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Protein

Kinetochore protein Nuf2

Gene

Nuf2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinetochore protein Nuf2
Alternative name(s):
Cell division cycle-associated protein 1
Gene namesi
Name:Nuf2
Synonyms:Cdca1, Nuf2r
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1914227. Nuf2.

Subcellular locationi

  • Nucleus By similarity
  • Chromosomecentromerekinetochore By similarity

  • Note: Localizes to kinetochores from late prophase to anaphase. Localizes specifically to the outer plate of the kinetochore (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Kinetochore protein Nuf2PRO_0000249814Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei247 – 2471PhosphoserineCombined sources

Post-translational modificationi

Can be phosphorylated by AURKA and AURKB.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99P69.
MaxQBiQ99P69.
PaxDbiQ99P69.
PRIDEiQ99P69.

Expressioni

Gene expression databases

BgeeiQ99P69.
ExpressionAtlasiQ99P69. baseline and differential.
GenevisibleiQ99P69. MM.

Interactioni

Subunit structurei

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028000.

Structurei

3D structure databases

ProteinModelPortaliQ99P69.
SMRiQ99P69. Positions 4-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 385385Interaction with the N-terminus of NDC80By similarityAdd
BLAST
Regioni386 – 46378Interaction with the C-terminus of NDC80 and the SPBC24-SPBC25 subcomplexBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili149 – 341193Sequence analysisAdd
BLAST
Coiled coili389 – 46375Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the NUF2 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4438. Eukaryota.
ENOG410ZI4C. LUCA.
GeneTreeiENSGT00390000004199.
HOGENOMiHOG000290701.
HOVERGENiHBG082069.
InParanoidiQ99P69.
KOiK11548.
OMAiDCYAKID.
OrthoDBiEOG76T9TP.
PhylomeDBiQ99P69.
TreeFamiTF101067.

Family and domain databases

InterProiIPR005549. Kinetochore_Nuf2.
[Graphical view]
PfamiPF03800. Nuf2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99P69-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
METLSFPRYN VAELVVHIRN KLLTGADGKN LSKSDFLPNP KSDVLYMIYM
60 70 80 90 100
KALQLVYGVR LEHFYMMPMN IEVTYPHLME GFLPVRSLFF YMDSFMPICR
110 120 130 140 150
VNDFEIVDIL NPRTNRTSRF LSGIINFIHF RETCLEKCEE FLLQNKSSMV
160 170 180 190 200
RMQQLSNVHQ EALMKLEKLN TVPAEEREEF KQFMDDIQEL QHLLNEEFRQ
210 220 230 240 250
KTTLLQEEYA KMKSDISEKT KHLNEQKLSL VSLKEVEDNL KSKIVDSPEK
260 270 280 290 300
LKNYKDKMKG TVQKLRSARE KVMEQYDIYR DSVDCLPSCQ LEVQLYQKKS
310 320 330 340 350
QDLADNREKL SSLLKESLNL EDQIESDSSE LKKLKTEENS LIRMTTVKKE
360 370 380 390 400
KLATARFKIN KKQEDVKHYK QAMIEDCNKV QEKRDAVCEQ VTTVNQEIHK
410 420 430 440 450
IKSAIQQLRD TKKREILKSQ EIFVNLKSAL EKYHEGIEKV AEERSAKLEE
460
KTAELKKRMV RMV
Length:463
Mass (Da):54,594
Last modified:September 19, 2006 - v2
Checksum:i7330FFDB6E28AEAC
GO
Isoform 2 (identifier: Q99P69-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     270-296: EKVMEQYDIYRDSVDCLPSCQLEVQLY → VSRFTLWHSLNYLVSVQISLLNFYAPL
     297-429: Missing.

Note: No experimental confirmation available.
Show »
Length:330
Mass (Da):39,010
Checksum:iC9A4AE4C35703D4B
GO

Sequence cautioni

The sequence BAC41008.1 differs from that shown. Reason: Frameshift at position 63. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41L → W in BAC41008 (PubMed:16141072).Curated
Sequence conflicti61 – 611L → R in BAC41008 (PubMed:16141072).Curated
Sequence conflicti101 – 1011V → G in BAB27973 (PubMed:16141072).Curated
Sequence conflicti137 – 1371K → E in AAK01427 (PubMed:11266451).Curated
Sequence conflicti144 – 1441Q → P in BAC41008 (PubMed:16141072).Curated
Sequence conflicti157 – 1571N → H in BAC41008 (PubMed:16141072).Curated
Sequence conflicti221 – 2211K → Q in BAC41008 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei270 – 29627EKVME…EVQLY → VSRFTLWHSLNYLVSVQISL LNFYAPL in isoform 2. 1 PublicationVSP_020553Add
BLAST
Alternative sequencei297 – 429133Missing in isoform 2. 1 PublicationVSP_020554Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF326732 mRNA. Translation: AAK01427.1.
AK012011 mRNA. Translation: BAB27973.1.
AK089939 mRNA. Translation: BAC41008.1. Frameshift.
AK132467 mRNA. Translation: BAE21183.1.
AK162249 mRNA. Translation: BAE36815.1.
BC020026 mRNA. Translation: AAH20026.1.
CCDSiCCDS15463.1. [Q99P69-1]
RefSeqiNP_075773.2. NM_023284.3. [Q99P69-1]
XP_006497021.1. XM_006496958.1. [Q99P69-1]
UniGeneiMm.151315.

Genome annotation databases

EnsembliENSMUST00000028000; ENSMUSP00000028000; ENSMUSG00000026683. [Q99P69-1]
ENSMUST00000111368; ENSMUSP00000106999; ENSMUSG00000026683. [Q99P69-1]
GeneIDi66977.
KEGGimmu:66977.
UCSCiuc007dlj.1. mouse. [Q99P69-1]
uc007dll.1. mouse. [Q99P69-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF326732 mRNA. Translation: AAK01427.1.
AK012011 mRNA. Translation: BAB27973.1.
AK089939 mRNA. Translation: BAC41008.1. Frameshift.
AK132467 mRNA. Translation: BAE21183.1.
AK162249 mRNA. Translation: BAE36815.1.
BC020026 mRNA. Translation: AAH20026.1.
CCDSiCCDS15463.1. [Q99P69-1]
RefSeqiNP_075773.2. NM_023284.3. [Q99P69-1]
XP_006497021.1. XM_006496958.1. [Q99P69-1]
UniGeneiMm.151315.

3D structure databases

ProteinModelPortaliQ99P69.
SMRiQ99P69. Positions 4-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028000.

Proteomic databases

EPDiQ99P69.
MaxQBiQ99P69.
PaxDbiQ99P69.
PRIDEiQ99P69.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028000; ENSMUSP00000028000; ENSMUSG00000026683. [Q99P69-1]
ENSMUST00000111368; ENSMUSP00000106999; ENSMUSG00000026683. [Q99P69-1]
GeneIDi66977.
KEGGimmu:66977.
UCSCiuc007dlj.1. mouse. [Q99P69-1]
uc007dll.1. mouse. [Q99P69-2]

Organism-specific databases

CTDi83540.
MGIiMGI:1914227. Nuf2.

Phylogenomic databases

eggNOGiKOG4438. Eukaryota.
ENOG410ZI4C. LUCA.
GeneTreeiENSGT00390000004199.
HOGENOMiHOG000290701.
HOVERGENiHBG082069.
InParanoidiQ99P69.
KOiK11548.
OMAiDCYAKID.
OrthoDBiEOG76T9TP.
PhylomeDBiQ99P69.
TreeFamiTF101067.

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.

Miscellaneous databases

NextBioi323196.
PROiQ99P69.
SOURCEiSearch...

Gene expression databases

BgeeiQ99P69.
ExpressionAtlasiQ99P69. baseline and differential.
GenevisibleiQ99P69. MM.

Family and domain databases

InterProiIPR005549. Kinetochore_Nuf2.
[Graphical view]
PfamiPF03800. Nuf2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Colon, Egg and Skin.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: Czech II.
    Tissue: Mammary tumor.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung.

Entry informationi

Entry nameiNUF2_MOUSE
AccessioniPrimary (citable) accession number: Q99P69
Secondary accession number(s): Q8BTK7, Q8VE05, Q9CST5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: September 19, 2006
Last modified: March 16, 2016
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.