STRP2_HUMAN - dbPTM
STRP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STRP2_HUMAN
UniProt AC Q9ULQ0
Protein Name Striatin-interacting protein 2
Gene Name STRIP2
Organism Homo sapiens (Human).
Sequence Length 834
Subcellular Localization Cytoplasm . Enriched in lamellipodia.
Protein Description Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape..
Protein Sequence MEDPAAPGTGGPPANGNGNGGGKGKQAAPKGREAFRSQRRESEGSVDCPTLEFEYGDADGHAAELSELYSYTENLEFTNNRRCFEEDFKTQVQGKEWLELEEDAQKAYIMGLLDRLEVVSRERRLKVARAVLYLAQGTFGECDSEVDVLHWSRYNCFLLYQMGTFSTFLELLHMEIDNSQACSSALRKPAVSIADSTELRVLLSVMYLMVENIRLERETDPCGWRTARETFRTELSFSMHNEEPFALLLFSMVTKFCSGLAPHFPIKKVLLLLWKVVMFTLGGFEHLQTLKVQKRAELGLPPLAEDSIQVVKSMRAASPPSYTLDLGESQLAPPPSKLRGRRGSRRQLLTKQDSLDIYNERDLFKTEEPATEEEEESAGDGERTLDGELDLLEQDPLVPPPPSQAPLSAERVAFPKGLPWAPKVRQKDIEHFLEMSRNKFIGFTLGQDTDTLVGLPRPIHESVKTLKQHKYISIADVQIKNEEELEKCPMSLGEEVVPETPCEILYQGMLYSLPQYMIALLKILLAAAPTSKAKTDSINILADVLPEEMPITVLQSMKLGIDVNRHKEIIVKSISTLLLLLLKHFKLNHIYQFEYVSQHLVFANCIPLILKFFNQNILSYITAKNSISVLDYPCCTIQDLPELTTESLEAGDNSQFCWRNLFSCINLLRLLNKLTKWKHSRTMMLVVFKSAPILKRALKVKQAMLQLYVLKLLKLQTKYLGRQWRKSNMKTMSAIYQKVRHRMNDDWAYGNDIDARPWDFQAEECTLRANIEAFNSRRYDRPQDSEFSPVDNCLQSVLGQRLDLPEDFHYSYELWLEREVFSQPICWEELLQNH
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
37PhosphorylationKGREAFRSQRRESEG
HHHHHHHHHHHHCCC
26437602
42PhosphorylationFRSQRRESEGSVDCP
HHHHHHHCCCCCCCC
22210691
63UbiquitinationGDADGHAAELSELYS
CCCCCCHHHHHHHHH
24816145
72PhosphorylationLSELYSYTENLEFTN
HHHHHHHHCCCCCCC
22210691
127UbiquitinationSRERRLKVARAVLYL
CHHHHHHHHHHHHHH
24816145
197PhosphorylationAVSIADSTELRVLLS
CCCCCCHHHHHHHHH
24719451
204UbiquitinationTELRVLLSVMYLMVE
HHHHHHHHHHHHHHH
24816145
207PhosphorylationRVLLSVMYLMVENIR
HHHHHHHHHHHHHCC
-
230UbiquitinationGWRTARETFRTELSF
CCHHHHHHHHHEECC
27667366
294UbiquitinationLQTLKVQKRAELGLP
HHHHCHHHHHHHCCC
27667366
318PhosphorylationVKSMRAASPPSYTLD
HHHHHHCCCCCEEEC
23401153
321PhosphorylationMRAASPPSYTLDLGE
HHHCCCCCEEECCCC
29255136
322PhosphorylationRAASPPSYTLDLGES
HHCCCCCEEECCCCC
30278072
323PhosphorylationAASPPSYTLDLGESQ
HCCCCCEEECCCCCC
29255136
329PhosphorylationYTLDLGESQLAPPPS
EEECCCCCCCCCCCH
23403867
336PhosphorylationSQLAPPPSKLRGRRG
CCCCCCCHHHCCCCC
23403867
350PhosphorylationGSRRQLLTKQDSLDI
CCHHHHCHHCHHCHH
30624053
354PhosphorylationQLLTKQDSLDIYNER
HHCHHCHHCHHHCCC
23401153
358PhosphorylationKQDSLDIYNERDLFK
HCHHCHHHCCCHHCC
23403867
365UbiquitinationYNERDLFKTEEPATE
HCCCHHCCCCCCCCH
24816145
371UbiquitinationFKTEEPATEEEEESA
CCCCCCCCHHHHHHC
27667366
408PhosphorylationPPSQAPLSAERVAFP
CCCCCCCCHHHCCCC
24719451
436UbiquitinationIEHFLEMSRNKFIGF
HHHHHHHCCCCCCEE
21890473
444PhosphorylationRNKFIGFTLGQDTDT
CCCCCEEECCCCCCC
-
449PhosphorylationGFTLGQDTDTLVGLP
EEECCCCCCCCCCCC
-
462PhosphorylationLPRPIHESVKTLKQH
CCCCHHHHHHHHHHC
-
465PhosphorylationPIHESVKTLKQHKYI
CHHHHHHHHHHCCCE
-
471PhosphorylationKTLKQHKYISIADVQ
HHHHHCCCEEEEEEE
27642862
473PhosphorylationLKQHKYISIADVQIK
HHHCCCEEEEEEEEC
-
491PhosphorylationELEKCPMSLGEEVVP
HHHHCCCCCCCCCCC
25072903
500UbiquitinationGEEVVPETPCEILYQ
CCCCCCCCHHHHHHC
21890473
500PhosphorylationGEEVVPETPCEILYQ
CCCCCCCCHHHHHHC
25072903
506PhosphorylationETPCEILYQGMLYSL
CCHHHHHHCCHHHCH
25072903
511PhosphorylationILYQGMLYSLPQYMI
HHHCCHHHCHHHHHH
25072903
512PhosphorylationLYQGMLYSLPQYMIA
HHCCHHHCHHHHHHH
25072903
516PhosphorylationMLYSLPQYMIALLKI
HHHCHHHHHHHHHHH
25072903
532UbiquitinationLAAAPTSKAKTDSIN
HHHCCCCCCCCCCCH
32015554
577UbiquitinationIVKSISTLLLLLLKH
HHHHHHHHHHHHHHH
23000965
695UbiquitinationFKSAPILKRALKVKQ
ECCHHHHHHHHHHHH
32015554
708PhosphorylationKQAMLQLYVLKLLKL
HHHHHHHHHHHHHHH
25690035
736PhosphorylationMKTMSAIYQKVRHRM
HHHHHHHHHHHHHHC
18083107
738UbiquitinationTMSAIYQKVRHRMND
HHHHHHHHHHHHCCC
23000965
738 (in isoform 1)Ubiquitination-21890473
738 (in isoform 2)Ubiquitination-21890473
788PhosphorylationRPQDSEFSPVDNCLQ
CCCCCCCCCHHHHHH
19081932

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 STRP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STRP2_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 STRP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

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 STRP2_HUMAN

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Related Literatures of Post-Translational Modification

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