STRP1_HUMAN - dbPTM
STRP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STRP1_HUMAN
UniProt AC Q5VSL9
Protein Name Striatin-interacting protein 1
Gene Name STRIP1
Organism Homo sapiens (Human).
Sequence Length 837
Subcellular Localization Cytoplasm . Enriched on the plasma membrane.
Protein Description Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape..
Protein Sequence MEPAVGGPGPLIVNNKQPQPPPPPPPAAAQPPPGAPRAAAGLLPGGKAREFNRNQRKDSEGYSESPDLEFEYADTDKWAAELSELYSYTEGPEFLMNRKCFEEDFRIHVTDKKWTELDTNQHRTHAMRLLDGLEVTAREKRLKVARAILYVAQGTFGECSSEAEVQSWMRYNIFLLLEVGTFNALVELLNMEIDNSAACSSAVRKPAISLADSTDLRVLLNIMYLIVETVHQECEGDKAEWRTMRQTFRAELGSPLYNNEPFAIMLFGMVTKFCSGHAPHFPMKKVLLLLWKTVLCTLGGFEELQSMKAEKRSILGLPPLPEDSIKVIRNMRAASPPASASDLIEQQQKRGRREHKALIKQDNLDAFNERDPYKADDSREEEEENDDDNSLEGETFPLERDEVMPPPLQHPQTDRLTCPKGLPWAPKVREKDIEMFLESSRSKFIGYTLGSDTNTVVGLPRPIHESIKTLKQHKYTSIAEVQAQMEEEYLRSPLSGGEEEVEQVPAETLYQGLLPSLPQYMIALLKILLAAAPTSKAKTDSINILADVLPEEMPTTVLQSMKLGVDVNRHKEVIVKAISAVLLLLLKHFKLNHVYQFEYMAQHLVFANCIPLILKFFNQNIMSYITAKNSISVLDYPHCVVHELPELTAESLEAGDSNQFCWRNLFSCINLLRILNKLTKWKHSRTMMLVVFKSAPILKRALKVKQAMMQLYVLKLLKVQTKYLGRQWRKSNMKTMSAIYQKVRHRLNDDWAYGNDLDARPWDFQAEECALRANIERFNARRYDRAHSNPDFLPVDNCLQSVLGQRVDLPEDFQMNYDLWLEREVFSKPISWEELLQ
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
1Acetylation-------MEPAVGGP
-------CCCCCCCC
22223895
18UbiquitinationLIVNNKQPQPPPPPP
EEECCCCCCCCCCCC
29967540
47UbiquitinationAGLLPGGKAREFNRN
HCCCCCCCHHCCCCC
29967540
57UbiquitinationEFNRNQRKDSEGYSE
CCCCCCCCCCCCCCC
29967540
59PhosphorylationNRNQRKDSEGYSESP
CCCCCCCCCCCCCCC
22167270
62PhosphorylationQRKDSEGYSESPDLE
CCCCCCCCCCCCCCC
22167270
63PhosphorylationRKDSEGYSESPDLEF
CCCCCCCCCCCCCCC
22167270
65PhosphorylationDSEGYSESPDLEFEY
CCCCCCCCCCCCCEE
25159151
72PhosphorylationSPDLEFEYADTDKWA
CCCCCCEECCHHHHH
29978859
75PhosphorylationLEFEYADTDKWAAEL
CCCEECCHHHHHHHH
21406692
99UbiquitinationPEFLMNRKCFEEDFR
CHHHHCCHHHHCCCE
-
113UbiquitinationRIHVTDKKWTELDTN
EEEECCCCCEECCCH
29967540
214PhosphorylationAISLADSTDLRVLLN
CCCCCCCCHHHHHHH
25332170
230UbiquitinationMYLIVETVHQECEGD
HHHHHHHHHHHCCCC
27667366
240PhosphorylationECEGDKAEWRTMRQT
HCCCCHHHHHHHHHH
32645325
244PhosphorylationDKAEWRTMRQTFRAE
CHHHHHHHHHHHHHH
33259812
265UbiquitinationNNEPFAIMLFGMVTK
CCCCCHHHHHHHHHH
29967540
271PhosphorylationIMLFGMVTKFCSGHA
HHHHHHHHHHHCCCC
-
275PhosphorylationGMVTKFCSGHAPHFP
HHHHHHHCCCCCCCC
29083192
313PhosphorylationSMKAEKRSILGLPPL
HHHHHHHCCCCCCCC
20068231
324PhosphorylationLPPLPEDSIKVIRNM
CCCCCHHHHHHHHHH
20068231
325UbiquitinationPPLPEDSIKVIRNMR
CCCCHHHHHHHHHHH
32015554
326UbiquitinationPLPEDSIKVIRNMRA
CCCHHHHHHHHHHHH
-
335PhosphorylationIRNMRAASPPASASD
HHHHHHCCCCCCHHH
19664994
339PhosphorylationRAASPPASASDLIEQ
HHCCCCCCHHHHHHH
30278072
341PhosphorylationASPPASASDLIEQQQ
CCCCCCHHHHHHHHH
29209046
360UbiquitinationREHKALIKQDNLDAF
HHHHHHHHHCCHHHH
29967540
373UbiquitinationAFNERDPYKADDSRE
HHHCCCCCCCCCCHH
29967540
390PhosphorylationEENDDDNSLEGETFP
HHCCCCCCCCCCEEC
26657352
416UbiquitinationQHPQTDRLTCPKGLP
CCCCCCCCCCCCCCC
27667366
420UbiquitinationTDRLTCPKGLPWAPK
CCCCCCCCCCCCCCC
32015554
436UbiquitinationREKDIEMFLESSRSK
CHHHHHHHHHHCCCC
21890473
441UbiquitinationEMFLESSRSKFIGYT
HHHHHHCCCCCCEEE
32015554
468UbiquitinationRPIHESIKTLKQHKY
CCHHHHHHHHHHCCC
29967540
489PhosphorylationQAQMEEEYLRSPLSG
HHHHHHHHHHCCCCC
-
492PhosphorylationMEEEYLRSPLSGGEE
HHHHHHHCCCCCCHH
-
522UbiquitinationPSLPQYMIALLKILL
CCHHHHHHHHHHHHH
22817900
536MalonylationLAAAPTSKAKTDSIN
HHHCCCCCCCCCCCH
26320211
536UbiquitinationLAAAPTSKAKTDSIN
HHHCCCCCCCCCCCH
32015554
538UbiquitinationAAPTSKAKTDSINIL
HCCCCCCCCCCCHHH
-
560PhosphorylationMPTTVLQSMKLGVDV
CCHHHHHHCCCCCCC
19060867
595PhosphorylationHFKLNHVYQFEYMAQ
HHCCCCCHHHHHHHH
-
599PhosphorylationNHVYQFEYMAQHLVF
CCCHHHHHHHHHHHH
-
604UbiquitinationFEYMAQHLVFANCIP
HHHHHHHHHHHHHHH
32015554
627UbiquitinationNIMSYITAKNSISVL
CHHHHHHHCCCCEEC
27667366
646UbiquitinationCVVHELPELTAESLE
CEECCCCCCCHHHHH
27667366
647UbiquitinationVVHELPELTAESLEA
EECCCCCCCHHHHHC
21890473
666UbiquitinationQFCWRNLFSCINLLR
HHHHHHHHHHHHHHH
21890473
677AcetylationNLLRILNKLTKWKHS
HHHHHHHHHHCCCCC
18585881
699UbiquitinationFKSAPILKRALKVKQ
ECCHHHHHHHHHHHH
32015554
712PhosphorylationKQAMMQLYVLKLLKV
HHHHHHHHHHHHHHH
-
722UbiquitinationKLLKVQTKYLGRQWR
HHHHHHHHHHCHHHH
27667366
722MethylationKLLKVQTKYLGRQWR
HHHHHHHHHHCHHHH
23644510
733UbiquitinationRQWRKSNMKTMSAIY
HHHHHHCHHHHHHHH
22817900
733 (in isoform 2)Ubiquitination-21906983
740PhosphorylationMKTMSAIYQKVRHRL
HHHHHHHHHHHHHHC
22817900
742UbiquitinationTMSAIYQKVRHRLND
HHHHHHHHHHHHCCC
21890473
752UbiquitinationHRLNDDWAYGNDLDA
HHCCCCCCCCCCCCC
22817900
788PhosphorylationRRYDRAHSNPDFLPV
HHHHCCCCCCCCCCH
28450419
828UbiquitinationLEREVFSKPISWEEL
HHHHHHCCCCCHHHH
22817900
828 (in isoform 1)Ubiquitination-21906983

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 STRP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STRP1_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 STRP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
2AAA_HUMANPPP2R1Aphysical
18782753
PP2AA_HUMANPPP2CAphysical
18782753
STRN_HUMANSTRNphysical
18782753
STRN3_HUMANSTRN3physical
18782753
STK26_HUMANSTK26physical
18782753
STRN4_HUMANSTRN4physical
18782753
PHOCN_HUMANMOB4physical
18782753
PDC10_HUMANPDCD10physical
18782753
CT2NL_HUMANCTTNBP2NLphysical
18782753
SIKE1_HUMANSIKE1physical
18782753
STRP2_HUMANSTRIP2physical
18782753
SLMAP_HUMANSLMAPphysical
18782753
FGOP2_HUMANFGFR1OP2physical
18782753
STRN4_HUMANSTRN4physical
22939629
POP1_HUMANPOP1physical
22939629
GT251_HUMANCOLGALT1physical
22939629
KATL2_HUMANKATNAL2physical
22939629
SPTN1_HUMANSPTAN1physical
22939629
FUBP2_HUMANKHSRPphysical
22939629
NU214_HUMANNUP214physical
22939629
RBM4_HUMANRBM4physical
22939629
SLMAP_HUMANSLMAPphysical
26344197

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 STRP1_HUMAN

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Related Literatures of Post-Translational Modification

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