NOE1_HUMAN - dbPTM
NOE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOE1_HUMAN
UniProt AC Q99784
Protein Name Noelin
Gene Name OLFM1
Organism Homo sapiens (Human).
Sequence Length 485
Subcellular Localization Secreted . Cell junction, synapse . Endoplasmic reticulum . Cell projection, axon . Perikaryon .
Protein Description Contributes to the regulation of axonal growth in the embryonic and adult central nervous system by inhibiting interactions between RTN4R and LINGO1. Inhibits RTN4R-mediated axon growth cone collapse (By similarity). May play an important role in regulating the production of neural crest cells by the neural tube (By similarity). May be required for normal responses to olfactory stimuli (By similarity)..
Protein Sequence MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNTTKLSAAGGGTLDRSTGVLPTNPEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISDPVTVKTSGSRFGSWMTDPLAPEGDNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDPVSLQTLQTWNTSYPKRSAGEAFIICGTLYVTNGYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGHQILYNVTLFHVIRSDEL
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
33N-linked_GlycosylationLPSLVGLNTTKLSAA
HHHHHCCCCCCCCCC		39.51UniProtKB CARBOHYD
48PhosphorylationGGGTLDRSTGVLPTN
CCCCCCCCCCCCCCC		29.2223879269
103N-linked_GlycosylationQLLEKVQNMSQSIEV
HHHHHHHHHHHHHHH		34.7516335952
107PhosphorylationKVQNMSQSIEVLDRR
HHHHHHHHHHHHHHH		17.26-
130AcetylationEKMENQMKGLESKFK
HHHHHHHHHHHHHHH		51.0519806657
135AcetylationQMKGLESKFKQVEES
HHHHHHHHHHHHHHH		47.4019806665
142PhosphorylationKFKQVEESHKQHLAR
HHHHHHHHHHHHHHH		23.60-
144UbiquitinationKQVEESHKQHLARQF
HHHHHHHHHHHHHHH		49.01-
187N-linked_GlycosylationQFKEEVQNLTSVLNE
HHHHHHHHHHHHHHH		50.9216335952
231PhosphorylationKLACGKLTGISDPVT
HHHHCCCCCCCCCEE		35.6429083192
234PhosphorylationCGKLTGISDPVTVKT
HCCCCCCCCCEEEEE		36.8929083192
238PhosphorylationTGISDPVTVKTSGSR
CCCCCCEEEEECCCC		22.9829083192
241PhosphorylationSDPVTVKTSGSRFGS
CCCEEEEECCCCCCC		33.7029083192
242PhosphorylationDPVTVKTSGSRFGSW
CCEEEEECCCCCCCE		29.1129083192
244PhosphorylationVTVKTSGSRFGSWMT
EEEEECCCCCCCEEC		24.9729083192
288N-linked_GlycosylationVDFMNTDNFTSHRLP
HHHHCCCCCCCCCCC		39.8016335952
307N-linked_GlycosylationGTGQVVYNGSIYFNK
CCCEEEECCEEEEEE		26.57UniProtKB CARBOHYD
327PhosphorylationIIRFDLKTETILKTR
EEEEECCCCEEEEEC		45.73-
338PhosphorylationLKTRSLDYAGYNNMY
EEECCCCCCCCCCCE		13.76-
380PhosphorylationNAGNIVVSRLDPVSL
CCCCEEEEECCCCCC		19.0724719451
394N-linked_GlycosylationLQTLQTWNTSYPKRS
CHHHHHCCCCCCCCC		23.6416335952
396PhosphorylationTLQTWNTSYPKRSAG
HHHHCCCCCCCCCCC		35.9024719451
431N-linked_GlycosylationVHYAYQTNASTYEYI
EEEEEECCCCEEEEE		19.17UniProtKB CARBOHYD
473N-linked_GlycosylationNGHQILYNVTLFHVI
CCEEEEEEEEEEEEE		19.49UniProtKB CARBOHYD
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 NOE1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOE1_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 NOE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ASPH_HUMANASPHphysical
26186194
TBA3C_HUMANTUBA3Cphysical
26186194
PCOC2_HUMANPCOLCE2physical
26186194
NOE2_HUMANOLFM2physical
26186194
TXD11_HUMANTXNDC11physical
26186194
MANEA_HUMANMANEAphysical
26186194
EDEM2_HUMANEDEM2physical
26186194
NOE2_HUMANOLFM2physical
28514442
MANEA_HUMANMANEAphysical
28514442
TBA3C_HUMANTUBA3Cphysical
28514442
BMAL2_HUMANARNTL2physical
28514442
EDEM2_HUMANEDEM2physical
28514442
ASPH_HUMANASPHphysical
28514442
PCOC2_HUMANPCOLCE2physical
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 NOE1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103; ASN-187; ASN-288 ANDASN-394, AND MASS SPECTROMETRY.

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