RMD3_HUMAN - dbPTM
RMD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RMD3_HUMAN
UniProt AC Q96TC7
Protein Name Regulator of microtubule dynamics protein 3
Gene Name RMDN3
Organism Homo sapiens (Human).
Sequence Length 470
Subcellular Localization Mitochondrion membrane
Single-pass membrane protein. Mitochondrion outer membrane. Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. In interphase localizes in the cytoplasm, and during mitosis localizes to
Protein Description Involved in cellular calcium homeostasis regulation. May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis..
Protein Sequence MSRLGALGGARAGLGLLLGTAAGLGFLCLLYSQRWKRTQRHGRSQSLPNSLDYTQTSDPGRHVMLLRAVPGGAGDASVLPSLPREGQEKVLDRLDFVLTSLVALRREVEELRSSLRGLAGEIVGEVRCHMEENQRVARRRRFPFVRERSDSTGSSSVYFTASSGATFTDAESEGGYTTANAESDNERDSDKESEDGEDEVSCETVKMGRKDSLDLEEEAASGASSALEAGGSSGLEDVLPLLQQADELHRGDEQGKREGFQLLLNNKLVYGSRQDFLWRLARAYSDMCELTEEVSEKKSYALDGKEEAEAALEKGDESADCHLWYAVLCGQLAEHESIQRRIQSGFSFKEHVDKAIALQPENPMAHFLLGRWCYQVSHLSWLEKKTATALLESPLSATVEDALQSFLKAEELQPGFSKAGRVYISKCYRELGKNSEARWWMKLALELPDVTKEDLAIQKDLEELEVILRD
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
44PhosphorylationRTQRHGRSQSLPNSL
HHHHCCCCCCCCCCC		28.8129255136
46PhosphorylationQRHGRSQSLPNSLDY
HHCCCCCCCCCCCCC		47.2225159151
50PhosphorylationRSQSLPNSLDYTQTS
CCCCCCCCCCCCCCC		22.2223927012
53PhosphorylationSLPNSLDYTQTSDPG
CCCCCCCCCCCCCCC		13.1723927012
54PhosphorylationLPNSLDYTQTSDPGR
CCCCCCCCCCCCCCC		25.6620164059
56PhosphorylationNSLDYTQTSDPGRHV
CCCCCCCCCCCCCEE		27.5723927012
57PhosphorylationSLDYTQTSDPGRHVM
CCCCCCCCCCCCEEE		31.8023927012
77PhosphorylationPGGAGDASVLPSLPR
CCCCCCCHHCCCCCC		29.0028857561
113PhosphorylationREVEELRSSLRGLAG
HHHHHHHHHHHHHHH		46.4821406692
114PhosphorylationEVEELRSSLRGLAGE
HHHHHHHHHHHHHHH		18.6920068231
149PhosphorylationFPFVRERSDSTGSSS
CCCEEECCCCCCCCC		31.0322817900
151PhosphorylationFVRERSDSTGSSSVY
CEEECCCCCCCCCEE		35.5922817900
152PhosphorylationVRERSDSTGSSSVYF
EEECCCCCCCCCEEE		46.1822817900
154PhosphorylationERSDSTGSSSVYFTA
ECCCCCCCCCEEEEE		21.3822817900
155PhosphorylationRSDSTGSSSVYFTAS
CCCCCCCCCEEEEEC		25.7622817900
156PhosphorylationSDSTGSSSVYFTASS
CCCCCCCCEEEEECC		23.6422817900
176PhosphorylationDAESEGGYTTANAES
ECCCCCCCCCCCCCC		16.2722544307
177PhosphorylationAESEGGYTTANAESD
CCCCCCCCCCCCCCC		23.78-
183PhosphorylationYTTANAESDNERDSD
CCCCCCCCCCCCCCC		43.2424275569
189PhosphorylationESDNERDSDKESEDG
CCCCCCCCCCCCCCC		57.7221815630
193PhosphorylationERDSDKESEDGEDEV
CCCCCCCCCCCCCCH		46.8823927012
201PhosphorylationEDGEDEVSCETVKMG
CCCCCCHHHEEEECC		12.2821815630
204PhosphorylationEDEVSCETVKMGRKD
CCCHHHEEEECCCCC		29.7429759185
206UbiquitinationEVSCETVKMGRKDSL
CHHHEEEECCCCCCC		42.95-
210SumoylationETVKMGRKDSLDLEE
EEEECCCCCCCCHHH		46.03-
210UbiquitinationETVKMGRKDSLDLEE
EEEECCCCCCCCHHH		46.03-
212PhosphorylationVKMGRKDSLDLEEEA
EECCCCCCCCHHHHH		27.1525159151
221PhosphorylationDLEEEAASGASSALE
CHHHHHHCCHHHHHH		41.7730278072
224PhosphorylationEEAASGASSALEAGG
HHHHCCHHHHHHHCC		21.4825159151
225PhosphorylationEAASGASSALEAGGS
HHHCCHHHHHHHCCC		36.0228176443
232PhosphorylationSALEAGGSSGLEDVL
HHHHHCCCCCHHHHH		21.9525159151
233PhosphorylationALEAGGSSGLEDVLP
HHHHCCCCCHHHHHH		51.1529632367
272PhosphorylationNNKLVYGSRQDFLWR
CCCCCCCCHHHHHHH		14.7424719451
284PhosphorylationLWRLARAYSDMCELT
HHHHHHHHHHHHHHC		10.3123898821
285PhosphorylationWRLARAYSDMCELTE
HHHHHHHHHHHHHCH		20.2023898821
291PhosphorylationYSDMCELTEEVSEKK
HHHHHHHCHHHHHHC		14.0623898821
295PhosphorylationCELTEEVSEKKSYAL
HHHCHHHHHHCCCCC		47.1523898821
2982-HydroxyisobutyrylationTEEVSEKKSYALDGK
CHHHHHHCCCCCCCH		44.65-
3052-HydroxyisobutyrylationKSYALDGKEEAEAAL
CCCCCCCHHHHHHHH		52.64-
305UbiquitinationKSYALDGKEEAEAAL
CCCCCCCHHHHHHHH		52.64-
314AcetylationEAEAALEKGDESADC
HHHHHHHHCCCCCHH		72.9419413330
318PhosphorylationALEKGDESADCHLWY
HHHHCCCCCHHHHHH		33.8619413330
325PhosphorylationSADCHLWYAVLCGQL
CCHHHHHHHHHHHHH		8.0019413330
337PhosphorylationGQLAEHESIQRRIQS
HHHHCHHHHHHHHHC		26.4019413330
344PhosphorylationSIQRRIQSGFSFKEH
HHHHHHHCCCCHHHH		39.1624961811
347PhosphorylationRRIQSGFSFKEHVDK
HHHHCCCCHHHHHHH		38.6519413330
388PhosphorylationWLEKKTATALLESPL
HHHHHHHHHHHHCCC		24.06-
393PhosphorylationTATALLESPLSATVE
HHHHHHHCCCCCCHH		30.9825159151
396PhosphorylationALLESPLSATVEDAL
HHHHCCCCCCHHHHH		25.8528348404
398PhosphorylationLESPLSATVEDALQS
HHCCCCCCHHHHHHH		22.5028348404
405PhosphorylationTVEDALQSFLKAEEL
CHHHHHHHHHHHHHH		33.1424719451
418UbiquitinationELQPGFSKAGRVYIS
HHCCCCCCCCCCHHH		53.23-
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
176YPhosphorylationKinaseLYNP07948
PSP
176YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RMD3_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 RMD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VATH_HUMANATP6V1Hphysical
22939629
VATA_HUMANATP6V1Aphysical
22939629
TOM40_HUMANTOMM40physical
22939629
TI17B_HUMANTIMM17Bphysical
22939629
1433B_HUMANYWHABphysical
25862004
RAF1_HUMANRAF1physical
25862004
MK01_HUMANMAPK1physical
25862004
PTN1_HUMANPTPN1physical
25862004
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 RMD3_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-46, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, 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-44 AND SER-212, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND MASSSPECTROMETRY.

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