NXPE4_HUMAN - dbPTM
NXPE4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NXPE4_HUMAN
UniProt AC Q6UWF7
Protein Name NXPE family member 4
Gene Name NXPE4
Organism Homo sapiens (Human).
Sequence Length 544
Subcellular Localization Secreted .
Protein Description
Protein Sequence MKISMINYKSLLALLFILASWIIFTVFQNSTKVWSALNLSISLHYWNNSTKSLFPKTPLISLKPLTETELRIKEIIEKLDQQIPPRPFTHVNTTTSATHSTATILNPRDTYCRGDQLHILLEVRDHLGRRKQYGGDFLRARMSSPALMAGASGKVTDFNNGTYLVSFTLFWEGQVSLSLLLIHPSEGVSALWSARNQGYDRVIFTGQFVNGTSQVHSECGLILNTNAELCQYLDNRDQEGFYCVRPQHMPCAALTHMYSKNKKVSYLSKQEKSLFERSNVGVEIMEKFNTISVSKCNKETVAMKEKCKFGMTSTIPSGHVWRNTWNPVSCSLATVKMKECLRGKLIYLMGDSTIRQWMEYFKASINTLKSVDLHESGKLQHQLAVDLDRNINIQWQKYCYPLIGSMTYSVKEMEYLTRAIDRTGGEKNTVIVISLGQHFRPFPIDVFIRRALNVHKAIQHLLLRSPDTMVIIKTENIREMYNDAERFSDFHGYIQYLIIKDIFQDLSVSIIDAWDITIAYGTNNVHPPQHVVGNQINILLNYIC
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
4Phosphorylation----MKISMINYKSL
----CCCCCCCHHHH
24719451
29N-linked_GlycosylationIIFTVFQNSTKVWSA
HHHHHHCCCHHHHHH
UniProtKB CARBOHYD
38N-linked_GlycosylationTKVWSALNLSISLHY
HHHHHHHEEEEEEEE
UniProtKB CARBOHYD
47N-linked_GlycosylationSISLHYWNNSTKSLF
EEEEEECCCCCCCCC
UniProtKB CARBOHYD
48N-linked_GlycosylationISLHYWNNSTKSLFP
EEEEECCCCCCCCCC
UniProtKB CARBOHYD
61PhosphorylationFPKTPLISLKPLTET
CCCCCCEECCCCCHH
24719451
66PhosphorylationLISLKPLTETELRIK
CEECCCCCHHHHHHH
-
92N-linked_GlycosylationPRPFTHVNTTTSATH
CCCCCCCCCCCCCCC
UniProtKB CARBOHYD
94AcetylationPFTHVNTTTSATHST
CCCCCCCCCCCCCCE
19413330
143PhosphorylationDFLRARMSSPALMAG
CHHHHHCCCCCHHCC
-
152PhosphorylationPALMAGASGKVTDFN
CCHHCCCCCEEEECC
-
160N-linked_GlycosylationGKVTDFNNGTYLVSF
CEEEECCCCEEEEEE
UniProtKB CARBOHYD
205PhosphorylationGYDRVIFTGQFVNGT
CCCEEEEEEECCCCC
-
210N-linked_GlycosylationIFTGQFVNGTSQVHS
EEEEECCCCCCCCCC
UniProtKB CARBOHYD
259PhosphorylationAALTHMYSKNKKVSY
HHHHHHHCCCCCHHH
24719451
292PhosphorylationMEKFNTISVSKCNKE
HHHHCEEEEECCCHH
24719451
304AcetylationNKETVAMKEKCKFGM
CHHHHHCCCCCCCCC
12433651
347PhosphorylationCLRGKLIYLMGDSTI
HHCCCEEECCCCHHH
-
352PhosphorylationLIYLMGDSTIRQWME
EEECCCCHHHHHHHH
22210691
378AcetylationVDLHESGKLQHQLAV
EEHHCCCCCEEEEEE
19413330
398PhosphorylationINIQWQKYCYPLIGS
CEEEEHHHHHHHHCC
23090842
400PhosphorylationIQWQKYCYPLIGSMT
EEEHHHHHHHHCCCE
23090842
405PhosphorylationYCYPLIGSMTYSVKE
HHHHHHCCCEEEHHH
27732954
407PhosphorylationYPLIGSMTYSVKEME
HHHHCCCEEEHHHHH
27732954
408PhosphorylationPLIGSMTYSVKEMEY
HHHCCCEEEHHHHHH
23090842
409PhosphorylationLIGSMTYSVKEMEYL
HHCCCEEEHHHHHHH
27732954
415PhosphorylationYSVKEMEYLTRAIDR
EEHHHHHHHHHHHHH
22964224
417PhosphorylationVKEMEYLTRAIDRTG
HHHHHHHHHHHHHCC
23090842

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 NXPE4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NXPE4_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 NXPE4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NXPE4_HUMAN !!

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 NXPE4_HUMAN

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Related Literatures of Post-Translational Modification

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