NOMO1_HUMAN - dbPTM
NOMO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOMO1_HUMAN
UniProt AC Q15155
Protein Name Nodal modulator 1
Gene Name NOMO1
Organism Homo sapiens (Human).
Sequence Length 1222
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description May antagonize Nodal signaling..
Protein Sequence MLVGQGAGPLGPAVVTAAVVLLLSGVGPAHGSEDIVVGCGGFVKSDVEINYSLIEIKLYTKHGTLKYQTDCAPNNGYFMIPLYDKGDFILKIEPPLGWSFEPTTVELHVDGVSDICTKGGDINFVFTGFSVNGKVLSKGQPLGPAGVQVSLRNTGTEAKIQSTVTQPGGKFAFFKVLPGDYEILATHPTWALKEASTTVRVTNSNANAASPLIVAGYNVSGSVRSDGEPMKGVKFLLFSSLVTKEDVLGCNVSPVPGFQPQDESLVYLCYTVSREDGSFSFYSLPSGGYTVIPFYRGERITFDVAPSRLDFTVEHDSLKIEPVFHVMGFSVTGRVLNGPEGDGVPEAVVTLNNQIKVKTKADGSFRLENITTGTYTIHAQKEHLYFETVTIKIAPNTPQLADIIATGFSVCGQISIIRFPDTVKQMNKYKVVLSSQDKDKSLVTVETDAHGSFCFKAKPGTYKVQVMVPEAETRAGLTLKPQTFPLTVTNRPMMDVAFVQFLASVSGKVSCLDTCGDLLVTLQSLSRQGEKRSLQLSGKVNAMTFTFDNVLPGKYKISIMHEDWCWKNKSLEVEVLEDDMSAVEFRQTGYMLRCSLSHAITLEFYQDGNGRENVGIYNLSKGVNRFCLSKPGVYKVTPRSCHRFEQAFYTYDTSSPSILTLTAIRHHVLGTITTDKMMDVTVTIKSSIDSEPALVLGPLKSVQELRREQQLAEIEARRQEREKNGNEEGEERMTKPPVQEMVDELQGPFSYDFSYWARSGEKITVTPSSKELLFYPPSMEAVVSGESCPGKLIEIHGKAGLFLEGQIHPELEGVEIVISEKGASSPLITVFTDDKGAYSVGPLHSDLEYTVTSQKEGYVLTAVEGTIGDFKAYALAGVSFEIKAEDDQPLPGVLLSLSGGLFRSNLLTQDNGILTFSNLSPGQYYFKPMMKEFRFEPSSQMIEVQEGQNLKITITGYRTAYSCYGTVSSLNGEPEQGVAMEAVGQNDCSIYGEDTVTDEEGKFRLRGLLPGCVYHVQLKAEGNDHIERALPHHRVIEVGNNDIDDVNIIVFRQINQFDLSGNVITSSEYLPTLWVKLYKSENLDNPIQTVSLGQSLFFHFPPLLRDGENYVVLLDSTLPRSQYDYILPQVSFTAVGYHKHITLIFNPTRKLPEQDIAQGSYIALPLTLLVLLAGYNHDKLIPLLLQLTSRLQGVRALGQAASDNSGPEDAKRQAKKQKTRRT
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
138UbiquitinationVNGKVLSKGQPLGPA
ECCEEECCCCCCCCC		58.3621906983
150PhosphorylationGPAGVQVSLRNTGTE
CCCCEEEEEECCCCC		12.4320068231
154PhosphorylationVQVSLRNTGTEAKIQ
EEEEEECCCCCEEEE		38.7622210691
156PhosphorylationVSLRNTGTEAKIQST
EEEECCCCCEEEEEE		30.6322210691
159SumoylationRNTGTEAKIQSTVTQ
ECCCCCEEEEEEEEC		34.74-
159UbiquitinationRNTGTEAKIQSTVTQ
ECCCCCEEEEEEEEC		34.7421906983
159SumoylationRNTGTEAKIQSTVTQ
ECCCCCEEEEEEEEC		34.74-
1702-HydroxyisobutyrylationTVTQPGGKFAFFKVL
EEECCCCEEEEEEEC		39.16-
170UbiquitinationTVTQPGGKFAFFKVL
EEECCCCEEEEEEEC		39.1623000965
170AcetylationTVTQPGGKFAFFKVL
EEECCCCEEEEEEEC		39.1612634879
175UbiquitinationGGKFAFFKVLPGDYE
CCEEEEEEECCCCEE		36.0923000965
181PhosphorylationFKVLPGDYEILATHP
EEECCCCEEEEECCC		15.70-
193UbiquitinationTHPTWALKEASTTVR
CCCCEECCCCCCEEE		43.4121906983
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
358UbiquitinationLNNQIKVKTKADGSF
ECCEEEEEECCCCCE		39.0322817900
360UbiquitinationNQIKVKTKADGSFRL
CEEEEEECCCCCEEE		38.4722817900
385PhosphorylationHAQKEHLYFETVTIK
EEECCCEEEEEEEEE		10.9820068231
397PhosphorylationTIKIAPNTPQLADII
EEEECCCCHHHHHHH		16.0222210691
415PhosphorylationFSVCGQISIIRFPDT
CCCCCEEEEEECCHH		12.2222210691
422PhosphorylationSIIRFPDTVKQMNKY
EEEECCHHHHHHCCE		29.8222210691
424UbiquitinationIRFPDTVKQMNKYKV
EECCHHHHHHCCEEE		46.0233845483
430UbiquitinationVKQMNKYKVVLSSQD
HHHHCCEEEEEECCC		27.7233845483
4382-HydroxyisobutyrylationVVLSSQDKDKSLVTV
EEEECCCCCCCCEEE		60.46-
438UbiquitinationVVLSSQDKDKSLVTV
EEEECCCCCCCCEEE		60.4629967540
440UbiquitinationLSSQDKDKSLVTVET
EECCCCCCCCEEEEE		51.97-
458UbiquitinationGSFCFKAKPGTYKVQ
CCEEEEECCCEEEEE		44.5727667366
539AcetylationRSLQLSGKVNAMTFT
CCEEEECCEEEEEEE		29.0112431459
554UbiquitinationFDNVLPGKYKISIMH
ECCCCCCCEEEEEEE		41.2421906983
556UbiquitinationNVLPGKYKISIMHED
CCCCCCEEEEEEECC		33.2022817900
618N-linked_GlycosylationRENVGIYNLSKGVNR
CEEEEEEECCCCCCC		35.6019159218
621UbiquitinationVGIYNLSKGVNRFCL
EEEEECCCCCCCCCC		70.7824816145
630UbiquitinationVNRFCLSKPGVYKVT
CCCCCCCCCCEEEEC		32.6122817900
630AcetylationVNRFCLSKPGVYKVT
CCCCCCCCCCEEEEC		32.6124664481
635UbiquitinationLSKPGVYKVTPRSCH
CCCCCEEEECCCCCC		36.9122817900
649PhosphorylationHRFEQAFYTYDTSSP
CCCEEEEEECCCCCC		13.86-
650PhosphorylationRFEQAFYTYDTSSPS
CCEEEEEECCCCCCC		14.41-
653PhosphorylationQAFYTYDTSSPSILT
EEEEECCCCCCCCHH		22.23-
660PhosphorylationTSSPSILTLTAIRHH
CCCCCCHHHHHHHCH		22.01-
700UbiquitinationALVLGPLKSVQELRR
EEEEEECHHHHHHHH		52.2821906983
762UbiquitinationYWARSGEKITVTPSS
EEECCCCEEEECCCC		47.4027667366
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
CCCCEEECCCCCEEC		18.8421963094
931UbiquitinationYYFKPMMKEFRFEPS
EEECCCCCEECCCCC		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-
1202PhosphorylationRALGQAASDNSGPED
HHHHHHHHCCCCHHH		40.1030266825
1205PhosphorylationGQAASDNSGPEDAKR
HHHHHCCCCHHHHHH		61.7930266825
1211UbiquitinationNSGPEDAKRQAKKQK
CCCHHHHHHHHHHHH		58.3227667366
1215UbiquitinationEDAKRQAKKQKTRRT
HHHHHHHHHHHHCCC		47.6122817900
1216UbiquitinationDAKRQAKKQKTRRT-
HHHHHHHHHHHCCC-		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 NOMO1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOMO1_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 NOMO1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BAG6_HUMANBAG6physical
16169070
TM1L1_HUMANTOM1L1physical
16169070
PLEC_HUMANPLECphysical
22939629
TIM10_HUMANTIMM10physical
22939629
STAT1_HUMANSTAT1physical
21988832
RPN1_HUMANRPN1physical
26344197
METL9_HUMANMETTL9physical
27173435
SERC1_HUMANSERINC1physical
27173435
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 NOMO1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-618, AND MASSSPECTROMETRY.

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