NCDN_HUMAN - dbPTM
NCDN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCDN_HUMAN
UniProt AC Q9UBB6
Protein Name Neurochondrin
Gene Name NCDN
Organism Homo sapiens (Human).
Sequence Length 729
Subcellular Localization Cytoplasm, cytosol. Cell projection, dendrite. Localizes to somatic regions of neurons.
Protein Description Probably involved in signal transduction, in the nervous system, via increasing cell surface localization of GRM5 and positively regulating its signaling (By similarity). Required for the spatial learning process. Acts as a negative regulator of Ca(2+)-calmodulin-dependent protein kinase 2 (CaMK2) phosphorylation. May play a role in modulating melanin-concentrating hormone-mediated functions via its interaction with MCHR1 that interferes with G protein-coupled signal transduction. May be involved in bone metabolism. May also be involved in neurite outgrowth..
Protein Sequence MSCCDLAAAGQLGKASIMASDCEPALNQAEGRNPTLERYLGALREAKNDSEQFAALLLVTKAVKAGDIDAKTRRRIFDAVGFTFPNRLLTTKEAPDGCPDHVLRALGVALLACFCSDPELAAHPQVLNKIPILSTFLTARGDPDDAARRSMIDDTYQCLTAVAGTPRGPRHLIAGGTVSALCQAYLGHGYGFDQALALLVGLLAAAETQCWKEAEPDLLAVLRGLSEDFQKAEDASKFELCQLLPLFLPPTTVPPECYRDLQAGLARILGSKLSSWQRNPALKLAARLAHACGSDWIPAGSSGSKFLALLVNLACVEVRLALEETGTEVKEDVVTACYALMELGIQECTRCEQSLLKEPQKVQLVSVMKEAIGAVIHYLLQVGSEKQKEPFVFASVRILGAWLAEETSSLRKEVCQLLPFLVRYAKTLYEEAEEANDLSQQVANLAISPTTPGPTWPGDALRLLLPGWCHLTVEDGPREILIKEGAPSLLCKYFLQQWELTSPGHDTSVLPDSVEIGLQTCCHIFLNLVVTAPGLIKRDACFTSLMNTLMTSLPALVQQQGRLLLAANVATLGLLMARLLSTSPALQGTPASRGFFAAAILFLSQSHVARATPGSDQAVLALSPEYEGIWADLQELWFLGMQAFTGCVPLLPWLAPAALRSRWPQELLQLLGSVSPNSVKPEMVAAYQGVLVELARANRLCREAMRLQAGEETASHYRMAALEQCLSEP
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------MSCCDLAAA
------CCHHHHHHC		24.3722814378
2 (in isoform 2)Acetylation-24.3722814378
2Phosphorylation------MSCCDLAAA
------CCHHHHHHC		24.3725159151
3 (in isoform 2)Phosphorylation-1.7025849741
3S-palmitoylation-----MSCCDLAAAG
-----CCHHHHHHCC		1.70-
4S-palmitoylation----MSCCDLAAAGQ
----CCHHHHHHCCC		3.63-
20PhosphorylationGKASIMASDCEPALN
CCHHHHHHCCHHHHH		25.9725850435
30UbiquitinationEPALNQAEGRNPTLE
HHHHHHHCCCCHHHH		49.2529967540
47UbiquitinationLGALREAKNDSEQFA
HHHHHHHCCCHHHHH		57.4429967540
50PhosphorylationLREAKNDSEQFAALL
HHHHCCCHHHHHHHH		42.5717924679
60PhosphorylationFAALLLVTKAVKAGD
HHHHHHHHHHHHHCC		17.1617924679
66 (in isoform 3)Ubiquitination-27.04-
75UbiquitinationIDAKTRRRIFDAVGF
CCHHHHHHHHHHHCC		30.5424816145
75MethylationIDAKTRRRIFDAVGF
CCHHHHHHHHHHHCC		30.54-
75Asymmetric dimethylarginineIDAKTRRRIFDAVGF
CCHHHHHHHHHHHCC		30.54-
92UbiquitinationPNRLLTTKEAPDGCP
CCCCCCCCCCCCCCC		46.7924816145
94 (in isoform 3)Ubiquitination-14.72-
158GlutathionylationMIDDTYQCLTAVAGT
HHCCHHHHHHHHCCC		2.2822555962
214UbiquitinationETQCWKEAEPDLLAV
HHHHHHHCCHHHHHH		29.8730230243
231UbiquitinationGLSEDFQKAEDASKF
HCCHHHHHHHHHHHH		54.4530230243
255UbiquitinationLPPTTVPPECYRDLQ
CCCCCCCHHHHHHHH		39.7021890473
255 (in isoform 2)Ubiquitination-39.7021890473
266UbiquitinationRDLQAGLARILGSKL
HHHHHHHHHHHCCCC		8.7822817900
266 (in isoform 2)Ubiquitination-8.7821890473
272 (in isoform 1)Ubiquitination-51.0621890473
272UbiquitinationLARILGSKLSSWQRN
HHHHHCCCCHHCCCC		51.0621890473
274 (in isoform 3)Ubiquitination-33.0121890473
283UbiquitinationWQRNPALKLAARLAH
CCCCHHHHHHHHHHH		37.8822817900
283 (in isoform 1)Ubiquitination-37.8821890473
285 (in isoform 3)Ubiquitination-6.7521890473
354PhosphorylationECTRCEQSLLKEPQK
HHHHHHHHHCCCCCH		17.2424719451
395UbiquitinationKEPFVFASVRILGAW
CCCEEEEEHHHHHHH		10.6430230243
407PhosphorylationGAWLAEETSSLRKEV
HHHHHHHCHHHHHHH		18.3424076635
408PhosphorylationAWLAEETSSLRKEVC
HHHHHHCHHHHHHHH		30.5628348404
409PhosphorylationWLAEETSSLRKEVCQ
HHHHHCHHHHHHHHH		39.3428348404
412UbiquitinationEETSSLRKEVCQLLP
HHCHHHHHHHHHHHH		60.8530230243
431PhosphorylationYAKTLYEEAEEANDL
HHHHHHHHHHHHCCH		48.0732142685
439PhosphorylationAEEANDLSQQVANLA
HHHHCCHHHHHHHHC		22.7928348404
448PhosphorylationQVANLAISPTTPGPT
HHHHHCCCCCCCCCC		15.5825159151
450PhosphorylationANLAISPTTPGPTWP
HHHCCCCCCCCCCCC		38.5429523821
451PhosphorylationNLAISPTTPGPTWPG
HHCCCCCCCCCCCCC		29.6329523821
455PhosphorylationSPTTPGPTWPGDALR
CCCCCCCCCCCHHHH		50.6529523821
466UbiquitinationDALRLLLPGWCHLTV
HHHHHHCCCEEEEEE		33.9223000965
483UbiquitinationGPREILIKEGAPSLL
CCCEEEEECCCHHHH		46.8023000965
485 (in isoform 3)Ubiquitination-37.47-
582PhosphorylationLMARLLSTSPALQGT
HHHHHHCCCHHHCCC		38.4024076635
583PhosphorylationMARLLSTSPALQGTP
HHHHHCCCHHHCCCC		12.5624076635
673PhosphorylationELLQLLGSVSPNSVK
HHHHHHCCCCCCCCC		21.2825332170
675PhosphorylationLQLLGSVSPNSVKPE
HHHHCCCCCCCCCHH		21.7725332170
678PhosphorylationLGSVSPNSVKPEMVA
HCCCCCCCCCHHHHH		34.6025332170
725GlutathionylationRMAALEQCLSEP---
HHHHHHHHHCCC---		3.0922555962
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 NCDN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCDN_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 NCDN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARLY_HUMANASLphysical
22863883
SLD5_HUMANGINS4physical
22863883
ODPA_HUMANPDHA1physical
22863883
IPP2_HUMANPPP1R2physical
22863883
EFHC2_HUMANEFHC2physical
25416956
ADAS_HUMANAGPSphysical
28561026
AL3A2_HUMANALDH3A2physical
28561026
ASAH1_HUMANASAH1physical
28561026
AT1A1_HUMANATP1A1physical
28561026
ATPA_HUMANATP5A1physical
28561026
ATPB_HUMANATP5Bphysical
28561026
CLP1L_HUMANCLPTM1Lphysical
28561026
COA1_HUMANCOA1physical
28561026
ECHP_HUMANEHHADHphysical
28561026
TBA8_HUMANEHHADHphysical
28561026
ESYT1_HUMANESYT1physical
28561026
GOGA5_HUMANGOLGA5physical
28561026
DHB12_HUMANHSD17B12physical
28561026
MPRI_HUMANIGF2Rphysical
28561026
ILVBL_HUMANILVBLphysical
28561026
LNP_HUMANKIAA1715physical
28561026
MOGS_HUMANMOGSphysical
28561026
NCDN_HUMANNCDNphysical
28561026
PGRC1_HUMANPGRMC1physical
28561026
RPN1_HUMANRPN1physical
28561026
S61A1_HUMANSEC61A1physical
28561026
AAAT_HUMANSLC1A5physical
28561026
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 NCDN_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-50 AND THR-60, AND MASSSPECTROMETRY.

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