NDC1_HUMAN - dbPTM
NDC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDC1_HUMAN
UniProt AC Q9BTX1
Protein Name Nucleoporin NDC1
Gene Name NDC1
Organism Homo sapiens (Human).
Sequence Length 674
Subcellular Localization Nucleus, nuclear pore complex. Nucleus membrane
Multi-pass membrane protein. Central core structure of the nuclear pore complex.
Protein Description Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane..
Protein Sequence MATAVSRPCAGRSRDILWRVLGWRIVASIVWSVLFLPICTTVFIIFSRIDLFHPIQWLSDSFSDLYSSYVIFYFLLLSVVIIIISIFNVEFYAVVPSIPCSRLALIGKIIHPQQLMHSFIHAAMGMVMAWCAAVITQGQYSFLVVPCTGTNSFGSPAAQTCLNEYHLFFLLTGAFMGYSYSLLYFVNNMNYLPFPIIQQYKFLRFRRSLLLLVKHSCVESLFLVRNFCILYYFLGYIPKAWISTAMNLHIDEQVHRPLDTVSGLLNLSLLYHVWLCGVFLLTTWYVSWILFKIYATEAHVFPVQPPFAEGSDECLPKVLNSNPPPIIKYLALQDLMLLSQYSPSRRQEVFSLSQPGGHPHNWTAISRECLNLLNGMTQKLILYQEAAATNGRVSSSYPVEPKKLNSPEETAFQTPKSSQMPRPSVPPLVKTSLFSSKLSTPDVVSPFGTPFGSSVMNRMAGIFDVNTCYGSPQSPQLIRRGPRLWTSASDQQMTEFSNPSPSTSISAEGKTMRQPSVIYSWIQNKREQIKNFLSKRVLIMYFFSKHPEASIQAVFSDAQMHIWALEGLSHLVAASFTEDRFGVVQTTLPAILNTLLTLQEAVDKYFKLPHASSKPPRISGSLVDTSYKTLRFAFRASLKTAIYRITTTFGEHLNAVQASAEHQKRLQQFLEFKE
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
339UbiquitinationLQDLMLLSQYSPSRR
HHHHHHHHCCCHHHH		24.1021963094
342PhosphorylationLMLLSQYSPSRRQEV
HHHHHCCCHHHHHEE		14.5728348404
344PhosphorylationLLSQYSPSRRQEVFS
HHHCCCHHHHHEEEE		33.87-
362UbiquitinationPGGHPHNWTAISREC
CCCCCCCHHHHHHHH		5.5633845483
363UbiquitinationGGHPHNWTAISRECL
CCCCCCHHHHHHHHH		21.3021963094
366PhosphorylationPHNWTAISRECLNLL
CCCHHHHHHHHHHHH		21.4032645325
376UbiquitinationCLNLLNGMTQKLILY
HHHHHCCHHHHHHHH		3.3133845483
378UbiquitinationNLLNGMTQKLILYQE
HHHCCHHHHHHHHHH		29.6621963094
379UbiquitinationLLNGMTQKLILYQEA
HHCCHHHHHHHHHHH		28.4721963094
390UbiquitinationYQEAAATNGRVSSSY
HHHHHHHCCCCCCCC		31.3923000965
394PhosphorylationAATNGRVSSSYPVEP
HHHCCCCCCCCCCCC		16.5319691289
395PhosphorylationATNGRVSSSYPVEPK
HHCCCCCCCCCCCCC		30.9119691289
396PhosphorylationTNGRVSSSYPVEPKK
HCCCCCCCCCCCCCC		26.4219691289
397PhosphorylationNGRVSSSYPVEPKKL
CCCCCCCCCCCCCCC		17.1628152594
397UbiquitinationNGRVSSSYPVEPKKL
CCCCCCCCCCCCCCC		17.1621963094
401UbiquitinationSSSYPVEPKKLNSPE
CCCCCCCCCCCCCCH		39.0422817900
402 (in isoform 2)Ubiquitination-57.2821890473
402UbiquitinationSSYPVEPKKLNSPEE
CCCCCCCCCCCCCHH		57.2821963094
403 (in isoform 1)Ubiquitination-64.7121890473
403 (in isoform 4)Ubiquitination-64.7121890473
403UbiquitinationSYPVEPKKLNSPEET
CCCCCCCCCCCCHHH		64.7121906983
406PhosphorylationVEPKKLNSPEETAFQ
CCCCCCCCCHHHCCC		44.0919664994
410PhosphorylationKLNSPEETAFQTPKS
CCCCCHHHCCCCCCH		30.9830266825
414PhosphorylationPEETAFQTPKSSQMP
CHHHCCCCCCHHCCC		26.6529255136
415UbiquitinationEETAFQTPKSSQMPR
HHHCCCCCCHHCCCC		24.6127667366
416UbiquitinationETAFQTPKSSQMPRP
HHCCCCCCHHCCCCC		67.1533845483
417PhosphorylationTAFQTPKSSQMPRPS
HCCCCCCHHCCCCCC		27.3225159151
418PhosphorylationAFQTPKSSQMPRPSV
CCCCCCHHCCCCCCC		36.3025159151
424PhosphorylationSSQMPRPSVPPLVKT
HHCCCCCCCCCCCCH		48.8425159151
429UbiquitinationRPSVPPLVKTSLFSS
CCCCCCCCCHHHHCC		8.6221890473
429 (in isoform 2)Ubiquitination-8.6221890473
429UbiquitinationRPSVPPLVKTSLFSS
CCCCCCCCCHHHHCC		8.6221890473
430 (in isoform 1)Ubiquitination-39.8321890473
430 (in isoform 4)Ubiquitination-39.8321890473
430UbiquitinationPSVPPLVKTSLFSSK
CCCCCCCCHHHHCCC		39.8323000965
431PhosphorylationSVPPLVKTSLFSSKL
CCCCCCCHHHHCCCC		24.1528122231
432PhosphorylationVPPLVKTSLFSSKLS
CCCCCCHHHHCCCCC		23.0021815630
435PhosphorylationLVKTSLFSSKLSTPD
CCCHHHHCCCCCCCC		31.6821815630
436 (in isoform 2)Ubiquitination-30.2221890473
436PhosphorylationVKTSLFSSKLSTPDV
CCHHHHCCCCCCCCC		30.2217192257
436UbiquitinationVKTSLFSSKLSTPDV
CCHHHHCCCCCCCCC		30.2221963094
436UbiquitinationVKTSLFSSKLSTPDV
CCHHHHCCCCCCCCC		30.2221890473
437 (in isoform 1)Ubiquitination-45.3021890473
437UbiquitinationKTSLFSSKLSTPDVV
CHHHHCCCCCCCCCC		45.3021963094
437 (in isoform 4)Ubiquitination-45.3021890473
439PhosphorylationSLFSSKLSTPDVVSP
HHHCCCCCCCCCCCC		41.4522617229
440PhosphorylationLFSSKLSTPDVVSPF
HHCCCCCCCCCCCCC		33.6626055452
445PhosphorylationLSTPDVVSPFGTPFG
CCCCCCCCCCCCCCC		17.8526055452
449PhosphorylationDVVSPFGTPFGSSVM
CCCCCCCCCCCHHHH		18.8026055452
453PhosphorylationPFGTPFGSSVMNRMA
CCCCCCCHHHHHHHC		21.8225850435
454PhosphorylationFGTPFGSSVMNRMAG
CCCCCCHHHHHHHCC		26.2625850435
467PhosphorylationAGIFDVNTCYGSPQS
CCCCCCCCCCCCCCC		13.6223663014
469PhosphorylationIFDVNTCYGSPQSPQ
CCCCCCCCCCCCCHH		20.7129255136
470UbiquitinationFDVNTCYGSPQSPQL
CCCCCCCCCCCCHHH		34.6921963094
471PhosphorylationDVNTCYGSPQSPQLI
CCCCCCCCCCCHHHH		8.0329255136
474PhosphorylationTCYGSPQSPQLIRRG
CCCCCCCCHHHHHCC		20.2829255136
486PhosphorylationRRGPRLWTSASDQQM
HCCCCCEECCCHHCC		21.0022199227
487PhosphorylationRGPRLWTSASDQQMT
CCCCCEECCCHHCCC		17.7522199227
489PhosphorylationPRLWTSASDQQMTEF
CCCEECCCHHCCCCC		35.4022199227
490UbiquitinationRLWTSASDQQMTEFS
CCEECCCHHCCCCCC		42.3129967540
494PhosphorylationSASDQQMTEFSNPSP
CCCHHCCCCCCCCCC		29.5522199227
495UbiquitinationASDQQMTEFSNPSPS
CCHHCCCCCCCCCCC		41.5624816145
497PhosphorylationDQQMTEFSNPSPSTS
HHCCCCCCCCCCCCC		41.4125159151
500PhosphorylationMTEFSNPSPSTSISA
CCCCCCCCCCCCCCC		35.4225159151
502PhosphorylationEFSNPSPSTSISAEG
CCCCCCCCCCCCCCC		38.8430278072
503PhosphorylationFSNPSPSTSISAEGK
CCCCCCCCCCCCCCC		33.2030278072
504PhosphorylationSNPSPSTSISAEGKT
CCCCCCCCCCCCCCC		20.9125159151
506PhosphorylationPSPSTSISAEGKTMR
CCCCCCCCCCCCCCC		21.7522199227
509 (in isoform 2)Ubiquitination-30.3721890473
509UbiquitinationSTSISAEGKTMRQPS
CCCCCCCCCCCCCCH		30.3721963094
510 (in isoform 1)Ubiquitination-30.5621890473
510UbiquitinationTSISAEGKTMRQPSV
CCCCCCCCCCCCCHH		30.5621906983
511PhosphorylationSISAEGKTMRQPSVI
CCCCCCCCCCCCHHH		28.57-
511 (in isoform 3)Ubiquitination-28.5721890473
530UbiquitinationQNKREQIKNFLSKRV
HCHHHHHHHHHHHHH		41.1429967540
534UbiquitinationEQIKNFLSKRVLIMY
HHHHHHHHHHHHHHH		17.8024816145
535UbiquitinationQIKNFLSKRVLIMYF
HHHHHHHHHHHHHHH		48.9924816145
541PhosphorylationSKRVLIMYFFSKHPE
HHHHHHHHHHHCCHH		8.4223909892
544PhosphorylationVLIMYFFSKHPEASI
HHHHHHHHCCHHHHH		21.8423909892
588UbiquitinationFGVVQTTLPAILNTL
CCCHHHHHHHHHHHH		2.8321890473
588UbiquitinationFGVVQTTLPAILNTL
CCCHHHHHHHHHHHH		2.8321890473
619O-linked_GlycosylationSSKPPRISGSLVDTS
CCCCCCCCCCEECCC		24.4928411811
621PhosphorylationKPPRISGSLVDTSYK
CCCCCCCCEECCCHH		20.5925247763
624UbiquitinationRISGSLVDTSYKTLR
CCCCCEECCCHHHHH		34.9229967540
625PhosphorylationISGSLVDTSYKTLRF
CCCCEECCCHHHHHH		26.8621815630
627UbiquitinationGSLVDTSYKTLRFAF
CCEECCCHHHHHHHH		15.3021890473
627 (in isoform 2)Ubiquitination-15.3021890473
627UbiquitinationGSLVDTSYKTLRFAF
CCEECCCHHHHHHHH		15.3021890473
628 (in isoform 1)Ubiquitination-40.6321890473
628UbiquitinationSLVDTSYKTLRFAFR
CEECCCHHHHHHHHH		40.6322817900
633UbiquitinationSYKTLRFAFRASLKT
CHHHHHHHHHHHHHH		6.1321963094
664UbiquitinationQASAEHQKRLQQFLE
HHHHHHHHHHHHHHH		57.9129967540
672UbiquitinationRLQQFLEFKE-----
HHHHHHHHCC-----		13.4921963094
673UbiquitinationLQQFLEFKE------
HHHHHHHCC------		53.8121963094
6732-HydroxyisobutyrylationLQQFLEFKE------
HHHHHHHCC------		53.81-
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 NDC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDC1_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 NDC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NDC1_HUMAN !!
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 NDC1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-406; THR-410; THR-414;SER-439; THR-440; SER-445; THR-449; SER-471 AND SER-474, 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-406; THR-414; SER-471AND SER-474, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, 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-471, 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-406 AND THR-414, ANDMASS SPECTROMETRY.

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