NF2L1_HUMAN - dbPTM
NF2L1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NF2L1_HUMAN
UniProt AC Q14494
Protein Name Endoplasmic reticulum membrane sensor NFE2L1 {ECO:0000305}
Gene Name NFE2L1
Organism Homo sapiens (Human).
Sequence Length 772
Subcellular Localization Endoplasmic reticulum membrane sensor NFE2L1: Endoplasmic reticulum membrane
Single-pass type II membrane protein . Endoplasmic reticulum membrane
Single-pass type III membrane protein . In normal conditions, probably has a single-pass type II me
Protein Description Endoplasmic reticulum membrane sensor NFE2L1: Endoplasmic reticulum membrane sensor that translocates into the nucleus in response to various stresses to act as a transcription factor. [PubMed: 20932482]
Protein Sequence MLSLKKYLTEGLLQFTILLSLIGVRVDVDTYLTSQLPPLREIILGPSSAYTQTQFHNLRNTLDGYGIHPKSIDLDNYFTARRLLSQVRALDRFQVPTTEVNAWLVHRDPEGSVSGSQPNSGLALESSSGLQDVTGPDNGVRESETEQGFGEDLEDLGAVAPPVSGDLTKEDIDLIDILWRQDIDLGAGREVFDYSHRQKEQDVEKELRDGGEQDTWAGEGAEALARNLLVDGETGESFPAQVPSGEDQTALSLEECLRLLEATCPFGENAEFPADISSITEAVPSESEPPALQNNLLSPLLTGTESPFDLEQQWQDLMSIMEMQAMEVNTSASEILYSAPPGDPLSTNYSLAPNTPINQNVSLHQASLGGCSQDFLLFSPEVESLPVASSSTLLPLAPSNSTSLNSTFGSTNLTGLFFPPQLNGTANDTAGPELPDPLGGLLDEAMLDEISLMDLAIEEGFNPVQASQLEEEFDSDSGLSLDSSHSPSSLSSSEGSSSSSSSSSSSSSSASSSASSSFSEEGAVGYSSDSETLDLEEAEGAVGYQPEYSKFCRMSYQDPAQLSCLPYLEHVGHNHTYNMAPSALDSADLPPPSALKKGSKEKQADFLDKQMSRDEHRARAMKIPFTNDKIINLPVEEFNELLSKYQLSEAQLSLIRDIRRRGKNKMAAQNCRKRKLDTILNLERDVEDLQRDKARLLREKVEFLRSLRQMKQKVQSLYQEVFGRLRDENGRPYSPSQYALQYAGDGSVLLIPRTMADQQARRQERKPKDRRK
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
3Phosphorylation-----MLSLKKYLTE
-----CCCHHHHHHH		36.52-
61PhosphorylationQFHNLRNTLDGYGIH
HHHHHHHCCCCCCCC		21.5729083192
65PhosphorylationLRNTLDGYGIHPKSI
HHHCCCCCCCCCCCC		16.7527174698
70 (in isoform 2)Ubiquitination-45.9721890473
70 (in isoform 1)Ubiquitination-45.9721890473
70UbiquitinationDGYGIHPKSIDLDNY
CCCCCCCCCCCCCCH		45.9721890473
71PhosphorylationGYGIHPKSIDLDNYF
CCCCCCCCCCCCCHH		26.2827174698
77PhosphorylationKSIDLDNYFTARRLL
CCCCCCCHHHHHHHH		11.2827174698
79PhosphorylationIDLDNYFTARRLLSQ
CCCCCHHHHHHHHHH		14.6427174698
98O-linked_GlycosylationDRFQVPTTEVNAWLV
HCCCCCCCEEEEEEE		31.69OGP
112PhosphorylationVHRDPEGSVSGSQPN
EEECCCCCCCCCCCC		16.0824275569
114PhosphorylationRDPEGSVSGSQPNSG
ECCCCCCCCCCCCCC		34.1324275569
116PhosphorylationPEGSVSGSQPNSGLA
CCCCCCCCCCCCCEE		34.6524275569
120PhosphorylationVSGSQPNSGLALESS
CCCCCCCCCEEEECC		41.7024275569
126PhosphorylationNSGLALESSSGLQDV
CCCEEEECCCCCCCC		30.5624275569
194PhosphorylationAGREVFDYSHRQKEQ
CCCCCCCCCHHHHHH		8.5623403867
195PhosphorylationGREVFDYSHRQKEQD
CCCCCCCCHHHHHHH		17.6523403867
199UbiquitinationFDYSHRQKEQDVEKE
CCCCHHHHHHHHHHH		58.25-
205UbiquitinationQKEQDVEKELRDGGE
HHHHHHHHHHHHCCC		62.99-
285PhosphorylationSITEAVPSESEPPAL
HHHHCCCCCCCCCHH		47.3524275569
348N-linked_GlycosylationPGDPLSTNYSLAPNT
CCCCCCCCCCCCCCC		22.48-
360N-linked_GlycosylationPNTPINQNVSLHQAS
CCCCCCCCCEECCCC		22.36-
379PhosphorylationSQDFLLFSPEVESLP
CCCEECCCCCHHCCC		21.81-
412N-linked_GlycosylationNSTFGSTNLTGLFFP
CCCCCCCCCCEEECC		36.98-
423N-linked_GlycosylationLFFPPQLNGTANDTA
EECCCCCCCCCCCCC		40.29-
498PhosphorylationSSSEGSSSSSSSSSS
CCCCCCCCCCCCCCC		35.62-
499PhosphorylationSSEGSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
500PhosphorylationSEGSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
501PhosphorylationEGSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
502PhosphorylationGSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
507PhosphorylationSSSSSSSSSSASSSA
CCCCCCCCCCCCCCC		30.20-
508PhosphorylationSSSSSSSSSASSSAS
CCCCCCCCCCCCCCC		31.69-
509PhosphorylationSSSSSSSSASSSASS
CCCCCCCCCCCCCCC		33.83-
528PhosphorylationEGAVGYSSDSETLDL
CCCCCCCCCCCEECH		36.35-
599 (in isoform 2)Ubiquitination-46.6621890473
599PhosphorylationPSALKKGSKEKQADF
HHHHCCCCHHHHHHH		46.6624448410
600AcetylationSALKKGSKEKQADFL
HHHCCCCHHHHHHHH		77.0626051181
602AcetylationLKKGSKEKQADFLDK
HCCCCHHHHHHHHHH		55.3025953088
609UbiquitinationKQADFLDKQMSRDEH
HHHHHHHHHCCHHHH		50.47-
622UbiquitinationEHRARAMKIPFTNDK
HHHHHHHCCCCCCCC		46.36-
629 (in isoform 1)Ubiquitination-47.7821890473
629UbiquitinationKIPFTNDKIINLPVE
CCCCCCCCEECCCHH		47.7821906983
643PhosphorylationEEFNELLSKYQLSEA
HHHHHHHHHHCCCHH		41.77-
645PhosphorylationFNELLSKYQLSEAQL
HHHHHHHHCCCHHHH		16.0017693683
648PhosphorylationLLSKYQLSEAQLSLI
HHHHHCCCHHHHHHH		18.5029978859
653PhosphorylationQLSEAQLSLIRDIRR
CCCHHHHHHHHHHHH		15.0729978859
675UbiquitinationAQNCRKRKLDTILNL
HHHHHHCHHHHHHCC		54.47-
678PhosphorylationCRKRKLDTILNLERD
HHHCHHHHHHCCHHC		37.4929083192
683 (in isoform 2)Ubiquitination-45.8421890473
693UbiquitinationVEDLQRDKARLLREK
HHHHHHHHHHHHHHH		37.28-
700UbiquitinationKARLLREKVEFLRSL
HHHHHHHHHHHHHHH		40.40-
713UbiquitinationSLRQMKQKVQSLYQE
HHHHHHHHHHHHHHH		36.402190698
713 (in isoform 1)Ubiquitination-36.4021890473
733PhosphorylationRDENGRPYSPSQYAL
CCCCCCCCCHHHHHE		31.6730108239
734PhosphorylationDENGRPYSPSQYALQ
CCCCCCCCHHHHHEE		22.2830108239
736PhosphorylationNGRPYSPSQYALQYA
CCCCCCHHHHHEEEC		29.8624719451
738PhosphorylationRPYSPSQYALQYAGD
CCCCHHHHHEEECCC		17.3930108239
742PhosphorylationPSQYALQYAGDGSVL
HHHHHEEECCCCCEE		17.2530108239
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
379SPhosphorylationKinaseGSK3BP49841
PSP
528SPhosphorylationKinaseCK2-Uniprot
599SPhosphorylationKinasePRKACAP27791
GPS
599SPhosphorylationKinasePKA-FAMILY-GPS
599SPhosphorylationKinasePKA-Uniprot
599SPhosphorylationKinasePKA_GROUP-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:24658274
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
528SPhosphorylation

15308669
599SPhosphorylation

15308669
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 NF2L1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBXW7_HUMANFBXW7physical
21953459
KEAP1_HUMANKEAP1physical
16687406
FBXW7_HUMANFBXW7physical
23623971
BACH2_HUMANBACH2physical
23661758
NF2L1_HUMANNFE2L1physical
23661758
MAFG_HUMANMAFGphysical
23661758
MAFF_HUMANMAFFphysical
23661758
RUSC2_HUMANRUSC2physical
26496610
WDFY3_HUMANWDFY3physical
26496610
CH033_HUMANC8orf33physical
26496610
BRD9_HUMANBRD9physical
26496610
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 NF2L1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-645, AND MASSSPECTROMETRY.

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