NU160_HUMAN - dbPTM
NU160_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NU160_HUMAN
UniProt AC Q12769
Protein Name Nuclear pore complex protein Nup160
Gene Name NUP160
Organism Homo sapiens (Human).
Sequence Length 1436
Subcellular Localization Nucleus, nuclear pore complex .
Protein Description Involved in poly(A)+ RNA transport..
Protein Sequence MLHLSAAPPAPPPEVTATARPCLCSVGRRGDGGKMAAAGALERSFVELSGAERERPRHFREFTVCSIGTANAVAGAVKYSESAGGFYYVESGKLFSVTRNRFIHWKTSGDTLELMEESLDINLLNNAIRLKFQNCSVLPGGVYVSETQNRVIILMLTNQTVHRLLLPHPSRMYRSELVVDSQMQSIFTDIGKVDFTDPCNYQLIPAVPGISPNSTASTAWLSSDGEALFALPCASGGIFVLKLPPYDIPGMVSVVELKQSSVMQRLLTGWMPTAIRGDQSPSDRPLSLAVHCVEHDAFIFALCQDHKLRMWSYKEQMCLMVADMLEYVPVKKDLRLTAGTGHKLRLAYSPTMGLYLGIYMHAPKRGQFCIFQLVSTESNRYSLDHISSLFTSQETLIDFALTSTDIWALWHDAENQTVVKYINFEHNVAGQWNPVFMQPLPEEEIVIRDDQDPREMYLQSLFTPGQFTNEALCKALQIFCRGTERNLDLSWSELKKEVTLAVENELQGSVTEYEFSQEEFRNLQQEFWCKFYACCLQYQEALSHPLALHLNPHTNMVCLLKKGYLSFLIPSSLVDHLYLLPYENLLTEDETTISDDVDIARDVICLIKCLRLIEESVTVDMSVIMEMSCYNLQSPEKAAEQILEDMITIDVENVMEDICSKLQEIRNPIHAIGLLIREMDYETEVEMEKGFNPAQPLNIRMNLTQLYGSNTAGYIVCRGVHKIASTRFLICRDLLILQQLLMRLGDAVIWGTGQLFQAQQDLLHRTAPLLLSYYLIKWGSECLATDVPLDTLESNLQHLSVLELTDSGALMANRFVSSPQTIVELFFQEVARKHIISHLFSQPKAPLSQTGLNWPEMITAITSYLLQLLWPSNPGCLFLECLMGNCQYVQLQDYIQLLHPWCQVNVGSCRFMLGRCYLVTGEGQKALECFCQAASEVGKEEFLDRLIRSEDGEIVSTPRLQYYDKVLRLLDVIGLPELVIQLATSAITEAGDDWKSQATLRTCIFKHHLDLGHNSQAYEALTQIPDSSRQLDCLRQLVVVLCERSQLQDLVEFPYVNLHNEVVGIIESRARAVDLMTHNYYELLYAFHIYRHNYRKAGTVMFEYGMRLGREVRTLRGLEKQGNCYLAALNCLRLIRPEYAWIVQPVSGAVYDRPGASPKRNHDGECTAAPTNRQIEILELEDLEKECSLARIRLTLAQHDPSAVAVAGSSSAEEMVTLLVQAGLFDTAISLCQTFKLPLTPVFEGLAFKCIKLQFGGEAAQAEAWAWLAANQLSSVITTKESSATDEAWRLLSTYLERYKVQNNLYHHCVINKLLSHGVPLPNWLINSYKKVDAAELLRLYLNYDLLEEAVDLVSEYVDAVLGKGHQYFGIEFPLSATAPMVWLPYSSIDQLLQALGENSANSHNIALSQKILDKLEDYQQKVDKATRDLLYRRTL
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
25PhosphorylationTARPCLCSVGRRGDG
CCCCCEECCCCCCCC		18.0424719451
44PhosphorylationAAGALERSFVELSGA
HHHHHHHHHEECCCC		25.0321815630
49PhosphorylationERSFVELSGAERERP
HHHHEECCCCCCCCC		23.5820860994
93UbiquitinationFYYVESGKLFSVTRN
EEEEECCEEEEEECC		56.4921963094
106AcetylationRNRFIHWKTSGDTLE
CCCEEEEECCCCHHH		20.7420167786
131AcetylationLNNAIRLKFQNCSVL
HHHHHHHHCCCCCCC		34.7526051181
131UbiquitinationLNNAIRLKFQNCSVL
HHHHHHHHCCCCCCC		34.7521963094
170PhosphorylationRLLLPHPSRMYRSEL
HHHCCCHHHCCCCEE		27.0123909892
246PhosphorylationFVLKLPPYDIPGMVS
EEEECCCCCCCCCEE		25.27-
258 (in isoform 1)Ubiquitination-34.3321890473
258UbiquitinationMVSVVELKQSSVMQR
CEEEEEECCCHHHHH		34.3321906983
260PhosphorylationSVVELKQSSVMQRLL
EEEEECCCHHHHHHH		24.2620860994
261PhosphorylationVVELKQSSVMQRLLT
EEEECCCHHHHHHHH		21.0824719451
268PhosphorylationSVMQRLLTGWMPTAI
HHHHHHHHCCCCCCC		33.1324043423
273PhosphorylationLLTGWMPTAIRGDQS
HHHCCCCCCCCCCCC		20.7224043423
285 (in isoform 3)Ubiquitination-31.1521906983
306 (in isoform 3)O-linked_Glycosylation-12.7423301498
307UbiquitinationFALCQDHKLRMWSYK
HHHHCCCCCCCCCHH		46.1821963094
314AcetylationKLRMWSYKEQMCLMV
CCCCCCHHHHHHHHH		35.6319809687
331UbiquitinationMLEYVPVKKDLRLTA
HHHHCCCCCCCEECC		34.2021963094
332UbiquitinationLEYVPVKKDLRLTAG
HHHCCCCCCCEECCC		63.3322817900
343UbiquitinationLTAGTGHKLRLAYSP
ECCCCCCCEEEEECC		36.3327667366
457PhosphorylationDQDPREMYLQSLFTP
CCCHHHHHHHHHCCC		9.24-
460PhosphorylationPREMYLQSLFTPGQF
HHHHHHHHHCCCCCC		23.90-
463PhosphorylationMYLQSLFTPGQFTNE
HHHHHHCCCCCCCHH		31.63-
468PhosphorylationLFTPGQFTNEALCKA
HCCCCCCCHHHHHHH		25.02-
481MethylationKALQIFCRGTERNLD
HHHHHHHCCCCCCCC		44.30115485821
490PhosphorylationTERNLDLSWSELKKE
CCCCCCCCHHHHHHH		28.3721815630
492PhosphorylationRNLDLSWSELKKEVT
CCCCCCHHHHHHHHH		29.6722167270
495 (in isoform 1)Ubiquitination-42.7221890473
495UbiquitinationDLSWSELKKEVTLAV
CCCHHHHHHHHHHHH		42.7221906983
496UbiquitinationLSWSELKKEVTLAVE
CCHHHHHHHHHHHHH		70.7822817900
513PhosphorylationLQGSVTEYEFSQEEF
HCCCCEEEECCHHHH		16.9527642862
561UbiquitinationTNMVCLLKKGYLSFL
CCCEEEECCCCHHHH		31.0721963094
562UbiquitinationNMVCLLKKGYLSFLI
CCEEEECCCCHHHHC		53.4022817900
608UbiquitinationRDVICLIKCLRLIEE
HHHHHHHHHHHHHHH		17.8021963094
608AcetylationRDVICLIKCLRLIEE
HHHHHHHHHHHHHHH		17.8026051181
648PhosphorylationQILEDMITIDVENVM
HHHHHCCCCCHHHHH		12.4226074081
660PhosphorylationNVMEDICSKLQEIRN
HHHHHHHHHHHHHHC		36.4126074081
683PhosphorylationIREMDYETEVEMEKG
HHHCCCCCCEEECCC		38.82-
687SulfoxidationDYETEVEMEKGFNPA
CCCCCEEECCCCCCC		8.5628465586
689UbiquitinationETEVEMEKGFNPAQP
CCCEEECCCCCCCCC		68.4421906983
689 (in isoform 1)Ubiquitination-68.4421890473
722UbiquitinationIVCRGVHKIASTRFL
EEECCCHHHHCCCHH		37.2521963094
773PhosphorylationTAPLLLSYYLIKWGS
HHHHHHHHHHHHCCH		11.40-
774PhosphorylationAPLLLSYYLIKWGSE
HHHHHHHHHHHCCHH		9.89-
833UbiquitinationFFQEVARKHIISHLF
HHHHHHHHHHHHHHH		29.44-
925UbiquitinationLVTGEGQKALECFCQ
EEECCCHHHHHHHHH		66.8421963094
935PhosphorylationECFCQAASEVGKEEF
HHHHHHHHHHCHHHH		35.51-
939AcetylationQAASEVGKEEFLDRL
HHHHHHCHHHHHHHH		60.2826051181
939UbiquitinationQAASEVGKEEFLDRL
HHHHHHCHHHHHHHH		60.2821963094
949PhosphorylationFLDRLIRSEDGEIVS
HHHHHHHCCCCCEEE		32.8023312004
956PhosphorylationSEDGEIVSTPRLQYY
CCCCCEEECCCHHHH		38.0523312004
957PhosphorylationEDGEIVSTPRLQYYD
CCCCEEECCCHHHHH		11.0921815630
962PhosphorylationVSTPRLQYYDKVLRL
EECCCHHHHHHHHHH		20.4423312004
963PhosphorylationSTPRLQYYDKVLRLL
ECCCHHHHHHHHHHH		9.0523312004
965 (in isoform 1)Ubiquitination-27.3521890473
965UbiquitinationPRLQYYDKVLRLLDV
CCHHHHHHHHHHHHH		27.3523000965
965AcetylationPRLQYYDKVLRLLDV
CCHHHHHHHHHHHHH		27.3526051181
995UbiquitinationTEAGDDWKSQATLRT
HHCCCCHHHHHHHHH		39.42-
1006AcetylationTLRTCIFKHHLDLGH
HHHHHHHHHHHCCCC		15.3726051181
1006UbiquitinationTLRTCIFKHHLDLGH
HHHHHHHHHHHCCCC		15.3721963094
1006MethylationTLRTCIFKHHLDLGH
HHHHHHHHHHHCCCC		15.37115974335
1018PhosphorylationLGHNSQAYEALTQIP
CCCCHHHHHHHHCCC		8.2927642862
1096 (in isoform 1)Ubiquitination-40.5921890473
1096UbiquitinationIYRHNYRKAGTVMFE
HHHCCCCCCCEEECC		40.5922817900
1114PhosphorylationRLGREVRTLRGLEKQ
HHCHHHHHHCCHHHC		26.4425367160
1120AcetylationRTLRGLEKQGNCYLA
HHHCCHHHCCCHHHH		69.4226051181
1120UbiquitinationRTLRGLEKQGNCYLA
HHHCCHHHCCCHHHH		69.4221963094
1123PhosphorylationRGLEKQGNCYLAALN
CCHHHCCCHHHHHHH		14.5722067460
1139PhosphorylationLRLIRPEYAWIVQPV
HHHHCCHHEEEEEEC		15.2130266825
1147PhosphorylationAWIVQPVSGAVYDRP
EEEEEECCCCCCCCC		27.9330266825
1151PhosphorylationQPVSGAVYDRPGASP
EECCCCCCCCCCCCC		13.0030266825
1157PhosphorylationVYDRPGASPKRNHDG
CCCCCCCCCCCCCCC		36.5525159151
1159UbiquitinationDRPGASPKRNHDGEC
CCCCCCCCCCCCCCC		64.4421963094
1167PhosphorylationRNHDGECTAAPTNRQ
CCCCCCCCCCCCCCC		22.8826074081
1171PhosphorylationGECTAAPTNRQIEIL
CCCCCCCCCCCEEEE		38.0026074081
1185UbiquitinationLELEDLEKECSLARI
EEHHHHHHHHCHHHH		71.9121963094
1240PhosphorylationQTFKLPLTPVFEGLA
HHCCCCCCCCCCCHH		18.57-
1249AcetylationVFEGLAFKCIKLQFG
CCCCHHHEEEEECCC		29.4626051181
1249UbiquitinationVFEGLAFKCIKLQFG
CCCCHHHEEEEECCC		29.4621963094
1252UbiquitinationGLAFKCIKLQFGGEA
CHHHEEEEECCCCHH		45.7822817900
1300UbiquitinationSTYLERYKVQNNLYH
HHHHHHHCCCCCHHH		43.4929967540
1306PhosphorylationYKVQNNLYHHCVINK
HCCCCCHHHHHHHHH		7.5228152594
1330UbiquitinationNWLINSYKKVDAAEL
HHHCHHCCCCCHHHH		46.2521963094
13312-HydroxyisobutyrylationWLINSYKKVDAAELL
HHCHHCCCCCHHHHH		36.79-
1331UbiquitinationWLINSYKKVDAAELL
HHCHHCCCCCHHHHH		36.7922817900
1355PhosphorylationEEAVDLVSEYVDAVL
HHHHHHHHHHHHHHC		30.4326074081
1357PhosphorylationAVDLVSEYVDAVLGK
HHHHHHHHHHHHCCC		8.9826074081
1368PhosphorylationVLGKGHQYFGIEFPL
HCCCCCCEEEEEECC		9.7126074081
1411UbiquitinationHNIALSQKILDKLED
HCHHHHHHHHHHHHH		41.6923000965
1415AcetylationLSQKILDKLEDYQQK
HHHHHHHHHHHHHHH		50.7827452117
1415UbiquitinationLSQKILDKLEDYQQK
HHHHHHHHHHHHHHH		50.7823000965
1415 (in isoform 1)Ubiquitination-50.7821890473
1422UbiquitinationKLEDYQQKVDKATRD
HHHHHHHHHHHHHHH		36.5521963094
1422 (in isoform 1)Ubiquitination-36.5521890473
1425UbiquitinationDYQQKVDKATRDLLY
HHHHHHHHHHHHHHH		55.4322817900
1427PhosphorylationQQKVDKATRDLLYRR
HHHHHHHHHHHHHHH		30.3828258704
1432PhosphorylationKATRDLLYRRTL---
HHHHHHHHHHCC---		12.8328258704
1435PhosphorylationRDLLYRRTL------
HHHHHHHCC------		28.0225921289
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 NU160_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NU160_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 NU160_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NU133_HUMANNUP133physical
26344197
NUP85_HUMANNUP85physical
26344197
WEE1_HUMANWEE1physical
24927568
NUP50_HUMANNUP50physical
24927568
P121A_HUMANPOM121physical
24927568
RL26L_HUMANRPL26L1physical
24927568
F102A_HUMANFAM102Aphysical
24927568
VASP_HUMANVASPphysical
24927568
STX5_HUMANSTX5physical
24927568
MAN1_HUMANLEMD3physical
24927568
RBP2_HUMANRANBP2physical
24927568
NUP98_HUMANNUP98physical
24927568
PGRC2_HUMANPGRMC2physical
24927568
ELYS_HUMANAHCTF1physical
24927568
NU153_HUMANNUP153physical
24927568
LAP2A_HUMANTMPOphysical
24927568
LAP2B_HUMANTMPOphysical
24927568
NUP85_HUMANNUP85physical
24927568
RAF1_HUMANRAF1physical
27173435
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 NU160_HUMAN

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Related Literatures of Post-Translational Modification
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-1157, 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-1157, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, AND MASSSPECTROMETRY.
"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-1157, AND MASSSPECTROMETRY.

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