NGDN_HUMAN - dbPTM
NGDN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NGDN_HUMAN
UniProt AC Q8NEJ9
Protein Name Neuroguidin
Gene Name NGDN
Organism Homo sapiens (Human).
Sequence Length 315
Subcellular Localization Nucleus. Nucleus, nucleolus . Chromosome, centromere . Cytoplasm. Cell projection, axon. Cell projection, dendrite. Cell projection, filopodium. Detected in axons, dendrites and filopodia. Colocalized with EIF4E in neurites (By similarity). Transloca
Protein Description Involved in the translational repression of cytoplasmic polyadenylation element (CPE)-containing mRNAs..
Protein Sequence MAALGVLESDLPSAVTLLKNLQEQVMAVTAQVKSLTQKVQAGAYPTEKGLSFLEVKDQLLLMYLMDLTHLILDKASGGSLQGHDAVLRLVEIRTVLEKLRPLDQKLKYQIDKLIKTAVTGSLSENDPLRFKPHPSNMMSKLSSEDEEEDEAEDDQSEASGKKSVKGVSKKYVPPRLVPVHYDETEAEREKKRLERAKRRALSSSVIRELKEQYSDAPEEIRDARHPHVTRQSQEDQHRINYEESMMVRLSVSKREKGRRKRANVMSSQLHSLTHFSDISALTGGTVHLDEDQNPIKKRKKIPQKGRKKKGFRRRR
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
2Acetylation------MAALGVLES
------CCHHHCCHH		16.0519413330
9PhosphorylationAALGVLESDLPSAVT
CHHHCCHHCCCHHHH		40.04-
13PhosphorylationVLESDLPSAVTLLKN
CCHHCCCHHHHHHHH		42.54-
16PhosphorylationSDLPSAVTLLKNLQE
HCCCHHHHHHHHHHH		26.53-
29PhosphorylationQEQVMAVTAQVKSLT
HHHHHHHHHHHHHHH		11.2228985074
33UbiquitinationMAVTAQVKSLTQKVQ
HHHHHHHHHHHHHHH		27.8922817900
33AcetylationMAVTAQVKSLTQKVQ
HHHHHHHHHHHHHHH		27.8926051181
33 (in isoform 1)Ubiquitination-27.8921906983
33 (in isoform 2)Ubiquitination-27.8921906983
38UbiquitinationQVKSLTQKVQAGAYP
HHHHHHHHHHCCCCC		30.9521906983
38 (in isoform 2)Ubiquitination-30.9521906983
38 (in isoform 1)Ubiquitination-30.9521906983
44PhosphorylationQKVQAGAYPTEKGLS
HHHHCCCCCCCCCCC		15.1221406692
46PhosphorylationVQAGAYPTEKGLSFL
HHCCCCCCCCCCCHH		37.3428152594
48UbiquitinationAGAYPTEKGLSFLEV
CCCCCCCCCCCHHHH		68.5721906983
48 (in isoform 2)Ubiquitination-68.5721906983
48 (in isoform 1)Ubiquitination-68.5721906983
482-HydroxyisobutyrylationAGAYPTEKGLSFLEV
CCCCCCCCCCCHHHH		68.57-
76 (in isoform 2)Phosphorylation-49.80-
76PhosphorylationHLILDKASGGSLQGH
HHHHHHCCCCCCCCH		49.8020068231
79 (in isoform 2)Phosphorylation-22.50-
79PhosphorylationLDKASGGSLQGHDAV
HHHCCCCCCCCHHHH		22.5020068231
982-HydroxyisobutyrylationEIRTVLEKLRPLDQK
HHHHHHHHHCCCCHH		45.71-
105AcetylationKLRPLDQKLKYQIDK
HHCCCCHHHHHHHHH		46.7626051181
105UbiquitinationKLRPLDQKLKYQIDK
HHCCCCHHHHHHHHH		46.7629967540
112AcetylationKLKYQIDKLIKTAVT
HHHHHHHHHHHHHHH		54.4626051181
112UbiquitinationKLKYQIDKLIKTAVT
HHHHHHHHHHHHHHH		54.46-
115UbiquitinationYQIDKLIKTAVTGSL
HHHHHHHHHHHHCCC		40.6529967540
119PhosphorylationKLIKTAVTGSLSEND
HHHHHHHHCCCCCCC		20.7020860994
121PhosphorylationIKTAVTGSLSENDPL
HHHHHHCCCCCCCCC		21.2528985074
123PhosphorylationTAVTGSLSENDPLRF
HHHHCCCCCCCCCCC		35.7323186163
131UbiquitinationENDPLRFKPHPSNMM
CCCCCCCCCCCCHHH		35.6629967540
135PhosphorylationLRFKPHPSNMMSKLS
CCCCCCCCHHHHHCC		34.0323927012
139PhosphorylationPHPSNMMSKLSSEDE
CCCCHHHHHCCCCCC		21.4823927012
139 (in isoform 2)Phosphorylation-21.48-
142 (in isoform 2)Phosphorylation-35.10-
142PhosphorylationSNMMSKLSSEDEEED
CHHHHHCCCCCCHHH		35.1022167270
143 (in isoform 2)Phosphorylation-60.55-
143PhosphorylationNMMSKLSSEDEEEDE
HHHHHCCCCCCHHHH		60.5522167270
156 (in isoform 2)Phosphorylation-41.97-
156PhosphorylationDEAEDDQSEASGKKS
HHHCCHHHHHHCCCC		41.9722167270
159 (in isoform 2)Phosphorylation-47.28-
159PhosphorylationEDDQSEASGKKSVKG
CCHHHHHHCCCCCCC		47.2822167270
168PhosphorylationKKSVKGVSKKYVPPR
CCCCCCCCCCCCCCC		31.9022115753
171PhosphorylationVKGVSKKYVPPRLVP
CCCCCCCCCCCCEEE		23.1722115753
184PhosphorylationVPVHYDETEAEREKK
EECCCCCCHHHHHHH		37.28-
190UbiquitinationETEAEREKKRLERAK
CCHHHHHHHHHHHHH		49.7924816145
191UbiquitinationTEAEREKKRLERAKR
CHHHHHHHHHHHHHH		58.42-
202 (in isoform 2)Phosphorylation-21.41-
202PhosphorylationRAKRRALSSSVIREL
HHHHHHHHHHHHHHH		21.4125159151
203 (in isoform 2)Phosphorylation-29.49-
203PhosphorylationAKRRALSSSVIRELK
HHHHHHHHHHHHHHH		29.4925159151
204 (in isoform 2)Phosphorylation-20.42-
204PhosphorylationKRRALSSSVIRELKE
HHHHHHHHHHHHHHH		20.4225159151
210 (in isoform 2)Ubiquitination-37.7121906983
210 (in isoform 1)Ubiquitination-37.7121906983
210UbiquitinationSSVIRELKEQYSDAP
HHHHHHHHHHHCCCC		37.7122817900
213 (in isoform 2)Phosphorylation-15.03-
213PhosphorylationIRELKEQYSDAPEEI
HHHHHHHHCCCCHHH		15.0329255136
214PhosphorylationRELKEQYSDAPEEIR
HHHHHHHCCCCHHHH		27.3029255136
214 (in isoform 2)Phosphorylation-27.30-
229PhosphorylationDARHPHVTRQSQEDQ
HCCCCCCCCCCHHHH		21.6930108239
232PhosphorylationHPHVTRQSQEDQHRI
CCCCCCCCHHHHHCC		32.0430108239
241PhosphorylationEDQHRINYEESMMVR
HHHHCCCHHHHHHHH		20.7827642862
244PhosphorylationHRINYEESMMVRLSV
HCCCHHHHHHHHHHH		10.5528555341
250PhosphorylationESMMVRLSVSKREKG
HHHHHHHHHHHHHHH		17.4929496963
271PhosphorylationVMSSQLHSLTHFSDI
HHHHHHHHHCCHHHH		43.48-
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 NGDN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NGDN_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 NGDN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AATF_HUMANAATFphysical
25416956
SAS10_HUMANUTP3physical
26344197
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 NGDN_HUMAN

loading...

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 ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-143; SER-202 ANDSER-204, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND SER-143, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory