NU155_HUMAN - dbPTM
NU155_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NU155_HUMAN
UniProt AC O75694
Protein Name Nuclear pore complex protein Nup155
Gene Name NUP155
Organism Homo sapiens (Human).
Sequence Length 1391
Subcellular Localization Nucleus, nuclear pore complex . Nucleus membrane
Peripheral membrane protein
Cytoplasmic side . Nucleus membrane
Peripheral membrane protein
Nucleoplasmic side . In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, be
Protein Description Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport..
Protein Sequence MPSSLLGAAMPASTSAAALQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNNPTVSGMSDMDYPLQGPGLLSVPNLPEISSIRRVPLPPELVEQFGHMQCNCMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPHVRHLLVLATPVDIVILGLSYANLQTGSGVLNDSLSGGMQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAYQAEAGWFSQRCRKINHSKSSLSFLVPSLLQFTFSEDDPILQIAIDNSRNILYTRSEKGVIQVYDLGQDGQGMSRVASVSQNAIVSAAGNIARTIDRSVFKPIVQIAVIENSESLDCQLLAVTHAGVRLYFSTCPFRQPLARPNTLTLVHVRLPPGFSASSTVEKPSKVHRALYSKGILLMAASENEDNDILWCVNHDTFPFQKPMMETQMTAGVDGHSWALSAIDELKVDKIITPLNKDHIPITDSPVVVQQHMLPPKKFVLLSAQGSLMFHKLRPVDQLRHLLVSNVGGDGEEIERFFKLHQEDQACATCLILACSTAACDREVSAWATRAFFRYGGEAQMRFPTTLPPPSNVGPILGSPVYSSSPVPSGSPYPNPSFLGTPSHGIQPPAMSTPVCALGNPATQATNMSCVTGPEIVYSGKHNGICIYFSRIMGNIWDASLVVERIFKSGNREITAIESSVPCQLLESVLQELKGLQEFLDRNSQFAGGPLGNPNTTAKVQQRLIGFMRPENGNPQQMQQELQRKFHEAQLSEKISLQAIQQLVRKSYQALALWKLLCEHQFTIIVAELQKELQEQLKITTFKDLVIRDKELTGALIASLINCYIRDNAAVDGISLHLQDICPLLYSTDDAICSKANELLQRSRQVQNKTEKERMLRESLKEYQKISNQVDLSNVCAQYRQVRFYEGVVELSLTAAEKKDPQGLGLHFYKHGEPEEDIVGLQAFQERLNSYKCITDTLQELVNQSKAAPQSPSVPKKPGPPVLSSDPNMLSNEEAGHHFEQMLKLSQRSKDELFSIALYNWLIQVDLADKLLQVASPFLEPHLVRMAKVDQNRVRYMDLLWRYYEKNRSFSNAARVLSRLADMHSTEISLQQRLEYIARAILSAKSSTAISSIAADGEFLHELEEKMEVARIQLQIQETLQRQYSHHSSVQDAVSQLDSELMDITKLYGEFADPFKLAECKLAIIHCAGYSDPILVQTLWQDIIEKELSDSVTLSSSDRMHALSLKIVLLGKIYAGTPRFFPLDFIVQFLEQQVCTLNWDVGFVIQTMNEIGVPLPRLLEVYDQLFKSRDPFWNRMKKPLHLLDCIHVLLIRYVENPSQVLNCERRRFTNLCLDAVCGYLVELQSMSSSVAVQAITGNFKSLQAKLERLH
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
3Phosphorylation-----MPSSLLGAAM
-----CCHHHHHHCC		45.5423401153
4Phosphorylation----MPSSLLGAAMP
----CCHHHHHHCCC		38.0429255136
13PhosphorylationLGAAMPASTSAAALQ
HHHCCCCCCHHHHHH		19.6123401153
14PhosphorylationGAAMPASTSAAALQE
HHCCCCCCHHHHHHH		25.2123401153
15PhosphorylationAAMPASTSAAALQEA
HCCCCCCHHHHHHHH		17.2623401153
82PhosphorylationVPNLPEISSIRRVPL
CCCCCCCCCCCCCCC		20.3224719451
83PhosphorylationPNLPEISSIRRVPLP
CCCCCCCCCCCCCCC		26.2725954137
169PhosphorylationRHLLVLATPVDIVIL
HHHHHHCCCCCEEEE		21.4921406692
179PhosphorylationDIVILGLSYANLQTG
CEEEECCCCCCCCCC		22.0221406692
180PhosphorylationIVILGLSYANLQTGS
EEEECCCCCCCCCCC		12.4521406692
185PhosphorylationLSYANLQTGSGVLND
CCCCCCCCCCCCCCC		36.1621406692
187PhosphorylationYANLQTGSGVLNDSL
CCCCCCCCCCCCCCC		29.1721406692
193PhosphorylationGSGVLNDSLSGGMQL
CCCCCCCCCCCCCCC		24.3026074081
195PhosphorylationGVLNDSLSGGMQLLP
CCCCCCCCCCCCCCC		36.9326074081
231UbiquitinationGRIFLAGKDGCLYEV
CEEEEEECCCCEEEE		45.39-
238 (in isoform 2)Ubiquitination-3.6721890473
254 (in isoform 2)Phosphorylation-2.65-
297UbiquitinationILYTRSEKGVIQVYD
EEEEECCCCEEEEEE		60.7821906983
297 (in isoform 1)Ubiquitination-60.7821890473
303PhosphorylationEKGVIQVYDLGQDGQ
CCCEEEEEECCCCCC		6.7820068231
313PhosphorylationGQDGQGMSRVASVSQ
CCCCCCHHHEEECCH		30.3520068231
369PhosphorylationTHAGVRLYFSTCPFR
ECCCCEEEEECCCCC		5.7328152594
404UbiquitinationSASSTVEKPSKVHRA
CCCCCCCCCCHHHHH		50.70-
407UbiquitinationSTVEKPSKVHRALYS
CCCCCCCHHHHHHHH		51.06-
445 (in isoform 2)Phosphorylation-4.96-
471UbiquitinationIDELKVDKIITPLNK
HHHCCCCEEECCCCC		38.71-
474PhosphorylationLKVDKIITPLNKDHI
CCCCEEECCCCCCCC		25.7928102081
478UbiquitinationKIITPLNKDHIPITD
EEECCCCCCCCCCCC		59.37-
484PhosphorylationNKDHIPITDSPVVVQ
CCCCCCCCCCCCEEE		25.6825627689
486PhosphorylationDHIPITDSPVVVQQH
CCCCCCCCCCEEEEC		15.7925159151
498UbiquitinationQQHMLPPKKFVLLSA
EECCCCCCEEEEEEC		57.83-
504PhosphorylationPKKFVLLSAQGSLMF
CCEEEEEECCCCCCC		17.8727251275
508PhosphorylationVLLSAQGSLMFHKLR
EEEECCCCCCCEECC		12.4627251275
526O-linked_GlycosylationQLRHLLVSNVGGDGE
HHHHHHHHCCCCCHH		26.26UniProtKB CARBOHYD
540UbiquitinationEEIERFFKLHQEDQA
HHHHHHHHHCHHHHH		42.20-
622 (in isoform 2)Phosphorylation-24.62-
681PhosphorylationMGNIWDASLVVERIF
CCCCCCHHHHHHHHH		21.1520068231
681 (in isoform 2)Ubiquitination-21.1521890473
689UbiquitinationLVVERIFKSGNREIT
HHHHHHHHCCCCEEE		55.90-
690PhosphorylationVVERIFKSGNREITA
HHHHHHHCCCCEEEE		30.4724719451
707 (in isoform 2)Ubiquitination-1.5821890473
723MethylationGLQEFLDRNSQFAGG
HHHHHHHCCCCCCCC		47.01115485813
725PhosphorylationQEFLDRNSQFAGGPL
HHHHHCCCCCCCCCC		27.8021712546
737PhosphorylationGPLGNPNTTAKVQQR
CCCCCCCCHHHHHHH		29.4125627689
738PhosphorylationPLGNPNTTAKVQQRL
CCCCCCCHHHHHHHH		30.9925627689
740SumoylationGNPNTTAKVQQRLIG
CCCCCHHHHHHHHHH		38.1828112733
740UbiquitinationGNPNTTAKVQQRLIG
CCCCCHHHHHHHHHH		38.1821890473
740 (in isoform 1)Ubiquitination-38.1821890473
765 (in isoform 2)Ubiquitination-57.1221890473
766SumoylationMQQELQRKFHEAQLS
HHHHHHHHHHHHHHH		37.80-
7662-HydroxyisobutyrylationMQQELQRKFHEAQLS
HHHHHHHHHHHHHHH		37.80-
766AcetylationMQQELQRKFHEAQLS
HHHHHHHHHHHHHHH		37.8026051181
766SumoylationMQQELQRKFHEAQLS
HHHHHHHHHHHHHHH		37.80-
766UbiquitinationMQQELQRKFHEAQLS
HHHHHHHHHHHHHHH		37.8021906983
766 (in isoform 1)Ubiquitination-37.8021890473
775UbiquitinationHEAQLSEKISLQAIQ
HHHHHHHHHCHHHHH		33.93-
819UbiquitinationKELQEQLKITTFKDL
HHHHHHHCCCCHHHH		37.39-
8242-HydroxyisobutyrylationQLKITTFKDLVIRDK
HHCCCCHHHHHHCCH		48.32-
824UbiquitinationQLKITTFKDLVIRDK
HHCCCCHHHHHHCCH		48.3221890473
824 (in isoform 1)Ubiquitination-48.3221890473
834PhosphorylationVIRDKELTGALIASL
HHCCHHHHHHHHHHH		22.8521601212
840PhosphorylationLTGALIASLINCYIR
HHHHHHHHHHHHHHH		23.8421601212
890UbiquitinationRSRQVQNKTEKERML
HHHHHCCHHHHHHHH		40.75-
893UbiquitinationQVQNKTEKERMLRES
HHCCHHHHHHHHHHH		56.71-
902UbiquitinationRMLRESLKEYQKISN
HHHHHHHHHHHHHHH		64.75-
906UbiquitinationESLKEYQKISNQVDL
HHHHHHHHHHHCCCH		47.39-
908PhosphorylationLKEYQKISNQVDLSN
HHHHHHHHHCCCHHH		28.3930108239
914PhosphorylationISNQVDLSNVCAQYR
HHHCCCHHHHHHHHH		23.8230108239
914 (in isoform 2)Ubiquitination-23.82-
917GlutathionylationQVDLSNVCAQYRQVR
CCCHHHHHHHHHHHE		1.9822555962
920PhosphorylationLSNVCAQYRQVRFYE
HHHHHHHHHHHEEEE		5.6330108239
926PhosphorylationQYRQVRFYEGVVELS
HHHHHEEEECEEEEE		10.95-
928 (in isoform 2)Ubiquitination-19.86-
933PhosphorylationYEGVVELSLTAAEKK
EECEEEEEEEEHHHC		15.3518691976
933 (in isoform 2)Phosphorylation-15.35-
935 (in isoform 2)Phosphorylation-22.05-
939 (in isoform 2)Ubiquitination-58.7221890473
9402-HydroxyisobutyrylationSLTAAEKKDPQGLGL
EEEEHHHCCCCCCEE		67.17-
940AcetylationSLTAAEKKDPQGLGL
EEEEHHHCCCCCCEE		67.1726051181
940UbiquitinationSLTAAEKKDPQGLGL
EEEEHHHCCCCCCEE		67.17-
951UbiquitinationGLGLHFYKHGEPEED
CCEEEEECCCCCHHH		44.16-
971PhosphorylationAFQERLNSYKCITDT
HHHHHHHHCCHHHHH		30.4720068230
971 (in isoform 2)Phosphorylation-30.47-
973UbiquitinationQERLNSYKCITDTLQ
HHHHHHCCHHHHHHH		20.98-
974S-nitrosocysteineERLNSYKCITDTLQE
HHHHHCCHHHHHHHH		2.84-
974GlutathionylationERLNSYKCITDTLQE
HHHHHCCHHHHHHHH		2.8422555962
974S-nitrosylationERLNSYKCITDTLQE
HHHHHCCHHHHHHHH		2.8419483679
978PhosphorylationSYKCITDTLQELVNQ
HCCHHHHHHHHHHHH		22.9926074081
986PhosphorylationLQELVNQSKAAPQSP
HHHHHHHHCCCCCCC		21.0426074081
987UbiquitinationQELVNQSKAAPQSPS
HHHHHHHCCCCCCCC		38.51-
992PhosphorylationQSKAAPQSPSVPKKP
HHCCCCCCCCCCCCC		20.3429255136
994PhosphorylationKAAPQSPSVPKKPGP
CCCCCCCCCCCCCCC		57.1929255136
998AcetylationQSPSVPKKPGPPVLS
CCCCCCCCCCCCCCC		49.4926051181
998UbiquitinationQSPSVPKKPGPPVLS
CCCCCCCCCCCCCCC		49.4921906983
998 (in isoform 1)Ubiquitination-49.4921890473
1005PhosphorylationKPGPPVLSSDPNMLS
CCCCCCCCCCCCCCC		32.6923401153
1006PhosphorylationPGPPVLSSDPNMLSN
CCCCCCCCCCCCCCC		53.5826074081
1010 (in isoform 2)Ubiquitination-5.44-
1012PhosphorylationSSDPNMLSNEEAGHH
CCCCCCCCCCHHHHH		31.2726074081
1025UbiquitinationHHFEQMLKLSQRSKD
HHHHHHHHHHHCCHH		40.53-
1030PhosphorylationMLKLSQRSKDELFSI
HHHHHHCCHHHHHHH		36.5022817900
1057PhosphorylationDKLLQVASPFLEPHL
HHHHHHHCHHCCHHH		19.8228112733
1067 (in isoform 2)Ubiquitination-3.1021890473
1069UbiquitinationPHLVRMAKVDQNRVR
HHHHHCCCCCHHHHH		36.68-
1084PhosphorylationYMDLLWRYYEKNRSF
HHHHHHHHHHHCCCH		12.37-
1085PhosphorylationMDLLWRYYEKNRSFS
HHHHHHHHHHCCCHH		16.32-
1088 (in isoform 2)Ubiquitination-32.6521890473
1090PhosphorylationRYYEKNRSFSNAARV
HHHHHCCCHHHHHHH		42.28-
1092PhosphorylationYEKNRSFSNAARVLS
HHHCCCHHHHHHHHH		27.1427251275
1099PhosphorylationSNAARVLSRLADMHS
HHHHHHHHHHHHCCC		23.53-
1104SulfoxidationVLSRLADMHSTEISL
HHHHHHHCCCCCCCH		1.9328183972
1126UbiquitinationARAILSAKSSTAISS
HHHHHHCCCCCHHHH		41.3822053931
1126 (in isoform 1)Ubiquitination-41.3821890473
1127PhosphorylationRAILSAKSSTAISSI
HHHHHCCCCCHHHHH		32.4130622161
1128PhosphorylationAILSAKSSTAISSIA
HHHHCCCCCHHHHHH		22.5830622161
1129PhosphorylationILSAKSSTAISSIAA
HHHCCCCCHHHHHHC		34.7930622161
1132PhosphorylationAKSSTAISSIAADGE
CCCCCHHHHHHCCCH		17.1530108239
1133PhosphorylationKSSTAISSIAADGEF
CCCCHHHHHHCCCHH		15.3330108239
1138 (in isoform 2)Ubiquitination-23.88-
1147UbiquitinationFLHELEEKMEVARIQ
HHHHHHHHHHHHHHH		30.8721906983
1147 (in isoform 1)Ubiquitination-30.8721890473
1165PhosphorylationQETLQRQYSHHSSVQ
HHHHHHHHCCCCHHH		16.5030108239
1166PhosphorylationETLQRQYSHHSSVQD
HHHHHHHCCCCHHHH		13.3430108239
1169PhosphorylationQRQYSHHSSVQDAVS
HHHHCCCCHHHHHHH		27.1230108239
1170PhosphorylationRQYSHHSSVQDAVSQ
HHHCCCCHHHHHHHH		21.3130108239
1176PhosphorylationSSVQDAVSQLDSELM
CHHHHHHHHHHHHHH		27.0927080861
1180PhosphorylationDAVSQLDSELMDITK
HHHHHHHHHHHHHHH		41.0227080861
1186PhosphorylationDSELMDITKLYGEFA
HHHHHHHHHHHHHCC		15.6727080861
1197AcetylationGEFADPFKLAECKLA
HHCCCHHHHHCCCEE		52.7725038526
1197UbiquitinationGEFADPFKLAECKLA
HHCCCHHHHHCCCEE		52.77-
1230PhosphorylationDIIEKELSDSVTLSS
HHHHHHCCCCCCCCC		29.0020860994
1232PhosphorylationIEKELSDSVTLSSSD
HHHHCCCCCCCCCHH		17.3920860994
1245PhosphorylationSDRMHALSLKIVLLG
HHHHHHHHHHHHHHC		28.5324719451
1249 (in isoform 2)Ubiquitination-3.2721890473
1258O-linked_GlycosylationLGKIYAGTPRFFPLD
HCHHHCCCCCCCCHH		11.7928510447
1288PhosphorylationDVGFVIQTMNEIGVP
CHHHHHEEHHHHCCC		15.7322210691
13082-HydroxyisobutyrylationEVYDQLFKSRDPFWN
HHHHHHHHCCCHHHH		53.85-
1308UbiquitinationEVYDQLFKSRDPFWN
HHHHHHHHCCCHHHH		53.8521890473
1308 (in isoform 1)Ubiquitination-53.8521890473
1386SumoylationNFKSLQAKLERLH--
CHHHHHHHHHHCC--		37.61-
1386AcetylationNFKSLQAKLERLH--
CHHHHHHHHHHCC--		37.6125953088
1386SumoylationNFKSLQAKLERLH--
CHHHHHHHHHHCC--		37.61-
1386UbiquitinationNFKSLQAKLERLH--
CHHHHHHHHHHCC--		37.61-
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 NU155_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NU155_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 NU155_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GLE1_HUMANGLE1physical
14645504
HDAC4_HUMANHDAC4physical
21464227
TACC2_HUMANTACC2physical
22939629
EFS_HUMANEFSphysical
25416956
REG1B_HUMANREG1Bphysical
26344197
Drug and Disease Associations
Kegg Disease
OMIM Disease
615770Atrial fibrillation, familial, 15 (ATFB15)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NU155_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992 AND SER-994, ANDMASS SPECTROMETRY.
"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-994, AND MASSSPECTROMETRY.

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