NOE3_HUMAN - dbPTM
NOE3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOE3_HUMAN
UniProt AC Q96PB7
Protein Name Noelin-3
Gene Name OLFM3
Organism Homo sapiens (Human).
Sequence Length 478
Subcellular Localization Secreted. Cell junction, synapse.
Protein Description
Protein Sequence MSPPLLKLGAVLSTMAMISNWMSQTLPSLVGLNTTRLSTPDTLTQISPKEGWQVYSSAQDPDGRCICTVVAPEQNLCSRDAKSRQLRQLLEKVQNMSQSIEVLNLRTQRDFQYVLKMETQMKGLKAKFRQIEDDRKTLMTKHFQELKEKMDELLPLIPVLEQYKTDAKLITQFKEEIRNLSAVLTGIQEEIGAYDYEELHQRVLSLETRLRDCMKKLTCGKLMKITGPVTVKTSGTRFGAWMTDPLASEKNNRVWYMDSYTNNKIVREYKSIADFVSGAESRTYNLPFKWAGTNHVVYNGSLYFNKYQSNIIIKYSFDMGRVLAQRSLEYAGFHNVYPYTWGGFSDIDLMADEIGLWAVYATNQNAGNIVISQLNQDTLEVMKSWSTGYPKRSAGESFMICGTLYVTNSHLTGAKVYYSYSTKTSTYEYTDIPFHNQYFHISMLDYNARDRALYAWNNGHQVLFNVTLFHIIKTEDDT
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
2Phosphorylation------MSPPLLKLG
------CCCCHHHHH
34.9121815630
4 (in isoform 6)Phosphorylation-42.9122496350
4 (in isoform 5)Phosphorylation-42.9122496350
4 (in isoform 4)Phosphorylation-42.9124043423
4 (in isoform 3)Phosphorylation-42.9124043423
5 (in isoform 4)Phosphorylation-8.1724043423
5 (in isoform 3)Phosphorylation-8.1724043423
14 (in isoform 4)Phosphorylation-12.5624043423
14 (in isoform 3)Phosphorylation-12.5624043423
22 (in isoform 4)Phosphorylation-2.2024043423
22 (in isoform 3)Phosphorylation-2.2024043423
33N-linked_GlycosylationLPSLVGLNTTRLSTP
HHHHCCCCCCCCCCC
33.21UniProtKB CARBOHYD
95N-linked_GlycosylationQLLEKVQNMSQSIEV
HHHHHHHHHHHHEEE
34.75UniProtKB CARBOHYD
97PhosphorylationLEKVQNMSQSIEVLN
HHHHHHHHHHEEEEE
28.4630622161
99PhosphorylationKVQNMSQSIEVLNLR
HHHHHHHHEEEEECC
17.2624043423
137PhosphorylationQIEDDRKTLMTKHFQ
HHHHHHHHHHHHHHH
23.7429449344
140PhosphorylationDDRKTLMTKHFQELK
HHHHHHHHHHHHHHH
25.2019413330
149AcetylationHFQELKEKMDELLPL
HHHHHHHHHHHHHHH
50.4920167786
179N-linked_GlycosylationQFKEEIRNLSAVLTG
HHHHHHHHHHHHHHH
43.97UniProtKB CARBOHYD
230PhosphorylationMKITGPVTVKTSGTR
EEEECCEEEEECCCC
21.3023403867
233PhosphorylationTGPVTVKTSGTRFGA
ECCEEEEECCCCCEE
28.2223403867
234PhosphorylationGPVTVKTSGTRFGAW
CCEEEEECCCCCEEE
32.2323403867
236PhosphorylationVTVKTSGTRFGAWMT
EEEEECCCCCEEEEC
23.6923403867
259PhosphorylationNRVWYMDSYTNNKIV
CEEEEEECCCCCHHH
19.8230576142
299N-linked_GlycosylationGTNHVVYNGSLYFNK
CCCEEEEECEEEEEC
23.20UniProtKB CARBOHYD
465N-linked_GlycosylationNGHQVLFNVTLFHII
CCEEEEEEEEEEEEE
23.00UniProtKB 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 NOE3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOE3_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 NOE3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYOC_HUMANMYOCphysical
12019210
A4_HUMANAPPphysical
21832049
NOE2_HUMANOLFM2physical
28514442
BRE1A_HUMANRNF20physical
28514442
LRP1B_HUMANLRP1Bphysical
28514442
EHD4_HUMANEHD4physical
28514442
AGRIN_HUMANAGRNphysical
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 NOE3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-140, AND MASSSPECTROMETRY.

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