NUDC3_HUMAN - dbPTM
NUDC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUDC3_HUMAN
UniProt AC Q8IVD9
Protein Name NudC domain-containing protein 3
Gene Name NUDCD3
Organism Homo sapiens (Human).
Sequence Length 361
Subcellular Localization
Protein Description
Protein Sequence METGAAELYDQALLGILQHVGNVQDFLRVLFGFLYRKTDFYRLLRHPSDRMGFPPGAAQALVLQVFKTFDHMARQDDEKRRQELEEKIRRKEEEEAKTVSAAAAEKEPVPVPVQEIEIDSTTELDGHQEVEKVQPPGPVKEMAHGSQEAEAPGAVAGAAEVPREPPILPRIQEQFQKNPDSYNGAVRENYTWSQDYTDLEVRVPVPKHVVKGKQVSVALSSSSIRVAMLEENGERVLMEGKLTHKINTESSLWSLEPGKCVLVNLSKVGEYWWNAILEGEEPIDIDKINKERSMATVDEEEQAVLDRLTFDYHQKLQGKPQSHELKVHEMLKKGWDAEGSPFRGQRFDPAMFNISPGAVQF
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
8UbiquitinationMETGAAELYDQALLG
CCCCHHHHHHHHHHH		4.9821890473
48PhosphorylationYRLLRHPSDRMGFPP
HHHHCCCHHHCCCCC		31.55-
87UbiquitinationRRQELEEKIRRKEEE
HHHHHHHHHHHHHHH		31.9429967540
98PhosphorylationKEEEEAKTVSAAAAE
HHHHHHHHHHHHHHH		27.0922468782
120PhosphorylationVQEIEIDSTTELDGH
CEEEEECCCCCCCCC		42.7825338102
122PhosphorylationEIEIDSTTELDGHQE
EEEECCCCCCCCCEE		38.2030576142
146PhosphorylationVKEMAHGSQEAEAPG
HHHHCCCCCCCCCCC		18.2517525332
177UbiquitinationRIQEQFQKNPDSYNG
HHHHHHHHCCCCCCC		72.2723000965
182PhosphorylationFQKNPDSYNGAVREN
HHHCCCCCCCCCCCC		25.6225839225
196PhosphorylationNYTWSQDYTDLEVRV
CEEECCCCCCEEEEE		8.4327642862
207UbiquitinationEVRVPVPKHVVKGKQ
EEEECCCCCEECCCE		49.6329967540
213UbiquitinationPKHVVKGKQVSVALS
CCCEECCCEEEEEEC		41.63-
220PhosphorylationKQVSVALSSSSIRVA
CEEEEEECCCCEEEE		20.5921406692
221PhosphorylationQVSVALSSSSIRVAM
EEEEEECCCCEEEEE		29.0221406692
222PhosphorylationVSVALSSSSIRVAML
EEEEECCCCEEEEEE		26.8021406692
223PhosphorylationSVALSSSSIRVAMLE
EEEECCCCEEEEEEE		19.1621406692
241UbiquitinationERVLMEGKLTHKINT
EEEEEEEEEEEEECC		36.5929967540
271PhosphorylationNLSKVGEYWWNAILE
EHHHCCHHHHHHHHC		15.1420090780
287UbiquitinationEEPIDIDKINKERSM
CCCCCHHHCCHHHCC		48.8129967540
293PhosphorylationDKINKERSMATVDEE
HHCCHHHCCCCCCHH		17.5425693802
294SulfoxidationKINKERSMATVDEEE
HCCHHHCCCCCCHHH		4.5521406390
307MethylationEEQAVLDRLTFDYHQ
HHHHHHHHHHHCHHH		31.31115485729
312PhosphorylationLDRLTFDYHQKLQGK
HHHHHHCHHHHHCCC		11.2727642862
315UbiquitinationLTFDYHQKLQGKPQS
HHHCHHHHHCCCCCC		29.4829967540
319UbiquitinationYHQKLQGKPQSHELK
HHHHHCCCCCCHHHC		27.2429967540
326UbiquitinationKPQSHELKVHEMLKK
CCCCHHHCHHHHHHC		38.2629967540
333UbiquitinationKVHEMLKKGWDAEGS
CHHHHHHCCCCCCCC		62.3629967540
340PhosphorylationKGWDAEGSPFRGQRF
CCCCCCCCCCCCCCC		16.6325159151
343MethylationDAEGSPFRGQRFDPA
CCCCCCCCCCCCCHH		43.66115485721
355PhosphorylationDPAMFNISPGAVQF-
CHHHCCCCCCCCCC-		20.5625159151
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 NUDC3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUDC3_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 NUDC3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CNOT9_HUMANRQCD1physical
22939629
SNF8_HUMANSNF8physical
22939629
RBGPR_HUMANRAB3GAP2physical
22863883
UBE4B_HUMANUBE4Bphysical
22863883
HCFC1_HUMANHCFC1physical
25036637
CARM1_HUMANCARM1physical
25036637
PKN3_HUMANPKN3physical
25036637
SORT_HUMANSORT1physical
25036637
CX057_HUMANCXorf57physical
25036637
SSBP_HUMANSSBP1physical
25036637
KBTB6_HUMANKBTBD6physical
25036637
SF3B3_HUMANSF3B3physical
25036637
KLHL9_HUMANKLHL9physical
25036637
F136A_HUMANFAM136Aphysical
25036637
FKBP5_HUMANFKBP5physical
25036637
CCDB1_HUMANCCNDBP1physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
ULA1_HUMANNAE1physical
26344197
LIS1_HUMANPAFAH1B1physical
16754861
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 NUDC3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND MASSSPECTROMETRY.

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