NCLN_HUMAN - dbPTM
NCLN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCLN_HUMAN
UniProt AC Q969V3
Protein Name Nicalin
Gene Name NCLN
Organism Homo sapiens (Human).
Sequence Length 563
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein .
Protein Description May antagonize Nodal signaling and subsequent organization of axial structures during mesodermal patterning..
Protein Sequence MLEEAGEVLENMLKASCLPLGFIVFLPAVLLLVAPPLPAADAAHEFTVYRMQQYDLQGQPYGTRNAVLNTEARTMAAEVLSRRCVLMRLLDFSYEQYQKALRQSAGAVVIILPRAMAAVPQDVVRQFMEIEPEMLAMETAVPVYFAVEDEALLSIYKQTQAASASQGSASAAEVLLRTATANGFQMVTSGVQSKAVSDWLIASVEGRLTGLGGEDLPTIVIVAHYDAFGVAPWLSLGADSNGSGVSVLLELARLFSRLYTYKRTHAAYNLLFFASGGGKFNYQGTKRWLEDNLDHTDSSLLQDNVAFVLCLDTVGRGSSLHLHVSKPPREGTLQHAFLRELETVAAHQFPEVRFSMVHKRINLAEDVLAWEHERFAIRRLPAFTLSHLESHRDGQRSSIMDVRSRVDSKTLTRNTRIIAEALTRVIYNLTEKGTPPDMPVFTEQMQIQQEQLDSVMDWLTNQPRAAQLVDKDSTFLSTLEHHLSRYLKDVKQHHVKADKRDPEFVFYDQLKQVMNAYRVKPAVFDLLLAVGIAAYLGMAYVAVQHFSLLYKTVQRLLVKAKTQ
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
75SulfoxidationLNTEARTMAAEVLSR
HCHHHHHHHHHHHHH		2.5021406390
94PhosphorylationMRLLDFSYEQYQKAL
HHHHCCCHHHHHHHH		13.6728152594
97PhosphorylationLDFSYEQYQKALRQS
HCCCHHHHHHHHHHH		10.4728152594
99 (in isoform 1)Ubiquitination-44.4421890473
99 (in isoform 2)Ubiquitination-44.4421890473
99UbiquitinationFSYEQYQKALRQSAG
CCHHHHHHHHHHHCC		44.4427667366
116SulfoxidationVIILPRAMAAVPQDV
EEECCHHHHCCCHHH		2.3121406390
178PhosphorylationAAEVLLRTATANGFQ
HHHHHHHHHHHCCEE		28.47-
193PhosphorylationMVTSGVQSKAVSDWL
EECCCCCCHHHCCHH		21.8520068231
194 (in isoform 1)Ubiquitination-35.4021890473
194UbiquitinationVTSGVQSKAVSDWLI
ECCCCCCHHHCCHHH		35.4021906983
194 (in isoform 2)Ubiquitination-35.4021890473
241N-linked_GlycosylationLSLGADSNGSGVSVL
HHCCCCCCCCHHHHH		49.55UniProtKB CARBOHYD
262UbiquitinationFSRLYTYKRTHAAYN
HHHHHHHCHHHHHHH		42.91-
275PhosphorylationYNLLFFASGGGKFNY
HHEEEEECCCCCCCC		32.58-
286UbiquitinationKFNYQGTKRWLEDNL
CCCCCCHHHHHHHCC		48.6921906983
286 (in isoform 1)Ubiquitination-48.6921890473
286 (in isoform 2)Ubiquitination-48.6921890473
2862-HydroxyisobutyrylationKFNYQGTKRWLEDNL
CCCCCCHHHHHHHCC		48.69-
318PhosphorylationLDTVGRGSSLHLHVS
EECCCCCCCEEEEEC		28.5027080861
319PhosphorylationDTVGRGSSLHLHVSK
ECCCCCCCEEEEECC		23.7227080861
326 (in isoform 2)Ubiquitination-58.9321890473
326 (in isoform 1)Ubiquitination-58.9321890473
326UbiquitinationSLHLHVSKPPREGTL
CEEEEECCCCCCCCH		58.9322817900
359UbiquitinationVRFSMVHKRINLAED
CCHHHHHHCCCHHHH		43.49-
3592-HydroxyisobutyrylationVRFSMVHKRINLAED
CCHHHHHHCCCHHHH		43.49-
397PhosphorylationSHRDGQRSSIMDVRS
HCCCCCCCCHHHHHH		19.14-
398PhosphorylationHRDGQRSSIMDVRSR
CCCCCCCCHHHHHHH		24.91-
409UbiquitinationVRSRVDSKTLTRNTR
HHHHCCCCCCCCHHH		42.9927667366
409 (in isoform 2)Ubiquitination-42.99-
423PhosphorylationRIIAEALTRVIYNLT
HHHHHHHHHHHHHHH		29.9120068231
428N-linked_GlycosylationALTRVIYNLTEKGTP
HHHHHHHHHHCCCCC		29.39UniProtKB CARBOHYD
434PhosphorylationYNLTEKGTPPDMPVF
HHHHCCCCCCCCCCC		42.5920068231
442PhosphorylationPPDMPVFTEQMQIQQ
CCCCCCCCHHHHHHH		26.0720068231
460PhosphorylationDSVMDWLTNQPRAAQ
HHHHHHHHCCHHHHH		27.7920068231
470 (in isoform 2)Ubiquitination-58.6021890473
470UbiquitinationPRAAQLVDKDSTFLS
HHHHHHCCCCCHHHH		58.6021963094
471AcetylationRAAQLVDKDSTFLST
HHHHHCCCCCHHHHH		46.2126051181
471 (in isoform 1)Ubiquitination-46.2121890473
471UbiquitinationRAAQLVDKDSTFLST
HHHHHCCCCCHHHHH		46.2121906983
487UbiquitinationEHHLSRYLKDVKQHH
HHHHHHHHHHHHHHH		3.5727667366
488UbiquitinationHHLSRYLKDVKQHHV
HHHHHHHHHHHHHHC		52.0927667366
490UbiquitinationLSRYLKDVKQHHVKA
HHHHHHHHHHHHCCC		6.5029967540
491UbiquitinationSRYLKDVKQHHVKAD
HHHHHHHHHHHCCCC		54.7929967540
4912-HydroxyisobutyrylationSRYLKDVKQHHVKAD
HHHHHHHHHHHCCCC		54.79-
495UbiquitinationKDVKQHHVKADKRDP
HHHHHHHCCCCCCCC		5.2622817900
496UbiquitinationDVKQHHVKADKRDPE
HHHHHHCCCCCCCCC		46.6522817900
498 (in isoform 2)Ubiquitination-40.5821890473
498UbiquitinationKQHHVKADKRDPEFV
HHHHCCCCCCCCCCC		40.5822817900
499 (in isoform 1)Ubiquitination-64.6621890473
499UbiquitinationQHHVKADKRDPEFVF
HHHCCCCCCCCCCCH		64.6621906983
510 (in isoform 2)Ubiquitination-3.7021890473
510UbiquitinationEFVFYDQLKQVMNAY
CCCHHHHHHHHHHHH		3.7022817900
511 (in isoform 1)Ubiquitination-34.9021890473
511UbiquitinationFVFYDQLKQVMNAYR
CCHHHHHHHHHHHHC		34.9022817900
558UbiquitinationKTVQRLLVKAKTQ--
HHHHHHHHHHHCC--		7.2027667366
559UbiquitinationTVQRLLVKAKTQ---
HHHHHHHHHHCC---		44.1027667366
560UbiquitinationVQRLLVKAKTQ----
HHHHHHHHHCC----		16.7924816145
561UbiquitinationQRLLVKAKTQ-----
HHHHHHHHCC-----		41.5624816145
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 NCLN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCLN_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 NCLN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NOMO1_HUMANNOMO1physical
15257293
RPN2_HUMANRPN2physical
26344197
SERC1_HUMANSERINC1physical
27173435
METL9_HUMANMETTL9physical
27173435
NOMO1_HUMANNOMO1physical
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 NCLN_HUMAN

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Related Literatures of Post-Translational Modification

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