NPL4_HUMAN - dbPTM
NPL4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NPL4_HUMAN
UniProt AC Q8TAT6
Protein Name Nuclear protein localization protein 4 homolog
Gene Name NPLOC4
Organism Homo sapiens (Human).
Sequence Length 608
Subcellular Localization Cytoplasm, cytosol . Endoplasmic reticulum . Nucleus . Associated with the endoplasmic reticulum and nuclear.
Protein Description The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope (By similarity). Acts as a negative regulator of type I interferon production via the complex formed with VCP and UFD1, which binds to DDX58/RIG-I and recruits RNF125 to promote ubiquitination and degradation of DDX58/RIG-I. [PubMed: 26471729]
Protein Sequence MAESIIIRVQSPDGVKRITATKRETAATFLKKVAKEFGFQNNGFSVYINRNKTGEITASSNKSLNLLKIKHGDLLFLFPSSLAGPSSEMETSVPPGFKVFGAPNVVEDEIDQYLSKQDGKIYRSRDPQLCRHGPLGKCVHCVPLEPFDEDYLNHLEPPVKHMSFHAYIRKLTGGADKGKFVALENISCKIKSGCEGHLPWPNGICTKCQPSAITLNRQKYRHVDNIMFENHTVADRFLDFWRKTGNQHFGYLYGRYTEHKDIPLGIRAEVAAIYEPPQIGTQNSLELLEDPKAEVVDEIAAKLGLRKVGWIFTDLVSEDTRKGTVRYSRNKDTYFLSSEECITAGDFQNKHPNMCRLSPDGHFGSKFVTAVATGGPDNQVHFEGYQVSNQCMALVRDECLLPCKDAPELGYAKESSSEQYVPDVFYKDVDKFGNEITQLARPLPVEYLIIDITTTFPKDPVYTFSISQNPFPIENRDVLGETQDFHSLATYLSQNTSSVFLDTISDFHLLLFLVTNEVMPLQDSISLLLEAVRTRNEELAQTWKRSEQWATIEQLCSTVGGQLPGLHEYGAVGGSTHTATAAMWACQHCTFMNQPGTGHCEMCSLPRT
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------MAESIIIRV
------CCCEEEEEE		21.1719413330
4Phosphorylation----MAESIIIRVQS
----CCCEEEEEEEC		15.0027251275
11PhosphorylationSIIIRVQSPDGVKRI
EEEEEEECCCCCEEE		23.3122199227
16UbiquitinationVQSPDGVKRITATKR
EECCCCCEEEEECCH		43.54-
21PhosphorylationGVKRITATKRETAAT
CCEEEEECCHHHHHH		23.22-
28PhosphorylationTKRETAATFLKKVAK
CCHHHHHHHHHHHHH		27.3428060719
31 (in isoform 2)Malonylation-40.8026320211
31 (in isoform 2)Ubiquitination-40.80-
31AcetylationETAATFLKKVAKEFG
HHHHHHHHHHHHHHC		40.8025953088
31MalonylationETAATFLKKVAKEFG
HHHHHHHHHHHHHHC		40.8026320211
31UbiquitinationETAATFLKKVAKEFG
HHHHHHHHHHHHHHC		40.80-
35 (in isoform 2)Ubiquitination-57.47-
35UbiquitinationTFLKKVAKEFGFQNN
HHHHHHHHHHCCCCC		57.47-
52 (in isoform 2)Ubiquitination-55.45-
52UbiquitinationSVYINRNKTGEITAS
EEEEECCCCCCEEEC		55.45-
53PhosphorylationVYINRNKTGEITASS
EEEECCCCCCEEECC		43.5328102081
57PhosphorylationRNKTGEITASSNKSL
CCCCCCEEECCCCCE		19.0429396449
59PhosphorylationKTGEITASSNKSLNL
CCCCEEECCCCCEEE		26.2925159151
60PhosphorylationTGEITASSNKSLNLL
CCCEEECCCCCEEEE		45.9021815630
62UbiquitinationEITASSNKSLNLLKI
CEEECCCCCEEEEEE		59.26-
62 (in isoform 2)Malonylation-59.2626320211
62 (in isoform 2)Ubiquitination-59.2621890473
62MalonylationEITASSNKSLNLLKI
CEEECCCCCEEEEEE		59.2626320211
62 (in isoform 1)Ubiquitination-59.2621890473
63PhosphorylationITASSNKSLNLLKIK
EEECCCCCEEEEEEE		27.0922617229
68UbiquitinationNKSLNLLKIKHGDLL
CCCEEEEEEECCCEE		53.53-
68MalonylationNKSLNLLKIKHGDLL
CCCEEEEEEECCCEE		53.5326320211
68 (in isoform 2)Malonylation-53.5326320211
68 (in isoform 1)Ubiquitination-53.5321890473
68 (in isoform 2)Ubiquitination-53.5321890473
80PhosphorylationDLLFLFPSSLAGPSS
CEEEEEEHHHCCCCH		30.5628348404
81PhosphorylationLLFLFPSSLAGPSSE
EEEEEEHHHCCCCHH		23.6028348404
86PhosphorylationPSSLAGPSSEMETSV
EHHHCCCCHHCCCCC		37.7028348404
87PhosphorylationSSLAGPSSEMETSVP
HHHCCCCHHCCCCCC		44.0628348404
91PhosphorylationGPSSEMETSVPPGFK
CCCHHCCCCCCCCCE		33.4428348404
92PhosphorylationPSSEMETSVPPGFKV
CCHHCCCCCCCCCEE		21.2228348404
113PhosphorylationVEDEIDQYLSKQDGK
CHHHHHHHHHHCCCC		14.8120562096
116 (in isoform 1)Ubiquitination-50.2221890473
116UbiquitinationEIDQYLSKQDGKIYR
HHHHHHHHCCCCEEE		50.22-
116 (in isoform 2)Ubiquitination-50.2221890473
120UbiquitinationYLSKQDGKIYRSRDP
HHHHCCCCEEECCCH		44.87-
137UbiquitinationCRHGPLGKCVHCVPL
HCCCCCCCCEEEEEC		40.54-
137 (in isoform 2)Ubiquitination-40.54-
151PhosphorylationLEPFDEDYLNHLEPP
CCCCCHHHHHCCCCC		13.8320562096
163PhosphorylationEPPVKHMSFHAYIRK
CCCCCCEEHHHHHHH		17.3828857561
172PhosphorylationHAYIRKLTGGADKGK
HHHHHHHHCCCCCCC		36.28-
177UbiquitinationKLTGGADKGKFVALE
HHHCCCCCCCEEEEE		64.56-
179AcetylationTGGADKGKFVALENI
HCCCCCCCEEEEECE		42.2625953088
187PhosphorylationFVALENISCKIKSGC
EEEEECEEEEEECCC		22.4228857561
188S-nitrosylationVALENISCKIKSGCE
EEEECEEEEEECCCC		4.7122178444
188S-nitrosocysteineVALENISCKIKSGCE
EEEECEEEEEECCCC		4.71-
189 (in isoform 2)Ubiquitination-46.51-
189UbiquitinationALENISCKIKSGCEG
EEECEEEEEECCCCC		46.51-
191 (in isoform 2)Ubiquitination-26.70-
191UbiquitinationENISCKIKSGCEGHL
ECEEEEEECCCCCCC		26.70-
207UbiquitinationWPNGICTKCQPSAIT
CCCCCCCCCCCCEEE		26.85-
207 (in isoform 2)Ubiquitination-26.85-
243UbiquitinationRFLDFWRKTGNQHFG
HHHHHHHHHCCCCCE		51.91-
243 (in isoform 2)Ubiquitination-51.9121890473
243 (in isoform 1)Ubiquitination-51.9121890473
251PhosphorylationTGNQHFGYLYGRYTE
HCCCCCEEEECCCCC		8.87-
260 (in isoform 2)Ubiquitination-51.6321890473
260 (in isoform 1)Ubiquitination-51.6321890473
260UbiquitinationYGRYTEHKDIPLGIR
ECCCCCCCCCCCCEE		51.63-
274PhosphorylationRAEVAAIYEPPQIGT
EEEEEEEECCCCCCC		20.04-
292UbiquitinationLELLEDPKAEVVDEI
HHHHHCCCHHHHHHH		70.29-
302 (in isoform 1)Ubiquitination-33.7821890473
302UbiquitinationVVDEIAAKLGLRKVG
HHHHHHHHHCCCHHH		33.78-
302 (in isoform 2)Ubiquitination-33.7821890473
307UbiquitinationAAKLGLRKVGWIFTD
HHHHCCCHHHEEEEE		50.58-
307 (in isoform 1)Ubiquitination-50.5821890473
307 (in isoform 2)Ubiquitination-50.5821890473
331UbiquitinationTVRYSRNKDTYFLSS
EEEEECCCCEEEECH		50.79-
350UbiquitinationTAGDFQNKHPNMCRL
CCCHHCCCCCCCEEE		50.05-
358PhosphorylationHPNMCRLSPDGHFGS
CCCCEEECCCCCCCC		11.1220873877
404 (in isoform 2)Ubiquitination-55.79-
404UbiquitinationDECLLPCKDAPELGY
CCCEEECCCCCCCCC		55.79-
413 (in isoform 2)Ubiquitination-50.0421890473
413 (in isoform 1)Ubiquitination-50.0421890473
413UbiquitinationAPELGYAKESSSEQY
CCCCCCCCCCCCCCC		50.04-
415PhosphorylationELGYAKESSSEQYVP
CCCCCCCCCCCCCCC		38.1630622161
416PhosphorylationLGYAKESSSEQYVPD
CCCCCCCCCCCCCCC		38.7030622161
417PhosphorylationGYAKESSSEQYVPDV
CCCCCCCCCCCCCCC		37.6930622161
427 (in isoform 2)Ubiquitination-39.5521890473
427 (in isoform 1)Ubiquitination-39.5521890473
427UbiquitinationYVPDVFYKDVDKFGN
CCCCCHHCCHHHHHH		39.55-
431UbiquitinationVFYKDVDKFGNEITQ
CHHCCHHHHHHHHHH		55.83-
431 (in isoform 1)Ubiquitination-55.8321890473
431 (in isoform 2)Ubiquitination-55.8321890473
544 (in isoform 2)Ubiquitination-49.8121890473
544UbiquitinationEELAQTWKRSEQWAT
HHHHHHHHHHHHHHH		49.81-
544 (in isoform 1)Ubiquitination-49.8121890473
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 NPL4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NPL4_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 NPL4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UFD1_HUMANUFD1Lphysical
18586029
TERA_HUMANVCPphysical
18586029
TERA_HUMANVCPphysical
18775313
UBC_HUMANUBCphysical
12644454
UFD1_HUMANUFD1Lphysical
22939629
RM19_HUMANMRPL19physical
22939629
RT09_HUMANMRPS9physical
22939629
IKBA_HUMANNFKBIAphysical
24248593
PUR8_HUMANADSLphysical
22863883
CBS_HUMANCBSphysical
22863883
NC2B_HUMANDR1physical
22863883
IF4A3_HUMANEIF4A3physical
22863883
DAAF5_HUMANDNAAF5physical
22863883
TRMB_HUMANMETTL1physical
22863883
PDE12_HUMANPDE12physical
22863883
PLIN3_HUMANPLIN3physical
22863883
RD23B_HUMANRAD23Bphysical
22863883
SAE1_HUMANSAE1physical
22863883
SRP14_HUMANSRP14physical
22863883
LA_HUMANSSBphysical
22863883
SAE2_HUMANUBA2physical
22863883
UBE3A_HUMANUBE3Aphysical
22863883
UBQL2_HUMANUBQLN2physical
22863883
WDR4_HUMANWDR4physical
22863883
CD2AP_HUMANCD2APphysical
26344197
NDUS3_HUMANNDUFS3physical
26344197
PICAL_HUMANPICALMphysical
26344197
NSF1C_HUMANNSFL1Cphysical
26389662
ASPC1_HUMANASPSCR1physical
26389662
TERA_HUMANVCPphysical
26389662
UFD1_HUMANUFD1Lphysical
26389662
FAF2_HUMANFAF2physical
26389662
ADK_HUMANADKphysical
26389662
FAF1_HUMANFAF1physical
26389662
UBAC2_HUMANUBAC2physical
26389662
VCIP1_HUMANVCPIP1physical
26389662
P5CR2_HUMANPYCR2physical
26389662
CIP4_HUMANTRIP10physical
26389662
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 NPL4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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