCCCCCCCCC
39.4625953088
985UbiquitinationTQQEGVLKDLRTVIP
CCCCHHHCHHCCCCC
52.92-
989PhosphorylationGVLKDLRTVIPYQES
HHHCHHCCCCCCCCC
30.0422468782
993PhosphorylationDLRTVIPYQESETQA
HHCCCCCCCCCCCCC
17.4922468782
996PhosphorylationTVIPYQESETQAVPL
CCCCCCCCCCCCCCC
30.3422468782
1019PhosphorylationIEYTHIVTSPNHTGP
EEEEEEECCCCCCCC
37.5523898821
1020PhosphorylationEYTHIVTSPNHTGPG
EEEEEECCCCCCCCC
16.8928122231
1024PhosphorylationIVTSPNHTGPGSEIA
EECCCCCCCCCCCCC
52.2728122231
1028PhosphorylationPNHTGPGSEIATSEK
CCCCCCCCCCCCCCC
29.0328122231
1081PhosphorylationQVLPLPHSSSPEHNR
CEECCCCCCCCCCCC
30.4826074081
1082PhosphorylationVLPLPHSSSPEHNRP
EECCCCCCCCCCCCC
47.0526074081
1083PhosphorylationLPLPHSSSPEHNRPT
ECCCCCCCCCCCCCC
37.0026074081
1090PhosphorylationSPEHNRPTDHPTSIL
CCCCCCCCCCCCCCC
43.6428464451
1094PhosphorylationNRPTDHPTSILSSPE
CCCCCCCCCCCCCCC
25.6128348404
1095PhosphorylationRPTDHPTSILSSPED
CCCCCCCCCCCCCCC
26.4428348404
1098PhosphorylationDHPTSILSSPEDRGS
CCCCCCCCCCCCCCC
42.0228348404
1099PhosphorylationHPTSILSSPEDRGSS
CCCCCCCCCCCCCCC
28.9428348404
1169PhosphorylationESQESPLSSGSEVPY
HHCCCCCCCCCCCCC
35.7228787133
1170PhosphorylationSQESPLSSGSEVPYK
HCCCCCCCCCCCCCC
54.7628787133
1182PhosphorylationPYKDSQLSSADLSLI
CCCCCCCCHHHHHHH
18.8230576142
1183PhosphorylationYKDSQLSSADLSLIS
CCCCCCCHHHHHHHH
34.1030576142
1187PhosphorylationQLSSADLSLISKLGD
CCCHHHHHHHHHHCC
24.9721815630
1191UbiquitinationADLSLISKLGDNTGE
HHHHHHHHHCCCCHH
49.88-
1215PhosphorylationVACRLPHSSSSENIK
EEECCCCCCCCCCHH
29.9423927012
1216PhosphorylationACRLPHSSSSENIKS
EECCCCCCCCCCHHH
34.5430278072
1217PhosphorylationCRLPHSSSSENIKSL
ECCCCCCCCCCHHHH
44.6923401153
1218PhosphorylationRLPHSSSSENIKSLS
CCCCCCCCCCHHHHC
36.2923927012
1223PhosphorylationSSSENIKSLSHSPGV
CCCCCHHHHCCCCCH
31.1630266825
1225PhosphorylationSENIKSLSHSPGVVK
CCCHHHHCCCCCHHH
29.0730266825
1227PhosphorylationNIKSLSHSPGVVKER
CHHHHCCCCCHHHHH
21.7030266825
1249PhosphorylationVVFQAGLTKPSQMRR
HHHHCCCCCHHHHHH
39.74-
1252PhosphorylationQAGLTKPSQMRRSAS
HCCCCCHHHHHHHHH
37.86-
1257PhosphorylationKPSQMRRSASLAKLG
CHHHHHHHHHHHHHH
16.3128102081
1259PhosphorylationSQMRRSASLAKLGYL
HHHHHHHHHHHHHHH
30.0623312004
1280PhosphorylationLPEREPASCESPHLK
CCCCCCCCCCCCCHH
29.1823401153
1283PhosphorylationREPASCESPHLKLLQ
CCCCCCCCCCHHHHH
23.1925159151
1295PhosphorylationLLQPFLRTDSGMHAM
HHHHHHHCCCCCCCC
36.3428450419
1297PhosphorylationQPFLRTDSGMHAMED
HHHHHCCCCCCCCCC
37.0928450419
1307PhosphorylationHAMEDQESLENPGAP
CCCCCHHHHCCCCCC
35.0429978859
1352PhosphorylationQYAKEFGSSQQYLLP
HHHHHHCCCCCEEEC
30.23-
1356PhosphorylationEFGSSQQYLLPRAGL
HHCCCCCEEECCCCC
11.5428796482
1400PhosphorylationPRQQHGRTHPLRRLK
CHHHCCCCCHHHHHH
32.2228152594
1408AcetylationHPLRRLKKANDKKRT
CHHHHHHHHCCCCCC
57.957377565
1412AcetylationRLKKANDKKRTTNPF
HHHHHCCCCCCCCCC
43.927377575
1413AcetylationLKKANDKKRTTNPFY
HHHHCCCCCCCCCCC
58.827377585
1415PhosphorylationKANDKKRTTNPFYNT
HHCCCCCCCCCCCCC
39.5426074081
1416PhosphorylationANDKKRTTNPFYNTM
HCCCCCCCCCCCCCC
44.9526074081
1420PhosphorylationKRTTNPFYNTM----
CCCCCCCCCCC----
15.8123403867
1422PhosphorylationTTNPFYNTM------
CCCCCCCCC------
16.9325159151

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

Oops, there are no upstream regulatory protein records of SSH2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSH2_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 SSH2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COF1_MOUSECfl1physical
11832213
MYO1D_HUMANMYO1Dphysical
27880917

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 SSH2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-487 ANDTHR-1422, AND MASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND MASSSPECTROMETRY.
"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-36 AND THR-1422, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, AND MASSSPECTROMETRY.

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