NECT3_HUMAN - dbPTM
NECT3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NECT3_HUMAN
UniProt AC Q9NQS3
Protein Name Nectin-3
Gene Name NECTIN3 {ECO:0000312|HGNC:HGNC:17664}
Organism Homo sapiens (Human).
Sequence Length 549
Subcellular Localization Cell membrane
Single-pass membrane protein . Cell junction, synapse, postsynaptic cell membrane.
Protein Description Plays a role in cell-cell adhesion through heterophilic trans-interactions with nectin-like proteins or nectins, such as trans-interaction with NECTIN2 at Sertoli-spermatid junctions. Trans-interaction with PVR induces activation of CDC42 and RAC small G proteins through common signaling molecules such as SRC and RAP1. Also involved in the formation of cell-cell junctions, including adherens junctions and synapses. Induces endocytosis-mediated down-regulation of PVR from the cell surface, resulting in reduction of cell movement and proliferation. Plays a role in the morphology of the ciliary body..
Protein Sequence MARTLRPSPLCPGGGKAQLSSASLLGAGLLLQPPTPPPLLLLLFPLLLFSRLCGALAGPIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGFSVQGEYQGRVLFKNYSLNDATITLHNIGFSDSGKYICKAVTFPLGNAQSSTTVTVLVEPTVSLIKGPDSLIDGGNETVAAICIAATGKPVAHIDWEGDLGEMESTTTSFPNETATIISQYKLFPTRFARGRRITCVVKHPALEKDIRYSFILDIQYAPEVSVTGYDGNWFVGRKGVNLKCNADANPPPFKSVWSRLDGQWPDGLLASDNTLHFVHPLTFNYSGVYICKVTNSLGQRSDQKVIYISDPPTTTTLQPTIQWHPSTADIEDLATEPKKLPFPLSTLATIKDDTIATIIASVVGGALFIVLVSVLAGIFCYRRRRTFRGDYFAKNYIPPSDMQKESQIDVLQQDELDSYPDSVKKENKNPVNNLIRKDYLEEPEKTQWNNVENLNRFERPMDYYEDLKMGMKFVSDEHYDENEDDLVSHVDGSVISRREWYV
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
43UbiquitinationPPPLLLLLFPLLLFS
CCCHHHHHHHHHHHH
27667366
73N-linked_GlycosylationVTAVWGKNVSLKCLI
EEEEECCCCEEEEEE
22902367
83N-linked_GlycosylationLKCLIEVNETITQIS
EEEEEEECCCCEEEE
UniProtKB CARBOHYD
125N-linked_GlycosylationQGRVLFKNYSLNDAT
ECEEEEEEEECCCCE
22902367
139UbiquitinationTITLHNIGFSDSGKY
EEEEEECCCCCCCCE
27667366
173PhosphorylationVLVEPTVSLIKGPDS
EEECCCEEEEECCCC
24719451
186N-linked_GlycosylationDSLIDGGNETVAAIC
CCCCCCCCHHEEEEE
22902367
222N-linked_GlycosylationSTTTSFPNETATIIS
EECCCCCCCHHEEEE
22902367
232UbiquitinationATIISQYKLFPTRFA
HEEEEEEEECCCHHC
27667366
239UbiquitinationKLFPTRFARGRRITC
EECCCHHCCCCEEEE
22817900
240UbiquitinationLFPTRFARGRRITCV
ECCCHHCCCCEEEEE
27667366
255UbiquitinationVKHPALEKDIRYSFI
EECHHHCCCCEEEEE
27667366
259UbiquitinationALEKDIRYSFILDIQ
HHCCCCEEEEEEEEE
22817900
260UbiquitinationLEKDIRYSFILDIQY
HCCCCEEEEEEEEEE
22817900
263UbiquitinationDIRYSFILDIQYAPE
CCEEEEEEEEEECCE
22817900
280UbiquitinationVTGYDGNWFVGRKGV
EECCCCCEEECCCCE
22817900
286UbiquitinationNWFVGRKGVNLKCNA
CEEECCCCEECCCCC
27667366
303UbiquitinationNPPPFKSVWSRLDGQ
CCCCCCHHHHHCCCC
22817900
307UbiquitinationFKSVWSRLDGQWPDG
CCHHHHHCCCCCCCC
22817900
328UbiquitinationTLHFVHPLTFNYSGV
CEEEECEEEECCCEE
27667366
331N-linked_GlycosylationFVHPLTFNYSGVYIC
EECEEEECCCEEEEE
22902367
336UbiquitinationTFNYSGVYICKVTNS
EECCCEEEEEEEECC
27667366
351UbiquitinationLGQRSDQKVIYISDP
CCCCCCCEEEEECCC
27667366
354PhosphorylationRSDQKVIYISDPPTT
CCCCEEEEECCCCCC
28348404
356PhosphorylationDQKVIYISDPPTTTT
CCEEEEECCCCCCCC
28348404
360PhosphorylationIYISDPPTTTTLQPT
EEECCCCCCCCCCCE
28348404
361PhosphorylationYISDPPTTTTLQPTI
EECCCCCCCCCCCEE
28348404
362PhosphorylationISDPPTTTTLQPTIQ
ECCCCCCCCCCCEEE
28348404
363PhosphorylationSDPPTTTTLQPTIQW
CCCCCCCCCCCEEEC
28348404
367O-linked_GlycosylationTTTTLQPTIQWHPST
CCCCCCCEEECCCCC
OGP
367PhosphorylationTTTTLQPTIQWHPST
CCCCCCCEEECCCCC
28348404
373PhosphorylationPTIQWHPSTADIEDL
CEEECCCCCCCHHHH
28348404
373O-linked_GlycosylationPTIQWHPSTADIEDL
CEEECCCCCCCHHHH
OGP
374PhosphorylationTIQWHPSTADIEDLA
EEECCCCCCCHHHHC
28348404
374O-linked_GlycosylationTIQWHPSTADIEDLA
EEECCCCCCCHHHHC
OGP
382UbiquitinationADIEDLATEPKKLPF
CCHHHHCCCCCCCCC
27667366
386 (in isoform 3)Phosphorylation-29514088
388UbiquitinationATEPKKLPFPLSTLA
CCCCCCCCCCHHHHE
33845483
403UbiquitinationTIKDDTIATIIASVV
ECCCCHHHHHHHHHH
29967540
418UbiquitinationGGALFIVLVSVLAGI
HHHHHHHHHHHHHHH
29967540
428UbiquitinationVLAGIFCYRRRRTFR
HHHHHHHHHHCCCCC
22817900
436UbiquitinationRRRRTFRGDYFAKNY
HHCCCCCCCHHHHCC
22817900
438PhosphorylationRRTFRGDYFAKNYIP
CCCCCCCHHHHCCCC
19901323
448UbiquitinationKNYIPPSDMQKESQI
HCCCCHHHCCCHHHC
22817900
449UbiquitinationNYIPPSDMQKESQID
CCCCHHHCCCHHHCC
22817900
451UbiquitinationIPPSDMQKESQIDVL
CCHHHCCCHHHCCCH
21906983
451 (in isoform 1)Ubiquitination-21906983
452UbiquitinationPPSDMQKESQIDVLQ
CHHHCCCHHHCCCHH
22817900
453PhosphorylationPSDMQKESQIDVLQQ
HHHCCCHHHCCCHHH
23403867
456UbiquitinationMQKESQIDVLQQDEL
CCCHHHCCCHHHHHH
22817900
457UbiquitinationQKESQIDVLQQDELD
CCHHHCCCHHHHHHH
22817900
460UbiquitinationSQIDVLQQDELDSYP
HHCCCHHHHHHHHCC
22817900
465PhosphorylationLQQDELDSYPDSVKK
HHHHHHHHCCHHHCC
30266825
466PhosphorylationQQDELDSYPDSVKKE
HHHHHHHCCHHHCCC
30266825
469UbiquitinationELDSYPDSVKKENKN
HHHHCCHHHCCCCCC
22817900
469PhosphorylationELDSYPDSVKKENKN
HHHHCCHHHCCCCCC
30266825
471 (in isoform 1)Ubiquitination-21906983
471UbiquitinationDSYPDSVKKENKNPV
HHCCHHHCCCCCCCC
21906983
472UbiquitinationSYPDSVKKENKNPVN
HCCHHHCCCCCCCCH
22817900
475UbiquitinationDSVKKENKNPVNNLI
HHHCCCCCCCCHHCC
22817900
477UbiquitinationVKKENKNPVNNLIRK
HCCCCCCCCHHCCCH
22817900
482UbiquitinationKNPVNNLIRKDYLEE
CCCCHHCCCHHHCCC
22817900
486PhosphorylationNNLIRKDYLEEPEKT
HHCCCHHHCCCCCHH
28152594
492 (in isoform 1)Ubiquitination-21906983
492UbiquitinationDYLEEPEKTQWNNVE
HHCCCCCHHCCCCHH
21906983
496UbiquitinationEPEKTQWNNVENLNR
CCCHHCCCCHHHCCC
22817900
500UbiquitinationTQWNNVENLNRFERP
HCCCCHHHCCCCCCC
22817900
502UbiquitinationWNNVENLNRFERPMD
CCCHHHCCCCCCCCH
22817900
503UbiquitinationNNVENLNRFERPMDY
CCHHHCCCCCCCCHH
22817900
504UbiquitinationNVENLNRFERPMDYY
CHHHCCCCCCCCHHH
22817900
506UbiquitinationENLNRFERPMDYYED
HHCCCCCCCCHHHHH
22817900
510PhosphorylationRFERPMDYYEDLKMG
CCCCCCHHHHHHHHH
25884760
511PhosphorylationFERPMDYYEDLKMGM
CCCCCHHHHHHHHHC
20007894
515 (in isoform 1)Ubiquitination-21906983
515UbiquitinationMDYYEDLKMGMKFVS
CHHHHHHHHHCEECC
22817900
519UbiquitinationEDLKMGMKFVSDEHY
HHHHHHCEECCHHHC
22817900
522PhosphorylationKMGMKFVSDEHYDEN
HHHCEECCHHHCCCC
27642862
523UbiquitinationMGMKFVSDEHYDENE
HHCEECCHHHCCCCC
22817900
526PhosphorylationKFVSDEHYDENEDDL
EECCHHHCCCCCCCC
25884760
535PhosphorylationENEDDLVSHVDGSVI
CCCCCCHHCCCCCEE
27422710
540PhosphorylationLVSHVDGSVISRREW
CHHCCCCCEEECEEC
27642862
543PhosphorylationHVDGSVISRREWYV-
CCCCCEEECEECCC-
27642862
546UbiquitinationGSVISRREWYV----
CCEEECEECCC----
22817900
550UbiquitinationSRREWYV--------
ECEECCC--------
22817900

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 NECT3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NECT3_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 NECT3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PARD3_HUMANPARD3physical
12515806
NECT3_HUMANPVRL3physical
10744716
AFAD_HUMANMLLT4physical
11024295
NECT1_HUMANPVRL1physical
21982860
NECT2_HUMANPVRL2physical
21982860
TIGIT_HUMANTIGITphysical
21982860
KRA42_HUMANKRTAP4-2physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
NECT1_HUMANPVRL1physical
26186194
NPTX1_HUMANNPTX1physical
26186194
SDF2_HUMANSDF2physical
26186194
ASPH_HUMANASPHphysical
26186194
FBX2_HUMANFBXO2physical
26186194
COEA1_HUMANCOL14A1physical
26186194
MAK_HUMANMAKphysical
26186194
NECT2_HUMANPVRL2physical
26186194
ERO1B_HUMANERO1LBphysical
26186194
INP5K_HUMANINPP5Kphysical
26186194
NECT1_HUMANPVRL1physical
28514442
NPTX1_HUMANNPTX1physical
28514442
MAK_HUMANMAKphysical
28514442
NECT2_HUMANPVRL2physical
28514442
ASPH_HUMANASPHphysical
28514442
FBX2_HUMANFBXO2physical
28514442
ERO1B_HUMANERO1LBphysical
28514442
COEA1_HUMANCOL14A1physical
28514442
INP5K_HUMANINPP5Kphysical
28514442
SDF2L_HUMANSDF2L1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NECT3_HUMAN

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Related Literatures of Post-Translational Modification

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