NOMO2_HUMAN - dbPTM
NOMO2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOMO2_HUMAN
UniProt AC Q5JPE7
Protein Name Nodal modulator 2
Gene Name NOMO2
Organism Homo sapiens (Human).
Sequence Length 1267
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein .
Protein Description May antagonize Nodal signaling and subsequent organization of axial structures during mesodermal patterning, via its interaction with NCLN..
Protein Sequence MLVGQGAGLLGPAVVTAAVVLLLSGVGPAHGSEDIVVGCGGFVKSDVEINYSLIEIKLYTKHGTLKYQTDCAPNNGYFMIPLYDKGDFILKIEPPLGWSFEPTTVELHVDGVSDICTKGGDINFVFTGFSVNGKVLSKGQPLGPAGVQVSLRNTGTEAKIQSTVTQPGGKFAFFKVLPGDYEILATHPTWALKEASTTVRVTNSNANAASPLIVAGYNVSGSVRSDGEPMKGVKFLLFSSLVTKEDVLGCNVSPVPGFQPQDESLVYLCYTVSREDGSFSFYSLPSGGYTVIPFYRGERITFDVAPSRLDFTVEHDSLKIEPVFHVMGFSVTGRVLNGPEGDGVPEAVVTLNNQIKVKTKADGSFRLENITTGTYTIHAQKEHLYFETVTIKIAPNTPQLADIVATGFSVCGRISIIRFPDTVKQMNKYKVVLSSQDKDKSLVTVETDAHGSFCFKAKPGTYKVQVMVPEAETRAGLTLKPQTFPLTVTDRPVMDVAFVQFLASVSGKVSCLDTCGDLLVTLQSLSRQGEKRSLQLSGKVNAMTFTFDNVLPGKYKISIMHEDWCWKNKSLEVEVLEDDVSAVEFRQTGYMLRCSLSHAITLEFYQDGNGRENVGIYNLSKGVNRFCLSKPGVYKVTPRSCHRFEQAFYTYDTSSPSILTLTAIRHHVLGTITTDKMMDVTVTIKSSIDSEPALVLGPLKSVQELRREQQLAEIEARRQEREKNGNEEGEERMTKPPVQEMVDELQGPFSYDFSYWARSGEKITVTPSSKELLFYPPSMEAVVSGESCPGKLIEIHGKAGLFLEGQIHPELEGVEIVISEKGASSPLITVFTDDKGAYSVGPLHSDLEYTVTSQKEGYVLTAVEGTIGDFKAYALAGVSFEIKAEDDQPLPGVLLSLSGGLFRSNLLTQDNGILTFSNLSPGQYYFKPMMKEFRFEPSSQMIEVQEGQNLKITITGYRTAYSCYGTVSSLNGEPEQGVAMEAVGQNDCSIYGEDTVTDEEGKFRLRGLLPGCVYHVQLKAEGNDHIERALPHHRVIEVGNNDIDDVNIIVFRQINQFDLSGNVITSSEYLPTLWVKLYKSENLDNPIQTVSLGQSLFFHFPPLLRDGENYVVLLDSTLPRSQYDYILPQVSFTAVGYHKHITLIFNPTRKLPEQDIAQGSYIALPLTLLVLLAGYNHDKLIPLLLQLTSRLQGVGALGQAASDNSGPEDAKRQAKKQKTRRTLRLQEEFQLMWCLVPWRGTLGIHLFSSLPFASEILLETTATCIHY
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
50N-linked_GlycosylationVKSDVEINYSLIEIK
CCCCCEECEEEEEEE		13.56UniProtKB CARBOHYD
61UbiquitinationIEIKLYTKHGTLKYQ
EEEEEEECCCEEEEE		26.8729967540
66UbiquitinationYTKHGTLKYQTDCAP
EECCCEEEEEEECCC		34.8429967540
85UbiquitinationFMIPLYDKGDFILKI
EEEEEEECCCEEEEE		46.9921963094
134UbiquitinationTGFSVNGKVLSKGQP
EEEEECCEEECCCCC		34.5021906983
134 (in isoform 1)Ubiquitination-34.5021890473
134 (in isoform 2)Ubiquitination-34.5021890473
138UbiquitinationVNGKVLSKGQPLGPA
ECCEEECCCCCCCCC		58.3621906983
138 (in isoform 1)Ubiquitination-58.3621890473
138 (in isoform 2)Ubiquitination-58.3621890473
150PhosphorylationGPAGVQVSLRNTGTE
CCCCEEEEEECCCCC		12.4320068231
150 (in isoform 2)Phosphorylation-12.43-
154PhosphorylationVQVSLRNTGTEAKIQ
EEEEEECCCCCEEEE		38.7622210691
156PhosphorylationVSLRNTGTEAKIQST
EEEECCCCCEEEEEE		30.6322210691
159SumoylationRNTGTEAKIQSTVTQ
ECCCCCEEEEEEEEC		34.74-
159SumoylationRNTGTEAKIQSTVTQ
ECCCCCEEEEEEEEC		34.74-
159UbiquitinationRNTGTEAKIQSTVTQ
ECCCCCEEEEEEEEC		34.7421906983
159 (in isoform 1)Ubiquitination-34.7421890473
159 (in isoform 2)Ubiquitination-34.7421890473
163O-linked_GlycosylationTEAKIQSTVTQPGGK
CCEEEEEEEECCCCE		15.93OGP
165O-linked_GlycosylationAKIQSTVTQPGGKFA
EEEEEEEECCCCEEE		29.18OGP
170UbiquitinationTVTQPGGKFAFFKVL
EEECCCCEEEEEEEC		39.1621890473
170AcetylationTVTQPGGKFAFFKVL
EEECCCCEEEEEEEC		39.1612634889
170UbiquitinationTVTQPGGKFAFFKVL
EEECCCCEEEEEEEC		39.1623000965
170 (in isoform 1)Ubiquitination-39.1621890473
170 (in isoform 2)Ubiquitination-39.1621890473
175UbiquitinationGGKFAFFKVLPGDYE
CCEEEEEEECCCCEE		36.0923000965
181PhosphorylationFKVLPGDYEILATHP
EEECCCCEEEEECCC		15.70-
193UbiquitinationTHPTWALKEASTTVR
CCCCEECCCCCCEEE		43.4121906983
193 (in isoform 1)Ubiquitination-43.4121890473
193 (in isoform 2)Ubiquitination-43.4121890473
218N-linked_GlycosylationPLIVAGYNVSGSVRS
CEEEEEEEECCEECC		22.14UniProtKB CARBOHYD
231UbiquitinationRSDGEPMKGVKFLLF
CCCCCCCCCCEEEEE		71.86-
239PhosphorylationGVKFLLFSSLVTKED
CCEEEEEECCCCHHH		23.8021406692
240PhosphorylationVKFLLFSSLVTKEDV
CEEEEEECCCCHHHH		21.3721406692
243PhosphorylationLLFSSLVTKEDVLGC
EEEECCCCHHHHCCC		33.7321406692
319UbiquitinationTVEHDSLKIEPVFHV
EEECCCEEEEECEEE		49.3121963094
356UbiquitinationVTLNNQIKVKTKADG
EEECCEEEEEECCCC		28.1021906983
356 (in isoform 1)Ubiquitination-28.1021890473
356 (in isoform 2)Ubiquitination-28.1021890473
358UbiquitinationLNNQIKVKTKADGSF
ECCEEEEEECCCCCE		39.0322817900
360UbiquitinationNQIKVKTKADGSFRL
CEEEEEECCCCCEEE		38.4722817900
385PhosphorylationHAQKEHLYFETVTIK
EEECCCEEEEEEEEE		10.9820068231
422PhosphorylationSIIRFPDTVKQMNKY
EEEECCHHHHHHCCE		29.82-
424UbiquitinationIRFPDTVKQMNKYKV
EECCHHHHHHCCEEE		46.02-
430UbiquitinationVKQMNKYKVVLSSQD
HHHHCCEEEEEECCC		27.7233845483
438UbiquitinationVVLSSQDKDKSLVTV
EEEECCCCCCCCEEE		60.4629967540
440UbiquitinationLSSQDKDKSLVTVET
EECCCCCCCCEEEEE		51.97-
458UbiquitinationGSFCFKAKPGTYKVQ
CCEEEEECCCEEEEE		44.5727667366
478PhosphorylationAETRAGLTLKPQTFP
CCCCCCCEECCCEEC		31.6420068231
483PhosphorylationGLTLKPQTFPLTVTD
CCEECCCEECCCCCC		35.4320068231
487PhosphorylationKPQTFPLTVTDRPVM
CCCEECCCCCCCCCH		22.9220068231
487 (in isoform 2)Phosphorylation-22.92-
489PhosphorylationQTFPLTVTDRPVMDV
CEECCCCCCCCCHHH		22.5120068231
489 (in isoform 2)Phosphorylation-22.51-
504PhosphorylationAFVQFLASVSGKVSC
HHHHHHHHCCCCEEE		20.9727732954
506PhosphorylationVQFLASVSGKVSCLD
HHHHHHCCCCEEECC		30.3327732954
539AcetylationRSLQLSGKVNAMTFT
CCEEEECCEEEEEEE		29.0112431525
539UbiquitinationRSLQLSGKVNAMTFT
CCEEEECCEEEEEEE		29.01-
554UbiquitinationFDNVLPGKYKISIMH
ECCCCCCCEEEEEEE		41.2421890473
554UbiquitinationFDNVLPGKYKISIMH
ECCCCCCCEEEEEEE		41.2421906983
554 (in isoform 1)Ubiquitination-41.2421890473
554 (in isoform 2)Ubiquitination-41.2421890473
556UbiquitinationNVLPGKYKISIMHED
CCCCCCEEEEEEECC		33.2022817900
618N-linked_GlycosylationRENVGIYNLSKGVNR
CEEEEEEECCCCCCC		35.60UniProtKB CARBOHYD
621UbiquitinationVGIYNLSKGVNRFCL
EEEEECCCCCCCCCC		70.7824816145
630UbiquitinationVNRFCLSKPGVYKVT
CCCCCCCCCCEEEEC		32.6121890473
630AcetylationVNRFCLSKPGVYKVT
CCCCCCCCCCEEEEC		32.6124664511
630UbiquitinationVNRFCLSKPGVYKVT
CCCCCCCCCCEEEEC		32.6122817900
630 (in isoform 1)Ubiquitination-32.6121890473
630 (in isoform 2)Ubiquitination-32.6121890473
635UbiquitinationLSKPGVYKVTPRSCH
CCCCCEEEECCCCCC		36.9122817900
649PhosphorylationHRFEQAFYTYDTSSP
CCCEEEEEECCCCCC		13.86-
650PhosphorylationRFEQAFYTYDTSSPS
CCEEEEEECCCCCCC		14.41-
653PhosphorylationQAFYTYDTSSPSILT
EEEEECCCCCCCCHH		22.23-
660PhosphorylationTSSPSILTLTAIRHH
CCCCCCHHHHHHHCH		22.01-
671O-linked_GlycosylationIRHHVLGTITTDKMM
HHCHHHCCCCCCCEE		15.81OGP
673O-linked_GlycosylationHHVLGTITTDKMMDV
CHHHCCCCCCCEEEE		28.87OGP
674O-linked_GlycosylationHVLGTITTDKMMDVT
HHHCCCCCCCEEEEE		29.76OGP
700UbiquitinationALVLGPLKSVQELRR
EEEEEECHHHHHHHH		52.2821906983
700 (in isoform 1)Ubiquitination-52.2821890473
700 (in isoform 2)Ubiquitination-52.2821890473
762UbiquitinationYWARSGEKITVTPSS
EEECCCCEEEECCCC		47.4021906983
762 (in isoform 1)Ubiquitination-47.4021890473
762 (in isoform 2)Ubiquitination-47.4021890473
770UbiquitinationITVTPSSKELLFYPP
EEECCCCCEEEECCC		57.6321963094
788GlutathionylationAVVSGESCPGKLIEI
EEECCCCCCCEEEEE		4.4822555962
791UbiquitinationSGESCPGKLIEIHGK
CCCCCCCEEEEEECC		31.2829967540
825PhosphorylationISEKGASSPLITVFT
EECCCCCCCEEEEEE		24.16-
835UbiquitinationITVFTDDKGAYSVGP
EEEEECCCCCEEECC		48.5329967540
845PhosphorylationYSVGPLHSDLEYTVT
EEECCCCCCEEEEEE		52.12-
849PhosphorylationPLHSDLEYTVTSQKE
CCCCCEEEEEECCCC		17.51-
855UbiquitinationEYTVTSQKEGYVLTA
EEEEECCCCCEEEEE		53.5329967540
858PhosphorylationVTSQKEGYVLTAVEG
EECCCCCEEEEEEEE		8.0620068231
861PhosphorylationQKEGYVLTAVEGTIG
CCCCEEEEEEEEECC		20.7220068231
927UbiquitinationSPGQYYFKPMMKEFR
CCCCEECCCCCCEEC		18.8421963094
931UbiquitinationYYFKPMMKEFRFEPS
EECCCCCCEECCCCC		47.6621963094
1019UbiquitinationCVYHVQLKAEGNDHI
CEEEEEEEECCCCHH		27.5733845483
1076UbiquitinationYLPTLWVKLYKSENL
CCCEEEEEEHHCCCC		34.2223503661
1079UbiquitinationTLWVKLYKSENLDNP
EEEEEEHHCCCCCCC		62.8333845483
1110PhosphorylationLLRDGENYVVLLDST
CCCCCCCEEEEEECC		6.40-
1123PhosphorylationSTLPRSQYDYILPQV
CCCCHHHCCEEECCC		16.38-
1125PhosphorylationLPRSQYDYILPQVSF
CCHHHCCEEECCCEE		10.22-
1137PhosphorylationVSFTAVGYHKHITLI
CEEEEEEECCEEEEE		10.90-
1202PhosphorylationGALGQAASDNSGPED
CHHHHHHHCCCCHHH		40.1030266825
1205PhosphorylationGQAASDNSGPEDAKR
HHHHHCCCCHHHHHH		61.7930266825
1205 (in isoform 2)Phosphorylation-61.79-
1211AcetylationNSGPEDAKRQAKKQK
CCCHHHHHHHHHHHH		58.3223895329
1211UbiquitinationNSGPEDAKRQAKKQK
CCCHHHHHHHHHHHH		58.3221906983
1211 (in isoform 1)Ubiquitination-58.3221890473
1211 (in isoform 2)Ubiquitination-58.3221890473
1215UbiquitinationEDAKRQAKKQKTRRT
HHHHHHHHHHHHHHH		47.6122817900
1216UbiquitinationDAKRQAKKQKTRRTL
HHHHHHHHHHHHHHH		61.1022817900
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 NOMO2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOMO2_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 NOMO2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAT1_HUMANSTAT1physical
21988832
RPN1_HUMANRPN1physical
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 NOMO2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1205, AND MASSSPECTROMETRY.

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