STRN4_HUMAN - dbPTM
STRN4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STRN4_HUMAN
UniProt AC Q9NRL3
Protein Name Striatin-4
Gene Name STRN4
Organism Homo sapiens (Human).
Sequence Length 753
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Cell projection, dendritic spine. CTTNBP2-binding may regulate dendritic spine distribution..
Protein Description Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein..
Protein Sequence MMEERAAAAVAAAASSCRPLGSGAGPGPTGAAPVSAPAPGPGPAGKGGGGGGSPGPTAGPEPLSLPGILHFIQHEWARFEAEKARWEAERAELQAQVAFLQGERKGQENLKTDLVRRIKMLEYALKQERAKYHKLKFGTDLNQGEKKADVSEQVSNGPVESVTLENSPLVWKEGRQLLRQYLEEVGYTDTILDMRSKRVRSLLGRSLELNGAVEPSEGAPRAPPGPAGLSGGESLLVKQIEEQIKRNAAGKDGKERLGGSVLGQIPFLQNCEDEDSDEDDELDSVQHKKQRVKLPSKALVPEMEDEDEEDDSEDAINEFDFLGSGEDGEGAPDPRRCTVDGSPHELESRRVKLQGILADLRDVDGLPPKVTGPPPGTPQPRPHEDVFIMDTIGGGEVSLGDLADLTVTNDNDLSCDLSDSKDAFKKTWNPKFTLRSHYDGIRSLAFHHSQSALLTASEDGTLKLWNLQKAVTAKKNAALDVEPIHAFRAHRGPVLAVAMGSNSEYCYSGGADACIHSWKIPDLSMDPYDGYDPSVLSHVLEGHGDAVWGLAFSPTSQRLASCSADGTVRIWDPSSSSPACLCTFPTASEHGVPTSVAFTSTEPAHIVASFRSGDTVLYDMEVGSALLTLESRGSSGPTQINQVVSHPNQPLTITAHDDRGIRFLDNRTGKPVHSMVAHLDAVTCLAVDPNGAFLMSGSHDCSLRLWSLDNKTCVQEITAHRKKHEEAIHAVACHPSKALIASAGADALAKVFV
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------MMEERAAAA
------CHHHHHHHH		8.02-
16PhosphorylationAVAAAASSCRPLGSG
HHHHHHHHCCCCCCC		14.9318452278
17UbiquitinationVAAAASSCRPLGSGA
HHHHHHHCCCCCCCC		4.87-
22PhosphorylationSSCRPLGSGAGPGPT
HHCCCCCCCCCCCCC		32.9026074081
29PhosphorylationSGAGPGPTGAAPVSA
CCCCCCCCCCCCCCC		45.4226074081
35PhosphorylationPTGAAPVSAPAPGPG
CCCCCCCCCCCCCCC		27.7226074081
53PhosphorylationKGGGGGGSPGPTAGP
CCCCCCCCCCCCCCC		29.9225159151
57PhosphorylationGGGSPGPTAGPEPLS
CCCCCCCCCCCCCCC		50.6022199227
64PhosphorylationTAGPEPLSLPGILHF
CCCCCCCCCCCHHHH		43.1428464451
111UbiquitinationRKGQENLKTDLVRRI
CCCHHHHCHHHHHHH		52.12-
126UbiquitinationKMLEYALKQERAKYH
HHHHHHHHHHHHHHH		41.77-
136UbiquitinationRAKYHKLKFGTDLNQ
HHHHHHCCCCCCCCC		46.69-
136AcetylationRAKYHKLKFGTDLNQ
HHHHHHCCCCCCCCC		46.6920167786
136UbiquitinationRAKYHKLKFGTDLNQ
HHHHHHCCCCCCCCC		46.69-
151PhosphorylationGEKKADVSEQVSNGP
CCCCCCHHHHHHCCC		23.9023898821
155PhosphorylationADVSEQVSNGPVESV
CCHHHHHHCCCCCEE		35.4529978859
161PhosphorylationVSNGPVESVTLENSP
HHCCCCCEEEECCCC		22.1930108239
163PhosphorylationNGPVESVTLENSPLV
CCCCCEEEECCCCCC		37.3230108239
167PhosphorylationESVTLENSPLVWKEG
CEEEECCCCCCHHHH		15.3825159151
196PhosphorylationDTILDMRSKRVRSLL
CHHHHHHHHHHHHHH		20.4124719451
201PhosphorylationMRSKRVRSLLGRSLE
HHHHHHHHHHCCCEE		25.7028857561
206PhosphorylationVRSLLGRSLELNGAV
HHHHHCCCEEECCCC		25.1330266825
216PhosphorylationLNGAVEPSEGAPRAP
ECCCCCCCCCCCCCC		34.8523186163
230PhosphorylationPPGPAGLSGGESLLV
CCCCCCCCCHHHHHH		43.7828555341
234PhosphorylationAGLSGGESLLVKQIE
CCCCCHHHHHHHHHH		30.2228555341
260PhosphorylationGKERLGGSVLGQIPF
CCHHCCCCCCCCCCC		16.6328464451
276PhosphorylationQNCEDEDSDEDDELD
CCCCCCCCCCCCHHH		40.6325159151
284PhosphorylationDEDDELDSVQHKKQR
CCCCHHHHHHHHHHH		35.9823927012
296PhosphorylationKQRVKLPSKALVPEM
HHHCCCCHHCCCCCC		40.7824719451
312PhosphorylationDEDEEDDSEDAINEF
CCCCCCCCHHHHHHH		50.0920873877
324PhosphorylationNEFDFLGSGEDGEGA
HHHCCCCCCCCCCCC		40.9526074081
338PhosphorylationAPDPRRCTVDGSPHE
CCCCCCCCCCCCHHH		21.5925850435
342PhosphorylationRRCTVDGSPHELESR
CCCCCCCCHHHHHHH		20.7225159151
348PhosphorylationGSPHELESRRVKLQG
CCHHHHHHHHHEHHH		37.7028985074
352UbiquitinationELESRRVKLQGILAD
HHHHHHHEHHHHHHH		33.03-
371PhosphorylationDGLPPKVTGPPPGTP
CCCCCCCCCCCCCCC		50.5326552605
377PhosphorylationVTGPPPGTPQPRPHE
CCCCCCCCCCCCCCC		25.2329255136
431UbiquitinationFKKTWNPKFTLRSHY
HHHHCCCCEEEECCC		48.0121890473
433PhosphorylationKTWNPKFTLRSHYDG
HHCCCCEEEECCCCH		27.6428450419
475MalonylationQKAVTAKKNAALDVE
HHHHHCCCCCCCCCC		49.7226320211
561PhosphorylationPTSQRLASCSADGTV
CCHHHHHCCCCCCCE		17.1327251275
563O-linked_GlycosylationSQRLASCSADGTVRI
HHHHHCCCCCCCEEE		27.2230379171
609PhosphorylationEPAHIVASFRSGDTV
CCCEEEEEECCCCEE		15.4224719451
718PhosphorylationKTCVQEITAHRKKHE
CHHHHHHHHHHHHHH		18.69-
722AcetylationQEITAHRKKHEEAIH
HHHHHHHHHHHHHHH		48.9226051181
723AcetylationEITAHRKKHEEAIHA
HHHHHHHHHHHHHHH		57.0926051181
723UbiquitinationEITAHRKKHEEAIHA
HHHHHHHHHHHHHHH		57.09-
736PhosphorylationHAVACHPSKALIASA
HHHHCCHHHHHHHHC		13.59-
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 STRN4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STRN4_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 STRN4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAD5_HUMANAK5physical
16169070
ASNS_HUMANASNSphysical
16169070
DX39B_HUMANDDX39Bphysical
16169070
CLD12_HUMANCLDN12physical
16169070
GDF9_HUMANGDF9physical
16169070
NBEA_HUMANNBEAphysical
16169070
ECSIT_HUMANECSITphysical
16169070
ADT3_HUMANSLC25A6physical
16169070
MTG1_HUMANMTG1physical
16169070
KLDC2_HUMANKLHDC2physical
16169070
TOX4_HUMANTOX4physical
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 STRN4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-276, AND MASS SPECTROMETRY.
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-206, AND MASSSPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-276, AND MASS SPECTROMETRY.
"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-276, AND MASSSPECTROMETRY.

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