NUF2_HUMAN - dbPTM
NUF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUF2_HUMAN
UniProt AC Q9BZD4
Protein Name Kinetochore protein Nuf2
Gene Name NUF2
Organism Homo sapiens (Human).
Sequence Length 464
Subcellular Localization Nucleus. Chromosome, centromere, kinetochore. Localizes to kinetochores from late prophase to anaphase. Localizes specifically to the outer plate of the kinetochore. NDC80 is required for efficient kinetochore localization.
Protein Description Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. [PubMed: 12438418]
Protein Sequence METLSFPRYNVAEIVIHIRNKILTGADGKNLTKNDLYPNPKPEVLHMIYMRALQIVYGIRLEHFYMMPVNSEVMYPHLMEGFLPFSNLVTHLDSFLPICRVNDFETADILCPKAKRTSRFLSGIINFIHFREACRETYMEFLWQYKSSADKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNQDFHQKTIVLQEGNSQKKSNISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNYKEKMKDTVQKLKNARQEVVEKYEIYGDSVDCLPSCQLEVQLYQKKIQDLSDNREKLASILKESLNLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTVIEDCNKVQEKRGAVYERVTTINQEIQKIKLGIQQLKDAAEREKLKSQEIFLNLKTALEKYHDGIEKAAEDSYAKIDEKTAELKRKMFKMST
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-------METLSFPR
-------CCCCCCCC		8.8422814378
5Phosphorylation---METLSFPRYNVA
---CCCCCCCCCCHH		40.3924719451
21UbiquitinationIVIHIRNKILTGADG
HHHHHHHHHHCCCCC		29.28-
29UbiquitinationILTGADGKNLTKNDL
HHCCCCCCCCCCCCC		49.7023000965
33UbiquitinationADGKNLTKNDLYPNP
CCCCCCCCCCCCCCC		52.1923000965
37PhosphorylationNLTKNDLYPNPKPEV
CCCCCCCCCCCCHHH		12.1127259358
57PhosphorylationMRALQIVYGIRLEHF
HHHHHHHHCCCCEEE		14.4124043423
67UbiquitinationRLEHFYMMPVNSEVM
CCEEEEEEECCCHHH		1.9821963094
69UbiquitinationEHFYMMPVNSEVMYP
EEEEEEECCCHHHCH		7.1822817900
113UbiquitinationTADILCPKAKRTSRF
CCCCCCCCCHHHHHH		66.5921963094
115UbiquitinationDILCPKAKRTSRFLS
CCCCCCCHHHHHHHH		63.4422817900
119UbiquitinationPKAKRTSRFLSGIIN
CCCHHHHHHHHHHHH		35.5921963094
151UbiquitinationQYKSSADKMQQLNAA
HHHCCHHHHHHHHHH		38.0229967540
155UbiquitinationSADKMQQLNAAHQEA
CHHHHHHHHHHHHHH		2.3722817900
165UbiquitinationAHQEALMKLERLDSV
HHHHHHHHHHHHCCC		48.3121906983
171PhosphorylationMKLERLDSVPVEEQE
HHHHHHCCCCHHHHH		32.6725159151
181UbiquitinationVEEQEEFKQLSDGIQ
HHHHHHHHHHHHHHH		54.3229967540
184PhosphorylationQEEFKQLSDGIQELQ
HHHHHHHHHHHHHHH		31.1520873877
188UbiquitinationKQLSDGIQELQQSLN
HHHHHHHHHHHHHHC		51.3722817900
193PhosphorylationGIQELQQSLNQDFHQ
HHHHHHHHHCCCHHH		19.1420873877
201UbiquitinationLNQDFHQKTIVLQEG
HCCCHHHHHHEEECC		31.4821906983
210PhosphorylationIVLQEGNSQKKSNIS
HEEECCCCHHCCCHH		54.9925159151
212UbiquitinationLQEGNSQKKSNISEK
EECCCCHHCCCHHHH		58.9729967540
213UbiquitinationQEGNSQKKSNISEKT
ECCCCHHCCCHHHHH		40.89-
234UbiquitinationKLSVVSLKEIQESLK
HHHEEEHHHHHHHHH		45.3122817900
239PhosphorylationSLKEIQESLKTKIVD
EHHHHHHHHHHCCCC		20.84-
241UbiquitinationKEIQESLKTKIVDSP
HHHHHHHHHCCCCCH		57.99-
242PhosphorylationEIQESLKTKIVDSPE
HHHHHHHHCCCCCHH		31.1523312004
243UbiquitinationIQESLKTKIVDSPEK
HHHHHHHCCCCCHHH		38.86-
247PhosphorylationLKTKIVDSPEKLKNY
HHHCCCCCHHHHHHH		24.8629255136
250UbiquitinationKIVDSPEKLKNYKEK
CCCCCHHHHHHHHHH		69.0529967540
261PhosphorylationYKEKMKDTVQKLKNA
HHHHHHHHHHHHHHH		21.2217924679
269UbiquitinationVQKLKNARQEVVEKY
HHHHHHHHHHHHHHH		42.4522817900
286UbiquitinationYGDSVDCLPSCQLEV
CCCCCCCCCCCHHHH		2.7922817900
287UbiquitinationGDSVDCLPSCQLEVQ
CCCCCCCCCCHHHHH		39.1122817900
289UbiquitinationSVDCLPSCQLEVQLY
CCCCCCCCHHHHHHH		5.1722817900
299UbiquitinationEVQLYQKKIQDLSDN
HHHHHHHHHHHCCCC		30.0329967540
304PhosphorylationQKKIQDLSDNREKLA
HHHHHHCCCCHHHHH		40.9225999147
309UbiquitinationDLSDNREKLASILKE
HCCCCHHHHHHHHHH		46.2229967540
312PhosphorylationDNREKLASILKESLN
CCHHHHHHHHHHHCC		38.6024719451
315UbiquitinationEKLASILKESLNLED
HHHHHHHHHHCCHHH		43.5221906983
317PhosphorylationLASILKESLNLEDQI
HHHHHHHHCCHHHHH		22.4429978859
326PhosphorylationNLEDQIESDESELKK
CHHHHHCCCHHHHHH		48.5929978859
329PhosphorylationDQIESDESELKKLKT
HHHCCCHHHHHHHHC		53.9029978859
332UbiquitinationESDESELKKLKTEEN
CCCHHHHHHHHCCCC		52.5921906983
333UbiquitinationSDESELKKLKTEENS
CCHHHHHHHHCCCCC		68.7722817900
335UbiquitinationESELKKLKTEENSFK
HHHHHHHHCCCCCCC		63.8722817900
342UbiquitinationKTEENSFKRLMIVKK
HCCCCCCCCEEEEEH		44.43-
348AcetylationFKRLMIVKKEKLATA
CCCEEEEEHHHHHHE		44.2724885425
356UbiquitinationKEKLATAQFKINKKH
HHHHHHEEEECCCCC		35.4927667366
358UbiquitinationKLATAQFKINKKHED
HHHHEEEECCCCCHH		33.0332015554
363UbiquitinationQFKINKKHEDVKQYK
EEECCCCCHHHHHHH		37.7922817900
367UbiquitinationNKKHEDVKQYKRTVI
CCCCHHHHHHHHHHH		61.3029967540
372PhosphorylationDVKQYKRTVIEDCNK
HHHHHHHHHHHHHHH		22.9929052541
379UbiquitinationTVIEDCNKVQEKRGA
HHHHHHHHHHHHHCC		52.1824816145
383UbiquitinationDCNKVQEKRGAVYER
HHHHHHHHHCCHHHH		38.75-
388PhosphorylationQEKRGAVYERVTTIN
HHHHCCHHHHHHHHH		9.4827642862
400UbiquitinationTINQEIQKIKLGIQQ
HHHHHHHHHHHHHHH		47.68-
401UbiquitinationINQEIQKIKLGIQQL
HHHHHHHHHHHHHHH		2.2627667366
402UbiquitinationNQEIQKIKLGIQQLK
HHHHHHHHHHHHHHH		47.9327667366
409UbiquitinationKLGIQQLKDAAEREK
HHHHHHHHHHHHHHH		40.7722817900
418UbiquitinationAAEREKLKSQEIFLN
HHHHHHHHHHHHHHH		62.25-
427UbiquitinationQEIFLNLKTALEKYH
HHHHHHHHHHHHHHH		30.5829967540
432UbiquitinationNLKTALEKYHDGIEK
HHHHHHHHHHHHHHH		49.0529967540
439UbiquitinationKYHDGIEKAAEDSYA
HHHHHHHHHHHHHHH		51.4829967540
447UbiquitinationAAEDSYAKIDEKTAE
HHHHHHHCCCHHHHH		42.3227667366
451UbiquitinationSYAKIDEKTAELKRK
HHHCCCHHHHHHHHH		49.65-
452PhosphorylationYAKIDEKTAELKRKM
HHCCCHHHHHHHHHH		24.2623090842
464PhosphorylationRKMFKMST-------
HHHHCCCC-------		38.8524719451
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 NUF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUF2_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 NUF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPC24_HUMANSPC24physical
22939629
SPC25_HUMANSPC25physical
22939629
NDC80_HUMANNDC80physical
14602875
AURKB_HUMANAURKBphysical
14602875
SDCB2_HUMANSDCBP2physical
21988832
I5P2_HUMANINPP5Bphysical
26496610
MYBB_HUMANMYBL2physical
26496610
SP100_HUMANSP100physical
26496610
CTDP1_HUMANCTDP1physical
26496610
PPIG_HUMANPPIGphysical
26496610
NDC80_HUMANNDC80physical
26496610
SRCAP_HUMANSRCAPphysical
26496610
KIF3A_HUMANKIF3Aphysical
26496610
ZWINT_HUMANZWINTphysical
26496610
PMF1_HUMANPMF1physical
26496610
NSL1_HUMANNSL1physical
26496610
HERC4_HUMANHERC4physical
26496610
CSN7A_HUMANCOPS7Aphysical
26496610
NSF1C_HUMANNSFL1Cphysical
26496610
KNL1_HUMANCASC5physical
26496610
SPC25_HUMANSPC25physical
26496610
MIS12_HUMANMIS12physical
26496610
DSN1_HUMANDSN1physical
26496610
ATG4A_HUMANATG4Aphysical
26496610
SPC24_HUMANSPC24physical
26496610
PKN3_HUMANPKN3physical
27173435
TFPT_HUMANTFPTphysical
27173435
YETS4_HUMANYEATS4physical
27173435
CLOCK_HUMANCLOCKphysical
27173435
PSMD9_HUMANPSMD9physical
27173435
VPS50_HUMANCCDC132physical
27173435
CAVN1_HUMANPTRFphysical
27173435
HAUS6_HUMANHAUS6physical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
BMAL1_HUMANARNTLphysical
27173435
RABX5_HUMANRABGEF1physical
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 NUF2_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-247, AND MASSSPECTROMETRY.
"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-247, 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-247, 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-247, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-261, AND MASSSPECTROMETRY.

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