RMD3_MOUSE - dbPTM
RMD3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RMD3_MOUSE
UniProt AC Q3UJU9
Protein Name Regulator of microtubule dynamics protein 3
Gene Name Rmdn3
Organism Mus musculus (Mouse).
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 (By similarity). May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis (By similarity)..
Protein Sequence MSRLGALGGSRAGLGLLLGTAAGLGFLCVLYSQRWKRTQRHGRSHSLPNSLDYAQASERGRQVTQFRAIPGEAGDAAILPSLSQEGQEKVLDRLDFVLTSLMALRREVEELQRSLQGLAGEIVGEVRSHIEENQRVARRRRFPFARERSDSTGSSSVYFTASSGAALTDAESEGGYTTANAESDYERDSDKESGDAEDEVSCETVRMGRKDSLDLDVEAASSPAAAALEEDDSSGREDVQLVLLQADELHQGSKQDKREGFQLLLNNKLAYGSRQDFLWRLARAYSDMSDLTEEESGKKSYALNGKEEAEAALKKGDESAACHLWYAVLCGQLAEHEGISKRIQSGFSFKEHVDKAIELQPEDPRGHFLLGRWCYQVSHLNWLEKKTATALFESPLSATVQDALQSFLKAEELQPGFSKAGRVYISKCYRELGKNSEARKWMKLAQELPDVTNEDSAFQKDLEELEVILG
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
44PhosphorylationRTQRHGRSHSLPNSL
HHHHCCCCCCCCCCC		23.2425521595
46PhosphorylationQRHGRSHSLPNSLDY
HHCCCCCCCCCCCCH		46.9324925903
50PhosphorylationRSHSLPNSLDYAQAS
CCCCCCCCCCHHHHH		22.2225521595
53PhosphorylationSLPNSLDYAQASERG
CCCCCCCHHHHHHHC		13.1025619855
57PhosphorylationSLDYAQASERGRQVT
CCCHHHHHHHCCCCE		18.7524925903
81PhosphorylationGDAAILPSLSQEGQE
CCCCCCCCCCHHHHH		36.8922324799
83PhosphorylationAAILPSLSQEGQEKV
CCCCCCCCHHHHHHH		30.4425521595
183PhosphorylationYTTANAESDYERDSD
CCCCCCCCCCCCCCC		42.98-
189PhosphorylationESDYERDSDKESGDA
CCCCCCCCCCCCCCC		57.7225521595
193PhosphorylationERDSDKESGDAEDEV
CCCCCCCCCCCCCCC		47.9525521595
201PhosphorylationGDAEDEVSCETVRMG
CCCCCCCHHHHHHCC		12.2825521595
212PhosphorylationVRMGRKDSLDLDVEA
HHCCCCCCCCCCHHH		27.1525521595
221PhosphorylationDLDVEAASSPAAAAL
CCCHHHHCCHHHHHH		43.8525159016
222PhosphorylationLDVEAASSPAAAALE
CCHHHHCCHHHHHHH		17.5225521595
233PhosphorylationAALEEDDSSGREDVQ
HHHHCCCCCCCHHHE		47.1925293948
234PhosphorylationALEEDDSSGREDVQL
HHHCCCCCCCHHHEE		49.1925293948
271PhosphorylationLLNNKLAYGSRQDFL
HHCCCCCCCCHHHHH		26.5221082442
273PhosphorylationNNKLAYGSRQDFLWR
CCCCCCCCHHHHHHH		17.6922817900
299MalonylationTEEESGKKSYALNGK
CCCHHCCCEECCCCH		52.8326320211
300PhosphorylationEEESGKKSYALNGKE
CCHHCCCEECCCCHH		21.0830387612
306UbiquitinationKSYALNGKEEAEAAL
CEECCCCHHHHHHHH		51.8422790023
306AcetylationKSYALNGKEEAEAAL
CEECCCCHHHHHHHH		51.8423864654
345PhosphorylationGISKRIQSGFSFKEH
CHHHHHHCCCCHHHH		39.1629472430
348PhosphorylationKRIQSGFSFKEHVDK
HHHHCCCCHHHHHHH		38.6522817900
386MalonylationHLNWLEKKTATALFE
HHHHHHHHHHHHHHC		33.7326073543
387PhosphorylationLNWLEKKTATALFES
HHHHHHHHHHHHHCC		40.0723984901
389PhosphorylationWLEKKTATALFESPL
HHHHHHHHHHHCCCC		29.1723984901
394PhosphorylationTATALFESPLSATVQ
HHHHHHCCCCCHHHH		24.6523984901
397PhosphorylationALFESPLSATVQDAL
HHHCCCCCHHHHHHH		25.8523984901
399PhosphorylationFESPLSATVQDALQS
HCCCCCHHHHHHHHH		18.4723984901
419UbiquitinationELQPGFSKAGRVYIS
HHCCCCCCCCHHHHH		53.2327667366
434AcetylationKCYRELGKNSEARKW
HHHHHHCCCHHHHHH		70.6723864654
436PhosphorylationYRELGKNSEARKWMK
HHHHCCCHHHHHHHH		35.8023140645
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 RMD3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RMD3_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RMD3_HUMANRMDN3physical
20360068
VAPB_HUMANVAPBphysical
20360068
VATA_HUMANATP6V1Aphysical
26496610
VATB2_HUMANATP6V1B2physical
26496610
VATE1_HUMANATP6V1E1physical
26496610
VPP1_HUMANATP6V0A1physical
26496610
CAV1_HUMANCAV1physical
26496610
CBPM_HUMANCPMphysical
26496610
STOM_HUMANSTOMphysical
26496610
FLOT2_HUMANFLOT2physical
26496610
GNAS3_HUMANGNASphysical
26496610
GNAS2_HUMANGNASphysical
26496610
ALEX_HUMANGNASphysical
26496610
GNAS1_HUMANGNASphysical
26496610
I5P2_HUMANINPP5Bphysical
26496610
MGST3_HUMANMGST3physical
26496610
NDUA2_HUMANNDUFA2physical
26496610
NDUA7_HUMANNDUFA7physical
26496610
NDUAA_HUMANNDUFA10physical
26496610
NDUB4_HUMANNDUFB4physical
26496610
NDUB8_HUMANNDUFB8physical
26496610
NDUS1_HUMANNDUFS1physical
26496610
NDUV1_HUMANNDUFV1physical
26496610
NDUS6_HUMANNDUFS6physical
26496610
NDUV2_HUMANNDUFV2physical
26496610
NDUV3_HUMANNDUFV3physical
26496610
PHB_HUMANPHBphysical
26496610
KPB2_HUMANPHKA2physical
26496610
ABCD3_HUMANABCD3physical
26496610
AAAT_HUMANSLC1A5physical
26496610
SOAT1_HUMANSOAT1physical
26496610
ICAM5_HUMANICAM5physical
26496610
QCR1_HUMANUQCRC1physical
26496610
QCR2_HUMANUQCRC2physical
26496610
UCRI_HUMANUQCRFS1physical
26496610
VDAC1_HUMANVDAC1physical
26496610
VDAC2_HUMANVDAC2physical
26496610
VDAC3_HUMANVDAC3physical
26496610
RAI3_HUMANGPRC5Aphysical
26496610
VA0D1_HUMANATP6V0D1physical
26496610
XPR1_HUMANXPR1physical
26496610
VAPB_HUMANVAPBphysical
26496610
VAPA_HUMANVAPAphysical
26496610
VATF_HUMANATP6V1Fphysical
26496610
VATG1_HUMANATP6V1G1physical
26496610
FLOT1_HUMANFLOT1physical
26496610
ERLN1_HUMANERLIN1physical
26496610
TXN4A_HUMANTXNL4Aphysical
26496610
CKAP4_HUMANCKAP4physical
26496610
MIC60_HUMANIMMTphysical
26496610
ERLN2_HUMANERLIN2physical
26496610
PHB2_HUMANPHB2physical
26496610
MTCH1_HUMANMTCH1physical
26496610
AT2C1_HUMANATP2C1physical
26496610
STML2_HUMANSTOML2physical
26496610
FA8A1_HUMANFAM8A1physical
26496610
OTU6B_HUMANOTUD6Bphysical
26496610
SARAF_HUMANSARAFphysical
26496610
MIC19_HUMANCHCHD3physical
26496610
DJC11_HUMANDNAJC11physical
26496610
PLRKT_HUMANPLGRKTphysical
26496610
NDUAC_HUMANNDUFA12physical
26496610
TOM22_HUMANTOMM22physical
26496610
KDIS_HUMANKIDINS220physical
26496610
E41L5_HUMANEPB41L5physical
26496610
DERL1_HUMANDERL1physical
26496610
MBOA7_HUMANMBOAT7physical
26496610
CYBR1_HUMANCYBRD1physical
26496610
TRM2_HUMANTRMT2Bphysical
26496610
TMUB1_HUMANTMUB1physical
26496610
MIC25_HUMANCHCHD6physical
26496610
ATAD1_HUMANATAD1physical
26496610
ACBD5_HUMANACBD5physical
26496610
MMGT1_HUMANMMGT1physical
26496610
CAVN3_HUMANPRKCDBPphysical
26496610
CC127_HUMANCCDC127physical
26496610
RMD2_HUMANRMDN2physical
26496610
CAVN1_HUMANPTRFphysical
26496610
RABL3_HUMANRABL3physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RMD3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASSSPECTROMETRY.
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS.";
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
Mol. Cell. Proteomics 6:669-676(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-212, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND MASSSPECTROMETRY.

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