NDC80_HUMAN - dbPTM
NDC80_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDC80_HUMAN
UniProt AC O14777
Protein Name Kinetochore protein NDC80 homolog
Gene Name NDC80
Organism Homo sapiens (Human).
Sequence Length 642
Subcellular Localization Nucleus. Chromosome, centromere, kinetochore. Localizes to kinetochores from late prophase to anaphase. Localizes specifically to the outer plate of the kinetochore.
Protein Description Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. [PubMed: 9315664]
Protein Sequence MKRSSVSSGGAGRLSMQELRSQDVNKQGLYTPQTKEKPTFGKLSINKPTSERKVSLFGKRTSGHGSRNSQLGIFSSSEKIKDPRPLNDKAFIQQCIRQLCEFLTENGYAHNVSMKSLQAPSVKDFLKIFTFLYGFLCPSYELPDTKFEEEVPRIFKDLGYPFALSKSSMYTVGAPHTWPHIVAALVWLIDCIKIHTAMKESSPLFDDGQPWGEETEDGIMHNKLFLDYTIKCYESFMSGADSFDEMNAELQSKLKDLFNVDAFKLESLEAKNRALNEQIARLEQEREKEPNRLESLRKLKASLQGDVQKYQAYMSNLESHSAILDQKLNGLNEEIARVELECETIKQENTRLQNIIDNQKYSVADIERINHERNELQQTINKLTKDLEAEQQKLWNEELKYARGKEAIETQLAEYHKLARKLKLIPKGAENSKGYDFEIKFNPEAGANCLVKYRAQVYVPLKELLNETEEEINKALNKKMGLEDTLEQLNAMITESKRSVRTLKEEVQKLDDLYQQKIKEAEEEDEKCASELESLEKHKHLLESTVNQGLSEAMNELDAVQREYQLVVQTTTEERRKVGNNLQRLLEMVATHVGSVEKHLEEQIAKVDREYEECMSEDLSENIKEIRDKYEKKATLIKSSEE
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
4Phosphorylation----MKRSSVSSGGA
----CCCCCCCCCCC
29.5825849741
5Phosphorylation---MKRSSVSSGGAG
---CCCCCCCCCCCC
30.0125849741
7Phosphorylation-MKRSSVSSGGAGRL
-CCCCCCCCCCCCCC
25.8026699800
8PhosphorylationMKRSSVSSGGAGRLS
CCCCCCCCCCCCCCC
38.8126699800
15PhosphorylationSGGAGRLSMQELRSQ
CCCCCCCCHHHHHCC
19.6321815630
20DimethylationRLSMQELRSQDVNKQ
CCCHHHHHCCCCHHC
31.36-
20MethylationRLSMQELRSQDVNKQ
CCCHHHHHCCCCHHC
31.3624377289
26UbiquitinationLRSQDVNKQGLYTPQ
HHCCCCHHCCCCCCC
45.6621890473
30PhosphorylationDVNKQGLYTPQTKEK
CCHHCCCCCCCCCCC
24.1725159151
31PhosphorylationVNKQGLYTPQTKEKP
CHHCCCCCCCCCCCC
17.6022199227
34PhosphorylationQGLYTPQTKEKPTFG
CCCCCCCCCCCCCCC
42.2322199227
35UbiquitinationGLYTPQTKEKPTFGK
CCCCCCCCCCCCCCC
59.50-
37UbiquitinationYTPQTKEKPTFGKLS
CCCCCCCCCCCCCCC
51.41-
39PhosphorylationPQTKEKPTFGKLSIN
CCCCCCCCCCCCCCC
56.9720860994
42UbiquitinationKEKPTFGKLSINKPT
CCCCCCCCCCCCCCC
34.57-
44PhosphorylationKPTFGKLSINKPTSE
CCCCCCCCCCCCCCC
27.8317129782
47UbiquitinationFGKLSINKPTSERKV
CCCCCCCCCCCCCEE
48.26-
49PhosphorylationKLSINKPTSERKVSL
CCCCCCCCCCCEEEE
44.8425159151
50PhosphorylationLSINKPTSERKVSLF
CCCCCCCCCCEEEEC
43.8825159151
53AcetylationNKPTSERKVSLFGKR
CCCCCCCEEEECCCC
31.937976623
55PhosphorylationPTSERKVSLFGKRTS
CCCCCEEEECCCCCC
22.4822617229
59UbiquitinationRKVSLFGKRTSGHGS
CEEEECCCCCCCCCC
45.21-
59MethylationRKVSLFGKRTSGHGS
CEEEECCCCCCCCCC
45.217976633
59AcetylationRKVSLFGKRTSGHGS
CEEEECCCCCCCCCC
45.217976633
61PhosphorylationVSLFGKRTSGHGSRN
EEECCCCCCCCCCCC
42.4125159151
62PhosphorylationSLFGKRTSGHGSRNS
EECCCCCCCCCCCCC
32.5925159151
66PhosphorylationKRTSGHGSRNSQLGI
CCCCCCCCCCCCCCC
23.7125159151
69PhosphorylationSGHGSRNSQLGIFSS
CCCCCCCCCCCCCCC
26.1819664994
75PhosphorylationNSQLGIFSSSEKIKD
CCCCCCCCCCCCCCC
30.9130266825
76PhosphorylationSQLGIFSSSEKIKDP
CCCCCCCCCCCCCCC
31.5923401153
77PhosphorylationQLGIFSSSEKIKDPR
CCCCCCCCCCCCCCC
41.5330266825
81UbiquitinationFSSSEKIKDPRPLND
CCCCCCCCCCCCCCH
73.14-
89UbiquitinationDPRPLNDKAFIQQCI
CCCCCCHHHHHHHHH
44.09-
123UbiquitinationSLQAPSVKDFLKIFT
CCCCCCHHHHHHHHH
47.2921890473
127UbiquitinationPSVKDFLKIFTFLYG
CCHHHHHHHHHHHHH
35.45-
153MethylationKFEEEVPRIFKDLGY
CHHHHHHHHHHHHCC
52.75115478397
156UbiquitinationEEVPRIFKDLGYPFA
HHHHHHHHHHCCCEE
50.07-
165PhosphorylationLGYPFALSKSSMYTV
HCCCEEECCCCCCCC
27.3618297113
201PhosphorylationIHTAMKESSPLFDDG
HHHHHHHCCCCCCCC
31.5625159151
202PhosphorylationHTAMKESSPLFDDGQ
HHHHHHCCCCCCCCC
27.0629523821
242PhosphorylationSFMSGADSFDEMNAE
HHHCCCCCHHHHHHH
33.78-
253UbiquitinationMNAELQSKLKDLFNV
HHHHHHHHHHHHHCC
46.74-
255UbiquitinationAELQSKLKDLFNVDA
HHHHHHHHHHHCCCH
57.00-
264UbiquitinationLFNVDAFKLESLEAK
HHCCCHHHHHHHHHH
53.7321890473
271UbiquitinationKLESLEAKNRALNEQ
HHHHHHHHHHHHHHH
37.28-
300UbiquitinationLESLRKLKASLQGDV
HHHHHHHHHHHHHCH
38.68-
309UbiquitinationSLQGDVQKYQAYMSN
HHHHCHHHHHHHHHC
38.90-
327UbiquitinationHSAILDQKLNGLNEE
CHHHHHHHHCCCCHH
43.5221890473
344PhosphorylationRVELECETIKQENTR
HHHHHHHHHHCCCHH
45.1730108239
346UbiquitinationELECETIKQENTRLQ
HHHHHHHHCCCHHHH
60.00-
350PhosphorylationETIKQENTRLQNIID
HHHHCCCHHHHHHHC
31.8130108239
360UbiquitinationQNIIDNQKYSVADIE
HHHHCCCCCCHHHHH
45.8321890473
361PhosphorylationNIIDNQKYSVADIER
HHHCCCCCCHHHHHH
9.90-
382UbiquitinationELQQTINKLTKDLEA
HHHHHHHHHHHHHHH
54.40-
393UbiquitinationDLEAEQQKLWNEELK
HHHHHHHHHHHHHHH
55.98-
400UbiquitinationKLWNEELKYARGKEA
HHHHHHHHHHHHHHH
39.89-
405UbiquitinationELKYARGKEAIETQL
HHHHHHHHHHHHHHH
38.1221890473
410PhosphorylationRGKEAIETQLAEYHK
HHHHHHHHHHHHHHH
23.8321406692
415PhosphorylationIETQLAEYHKLARKL
HHHHHHHHHHHHHHC
9.9221406692
417UbiquitinationTQLAEYHKLARKLKL
HHHHHHHHHHHHCCC
42.83-
433UbiquitinationPKGAENSKGYDFEIK
CCCCCCCCCCCEEEE
73.42-
452UbiquitinationAGANCLVKYRAQVYV
CCCCCEEEEEEEEEE
18.97-
458PhosphorylationVKYRAQVYVPLKELL
EEEEEEEEEEHHHHH
5.5822817900
462UbiquitinationAQVYVPLKELLNETE
EEEEEEHHHHHHHCH
40.0021890473
474UbiquitinationETEEEINKALNKKMG
HCHHHHHHHHHHHCC
60.97-
485PhosphorylationKKMGLEDTLEQLNAM
HHCCHHHHHHHHHHH
23.8729759185
494PhosphorylationEQLNAMITESKRSVR
HHHHHHHHHHHHHHH
22.5620860994
496PhosphorylationLNAMITESKRSVRTL
HHHHHHHHHHHHHHH
25.3929759185
499PhosphorylationMITESKRSVRTLKEE
HHHHHHHHHHHHHHH
21.4920860994
502PhosphorylationESKRSVRTLKEEVQK
HHHHHHHHHHHHHHH
39.7720860994
504UbiquitinationKRSVRTLKEEVQKLD
HHHHHHHHHHHHHHH
51.74-
509UbiquitinationTLKEEVQKLDDLYQQ
HHHHHHHHHHHHHHH
60.09-
517UbiquitinationLDDLYQQKIKEAEEE
HHHHHHHHHHHHHHH
39.97-
517AcetylationLDDLYQQKIKEAEEE
HHHHHHHHHHHHHHH
39.9723236377
527AcetylationEAEEEDEKCASELES
HHHHHHHHHHHHHHH
47.6320167786
530PhosphorylationEEDEKCASELESLEK
HHHHHHHHHHHHHHH
52.7827251275
534PhosphorylationKCASELESLEKHKHL
HHHHHHHHHHHHHHH
55.2221815630
591PhosphorylationRLLEMVATHVGSVEK
HHHHHHHHHHHHHHH
12.99-
595PhosphorylationMVATHVGSVEKHLEE
HHHHHHHHHHHHHHH
26.4727251275
606UbiquitinationHLEEQIAKVDREYEE
HHHHHHHHHHHHHHH
46.42-
611PhosphorylationIAKVDREYEECMSED
HHHHHHHHHHHHCCC
20.2327642862
616PhosphorylationREYEECMSEDLSENI
HHHHHHHCCCHHHHH
39.3528348404
639PhosphorylationKKATLIKSSEE----
HHHHHHHCCCC----
35.6724719451

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
5SPhosphorylationKinaseAURKBQ96GD4
GPS
15SPhosphorylationKinaseAURKBQ96GD4
GPS
44SPhosphorylationKinaseAURKAO14965
GPS
44SPhosphorylationKinaseAURKBQ96GD4
GPS
49TPhosphorylationKinaseAURKBQ96GD4
GPS
55SPhosphorylationKinaseAURKAO14965
GPS
55SPhosphorylationKinaseAURKBQ96GD4
GPS
69SPhosphorylationKinaseAURKAO14965
GPS
69SPhosphorylationKinaseAURKBQ96GD4
GPS
165SPhosphorylationKinaseNEK1Q96PY6
PSP
165SPhosphorylationKinaseNEK2P51955
Uniprot
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:21199005

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDC80_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 NDC80_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BL1S6_HUMANBLOC1S6physical
16189514
KLH12_HUMANKLHL12physical
16189514
WASC3_HUMANCCDC53physical
16189514
USBP1_HUMANUSHBP1physical
16189514
AMOL2_HUMANAMOTL2physical
16189514
CACO1_HUMANCALCOCO1physical
16189514
SPC24_HUMANSPC24physical
14699129
SPC25_HUMANSPC25physical
14699129
NUF2_HUMANNUF2physical
14699129
TM1L1_HUMANTOM1L1physical
16169070
NEK2_HUMANNEK2physical
12386167
KIN3_YEASTKIN3physical
12386167
NEK2_HUMANNEK2physical
9295362
PRS7_HUMANPSMC2physical
9295362
NDC80_HUMANNDC80physical
20360068
SPC24_HUMANSPC24physical
20360068
SPC25_HUMANSPC25physical
20360068
NUF2_HUMANNUF2physical
20360068
SPC25_HUMANSPC25physical
22939629
NUF2_HUMANNUF2physical
22939629
SPC24_HUMANSPC24physical
22939629
NSL1_HUMANNSL1physical
22939629
PLK1_HUMANPLK1physical
22939629
SKA1_HUMANSKA1physical
17093495
NUF2_HUMANNUF2physical
14602875
NDC80_HUMANNDC80physical
14602875
AURKB_HUMANAURKBphysical
14602875
CENPH_HUMANCENPHphysical
15713649
NDC80_HUMANNDC80physical
25416956
TFP11_HUMANTFIP11physical
25416956
MED4_HUMANMED4physical
25416956
WASC3_HUMANCCDC53physical
25416956
CCHCR_HUMANCCHCR1physical
25416956
CACO1_HUMANCALCOCO1physical
25416956
NDEL1_HUMANNDEL1physical
25416956
IFT20_HUMANIFT20physical
25416956
SGF29_HUMANCCDC101physical
25416956
HAUS1_HUMANHAUS1physical
25416956
SFR1_HUMANSFR1physical
25416956
KLC3_HUMANKLC3physical
25416956
TXLNA_HUMANTXLNAphysical
25416956
RUFY4_HUMANRUFY4physical
25416956
PLSI_HUMANPLS1physical
26344197

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 NDC80_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-31; THR-34; SER-44;SER-55 AND SER-69, AND MASS SPECTROMETRY.
"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-55; SER-62; SER-76 ANDSER-77, AND MASS SPECTROMETRY.
"Phosphorylation of the mitotic regulator protein Hec1 by Nek2 kinaseis essential for faithful chromosome segregation.";
Chen Y., Riley D.J., Zheng L., Chen P.-L., Lee W.-H.;
J. Biol. Chem. 277:49408-49416(2002).
Cited for: INTERACTION WITH NEK2, AND PHOSPHORYLATION AT SER-165 BY NEK2.

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