UFD1_HUMAN - dbPTM
UFD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UFD1_HUMAN
UniProt AC Q92890
Protein Name Ubiquitin recognition factor in ER-associated degradation protein 1 {ECO:0000312|HGNC:HGNC:12520}
Gene Name UFD1 {ECO:0000312|HGNC:HGNC:12520}
Organism Homo sapiens (Human).
Sequence Length 307
Subcellular Localization Nucleus . Cytoplasm, cytosol .
Protein Description Essential component of the ubiquitin-dependent proteolytic pathway which degrades ubiquitin fusion proteins. 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. It may be involved in the development of some ectoderm-derived structures (By similarity). Acts as a negative regulator of type I interferon production via the complex formed with VCP and NPLOC4, which binds to DDX58/RIG-I and recruits RNF125 to promote ubiquitination and degradation of DDX58/RIG-I. [PubMed: 26471729]
Protein Sequence MFSFNMFDHPIPRVFQNRFSTQYRCFSVSMLAGPNDRSDVEKGGKIIMPPSALDQLSRLNITYPMLFKLTNKNSDRMTHCGVLEFVADEGICYLPHWMMQNLLLEEGGLVQVESVNLQVATYSKFQPQSPDFLDITNPKAVLENALRNFACLTTGDVIAINYNEKIYELRVMETKPDKAVSIIECDMNVDFDAPLGYKEPERQVQHEESTEGEADHSGYAGELGFRAFSGSGNRLDGKKKGVEPSPSPIKPGDIKRGIPNYEFKLGKITFIRNSRPLVKKVEEDEAGGRFVAFSGEGQSLRKKGRKP
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
1Acetylation-------MFSFNMFD
-------CCCCCCCC		5.9919413330
3Phosphorylation-----MFSFNMFDHP
-----CCCCCCCCCC		17.8920068231
20PhosphorylationRVFQNRFSTQYRCFS
HHHCCCCCCCEEEEE		16.0322210691
21PhosphorylationVFQNRFSTQYRCFSV
HHCCCCCCCEEEEEE		27.2322210691
27PhosphorylationSTQYRCFSVSMLAGP
CCCEEEEEEEHCCCC		19.5322210691
29PhosphorylationQYRCFSVSMLAGPND
CEEEEEEEHCCCCCC		13.59-
45UbiquitinationSDVEKGGKIIMPPSA
HHHHCCCEEECCHHH		37.4121906983
45 (in isoform 2)Ubiquitination-37.4121890473
45 (in isoform 1)Ubiquitination-37.4121890473
68UbiquitinationITYPMLFKLTNKNSD
CHHHHHEECCCCCCC		50.90-
68 (in isoform 1)Ubiquitination-50.90-
72 (in isoform 1)Ubiquitination-53.2221890473
72 (in isoform 2)Ubiquitination-53.2221890473
72UbiquitinationMLFKLTNKNSDRMTH
HHEECCCCCCCCCCE		53.2221906983
78PhosphorylationNKNSDRMTHCGVLEF
CCCCCCCCEEEEEEH		18.21-
124UbiquitinationLQVATYSKFQPQSPD
EEEEEEECCCCCCCC		37.29-
129PhosphorylationYSKFQPQSPDFLDIT
EECCCCCCCCCCCCC		32.8729255136
136PhosphorylationSPDFLDITNPKAVLE
CCCCCCCCCHHHHHH		45.1725159151
139UbiquitinationFLDITNPKAVLENAL
CCCCCCHHHHHHHHH		53.8721906983
139 (in isoform 2)Ubiquitination-53.8721890473
165UbiquitinationIAINYNEKIYELRVM
EEEECCCEEEEEEEE		47.12-
167PhosphorylationINYNEKIYELRVMET
EECCCEEEEEEEEEC		21.7018083107
170MethylationNEKIYELRVMETKPD
CCEEEEEEEEECCCC		17.50115919489
175 (in isoform 2)Ubiquitination-37.6021890473
175 (in isoform 1)Ubiquitination-37.6021890473
175UbiquitinationELRVMETKPDKAVSI
EEEEEECCCCCCEEE		37.6021906983
178 (in isoform 2)Ubiquitination-60.2521890473
178UbiquitinationVMETKPDKAVSIIEC
EEECCCCCCEEEEEE		60.2521906983
198UbiquitinationFDAPLGYKEPERQVQ
CCCCCCCCCCCHHCC		66.06-
209PhosphorylationRQVQHEESTEGEADH
HHCCCCCCCCCCCCC		28.8625159151
210PhosphorylationQVQHEESTEGEADHS
HCCCCCCCCCCCCCC		51.8225159151
210 (in isoform 3)Phosphorylation-51.82-
211 (in isoform 1)Ubiquitination-65.4021890473
217PhosphorylationTEGEADHSGYAGELG
CCCCCCCCCCCCCCE		33.7625159151
219PhosphorylationGEADHSGYAGELGFR
CCCCCCCCCCCCEEE		17.9128796482
229PhosphorylationELGFRAFSGSGNRLD
CCEEEEECCCCCCCC		30.9425159151
231 (in isoform 3)Phosphorylation-31.53-
231PhosphorylationGFRAFSGSGNRLDGK
EEEEECCCCCCCCCC		31.5325159151
233 (in isoform 1)Phosphorylation-42.9327642862
238AcetylationSGNRLDGKKKGVEPS
CCCCCCCCCCCCCCC		51.4812435517
245 (in isoform 1)Phosphorylation-25.2227642862
245 (in isoform 3)Phosphorylation-25.22-
245PhosphorylationKKKGVEPSPSPIKPG
CCCCCCCCCCCCCCC		25.2229255136
247 (in isoform 3)Phosphorylation-43.53-
247PhosphorylationKGVEPSPSPIKPGDI
CCCCCCCCCCCCCCC		43.5329255136
250UbiquitinationEPSPSPIKPGDIKRG
CCCCCCCCCCCCCCC		46.46-
250AcetylationEPSPSPIKPGDIKRG
CCCCCCCCCCCCCCC		46.4666727623
255 (in isoform 1)Phosphorylation-49.6827642862
2552-HydroxyisobutyrylationPIKPGDIKRGIPNYE
CCCCCCCCCCCCCCE		49.68-
255UbiquitinationPIKPGDIKRGIPNYE
CCCCCCCCCCCCCCE		49.68-
261PhosphorylationIKRGIPNYEFKLGKI
CCCCCCCCEEEECCE		19.8625159151
264 (in isoform 2)Ubiquitination-44.3721890473
264UbiquitinationGIPNYEFKLGKITFI
CCCCCEEEECCEEEE		44.3721906983
267 (in isoform 2)Ubiquitination-49.3521890473
267UbiquitinationNYEFKLGKITFIRNS
CCEEEECCEEEEECC		49.3521890473
279 (in isoform 2)Ubiquitination-59.8021890473
279UbiquitinationRNSRPLVKKVEEDEA
ECCCCCEEEEEECCC		59.8021906983
281PhosphorylationSRPLVKKVEEDEAGG
CCCCEEEEEECCCCC		8.9118669648
283PhosphorylationPLVKKVEEDEAGGRF
CCEEEEEECCCCCEE		65.2318669648
283 (in isoform 1)Phosphorylation-65.2321406692
294PhosphorylationGGRFVAFSGEGQSLR
CCEEEEECCCCCHHH		26.6325159151
299PhosphorylationAFSGEGQSLRKKGRK
EECCCCCHHHHCCCC		40.7819664994
300 (in isoform 1)Ubiquitination-7.7621890473
303 (in isoform 1)Ubiquitination-58.4721890473
303UbiquitinationEGQSLRKKGRKP---
CCCHHHHCCCCC---		58.47-
315 (in isoform 1)Ubiquitination-21890473
330 (in isoform 1)Phosphorylation-21406692
335Phosphorylation-----------------------------------
-----------------------------------		18669648
335 (in isoform 1)Phosphorylation-21406692
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 UFD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UFD1_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 UFD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NPL4_HUMANNPLOC4physical
11574150
AMFR_HUMANAMFRphysical
17681147
BIRC5_HUMANBIRC5physical
16322459
NPL4_HUMANNPLOC4physical
16322459
UBP13_HUMANUSP13physical
21571647
PSMD2_HUMANPSMD2physical
21571647
SKP2_HUMANSKP2physical
21571647
A2MG_HUMANA2Mphysical
21900206
TAF1C_HUMANTAF1Cphysical
21900206
F13A_HUMANF13A1physical
21900206
P53_HUMANTP53physical
21900206
PPHLN_HUMANPPHLN1physical
21900206
ANC2_HUMANANAPC2physical
21900206
TNR16_HUMANNGFRphysical
21900206
MASP1_HUMANMASP1physical
21900206
TIAM2_HUMANTIAM2physical
21900206
SNX1_HUMANSNX1physical
21900206
TERA_HUMANVCPphysical
19275885
UBXN6_HUMANUBXN6physical
19275885
TERA_HUMANVCPphysical
15371428
NPL4_HUMANNPLOC4physical
15371428
VP33B_HUMANVPS33Bphysical
22939629
UN45A_HUMANUNC45Aphysical
22939629
NUB1_HUMANNUB1physical
24019527
TERA_MOUSEVcpphysical
24089527
IKBA_HUMANNFKBIAphysical
24248593
NPL4_HUMANNPLOC4physical
24248593
TERA_HUMANVCPphysical
24248593
UBC_HUMANUBCphysical
16004872
NPL4_HUMANNPLOC4physical
17202270
CHM2A_HUMANCHMP2Aphysical
26040713
ARMC1_HUMANARMC1physical
26344197
ARP5L_HUMANARPC5Lphysical
26344197
ASNS_HUMANASNSphysical
26344197
CAP1_HUMANCAP1physical
26344197
CD2AP_HUMANCD2APphysical
26344197
DHX15_HUMANDHX15physical
26344197
DPH5_HUMANDPH5physical
26344197
FUS_HUMANFUSphysical
26344197
GARS_HUMANGARSphysical
26344197
MTMRC_HUMANMTMR12physical
26344197
NPL4_HUMANNPLOC4physical
26344197
NSF1C_HUMANNSFL1Cphysical
26344197
PAPOA_HUMANPAPOLAphysical
26344197
RTCB_HUMANRTCBphysical
26344197
SH3K1_HUMANSH3KBP1physical
26344197
STIP1_HUMANSTIP1physical
26344197
SUMO3_HUMANSUMO3physical
26344197
TTC27_HUMANTTC27physical
26344197
TERA_HUMANVCPphysical
26712280
TERA_HUMANVCPphysical
26389662
NPL4_HUMANNPLOC4physical
26389662
NUBPL_HUMANNUBPLphysical
26389662
FAF2_HUMANFAF2physical
26389662
UBAC2_HUMANUBAC2physical
26389662
FAF1_HUMANFAF1physical
26389662
HMGB1_HUMANHMGB1physical
26389662
NSF1C_HUMANNSFL1Cphysical
26389662
PLST_HUMANPLS3physical
26389662
RADI_HUMANRDXphysical
26389662
VCIP1_HUMANVCPIP1physical
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 UFD1_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 MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-247 ANDSER-299, AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASSSPECTROMETRY.

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