UBN1_HUMAN - dbPTM
UBN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBN1_HUMAN
UniProt AC Q9NPG3
Protein Name Ubinuclein-1
Gene Name UBN1
Organism Homo sapiens (Human).
Sequence Length 1134
Subcellular Localization Nucleus, nucleoplasm. Nucleus, PML body. Cell junction, tight junction. Localized as a nuclear speckled-like pattern in proliferating primary fibroblasts. Colocalizes with HIRA, PML and SP100 in PML bodies of senescent cells. Colocalizes with TJP1 an
Protein Description Acts as a novel regulator of senescence. Involved in the formation of senescence-associated heterochromatin foci (SAHF), which represses expression of proliferation-promoting genes. Binds to proliferation-promoting genes. May be required for replication-independent chromatin assembly..
Protein Sequence MSEPHRVQFTSLPGSLNPAFLKKSRKEEAGAGEQHQDCEPAAAAVRITLTLFEPDHKRCPEFFYPELVKNIRGKVKGLQPGDKKKDLSDPFNDEEKERHKVEALARKFEEKYGGKKRRKDRIQDLIDMGYGYDESDSFIDNSEAYDELVPASLTTKYGGFYINSGTLQFRQASESEDDFIKEKKKKSPKKRKLKEGGEKIKKKKKDDTYDKEKKSKKSKFSKAGFTALNASKEKKKKKYSGALSVKEMLKKFQKEKEAQKKREEEHKPVAVPSAEAQGLRELEGASDPLLSLFGSTSDNDLLQAATAMDSLTDLDLEHLLSESPEGSPFRDMDDGSDSLGVGLDQEFRQPSSLPEGLPAPLEKRVKELAQAARAAEGESRQKFFTQDINGILLDIEAQTRELSSQVRSGVYAYLASFLPCSKDALLKRARKLHLYEQGGRLKEPLQKLKEAIGRAMPEQMAKYQDECQAHTQAKVAKMLEEEKDKEQRDRICSDEEEDEEKGGRRIMGPRKKFQWNDEIRELLCQVVKIKLESQDLERNNKAQAWEDCVKGFLDAEVKPLWPKGWMQARTLFKESRRGHGHLTSILAKKKVMAPSKIKVKESSTKPDKKVSVPSGQIGGPIALPSDHQTGGLSIGASSRELPSQASGGLANPPPVNLEDSLDEDLIRNPASSVEAVSKELAALNSRAAGNSEFTLPAPSKAPAEKVGGVLCTEEKRNFAKPSPSAPPPASSLQSPLNFLAEQALALGQSSQEKKPESSGYKELSCQAPLNKGLPEVHQSKAKHHSLPRTSHGPQVAVPVPGPQVKVFHAGTQQQKNFTPPSPFANKLQGPKASPTQCHRSLLQLVKTAAKGQGFHPSAPATSGGLSASSSSSHKTPASSSSALSHPAKPHSVSSAGSSYKNNPFASSISKHGVSSGSSSSGGTPVQSSVSGSLVPGIQPPSVGQATSRPVPSSAGKKMPVSQKLTLVAPPGGPNGDSSGGTQGVAKLLTSPSLKPSAVSSVTSSTSLSKGASGTVLLAGSSLMASPYKSSSPKLSGAMSSNSLGIITPVPIPVHVLSFSADSSAKAGVSKDAIVTGPAPGSFHHGLGHSLLAGLHSSPPHAAPLPHAAVPTHIPQSLPGASQLHGKGPAVPRKL
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
10PhosphorylationEPHRVQFTSLPGSLN
CCCCEEECCCCCCCC
16.56-
11PhosphorylationPHRVQFTSLPGSLNP
CCCEEECCCCCCCCH
33.5827251275
15PhosphorylationQFTSLPGSLNPAFLK
EECCCCCCCCHHHHH
24.04-
26AcetylationAFLKKSRKEEAGAGE
HHHHHHHHHCCCCCC
67.9826051181
64PhosphorylationKRCPEFFYPELVKNI
HCCHHHHCHHHHHHH
10.9120068231
88PhosphorylationGDKKKDLSDPFNDEE
CCCCCCCCCCCCHHH
54.0627134283
107AcetylationKVEALARKFEEKYGG
HHHHHHHHHHHHHCC
52.0730593227
112PhosphorylationARKFEEKYGGKKRRK
HHHHHHHHCCCCCCH
34.10-
130PhosphorylationQDLIDMGYGYDESDS
HHHHHCCCCCCCCCC
13.08-
164PhosphorylationYGGFYINSGTLQFRQ
ECCEEECCCEEEEEE
24.4823186163
166PhosphorylationGFYINSGTLQFRQAS
CEEECCCEEEEEECC
19.7330108239
173PhosphorylationTLQFRQASESEDDFI
EEEEEECCCCCCHHH
33.0629255136
175PhosphorylationQFRQASESEDDFIKE
EEEECCCCCCHHHHH
43.7829255136
187PhosphorylationIKEKKKKSPKKRKLK
HHHHHHCCCHHHCCH
51.32-
199AcetylationKLKEGGEKIKKKKKD
CCHHHHHHHHHHCCC
64.2025953088
222AcetylationSKKSKFSKAGFTALN
CHHHHHHHHHHHHHH
56.5119608861
226PhosphorylationKFSKAGFTALNASKE
HHHHHHHHHHHCCHH
29.3527690223
231PhosphorylationGFTALNASKEKKKKK
HHHHHHCCHHHHCCC
40.0330576142
232AcetylationFTALNASKEKKKKKY
HHHHHCCHHHHCCCC
71.7526051181
239PhosphorylationKEKKKKKYSGALSVK
HHHHCCCCCCCCCHH
22.6329759185
240PhosphorylationEKKKKKYSGALSVKE
HHHCCCCCCCCCHHH
26.8625159151
244PhosphorylationKKYSGALSVKEMLKK
CCCCCCCCHHHHHHH
30.5229759185
246AcetylationYSGALSVKEMLKKFQ
CCCCCCHHHHHHHHH
33.7525953088
261AcetylationKEKEAQKKREEEHKP
HHHHHHHHHHHHCCC
53.6219608861
267AcetylationKKREEEHKPVAVPSA
HHHHHHCCCCCCCCH
44.4623749302
321PhosphorylationLDLEHLLSESPEGSP
CCHHHHHCCCCCCCC
42.2526074081
323PhosphorylationLEHLLSESPEGSPFR
HHHHHCCCCCCCCCC
25.5226074081
327PhosphorylationLSESPEGSPFRDMDD
HCCCCCCCCCCCCCC
21.1422468782
336PhosphorylationFRDMDDGSDSLGVGL
CCCCCCCCCCCCCCC
30.9029255136
338PhosphorylationDMDDGSDSLGVGLDQ
CCCCCCCCCCCCCCH
28.8129255136
351PhosphorylationDQEFRQPSSLPEGLP
CHHHCCCCCCCCCCC
35.8528674151
352PhosphorylationQEFRQPSSLPEGLPA
HHHCCCCCCCCCCCC
55.4128674151
4492-HydroxyisobutyrylationKEPLQKLKEAIGRAM
HHHHHHHHHHHHHHC
52.73-
449SuccinylationKEPLQKLKEAIGRAM
HHHHHHHHHHHHHHC
52.7323954790
474AcetylationCQAHTQAKVAKMLEE
HHHHHHHHHHHHHHH
32.6726051181
474UbiquitinationCQAHTQAKVAKMLEE
HHHHHHHHHHHHHHH
32.6729967540
477AcetylationHTQAKVAKMLEEEKD
HHHHHHHHHHHHHCC
47.187959869
493PhosphorylationEQRDRICSDEEEDEE
HHHHHCCCCHHHHHH
45.7629255136
530SumoylationLCQVVKIKLESQDLE
HHHHHHHHHHHHHHH
40.25-
530SumoylationLCQVVKIKLESQDLE
HHHHHHHHHHHHHHH
40.25-
541AcetylationQDLERNNKAQAWEDC
HHHHHHHHHHHHHHH
45.4825953088
541UbiquitinationQDLERNNKAQAWEDC
HHHHHHHHHHHHHHH
45.4829967540
573MethylationMQARTLFKESRRGHG
HHHHHHHHHHHCCCC
58.87115978995
575PhosphorylationARTLFKESRRGHGHL
HHHHHHHHHCCCCCH
28.0625278378
583PhosphorylationRRGHGHLTSILAKKK
HCCCCCHHHHHHHCC
14.1925278378
584PhosphorylationRGHGHLTSILAKKKV
CCCCCHHHHHHHCCC
23.2025278378
596AcetylationKKVMAPSKIKVKESS
CCCCCCCCCEEECCC
45.5525953088
603PhosphorylationKIKVKESSTKPDKKV
CCEEECCCCCCCCCE
41.3520068231
604PhosphorylationIKVKESSTKPDKKVS
CEEECCCCCCCCCEE
56.7420068231
633PhosphorylationDHQTGGLSIGASSRE
CCCCCCEECCCCCCC
23.4227135362
637PhosphorylationGGLSIGASSRELPSQ
CCEECCCCCCCCCCC
25.3930631047
643PhosphorylationASSRELPSQASGGLA
CCCCCCCCCCCCCCC
51.5130108239
646PhosphorylationRELPSQASGGLANPP
CCCCCCCCCCCCCCC
26.2530108239
660PhosphorylationPPVNLEDSLDEDLIR
CCCCCCCCCCHHHHH
28.4830266825
671PhosphorylationDLIRNPASSVEAVSK
HHHHCCHHHHHHHHH
35.8530243723
672PhosphorylationLIRNPASSVEAVSKE
HHHCCHHHHHHHHHH
26.5330266825
677PhosphorylationASSVEAVSKELAALN
HHHHHHHHHHHHHHH
27.7122199227
685PhosphorylationKELAALNSRAAGNSE
HHHHHHHCCCCCCCC
24.9330001349
700AcetylationFTLPAPSKAPAEKVG
CCCCCCCCCCHHHHC
58.2825953088
705AcetylationPSKAPAEKVGGVLCT
CCCCCHHHHCCEECC
48.5725953088
715AcetylationGVLCTEEKRNFAKPS
CEECCHHHCCCCCCC
46.5426051181
722PhosphorylationKRNFAKPSPSAPPPA
HCCCCCCCCCCCCCH
30.6825627689
730PhosphorylationPSAPPPASSLQSPLN
CCCCCCHHHCCCHHH
37.0428348404
731PhosphorylationSAPPPASSLQSPLNF
CCCCCHHHCCCHHHH
32.3128348404
734PhosphorylationPPASSLQSPLNFLAE
CCHHHCCCHHHHHHH
36.3325159151
754AcetylationGQSSQEKKPESSGYK
CCCCCCCCCCCCCCC
53.9525953088
761AcetylationKPESSGYKELSCQAP
CCCCCCCCEEECCCC
56.5625953088
764PhosphorylationSSGYKELSCQAPLNK
CCCCCEEECCCCCCC
12.7925159151
771AcetylationSCQAPLNKGLPEVHQ
ECCCCCCCCCCHHHH
70.3026051181
780AcetylationLPEVHQSKAKHHSLP
CCHHHHHHHHCCCCC
55.6825953088
790PhosphorylationHHSLPRTSHGPQVAV
CCCCCCCCCCCEEEE
27.9428555341
805AcetylationPVPGPQVKVFHAGTQ
ECCCCEEEEEECCCC
33.6622424773
818PhosphorylationTQQQKNFTPPSPFAN
CCCCCCCCCCCCCHH
43.6225159151
821PhosphorylationQKNFTPPSPFANKLQ
CCCCCCCCCCHHHCC
33.5825159151
826AcetylationPPSPFANKLQGPKAS
CCCCCHHHCCCCCCC
38.4625953088
833PhosphorylationKLQGPKASPTQCHRS
HCCCCCCCHHHHHHH
34.3123898821
840PhosphorylationSPTQCHRSLLQLVKT
CHHHHHHHHHHHHHH
15.1228555341
850AcetylationQLVKTAAKGQGFHPS
HHHHHHHCCCCCCCC
49.6726051181
861O-linked_GlycosylationFHPSAPATSGGLSAS
CCCCCCCCCCCCCCC
27.1830059200
862O-linked_GlycosylationHPSAPATSGGLSASS
CCCCCCCCCCCCCCC
32.7330059200
866O-linked_GlycosylationPATSGGLSASSSSSH
CCCCCCCCCCCCCCC
29.4030059200
870PhosphorylationGGLSASSSSSHKTPA
CCCCCCCCCCCCCCC
33.1128555341
871PhosphorylationGLSASSSSSHKTPAS
CCCCCCCCCCCCCCC
38.1128555341
872O-linked_GlycosylationLSASSSSSHKTPASS
CCCCCCCCCCCCCCC
30.8330059200
875O-linked_GlycosylationSSSSSHKTPASSSSA
CCCCCCCCCCCCCCH
20.7530059200
878O-linked_GlycosylationSSHKTPASSSSALSH
CCCCCCCCCCCHHCC
31.7730059200
879O-linked_GlycosylationSHKTPASSSSALSHP
CCCCCCCCCCHHCCC
30.3430059200
880O-linked_GlycosylationHKTPASSSSALSHPA
CCCCCCCCCHHCCCC
19.6930059200
881O-linked_GlycosylationKTPASSSSALSHPAK
CCCCCCCCHHCCCCC
34.8730059200
888AcetylationSALSHPAKPHSVSSA
CHHCCCCCCCCCCCC
47.9523749302
891O-linked_GlycosylationSHPAKPHSVSSAGSS
CCCCCCCCCCCCCCC
32.0230059200
891PhosphorylationSHPAKPHSVSSAGSS
CCCCCCCCCCCCCCC
32.0228555341
894O-linked_GlycosylationAKPHSVSSAGSSYKN
CCCCCCCCCCCCCCC
34.2030059200
897O-linked_GlycosylationHSVSSAGSSYKNNPF
CCCCCCCCCCCCCCC
30.1530059200
906PhosphorylationYKNNPFASSISKHGV
CCCCCCHHHHHHCCC
28.6928348404
907PhosphorylationKNNPFASSISKHGVS
CCCCCHHHHHHCCCC
27.7028348404
909PhosphorylationNPFASSISKHGVSSG
CCCHHHHHHCCCCCC
22.1328348404
941PhosphorylationVPGIQPPSVGQATSR
CCCCCCCCCCCCCCC
45.6325332170
952PhosphorylationATSRPVPSSAGKKMP
CCCCCCCCCCCCCCC
32.8127732954
953PhosphorylationTSRPVPSSAGKKMPV
CCCCCCCCCCCCCCC
34.6627732954
956AcetylationPVPSSAGKKMPVSQK
CCCCCCCCCCCCCCE
45.6925953088
957AcetylationVPSSAGKKMPVSQKL
CCCCCCCCCCCCCEE
47.7425953088
963AcetylationKKMPVSQKLTLVAPP
CCCCCCCEEEEEECC
35.6125953088
965PhosphorylationMPVSQKLTLVAPPGG
CCCCCEEEEEECCCC
26.6529514088
977PhosphorylationPGGPNGDSSGGTQGV
CCCCCCCCCCCHHHH
32.0825262027
978PhosphorylationGGPNGDSSGGTQGVA
CCCCCCCCCCHHHHH
46.0825262027
981PhosphorylationNGDSSGGTQGVAKLL
CCCCCCCHHHHHHHH
26.1925262027
989O-linked_GlycosylationQGVAKLLTSPSLKPS
HHHHHHHCCCCCCHH
49.3730059200
989PhosphorylationQGVAKLLTSPSLKPS
HHHHHHHCCCCCCHH
49.3728450419
990PhosphorylationGVAKLLTSPSLKPSA
HHHHHHCCCCCCHHH
16.6828464451
992PhosphorylationAKLLTSPSLKPSAVS
HHHHCCCCCCHHHCE
49.1128450419
994AcetylationLLTSPSLKPSAVSSV
HHCCCCCCHHHCEEC
41.0626051181
996PhosphorylationTSPSLKPSAVSSVTS
CCCCCCHHHCEECCC
39.4528450419
999O-linked_GlycosylationSLKPSAVSSVTSSTS
CCCHHHCEECCCCCC
20.8630059200
999PhosphorylationSLKPSAVSSVTSSTS
CCCHHHCEECCCCCC
20.8628450419
1003O-linked_GlycosylationSAVSSVTSSTSLSKG
HHCEECCCCCCCCCC
29.4830059200
1003PhosphorylationSAVSSVTSSTSLSKG
HHCEECCCCCCCCCC
29.4825627689
1004O-linked_GlycosylationAVSSVTSSTSLSKGA
HCEECCCCCCCCCCC
16.7930059200
1012PhosphorylationTSLSKGASGTVLLAG
CCCCCCCCCEEEEEC
43.6024400094
1014PhosphorylationLSKGASGTVLLAGSS
CCCCCCCEEEEECCC
12.8924400094
1020PhosphorylationGTVLLAGSSLMASPY
CEEEEECCCHHCCCC
18.0727080861
1021PhosphorylationTVLLAGSSLMASPYK
EEEEECCCHHCCCCC
22.6528450419
1025PhosphorylationAGSSLMASPYKSSSP
ECCCHHCCCCCCCCC
18.1325159151
1027PhosphorylationSSLMASPYKSSSPKL
CCHHCCCCCCCCCCC
22.4728450419
1029PhosphorylationLMASPYKSSSPKLSG
HHCCCCCCCCCCCCC
30.1521712546
1030PhosphorylationMASPYKSSSPKLSGA
HCCCCCCCCCCCCCC
46.6521712546
1031PhosphorylationASPYKSSSPKLSGAM
CCCCCCCCCCCCCCC
32.9021712546

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 UBN1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBN1_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 UBN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HIRA_HUMANHIRAphysical
22195966
CABIN_HUMANCABIN1physical
22195966
RPB1_HUMANPOLR2Aphysical
22195966
HIRA_HUMANHIRAphysical
22401310
CABIN_HUMANCABIN1physical
22401310
ASF1A_HUMANASF1Aphysical
22401310
ZN606_HUMANZNF606physical
22939629
WDR36_HUMANWDR36physical
22939629
ZO2_HUMANTJP2physical
22939629

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 UBN1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, 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-336; SER-660; SER-677AND SER-1025, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-175 ANDSER-493, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND MASSSPECTROMETRY.

TOP