DEMA_HUMAN - dbPTM
DEMA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DEMA_HUMAN
UniProt AC Q08495
Protein Name Dematin
Gene Name DMTN
Organism Homo sapiens (Human).
Sequence Length 405
Subcellular Localization Cytoplasm. Cytoplasm, cytosol. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane. Membrane. Endomembrane system. Cell projection. Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellular
Protein Description Membrane-cytoskeleton-associated protein with F-actin-binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Plays also a role as a modulator of actin dynamics in fibroblasts; acts as a negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation..
Protein Sequence MERLQKQPLTSPGSVSPSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPRSRERSLSPKSTSPPPSPEVWADSRSPGIISQASAPRTTGTPRTSLPHFHHPETSRPDSNIYKKPPIYKQRESVGGSPQTKHLIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQREELSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHQGTSKSSSLPAYGRTTLSRLQSTEFSPSGSETGSPGLQNGEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNKGRTKLPPGVDRMRLERHLSAEDFSRVFAMSPEEFGKLALWKRNELKKKASLF
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
10PhosphorylationRLQKQPLTSPGSVSP
HHHCCCCCCCCCCCC		39.2929255136
11PhosphorylationLQKQPLTSPGSVSPS
HHCCCCCCCCCCCCC		34.6429255136
14PhosphorylationQPLTSPGSVSPSRDS
CCCCCCCCCCCCCCC		23.8630266825
16PhosphorylationLTSPGSVSPSRDSSV
CCCCCCCCCCCCCCC		20.8923401153
18O-linked_GlycosylationSPGSVSPSRDSSVPG
CCCCCCCCCCCCCCC		41.0130379171
18PhosphorylationSPGSVSPSRDSSVPG
CCCCCCCCCCCCCCC		41.0130266825
21PhosphorylationSVSPSRDSSVPGSPS
CCCCCCCCCCCCCCH		31.9329255136
22PhosphorylationVSPSRDSSVPGSPSS
CCCCCCCCCCCCCHH		36.3029255136
26PhosphorylationRDSSVPGSPSSIVAK
CCCCCCCCCHHHEEE		18.6223401153
28PhosphorylationSSVPGSPSSIVAKMD
CCCCCCCHHHEEEEC		34.1030266825
29PhosphorylationSVPGSPSSIVAKMDN
CCCCCCHHHEEEECC		25.1930266825
41PhosphorylationMDNQVLGYKDLAAIP
ECCCCCCCCHHHCCC		9.36-
64PhosphorylationERPDLMIYEPHFTYS
CCCCEEEECCCCCHH		14.9425884760
69PhosphorylationMIYEPHFTYSLLEHV
EEECCCCCHHHHHHC		14.7928348404
70PhosphorylationIYEPHFTYSLLEHVE
EECCCCCHHHHHHCC		9.0725884760
71PhosphorylationYEPHFTYSLLEHVEL
ECCCCCHHHHHHCCC		24.3433259812
81PhosphorylationEHVELPRSRERSLSP
HHCCCCCCCCCCCCC		36.2324719451
85PhosphorylationLPRSRERSLSPKSTS
CCCCCCCCCCCCCCC		28.5729691806
87PhosphorylationRSRERSLSPKSTSPP
CCCCCCCCCCCCCCC		31.3729691806
90PhosphorylationERSLSPKSTSPPPSP
CCCCCCCCCCCCCCH		37.1923401153
91PhosphorylationRSLSPKSTSPPPSPE
CCCCCCCCCCCCCHH		51.9130266825
92PhosphorylationSLSPKSTSPPPSPEV
CCCCCCCCCCCCHHH		42.3623927012
96PhosphorylationKSTSPPPSPEVWADS
CCCCCCCCHHHCCCC		39.1923927012
103PhosphorylationSPEVWADSRSPGIIS
CHHHCCCCCCCCCCC		27.2323927012
105PhosphorylationEVWADSRSPGIISQA
HHCCCCCCCCCCCCC		31.2825159151
110PhosphorylationSRSPGIISQASAPRT
CCCCCCCCCCCCCCC		20.1323025827
110O-linked_GlycosylationSRSPGIISQASAPRT
CCCCCCCCCCCCCCC		20.1330379171
113PhosphorylationPGIISQASAPRTTGT
CCCCCCCCCCCCCCC		31.0423025827
123PhosphorylationRTTGTPRTSLPHFHH
CCCCCCCCCCCCCCC		35.5024275569
124PhosphorylationTTGTPRTSLPHFHHP
CCCCCCCCCCCCCCC		40.9824275569
133PhosphorylationPHFHHPETSRPDSNI
CCCCCCCCCCCCCCC		34.1928555341
138PhosphorylationPETSRPDSNIYKKPP
CCCCCCCCCCCCCCC		28.0128555341
141PhosphorylationSRPDSNIYKKPPIYK
CCCCCCCCCCCCCCC		19.7427642862
143AcetylationPDSNIYKKPPIYKQR
CCCCCCCCCCCCCCC		38.777834059
152PhosphorylationPIYKQRESVGGSPQT
CCCCCCHHCCCCHHH		28.4029691806
156PhosphorylationQRESVGGSPQTKHLI
CCHHCCCCHHHHHHH		14.1229255136
159PhosphorylationSVGGSPQTKHLIEDL
HCCCCHHHHHHHHHH		24.6629255136
191PhosphorylationPAKIETDYWPCPPSL
CCCEECCCCCCCCCC		20.7627642862
211PhosphorylationEWRKRKASRRGAEEE
HHHHHHHHHCCCHHH		26.08-
226PhosphorylationEEEEDDDSGEEMKAL
HHHCCCCCHHHHHHH		55.9125159151
234PhosphorylationGEEMKALRERQREEL
HHHHHHHHHHHHHHH		41.7432645325
245PhosphorylationREELSKVTSNLGKMI
HHHHHHHHHHHHHHH		18.6828060719
246PhosphorylationEELSKVTSNLGKMIL
HHHHHHHHHHHHHHH		32.8028060719
249PhosphorylationSKVTSNLGKMILKEE
HHHHHHHHHHHHHHH		23.0332645325
259PhosphorylationILKEEMEKSLPIRRK
HHHHHHHHCCCCCCC		56.8532645325
259AcetylationILKEEMEKSLPIRRK
HHHHHHHHCCCCCCC		56.8519814881
260PhosphorylationLKEEMEKSLPIRRKT
HHHHHHHCCCCCCCC		26.5224719451
266AcetylationKSLPIRRKTRSLPDR
HCCCCCCCCCCCCCC		38.147712297
267PhosphorylationSLPIRRKTRSLPDRT
CCCCCCCCCCCCCCC		24.5528857561
269PhosphorylationPIRRKTRSLPDRTPF
CCCCCCCCCCCCCCC		49.8623401153
274PhosphorylationTRSLPDRTPFHTSLH
CCCCCCCCCCCCCCC		37.3727987026
278 (in isoform 3)Phosphorylation-33.1026657352
278PhosphorylationPDRTPFHTSLHQGTS
CCCCCCCCCCCCCCC		33.1023401153
279 (in isoform 3)Phosphorylation-18.4526657352
279PhosphorylationDRTPFHTSLHQGTSK
CCCCCCCCCCCCCCC		18.4523927012
282 (in isoform 3)Phosphorylation-63.2522210691
284PhosphorylationHTSLHQGTSKSSSLP
CCCCCCCCCCCCCCC		26.8123927012
285PhosphorylationTSLHQGTSKSSSLPA
CCCCCCCCCCCCCCC		37.0523927012
287PhosphorylationLHQGTSKSSSLPAYG
CCCCCCCCCCCCCCC		25.5630266825
288PhosphorylationHQGTSKSSSLPAYGR
CCCCCCCCCCCCCCC		39.3630266825
289PhosphorylationQGTSKSSSLPAYGRT
CCCCCCCCCCCCCCC		45.5223401153
293PhosphorylationKSSSLPAYGRTTLSR
CCCCCCCCCCCCHHH		12.7524702127
296PhosphorylationSLPAYGRTTLSRLQS
CCCCCCCCCHHHHHC		27.9422210691
297PhosphorylationLPAYGRTTLSRLQST
CCCCCCCCHHHHHCC		22.7522210691
299PhosphorylationAYGRTTLSRLQSTEF
CCCCCCHHHHHCCCC		28.9322210691
303 (in isoform 2)Phosphorylation-34.2026657352
303PhosphorylationTTLSRLQSTEFSPSG
CCHHHHHCCCCCCCC		34.2027273156
304PhosphorylationTLSRLQSTEFSPSGS
CHHHHHCCCCCCCCC		28.2628348404
304 (in isoform 2)Phosphorylation-28.2626657352
307PhosphorylationRLQSTEFSPSGSETG
HHHCCCCCCCCCCCC		16.3625850435
307 (in isoform 2)Phosphorylation-16.3622210691
309PhosphorylationQSTEFSPSGSETGSP
HCCCCCCCCCCCCCC		54.4725850435
311PhosphorylationTEFSPSGSETGSPGL
CCCCCCCCCCCCCCC		36.0028857561
313PhosphorylationFSPSGSETGSPGLQN
CCCCCCCCCCCCCCC		44.6628857561
315PhosphorylationPSGSETGSPGLQNGE
CCCCCCCCCCCCCCC		24.1828060719
333PhosphorylationGRMDRGNSLPCVLEQ
CCCCCCCCCCEEEEC		36.1923401153
343PhosphorylationCVLEQKIYPYEMLVV
EEEECEECCEEEEEE		13.54-
372PhosphorylationMRLERHLSAEDFSRV
HHHHHHCCHHHHHHH		24.4023401153
377PhosphorylationHLSAEDFSRVFAMSP
HCCHHHHHHHHCCCH		39.6023025827
383PhosphorylationFSRVFAMSPEEFGKL
HHHHHCCCHHHHHHH		26.2321815630
403PhosphorylationNELKKKASLF-----
HHHHHHHHCC-----		38.918341682
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
90SPhosphorylationKinaseERK2P28482
PSP
96SPhosphorylationKinaseERK2P28482
PSP
403SPhosphorylationKinasePRKACAP17612
GPS
403SPhosphorylationKinasePKA-FAMILY-GPS
403SPhosphorylationKinasePKA-Uniprot
403SPhosphorylationKinasePKA_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
403SPhosphorylation

21084299
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 DEMA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPCR_HUMANPROCRphysical
16169070
DC1L2_HUMANDYNC1LI2physical
16169070
A4_HUMANAPPphysical
21832049
GOGA2_HUMANGOLGA2physical
25416956
1433E_HUMANYWHAEphysical
26186194
1433Z_HUMANYWHAZphysical
26186194
TPC10_HUMANTRAPPC10physical
26186194
NU188_HUMANNUP188physical
26186194
UBR1_HUMANUBR1physical
26186194
DPP9_HUMANDPP9physical
26186194
DPP9_HUMANDPP9physical
28514442
1433Z_HUMANYWHAZphysical
28514442
UBR1_HUMANUBR1physical
28514442
1433G_HUMANYWHAGphysical
28514442
1433B_HUMANYWHABphysical
28514442
1433E_HUMANYWHAEphysical
28514442
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 DEMA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A phosphorylation-induced conformation change in dematin headpiece.";
Jiang Z.G., McKnight C.J.;
Structure 14:379-387(2006).
Cited for: STRUCTURE BY NMR OF 342-405, AND PHOSPHORYLATION AT SER-403.
"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-96 AND SER-105, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10; SER-14; SER-16;SER-22; SER-26; SER-28; SER-92; SER-96; SER-105; SER-156; SER-226;SER-289; SER-333 AND SER-372, AND MASS SPECTROMETRY.

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