NFIP1_HUMAN - dbPTM
NFIP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NFIP1_HUMAN
UniProt AC Q9BT67
Protein Name NEDD4 family-interacting protein 1
Gene Name NDFIP1
Organism Homo sapiens (Human).
Sequence Length 221
Subcellular Localization Endosome membrane
Multi-pass membrane protein . Golgi apparatus membrane . Cell junction, synapse, synaptosome . Cell projection, dendrite . Secreted . Detected in exosomes and secreted via the exosomal pathway (PubMed:18819914).
Protein Description Activates HECT domain-containing E3 ubiquitin-protein ligases, including NEDD4 and ITCH, and consequently modulates the stability of their targets. As a result, controls many cellular processes. Prevents chronic T-helper cell-mediated inflammation by activating ITCH and thus controlling JUNB degradation (By similarity). Promotes pancreatic beta cell death through degradation of JUNB and inhibition of the unfolded protein response, leading to reduction of insulin secretion. [PubMed: 26319551 Restricts the production of proinflammatory cytokines in effector Th17 T-cells by promoting ITCH-mediated ubiquitination and degradation of RORC (By similarity Together with NDFIP2, limits the cytokine signaling and expansion of effector Th2 T-cells by promoting degradation of JAK1, probably by ITCH- and NEDD4L-mediated ubiquitination (By similarity Regulates peripheral T-cell tolerance to self and foreign antigens, forcing the exit of naive CD4+ T-cells from the cell cycle before they become effector T-cells (By similarity Negatively regulates RLR-mediated antiviral response by promoting SMURF1-mediated ubiquitination and subsequent degradation of MAVS]
Protein Sequence MALALAALAAVEPACGSRYQQLQNEEESGEPEQAAGDAPPPYSSISAESAAYFDYKDESGFPKPPSYNVATTLPSYDEAERTKAEATIPLVPGRDEDFVGRDDFDDADQLRIGNDGIFMLTFFMAFLFNWIGFFLSFCLTTSAAGRYGAISGFGLSLIKWILIVRFSTYFPGYFDGQYWLWWVFLVLGFLLFLRGFINYAKVRKMPETFSNLPRTRVLFIY
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
2Acetylation------MALALAALA
------CHHHHHHHH
11.0922223895
15S-palmitoylationLAAVEPACGSRYQQL
HHHHCHHHCHHHHHH
8.1219801377
17PhosphorylationAVEPACGSRYQQLQN
HHCHHHCHHHHHHHC
27.9128348404
19PhosphorylationEPACGSRYQQLQNEE
CHHHCHHHHHHHCCH
11.4325884760
42PhosphorylationAGDAPPPYSSISAES
CCCCCCCCCCCCHHH
22.3325884760
43PhosphorylationGDAPPPYSSISAESA
CCCCCCCCCCCHHHH
27.28-
49PhosphorylationYSSISAESAAYFDYK
CCCCCHHHHHCCCCC
20.2325884760
52PhosphorylationISAESAAYFDYKDES
CCHHHHHCCCCCCCC
9.1925884760
55PhosphorylationESAAYFDYKDESGFP
HHHHCCCCCCCCCCC
15.5025884760
56UbiquitinationSAAYFDYKDESGFPK
HHHCCCCCCCCCCCC
57.7929967540
59PhosphorylationYFDYKDESGFPKPPS
CCCCCCCCCCCCCCC
56.7326356563
63 (in isoform 1)Ubiquitination-68.2621890473
63UbiquitinationKDESGFPKPPSYNVA
CCCCCCCCCCCCCCC
68.2622817900
66PhosphorylationSGFPKPPSYNVATTL
CCCCCCCCCCCCCCC
37.5626356563
67PhosphorylationGFPKPPSYNVATTLP
CCCCCCCCCCCCCCC
21.3025884760
75PhosphorylationNVATTLPSYDEAERT
CCCCCCCCCCHHHHH
48.6126356563
76PhosphorylationVATTLPSYDEAERTK
CCCCCCCCCHHHHHH
18.8325884760
83 (in isoform 1)Ubiquitination-50.9121890473
83UbiquitinationYDEAERTKAEATIPL
CCHHHHHHCEEEECC
50.9132142685
147PhosphorylationTTSAAGRYGAISGFG
HHCHHHHCCCCCHHH
15.2520068231
151PhosphorylationAGRYGAISGFGLSLI
HHHCCCCCHHHHHHH
27.7720068231
156PhosphorylationAISGFGLSLIKWILI
CCCHHHHHHHHHHHH
28.5520068231
201UbiquitinationRGFINYAKVRKMPET
HHHHHHHHHHCCCHH
32.0122817900
204UbiquitinationINYAKVRKMPETFSN
HHHHHHHCCCHHHCC
62.8932142685
204 (in isoform 1)Ubiquitination-62.8921890473
208PhosphorylationKVRKMPETFSNLPRT
HHHCCCHHHCCCCCE
26.8829759185
210PhosphorylationRKMPETFSNLPRTRV
HCCCHHHCCCCCEEE
44.8929759185

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
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:15252135

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NFIP1_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 NFIP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NRAM2_HUMANSLC11A2physical
19706893
PTEN_HUMANPTENphysical
20534535
EGFR_HUMANEGFRphysical
20534535
PTEN_HUMANPTENphysical
22213801
NED4L_HUMANNEDD4Lphysical
22213801
MAVS_HUMANMAVSphysical
23087404
SMUF1_HUMANSMURF1physical
23087404
UB2L3_HUMANUBE2L3physical
25632008
ITCH_HUMANITCHphysical
25632008
ITCH_HUMANITCHphysical
26245901
NEDD4_HUMANNEDD4physical
27173227
SYUA_HUMANSNCAphysical
27173227

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 NFIP1_HUMAN

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Related Literatures of Post-Translational Modification

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