NUP88_HUMAN - dbPTM
NUP88_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUP88_HUMAN
UniProt AC Q99567
Protein Name Nuclear pore complex protein Nup88
Gene Name NUP88
Organism Homo sapiens (Human).
Sequence Length 741
Subcellular Localization Nucleus, nuclear pore complex.
Protein Description Essential component of nuclear pore complex..
Protein Sequence MAAAEGPVGDGELWQTWLPNHVVFLRLREGLKNQSPTEAEKPASSSLPSSPPPQLLTRNVVFGLGGELFLWDGEDSSFLVVRLRGPSGGGEEPALSQYQRLLCINPPLFEIYQVLLSPTQHHVALIGIKGLMVLELPKRWGKNSEFEGGKSTVNCSTTPVAERFFTSSTSLTLKHAAWYPSEILDPHVVLLTSDNVIRIYSLREPQTPTNVIILSEAEEESLVLNKGRAYTASLGETAVAFDFGPLAAVPKTLFGQNGKDEVVAYPLYILYENGETFLTYISLLHSPGNIGKLLGPLPMHPAAEDNYGYDACAVLCLPCVPNILVIATESGMLYHCVVLEGEEEDDHTSEKSWDSRIDLIPSLYVFECVELELALKLASGEDDPFDSDFSCPVKLHRDPKCPSRYHCTHEAGVHSVGLTWIHKLHKFLGSDEEDKDSLQELSTEQKCFVEHILCTKPLPCRQPAPIRGFWIVPDILGPTMICITSTYECLIWPLLSTVHPASPPLLCTREDVEVAESPLRVLAETPDSFEKHIRSILQRSVANPAFLKASEKDIAPPPEECLQLLSRATQVFREQYILKQDLAKEEIQRRVKLLCDQKKKQLEDLSYCREERKSLREMAERLADKYEEAKEKQEDIMNRMKKLLHSFHSELPVLSDSERDMKKELQLIPDQLRHLGNAIKQVTMKKDYQQQKMEKVLSLPKPTIILSAYQRKCIQSILKEEGEHIREMVKQINDIRNHVNF
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------MAAAEGPVG
------CCCCCCCCC		18.5122223895
35PhosphorylationREGLKNQSPTEAEKP
HHHHCCCCCCCCCCC		43.0922167270
37PhosphorylationGLKNQSPTEAEKPAS
HHCCCCCCCCCCCCC		53.7429255136
41UbiquitinationQSPTEAEKPASSSLP
CCCCCCCCCCCCCCC		53.5921906983
44PhosphorylationTEAEKPASSSLPSSP
CCCCCCCCCCCCCCC		29.0530266825
45PhosphorylationEAEKPASSSLPSSPP
CCCCCCCCCCCCCCC		37.6930266825
46PhosphorylationAEKPASSSLPSSPPP
CCCCCCCCCCCCCCC		41.6329255136
49PhosphorylationPASSSLPSSPPPQLL
CCCCCCCCCCCCCHH		61.8529255136
50PhosphorylationASSSLPSSPPPQLLT
CCCCCCCCCCCCHHC		39.2129255136
57PhosphorylationSPPPQLLTRNVVFGL
CCCCCHHCCCEEEEE		28.8730266825
96PhosphorylationGGEEPALSQYQRLLC
CCCCCCHHHHHHHHC		29.0217525332
98PhosphorylationEEPALSQYQRLLCIN
CCCCHHHHHHHHCCC		7.6928152594
138UbiquitinationLMVLELPKRWGKNSE
EEEEECCHHCCCCCC		73.70-
142UbiquitinationELPKRWGKNSEFEGG
ECCHHCCCCCCCCCC		50.7921906983
150UbiquitinationNSEFEGGKSTVNCST
CCCCCCCCCEECCCC		54.5321906983
150AcetylationNSEFEGGKSTVNCST
CCCCCCCCCEECCCC		54.5326051181
155S-nitrosylationGGKSTVNCSTTPVAE
CCCCEECCCCCHHHH		3.122212679
166PhosphorylationPVAERFFTSSTSLTL
HHHHHHCCCCCEEEE		21.0325159151
167PhosphorylationVAERFFTSSTSLTLK
HHHHHCCCCCEEEEE		26.8529255136
168PhosphorylationAERFFTSSTSLTLKH
HHHHCCCCCEEEEEE		20.9629255136
169PhosphorylationERFFTSSTSLTLKHA
HHHCCCCCEEEEEEE		27.7629255136
170PhosphorylationRFFTSSTSLTLKHAA
HHCCCCCEEEEEEEE		22.7029255136
172PhosphorylationFTSSTSLTLKHAAWY
CCCCCEEEEEEEECC		33.2629255136
201PhosphorylationDNVIRIYSLREPQTP
CCEEEEEECCCCCCC		20.6924719451
209PhosphorylationLREPQTPTNVIILSE
CCCCCCCCEEEEEEC		45.5721712546
215PhosphorylationPTNVIILSEAEEESL
CCEEEEEECCCHHHC		25.0928348404
221PhosphorylationLSEAEEESLVLNKGR
EECCCHHHCEECCCC		27.3621712546
226UbiquitinationEESLVLNKGRAYTAS
HHHCEECCCCEEEEE		45.6821906983
230PhosphorylationVLNKGRAYTASLGET
EECCCCEEEEECCCE		11.0728634298
231PhosphorylationLNKGRAYTASLGETA
ECCCCEEEEECCCEE		14.5828348404
233PhosphorylationKGRAYTASLGETAVA
CCCEEEEECCCEEEE		29.1628348404
237PhosphorylationYTASLGETAVAFDFG
EEEECCCEEEEEECC		25.3228634298
265PhosphorylationGKDEVVAYPLYILYE
CCCCEEEEEEEEEEE		5.1228985074
280PhosphorylationNGETFLTYISLLHSP
CCCCHHHHHHHHCCC		7.2328985074
286PhosphorylationTYISLLHSPGNIGKL
HHHHHHCCCCCHHHH		34.1828985074
349PhosphorylationEEEDDHTSEKSWDSR
CCCCCCCCCCCHHHH		39.3424275569
352PhosphorylationDDHTSEKSWDSRIDL
CCCCCCCCHHHHCCC		31.8724275569
379PhosphorylationELALKLASGEDDPFD
HHHHHHHCCCCCCCC		53.8322199227
387PhosphorylationGEDDPFDSDFSCPVK
CCCCCCCCCCCCCEE		40.7230108239
390PhosphorylationDPFDSDFSCPVKLHR
CCCCCCCCCCEEECC		23.6230108239
394UbiquitinationSDFSCPVKLHRDPKC
CCCCCCEEECCCCCC		24.58-
400UbiquitinationVKLHRDPKCPSRYHC
EEECCCCCCCCCCCC		64.17-
426UbiquitinationTWIHKLHKFLGSDEE
HHHHHHHHHHCCCHH		53.36-
430PhosphorylationKLHKFLGSDEEDKDS
HHHHHHCCCHHCHHH		43.9523927012
435UbiquitinationLGSDEEDKDSLQELS
HCCCHHCHHHHHHHH		53.1221906983
435AcetylationLGSDEEDKDSLQELS
HCCCHHCHHHHHHHH		53.1226051181
437PhosphorylationSDEEDKDSLQELSTE
CCHHCHHHHHHHHHH		37.3830266825
442PhosphorylationKDSLQELSTEQKCFV
HHHHHHHHHHHCHHH		29.1923401153
443PhosphorylationDSLQELSTEQKCFVE
HHHHHHHHHHCHHHE		55.8730266825
456AcetylationVEHILCTKPLPCRQP
HEEEEECCCCCCCCC		43.4925953088
456UbiquitinationVEHILCTKPLPCRQP
HEEEEECCCCCCCCC		43.49-
496PhosphorylationCLIWPLLSTVHPASP
HHHHHHHHCCCCCCC		35.75-
497PhosphorylationLIWPLLSTVHPASPP
HHHHHHHCCCCCCCC		23.8521552520
502PhosphorylationLSTVHPASPPLLCTR
HHCCCCCCCCCCCCH		31.3426657352
517PhosphorylationEDVEVAESPLRVLAE
HCHHHCCCCHHHHCC		21.3519664994
525PhosphorylationPLRVLAETPDSFEKH
CHHHHCCCCCCHHHH		27.1329255136
528PhosphorylationVLAETPDSFEKHIRS
HHCCCCCCHHHHHHH		36.1930266825
531UbiquitinationETPDSFEKHIRSILQ
CCCCCHHHHHHHHHH		42.1821906983
531AcetylationETPDSFEKHIRSILQ
CCCCCHHHHHHHHHH		42.1826822725
535PhosphorylationSFEKHIRSILQRSVA
CHHHHHHHHHHHHCC		27.3522199227
540PhosphorylationIRSILQRSVANPAFL
HHHHHHHHCCCHHHH		16.7830266825
548UbiquitinationVANPAFLKASEKDIA
CCCHHHHHHHHCCCC		43.3321906983
550PhosphorylationNPAFLKASEKDIAPP
CHHHHHHHHCCCCCC		43.5220068231
552AcetylationAFLKASEKDIAPPPE
HHHHHHHCCCCCCHH		52.5226051181
552UbiquitinationAFLKASEKDIAPPPE
HHHHHHHCCCCCCHH		52.52-
579AcetylationFREQYILKQDLAKEE
HHHHHHHCHHHHHHH		32.0126822725
579UbiquitinationFREQYILKQDLAKEE
HHHHHHHCHHHHHHH		32.0121906983
584AcetylationILKQDLAKEEIQRRV
HHCHHHHHHHHHHHH		64.2823749302
584UbiquitinationILKQDLAKEEIQRRV
HHCHHHHHHHHHHHH		64.28-
592AcetylationEEIQRRVKLLCDQKK
HHHHHHHHHHHHHHH		33.6523749302
592MalonylationEEIQRRVKLLCDQKK
HHHHHHHHHHHHHHH		33.6526320211
592UbiquitinationEEIQRRVKLLCDQKK
HHHHHHHHHHHHHHH		33.65-
598UbiquitinationVKLLCDQKKKQLEDL
HHHHHHHHHHHHHHH		49.00-
5982-HydroxyisobutyrylationVKLLCDQKKKQLEDL
HHHHHHHHHHHHHHH		49.00-
600UbiquitinationLLCDQKKKQLEDLSY
HHHHHHHHHHHHHHH		68.12-
606PhosphorylationKKQLEDLSYCREERK
HHHHHHHHHHHHHHH		34.21-
625UbiquitinationMAERLADKYEEAKEK
HHHHHHHHHHHHHHH		49.2921906983
6252-HydroxyisobutyrylationMAERLADKYEEAKEK
HHHHHHHHHHHHHHH		49.29-
630UbiquitinationADKYEEAKEKQEDIM
HHHHHHHHHHHHHHH		69.5821906983
642UbiquitinationDIMNRMKKLLHSFHS
HHHHHHHHHHHHHHH		47.11-
646PhosphorylationRMKKLLHSFHSELPV
HHHHHHHHHHHCCCC		25.3222817900
655PhosphorylationHSELPVLSDSERDMK
HHCCCCCCCCHHHHH		39.0523186163
663UbiquitinationDSERDMKKELQLIPD
CCHHHHHHHHCCCHH		57.95-
680UbiquitinationRHLGNAIKQVTMKKD
HHHHHHHHHHHCCHH		35.9821906983
688PhosphorylationQVTMKKDYQQQKMEK
HHHCCHHHHHHHHHH		19.66-
692UbiquitinationKKDYQQQKMEKVLSL
CHHHHHHHHHHHHCC		44.6921906983
695UbiquitinationYQQQKMEKVLSLPKP
HHHHHHHHHHCCCCC		45.00-
698PhosphorylationQKMEKVLSLPKPTII
HHHHHHHCCCCCEEE		45.68-
712UbiquitinationILSAYQRKCIQSILK
EEEHHHHHHHHHHHH		21.8421906983
716PhosphorylationYQRKCIQSILKEEGE
HHHHHHHHHHHHCHH		15.2424719451
719UbiquitinationKCIQSILKEEGEHIR
HHHHHHHHHCHHHHH		52.6421906983
730UbiquitinationEHIREMVKQINDIRN
HHHHHHHHHHHHHHH		44.12-
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 NUP88_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUP88_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 NUP88_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUP98_MOUSENup98physical
22480613
NUP98_HUMANNUP98physical
22480613
RBM42_HUMANRBM42physical
22939629
NUP62_HUMANNUP62physical
26344197
RBM42_HUMANRBM42physical
26344197
N62CL_HUMANNUP62CLphysical
28514442
NU214_HUMANNUP214physical
28514442
TRI62_HUMANTRIM62physical
28514442
NUP62_HUMANNUP62physical
28514442
NUP98_HUMANNUP98physical
28514442
COG6_HUMANCOG6physical
28514442
PLEC_HUMANPLECphysical
27173435
VIP2_HUMANPPIP5K2physical
27173435
AAK1_HUMANAAK1physical
27173435
SC24B_HUMANSEC24Bphysical
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 NUP88_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-517 AND THR-525, ANDMASS SPECTROMETRY.
"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-442, 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-45; SER-50; SER-517;THR-525 AND SER-540, AND MASS 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-35; SER-50; SER-442;SER-517 AND THR-525, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517 AND THR-525, ANDMASS 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-517, AND MASSSPECTROMETRY.

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