NUP85_HUMAN - dbPTM
NUP85_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUP85_HUMAN
UniProt AC Q9BW27
Protein Name Nuclear pore complex protein Nup85
Gene Name NUP85
Organism Homo sapiens (Human).
Sequence Length 656
Subcellular Localization Nucleus, nuclear pore complex . Chromosome, centromere, kinetochore . Cytoplasm, cytoskeleton, spindle . Cytoplasm . Nucleus membrane . During mitosis, localizes to the kinetochores and spindle poles (PubMed:12718872, PubMed:16807356). Upon CCl2 stim
Protein Description Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. [PubMed: 12718872 As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP96/Nup98 and NUP153 to the nucleus]
Protein Sequence MEELDGEPTVTLIPGVNSKKNQMYFDWGPGEMLVCETSFNKKEKSEMVPSCPFIYIIRKDVDVYSQILRKLFNESHGIFLGLQRIDEELTGKSRKSQLVRVSKNYRSVIRACMEEMHQVAIAAKDPANGRQFSSQVSILSAMELIWNLCEILFIEVAPAGPLLLHLLDWVRLHVCEVDSLSADVLGSENPSKHDSFWNLVTILVLQGRLDEARQMLSKEADASPASAGICRIMGDLMRTMPILSPGNTQTLTELELKWQHWHEECERYLQDSTFATSPHLESLLKIMLGDEAALLEQKELLSNWYHFLVTRLLYSNPTVKPIDLHYYAQSSLDLFLGGESSPEPLDNILLAAFEFDIHQVIKECSIALSNWWFVAHLTDLLDHCKLLQSHNLYFGSNMREFLLLEYASGLFAHPSLWQLGVDYFDYCPELGRVSLELHIERIPLNTEQKALKVLRICEQRQMTEQVRSICKILAMKAVRNNRLGSALSWSIRAKDAAFATLVSDRFLRDYCERGCFSDLDLIDNLGPAMMLSDRLTFLGKYREFHRMYGEKRFADAASLLLSLMTSRIAPRSFWMTLLTDALPLLEQKQVIFSAEQTYELMRCLEDLTSRRPVHGESDTEQLQDDDIETTKVEMLRLSLARNLARAIIREGSLEGS
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-------MEELDGEP
-------CCCCCCCC		9.0119413330
9PhosphorylationEELDGEPTVTLIPGV
CCCCCCCEEEECCCC		23.0920860994
11PhosphorylationLDGEPTVTLIPGVNS
CCCCCEEEECCCCCC		22.8120860994
13UbiquitinationGEPTVTLIPGVNSKK
CCCEEEECCCCCCCC		1.72-
18PhosphorylationTLIPGVNSKKNQMYF
EECCCCCCCCCEEEE		42.4728450419
19UbiquitinationLIPGVNSKKNQMYFD
ECCCCCCCCCEEEEE		51.01-
20UbiquitinationIPGVNSKKNQMYFDW
CCCCCCCCCEEEEEC		52.84-
24UbiquitinationNSKKNQMYFDWGPGE
CCCCCEEEEECCCCC		6.66-
24PhosphorylationNSKKNQMYFDWGPGE
CCCCCEEEEECCCCC		6.6626552605
37PhosphorylationGEMLVCETSFNKKEK
CCEEEEECCCCHHHH		33.2330576142
38PhosphorylationEMLVCETSFNKKEKS
CEEEEECCCCHHHHC		12.4330576142
44UbiquitinationTSFNKKEKSEMVPSC
CCCCHHHHCCCCCCC		61.67-
45PhosphorylationSFNKKEKSEMVPSCP
CCCHHHHCCCCCCCC		31.8329083192
46UbiquitinationFNKKEKSEMVPSCPF
CCHHHHCCCCCCCCE		56.09-
50PhosphorylationEKSEMVPSCPFIYII
HHCCCCCCCCEEEEE		24.0227794612
55PhosphorylationVPSCPFIYIIRKDVD
CCCCCEEEEEECCHH		7.2329083192
59AcetylationPFIYIIRKDVDVYSQ
CEEEEEECCHHHHHH		52.2526051181
592-HydroxyisobutyrylationPFIYIIRKDVDVYSQ
CEEEEEECCHHHHHH		52.25-
59UbiquitinationPFIYIIRKDVDVYSQ
CEEEEEECCHHHHHH		52.2521890473
64PhosphorylationIRKDVDVYSQILRKL
EECCHHHHHHHHHHH		7.1520068231
65PhosphorylationRKDVDVYSQILRKLF
ECCHHHHHHHHHHHH		15.5920068231
70UbiquitinationVYSQILRKLFNESHG
HHHHHHHHHHHHCCC		54.7221890473
78UbiquitinationLFNESHGIFLGLQRI
HHHHCCCCEEEHHHC		1.84-
90PhosphorylationQRIDEELTGKSRKSQ
HHCCHHHHCCCCHHH		45.9321815630
92AcetylationIDEELTGKSRKSQLV
CCHHHHCCCCHHHHH		41.6825953088
92UbiquitinationIDEELTGKSRKSQLV
CCHHHHCCCCHHHHH		41.68-
92MalonylationIDEELTGKSRKSQLV
CCHHHHCCCCHHHHH		41.6826320211
96PhosphorylationLTGKSRKSQLVRVSK
HHCCCCHHHHHHHCH		27.8623312004
124UbiquitinationHQVAIAAKDPANGRQ
HHHHHHHCCCCCCCC		56.05-
124AcetylationHQVAIAAKDPANGRQ
HHHHHHHCCCCCCCC		56.0526051181
172UbiquitinationHLLDWVRLHVCEVDS
HHHHHHHHCCCCCCC		2.28-
211UbiquitinationVLQGRLDEARQMLSK
HHCCCHHHHHHHHHH		50.79-
218UbiquitinationEARQMLSKEADASPA
HHHHHHHHHCCCCHH		53.62-
223PhosphorylationLSKEADASPASAGIC
HHHHCCCCHHHHHHH		22.8825159151
226PhosphorylationEADASPASAGICRIM
HCCCCHHHHHHHHHH		30.3425262027
239PhosphorylationIMGDLMRTMPILSPG
HHHHHHHHCCEECCC		17.21-
244PhosphorylationMRTMPILSPGNTQTL
HHHCCEECCCCCCCC		31.3327050516
248PhosphorylationPILSPGNTQTLTELE
CEECCCCCCCCCHHH		28.92-
252PhosphorylationPGNTQTLTELELKWQ
CCCCCCCCHHHHHHH		41.74-
257UbiquitinationTLTELELKWQHWHEE
CCCHHHHHHHHHHHH		35.12-
277PhosphorylationQDSTFATSPHLESLL
CCCCCCCCCCHHHHH		13.59-
281UbiquitinationFATSPHLESLLKIML
CCCCCCHHHHHHHHH		35.9821890473
282PhosphorylationATSPHLESLLKIMLG
CCCCCHHHHHHHHHC		45.4124719451
287SulfoxidationLESLLKIMLGDEAAL
HHHHHHHHHCCHHHH		3.0621406390
302PhosphorylationLEQKELLSNWYHFLV
HHHHHHHHHHHHHHH		37.6324719451
326UbiquitinationVKPIDLHYYAQSSLD
CCCCCHHEEHHHCCC		14.0621890473
372UbiquitinationSIALSNWWFVAHLTD
HHHHHCHHHHHHHHH		5.1021890473
393PhosphorylationLLQSHNLYFGSNMRE
HHHHCCCCCCCCHHH		15.9427642862
403UbiquitinationSNMREFLLLEYASGL
CCHHHHHHHHHHHCC		4.08-
406UbiquitinationREFLLLEYASGLFAH
HHHHHHHHHHCCCCC		13.16-
425UbiquitinationQLGVDYFDYCPELGR
HCCCCHHHCCHHHCC		37.58-
430UbiquitinationYFDYCPELGRVSLEL
HHHCCHHHCCEEEEE		2.99-
448UbiquitinationRIPLNTEQKALKVLR
ECCCCHHHHHHHHHH		33.99-
449UbiquitinationIPLNTEQKALKVLRI
CCCCHHHHHHHHHHH		49.8321906983
452UbiquitinationNTEQKALKVLRICEQ
CHHHHHHHHHHHHHH		44.05-
471UbiquitinationEQVRSICKILAMKAV
HHHHHHHHHHHHHHH		38.80-
471AcetylationEQVRSICKILAMKAV
HHHHHHHHHHHHHHH		38.807971403
476AcetylationICKILAMKAVRNNRL
HHHHHHHHHHHCCCC		37.827971413
476UbiquitinationICKILAMKAVRNNRL
HHHHHHHHHHHCCCC		37.82-
485PhosphorylationVRNNRLGSALSWSIR
HHCCCCHHHHHHHHH		30.5420068231
488PhosphorylationNRLGSALSWSIRAKD
CCCHHHHHHHHHHHH		20.6320873877
490PhosphorylationLGSALSWSIRAKDAA
CHHHHHHHHHHHHHH		9.9820068231
4942-HydroxyisobutyrylationLSWSIRAKDAAFATL
HHHHHHHHHHHHHHH		37.74-
494UbiquitinationLSWSIRAKDAAFATL
HHHHHHHHHHHHHHH		37.7421890473
494UbiquitinationLSWSIRAKDAAFATL
HHHHHHHHHHHHHHH		37.74-
505MethylationFATLVSDRFLRDYCE
HHHHHCHHHHHHHHH		25.62115485883
510PhosphorylationSDRFLRDYCERGCFS
CHHHHHHHHHCCCCC		6.9729496907
540AcetylationDRLTFLGKYREFHRM
HHHHHHHHHHHHHHH		43.1926051181
540UbiquitinationDRLTFLGKYREFHRM
HHHHHHHHHHHHHHH		43.1921890473
558PhosphorylationKRFADAASLLLSLMT
HHHHHHHHHHHHHHH		22.6724719451
562PhosphorylationDAASLLLSLMTSRIA
HHHHHHHHHHHCCCC		18.9620860994
565PhosphorylationSLLLSLMTSRIAPRS
HHHHHHHHCCCCCHH		21.8324719451
566PhosphorylationLLLSLMTSRIAPRSF
HHHHHHHCCCCCHHH		14.0224719451
575SulfoxidationIAPRSFWMTLLTDAL
CCCHHHHHHHHHHHH		1.4628465586
585UbiquitinationLTDALPLLEQKQVIF
HHHHHHHHHHCCCEE		6.5621890473
593PhosphorylationEQKQVIFSAEQTYEL
HHCCCEECHHHHHHH		21.5524043423
597PhosphorylationVIFSAEQTYELMRCL
CEECHHHHHHHHHHH		15.5224043423
598PhosphorylationIFSAEQTYELMRCLE
EECHHHHHHHHHHHH		13.5324043423
608PhosphorylationMRCLEDLTSRRPVHG
HHHHHHHHHCCCCCC		32.2920860994
617PhosphorylationRRPVHGESDTEQLQD
CCCCCCCCCHHHHCC		55.1929255136
619PhosphorylationPVHGESDTEQLQDDD
CCCCCCCHHHHCCCC		34.6029255136
629PhosphorylationLQDDDIETTKVEMLR
HCCCCCCHHHHHHHH		32.0523312004
631UbiquitinationDDDIETTKVEMLRLS
CCCCCHHHHHHHHHH		43.5521890473
652PhosphorylationRAIIREGSLEGS---
HHHHHHCCCCCC---		20.6324670416
656PhosphorylationREGSLEGS-------
HHCCCCCC-------		27.8928102081
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 NUP85_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUP85_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 NUP85_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EF1G_HUMANEEF1Gphysical
16169070
DCTN3_HUMANDCTN3physical
22863883
GBF1_HUMANGBF1physical
22863883
RABL6_HUMANRABL6physical
22863883
NU107_HUMANNUP107physical
26344197
NUP98_HUMANNUP98physical
26344197
PRKDC_HUMANPRKDCphysical
24927568
UN45A_HUMANUNC45Aphysical
24927568
NU160_HUMANNUP160physical
24927568
FMN1_HUMANFMN1physical
24927568
IMB1_HUMANKPNB1physical
24927568
ZN740_HUMANZNF740physical
24927568
NUP98_HUMANNUP98physical
24927568
NUP43_HUMANNUP43physical
24927568
P121A_HUMANPOM121physical
24927568
HS90B_HUMANHSP90AB1physical
24927568
NU107_HUMANNUP107physical
24927568
NUDC_HUMANNUDCphysical
24927568
NUP88_HUMANNUP88physical
24927568
RAGP1_HUMANRANGAP1physical
24927568
NUP62_HUMANNUP62physical
24927568
SEH1_HUMANSEH1Lphysical
24927568
NU214_HUMANNUP214physical
24927568
RBP2_HUMANRANBP2physical
24927568
NUP50_HUMANNUP50physical
24927568
NU153_HUMANNUP153physical
24927568
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 NUP85_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
"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-223, AND MASSSPECTROMETRY.

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