CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000296
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Kinetochore protein NDC80 homolog 
Protein Synonyms/Alias
 Highly expressed in cancer protein; Kinetochore protein Hec1; HsHec1; Kinetochore-associated protein 2; Retinoblastoma-associated protein HEC 
Gene Name
 NDC80 
Gene Synonyms/Alias
 HEC; HEC1; KNTC2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
26LRSQDVNKQGLYTPQubiquitination[1, 2, 3]
35GLYTPQTKEKPTFGKubiquitination[3]
37YTPQTKEKPTFGKLSubiquitination[3]
47FGKLSINKPTSERKVubiquitination[3]
59RKVSLFGKRTSGHGSubiquitination[3]
89DPRPLNDKAFIQQCIubiquitination[3, 4]
123SLQAPSVKDFLKIFTubiquitination[3, 5]
127PSVKDFLKIFTFLYGubiquitination[3]
156EEVPRIFKDLGYPFAubiquitination[3]
255AELQSKLKDLFNVDAubiquitination[3]
264LFNVDAFKLESLEAKubiquitination[1, 3]
271KLESLEAKNRALNEQubiquitination[3]
300LESLRKLKASLQGDVubiquitination[3, 4]
309SLQGDVQKYQAYMSNubiquitination[3]
327HSAILDQKLNGLNEEubiquitination[1]
346ELECETIKQENTRLQubiquitination[3, 4]
360QNIIDNQKYSVADIEubiquitination[1, 3, 4, 6, 7]
393DLEAEQQKLWNEELKubiquitination[1, 3]
400KLWNEELKYARGKEAubiquitination[3]
405ELKYARGKEAIETQLubiquitination[1, 3]
417TQLAEYHKLARKLKLubiquitination[3]
433PKGAENSKGYDFEIKubiquitination[3]
452AGANCLVKYRAQVYVubiquitination[3]
462AQVYVPLKELLNETEubiquitination[1, 3]
504KRSVRTLKEEVQKLDubiquitination[3]
517LDDLYQQKIKEAEEEacetylation[8]
527EAEEEDEKCASELESacetylation[9]
606HLEEQIAKVDREYEEubiquitination[3]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 Acts as a component of the essential kinetochore- associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. 
Sequence Annotation
 REGION 1 445 Interaction with the N-terminus of CDCA1.
 REGION 1 250 Nuclear localization.
 REGION 128 251 Interaction with RB1.
 REGION 251 618 Interaction with NEK2 and ZWINT.
 REGION 251 431 Interaction with SMC1A.
 REGION 361 547 Interaction with PSMC2 and SMC1A.
 REGION 446 642 Interaction with the C-terminus of CDCA1
 MOD_RES 69 69 Phosphoserine.
 MOD_RES 165 165 Phosphoserine; by NEK2.  
Keyword
 3D-structure; Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Complete proteome; Kinetochore; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 642 AA 
Protein Sequence
MKRSSVSSGG AGRLSMQELR SQDVNKQGLY TPQTKEKPTF GKLSINKPTS ERKVSLFGKR 60
TSGHGSRNSQ LGIFSSSEKI KDPRPLNDKA FIQQCIRQLC EFLTENGYAH NVSMKSLQAP 120
SVKDFLKIFT FLYGFLCPSY ELPDTKFEEE VPRIFKDLGY PFALSKSSMY TVGAPHTWPH 180
IVAALVWLID CIKIHTAMKE SSPLFDDGQP WGEETEDGIM HNKLFLDYTI KCYESFMSGA 240
DSFDEMNAEL QSKLKDLFNV DAFKLESLEA KNRALNEQIA RLEQEREKEP NRLESLRKLK 300
ASLQGDVQKY QAYMSNLESH SAILDQKLNG LNEEIARVEL ECETIKQENT RLQNIIDNQK 360
YSVADIERIN HERNELQQTI NKLTKDLEAE QQKLWNEELK YARGKEAIET QLAEYHKLAR 420
KLKLIPKGAE NSKGYDFEIK FNPEAGANCL VKYRAQVYVP LKELLNETEE EINKALNKKM 480
GLEDTLEQLN AMITESKRSV RTLKEEVQKL DDLYQQKIKE AEEEDEKCAS ELESLEKHKH 540
LLESTVNQGL SEAMNELDAV QREYQLVVQT TTEERRKVGN NLQRLLEMVA THVGSVEKHL 600
EEQIAKVDRE YEECMSEDLS ENIKEIRDKY EKKATLIKSS EE 642 
Gene Ontology
 GO:0000942; C:condensed nuclear chromosome outer kinetochore; IDA:BHF-UCL.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031262; C:Ndc80 complex; IDA:UniProtKB.
 GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
 GO:0000070; P:mitotic sister chromatid segregation; TAS:ProtInc.
 GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
 GO:0048015; P:phosphatidylinositol-mediated signaling; NAS:UniProtKB. 
Interpro
 IPR005550; Kinetochore_Ndc80. 
Pfam
 PF03801; Ndc80_HEC 
SMART
  
PROSITE
  
PRINTS