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Reviewed, UniProtKB/Swiss-Prot Q9BZD4 (NUF2_HUMAN)

Last modified July 7, 2009. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Kinetochore protein Nuf2
      Short name=hsNuf2
      Short name=hNuf2
      Short name=hNuf2R
Alternative name(s):
    Cell division cycle-associated protein 1
Gene names
Name: NUF2
Synonyms: CDCA1, NUF2R
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.14

Subunit structure

Component of the NDC80 complex, which consists of NDC80/HEC1, CDCA1, SPBC24 and SPBC25. The NDC80 complex is formed by two subcomplexes composed of NDC80/HEC1-CDCA1 and SPBC24-SPBC25. Each subcomplex is formed by parallel interactions through the coiled-coil domains of individual subunits. Formation of a tetrameric complex is mediated by interactions between the C-terminal regions of both subunits of the NDC80/HEC1-CDCA1 subcomplex and the N-terminal regions of both subunits of the SPBC24-SPBC25 complex. The tetrameric NDC80 complex has an elongated rod-like structure with globular domains at either end. May interact with AURKB/Aurora-B.

Subcellular location

Nucleus. Kinetochore. Note: Localizes to kinetochores from late prophase to anaphase. Localizes specifically to the outer plate of the kinetochore. Ref.7 Ref.8 Ref.10 Ref.13

Post-translational modification

Can be phosphorylated by AURKA and AURKB. Ref.12 Ref.15 Ref.16 Ref.17 Ref.18

Sequence similarities

Belongs to the NUF2 family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentKinetochore
Nucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

chromosome segregation Ref.2

Non-traceable author statement. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcondensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding Ref.13

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Kinetochore protein Nuf2
PRO_0000249813

Regions

Region1 – 385385Interaction with the N-terminus of NDC80
Region386 – 46479Interaction with the C-terminus of NDC80 and the SPBC24-SPBC25 subcomplex
Coiled coil147 – 345199 Potential
Coiled coil389 – 45971 Potential

Amino acid modifications

Modified residue2471Phosphoserine Ref.15 Ref.16 Ref.18
Modified residue2611Phosphothreonine Ref.17

Natural variations

Natural variant2291S → L: dbSNP rs11802875. Ref.1 Ref.2
VAR_027490
Natural variant2391S → R: dbSNP rs16852767.
VAR_027491

Sequences

Sequence LengthMass (Da)Tools
Q9BZD4-1 [UniParc].

Last modified September 19, 2006. Version 2.
Checksum: 250BFED5AD87153B

FASTA46454,304
        10         20         30         40         50         60 
METLSFPRYN VAEIVIHIRN KILTGADGKN LTKNDLYPNP KPEVLHMIYM RALQIVYGIR 

        70         80         90        100        110        120 
LEHFYMMPVN SEVMYPHLME GFLPFSNLVT HLDSFLPICR VNDFETADIL CPKAKRTSRF 

       130        140        150        160        170        180 
LSGIINFIHF REACRETYME FLWQYKSSAD KMQQLNAAHQ EALMKLERLD SVPVEEQEEF 

       190        200        210        220        230        240 
KQLSDGIQEL QQSLNQDFHQ KTIVLQEGNS QKKSNISEKT KRLNELKLSV VSLKEIQESL 

       250        260        270        280        290        300 
KTKIVDSPEK LKNYKEKMKD TVQKLKNARQ EVVEKYEIYG DSVDCLPSCQ LEVQLYQKKI 

       310        320        330        340        350        360 
QDLSDNREKL ASILKESLNL EDQIESDESE LKKLKTEENS FKRLMIVKKE KLATAQFKIN 

       370        380        390        400        410        420 
KKHEDVKQYK RTVIEDCNKV QEKRGAVYER VTTINQEIQK IKLGIQQLKD AAEREKLKSQ 

       430        440        450        460 
EIFLNLKTAL EKYHDGIEKA AEDSYAKIDE KTAELKRKMF KMST 

« Hide

References

« Hide 'large scale' references
[1]"A conserved protein, Nuf2, is implicated in connecting the centromere to the spindle during chromosome segregation: a link between the kinetochore function and the spindle checkpoint."
Nabetani A., Koujin T., Tsutsumi C., Haraguchi T., Hiraoka Y.
Chromosoma 110:322-334(2001) [PubMed: 11685532] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-229.
[2]"The Ndc80p complex from Saccharomyces cerevisiae contains conserved centromere components and has a function in chromosome segregation."
Wigge P.A., Kilmartin J.V.
J. Cell Biol. 152:349-360(2001) [PubMed: 11266451] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-229.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Chronic myeloid leukemia cell and Lung.
[6]"hNuf2 inhibition blocks stable kinetochore-microtubule attachment and induces mitotic cell death in HeLa cells."
DeLuca J.G., Moree B., Hickey J.M., Kilmartin J.V., Salmon E.D.
J. Cell Biol. 159:549-555(2002) [PubMed: 12438418] [Abstract]
Cited for: FUNCTION.
[7]"Nuf2 and Hec1 are required for retention of the checkpoint proteins Mad1 and Mad2 to kinetochores."
DeLuca J.G., Howell B.J., Canman J.C., Hickey J.M., Fang G., Salmon E.D.
Curr. Biol. 13:2103-2109(2003) [PubMed: 14654001] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Kinetochore localization and microtubule interaction of the human spindle checkpoint kinase Mps1."
Stucke V.M., Baumann C., Nigg E.A.
Chromosoma 113:1-15(2004) [PubMed: 15235793] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo."
Joseph J., Liu S.-T., Jablonski S.A., Yen T.J., Dasso M.
Curr. Biol. 14:611-617(2004) [PubMed: 15062103] [Abstract]
Cited for: FUNCTION.
[10]"Timing and checkpoints in the regulation of mitotic progression."
Meraldi P., Draviam V.M., Sorger P.K.
Dev. Cell 7:45-60(2004) [PubMed: 15239953] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"Identification of two novel components of the human NDC80 kinetochore complex."
Bharadwaj R., Qi W., Yu H.
J. Biol. Chem. 279:13076-13085(2004) [PubMed: 14699129] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NDC80 COMPLEX.
[12]"Identification of the substrates and interaction proteins of aurora kinases from a protein-protein interaction model."
Tien A.-C., Lin M.-H., Su L.-J., Hong Y.-R., Cheng T.-S., Lee Y.-C.G., Lin W.-J., Still I.H., Huang C.-Y.F.
Mol. Cell. Proteomics 3:93-104(2004) [PubMed: 14602875] [Abstract]
Cited for: INTERACTION WITH AURKB AND NDC80, PHOSPHORYLATION BY AURKA AND AURKB.
[13]"Architecture of the human Ndc80-Hec1 complex, a critical constituent of the outer kinetochore."
Ciferri C., De Luca J., Monzani S., Ferrari K.J., Ristic D., Wyman C., Stark H., Kilmartin J., Salmon E.D., Musacchio A.
J. Biol. Chem. 280:29088-29095(2005) [PubMed: 15961401] [Abstract]
Cited for: CHARACTERIZATION OF THE NDC80 COMPLEX, SUBCELLULAR LOCATION.
[14]"Hec1 and Nuf2 are core components of the kinetochore outer plate essential for organizing microtubule attachment sites."
DeLuca J.G., Dong Y., Hergert P., Strauss J., Hickey J.M., Salmon E.D., McEwen B.F.
Mol. Biol. Cell 16:519-531(2005) [PubMed: 15548592] [Abstract]
Cited for: FUNCTION.
[15]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, MASS SPECTROMETRY.
Tissue: Epithelium.
[16]"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) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, MASS SPECTROMETRY.
Tissue: Epithelium.
[17]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells 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) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-261, MASS SPECTROMETRY.
Tissue: Epithelium.
[18]"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) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, MASS SPECTROMETRY.
[19]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB050577 mRNA. Translation: BAB59141.1.
AB050578 mRNA. Translation: BAB59142.1.
AF326731 mRNA. Translation: AAK01426.1.
AK093348 mRNA. Translation: BAC04140.1.
AL592435 Genomic DNA. Translation: CAI16706.1.
BC008489 mRNA. Translation: AAH08489.1.
BC021171 mRNA. Translation: AAH21171.2.
IPIIPI00305887.
RefSeqNP_113611.2.
NP_663735.2.
UniGeneHs.651950

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2VE7X-ray2.88C/D1-169[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9BZD4. 6 interactions.

PTM databases

PhosphoSiteQ9BZD4.

Proteomic databases

PeptideAtlasQ9BZD4.
PRIDEQ9BZD4.

Genome annotation databases

EnsemblENSG00000143228. Homo sapiens. [Contig view]
GeneID83540.
KEGGhsa:83540.
UCSCuc001gcq.1. human.

Organism-specific databases

GeneCardsGC01P161559.
HGNCHGNC:14621. NUF2.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9BZD4.
OMAQ9BZD4. DILYPKA.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpressQ9BZD4.
BgeeQ9BZD4.
CleanExHS_NUF2.
GermOnlineENSG00000143228. Homo sapiens.

Family and domain databases

InterProIPR005549. Kinetochore_Nuf2.
[Graphical view]
PANTHERPTHR21650:SF2. Nuf2. 1 hit.
PfamPF03800. Nuf2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio72453.

Entry information

Entry nameNUF2_HUMAN
AccessionPrimary (citable) accession number: Q9BZD4
Secondary accession number(s): Q8WU69, Q96HJ4, Q96Q78
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: September 19, 2006
Last modified: July 7, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents