NMD3_HUMAN - dbPTM
NMD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NMD3_HUMAN
UniProt AC Q96D46
Protein Name 60S ribosomal export protein NMD3
Gene Name NMD3
Organism Homo sapiens (Human).
Sequence Length 503
Subcellular Localization Cytoplasm . Nucleus . Shuttles between the nucleus/nucleolus and the cytoplasm in a XPO1/CRM1-dependent manner.
Protein Description Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit..
Protein Sequence MEYMAESTDRSPGHILCCECGVPISPNPANICVACLRSKVDISQGIPKQVSISFCKQCQRYFQPPGTWIQCALESRELLALCLKKIKAPLSKVRLVDAGFVWTEPHSKRLKVKLTIQKEVMNGAILQQVFVVDYVVQSQMCGDCHRVEAKDFWKAVIQVRQKTLHKKTFYYLEQLILKYGMHQNTLRIKEIHDGLDFYYSSKQHAQKMVEFLQCTVPCRYKASQRLISQDIHSNTYNYKSTFSVEIVPICKDNVVCLSPKLAQSLGNMNQICVCIRVTSAIHLIDPNTLQVADIDGSTFWSHPFNSLCHPKQLEEFIVMECSIVQDIKRAAGAGMISKKHTLGEVWVQKTSEMNTDKQYFCRTHLGHLLNPGDLVLGFDLANCNLNDEHVNKMNSDRVPDVVLIKKSYDRTKRQRRRNWKLKELARERENMDTDDERQYQDFLEDLEEDEAIRKNVNIYRDSAIPVESDTDDEGAPRISLAEMLEDLHISQDATGEEGASMLT
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
1Acetylation-------MEYMAEST
-------CCCCCCCC		8.2122814378
3Phosphorylation-----MEYMAESTDR
-----CCCCCCCCCC		10.5928122231
7Phosphorylation-MEYMAESTDRSPGH
-CCCCCCCCCCCCCE		26.5225159151
8PhosphorylationMEYMAESTDRSPGHI
CCCCCCCCCCCCCEE		27.2625159151
11PhosphorylationMAESTDRSPGHILCC
CCCCCCCCCCEEEEE		37.7328450419
25PhosphorylationCECGVPISPNPANIC
EECCCCCCCCHHHHH		16.7425159151
39UbiquitinationCVACLRSKVDISQGI
HHHHHHCCCCCCCCC		37.18-
43PhosphorylationLRSKVDISQGIPKQV
HHCCCCCCCCCCCEE		20.2124300666
51PhosphorylationQGIPKQVSISFCKQC
CCCCCEEEHHHHHHH		15.26-
84AcetylationELLALCLKKIKAPLS
HHHHHHHHHCCCCHH		52.0026051181
84UbiquitinationELLALCLKKIKAPLS
HHHHHHHHHCCCCHH		52.00-
85AcetylationLLALCLKKIKAPLSK
HHHHHHHHCCCCHHH		36.1791345
108UbiquitinationVWTEPHSKRLKVKLT
EECCCCCCCEEEEEE		59.73-
150UbiquitinationDCHRVEAKDFWKAVI
CCEEEEHHHHHHHHH		39.7021890473
189AcetylationHQNTLRIKEIHDGLD
CCCEEEEEEHHHHHC		44.1526051181
202AcetylationLDFYYSSKQHAQKMV
HCEECCCHHHHHHHH		39.9126051181
202UbiquitinationLDFYYSSKQHAQKMV
HCEECCCHHHHHHHH		39.91-
228PhosphorylationKASQRLISQDIHSNT
HHHHHHHHCCCCCCC		26.7928555341
233PhosphorylationLISQDIHSNTYNYKS
HHHCCCCCCCCCCCC		31.0728152594
235PhosphorylationSQDIHSNTYNYKSTF
HCCCCCCCCCCCCEE		19.0328152594
236PhosphorylationQDIHSNTYNYKSTFS
CCCCCCCCCCCCEEE		22.2725159151
238PhosphorylationIHSNTYNYKSTFSVE
CCCCCCCCCCEEEEE		8.9025884760
258PhosphorylationKDNVVCLSPKLAQSL
CCCEEEECHHHHHHH		18.1821815630
335SulfoxidationKRAAGAGMISKKHTL
HHHCCCCCCCCCCCC		2.8730846556
337PhosphorylationAAGAGMISKKHTLGE
HCCCCCCCCCCCCCC		27.1024667141
338AcetylationAGAGMISKKHTLGEV
CCCCCCCCCCCCCCE		37.3330590781
339UbiquitinationGAGMISKKHTLGEVW
CCCCCCCCCCCCCEE		34.72-
341PhosphorylationGMISKKHTLGEVWVQ
CCCCCCCCCCCEEEE		45.3924719451
349UbiquitinationLGEVWVQKTSEMNTD
CCCEEEEECCCCCCC		44.38-
357AcetylationTSEMNTDKQYFCRTH
CCCCCCCCCEEHHHH		44.8826051181
357UbiquitinationTSEMNTDKQYFCRTH
CCCCCCCCCEEHHHH		44.88-
359PhosphorylationEMNTDKQYFCRTHLG
CCCCCCCEEHHHHHH		15.4729496907
395PhosphorylationEHVNKMNSDRVPDVV
HHHHHCCCCCCCCEE		24.24-
397MethylationVNKMNSDRVPDVVLI
HHHCCCCCCCCEEEE		41.51115485085
4052-HydroxyisobutyrylationVPDVVLIKKSYDRTK
CCCEEEEECCCCHHH		31.35-
433PhosphorylationRERENMDTDDERQYQ
HHHHCCCCCCHHHHH		34.2823401153
437MethylationNMDTDDERQYQDFLE
CCCCCCHHHHHHHHH		47.72115485077
439PhosphorylationDTDDERQYQDFLEDL
CCCCHHHHHHHHHHH		19.1030576142
454UbiquitinationEEDEAIRKNVNIYRD
HHHHHHHHHCCEECC		60.17-
459PhosphorylationIRKNVNIYRDSAIPV
HHHHCCEECCCCCCC		11.8123663014
462PhosphorylationNVNIYRDSAIPVESD
HCCEECCCCCCCCCC		21.0630266825
468PhosphorylationDSAIPVESDTDDEGA
CCCCCCCCCCCCCCC		46.1529255136
470PhosphorylationAIPVESDTDDEGAPR
CCCCCCCCCCCCCCC		55.4129255136
479PhosphorylationDEGAPRISLAEMLED
CCCCCCCCHHHHHHH		23.8620068231
490PhosphorylationMLEDLHISQDATGEE
HHHHCCCCCCCCCCC		15.9720068231
494PhosphorylationLHISQDATGEEGASM
CCCCCCCCCCCCCCC		54.1127732954
500PhosphorylationATGEEGASMLT----
CCCCCCCCCCC----		25.7820068231
503PhosphorylationEEGASMLT-------
CCCCCCCC-------		28.1120068231
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 NMD3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NMD3_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 NMD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XPO1_HUMANXPO1physical
12724356
UBA1_HUMANUBA1physical
22939629
STAT1_HUMANSTAT1physical
22939629
RHG01_HUMANARHGAP1physical
26344197
CNBP_HUMANCNBPphysical
26344197
RRP44_HUMANDIS3physical
26344197
FLNA_HUMANFLNAphysical
26344197
GDIA_HUMANGDI1physical
26344197
GFPT1_HUMANGFPT1physical
26344197
IMDH2_HUMANIMPDH2physical
26344197
LSM7_HUMANLSM7physical
26344197
NOP58_HUMANNOP58physical
26344197
TRUA_HUMANPUS1physical
26344197
PUS7_HUMANPUS7physical
26344197
RD23B_HUMANRAD23Bphysical
26344197
RFC5_HUMANRFC5physical
26344197
SDA1_HUMANSDAD1physical
26344197
TRM6_HUMANTRMT6physical
26344197
HMMR_HUMANHMMRphysical
28514442
POTEF_HUMANPOTEFphysical
28514442
FA83D_HUMANFAM83Dphysical
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 NMD3_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-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-468 AND THR-470, 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-468 AND THR-470, ANDMASS SPECTROMETRY.
"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-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-468 AND THR-470, 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 THR-433; SER-468 ANDTHR-470, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND THR-470, ANDMASS SPECTROMETRY.

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