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Protein

Kinetochore-associated protein 1

Gene

Kntc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex (By similarity).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-associated protein 1
Gene namesi
Name:Kntc1
Synonyms:Kiaa0166
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2673709. Kntc1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Chromosomecentromerekinetochore By similarity
  • Cytoplasmcytoskeletonspindle By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22072207Kinetochore-associated protein 1PRO_0000084313Add
BLAST

Proteomic databases

EPDiQ8C3Y4.
MaxQBiQ8C3Y4.
PaxDbiQ8C3Y4.
PeptideAtlasiQ8C3Y4.
PRIDEiQ8C3Y4.

PTM databases

iPTMnetiQ8C3Y4.
PhosphoSiteiQ8C3Y4.

Expressioni

Gene expression databases

BgeeiQ8C3Y4.
CleanExiMM_KNTC1.
ExpressionAtlasiQ8C3Y4. baseline and differential.
GenevisibleiQ8C3Y4. MM.

Interactioni

Subunit structurei

Interacts with ZW10. This interaction is required for stable association with the kinetochore. Component of the RZZ complex composed of KNTC1/ROD, ZW10 and ZWILCH (By similarity).By similarity

Protein-protein interaction databases

BioGridi228995. 2 interactions.
IntActiQ8C3Y4. 2 interactions.
MINTiMINT-8178482.
STRINGi10090.ENSMUSP00000031366.

Family & Domainsi

Phylogenomic databases

eggNOGiKOG4256. Eukaryota.
ENOG410YKFS. LUCA.
GeneTreeiENSGT00390000007883.
HOGENOMiHOG000001565.
HOVERGENiHBG052269.
InParanoidiQ8C3Y4.
KOiK11577.
OMAiREQGEDC.
OrthoDBiEOG7QNVK5.
PhylomeDBiQ8C3Y4.
TreeFamiTF101176.

Family and domain databases

InterProiIPR019527. RZZ-complex_KNTC1/ROD_C.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF10493. Rod_C. 1 hit.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8C3Y4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWNNIELLTS DDTGSGCLSV GSRKENVTAL YQADLLGKIS SEKTSLSPKI
60 70 80 90 100
QAFSLSHGFI IVADQSVILL DSICRSLQLF LIFDTDVDVV GLCQEGKFLF
110 120 130 140 150
VGERSGNFHL IYVTSKQTLF TKAFVEKALD ESQRTYRNLI IEKDGSNEGT
160 170 180 190 200
YYMLLLTNNG FFYITNLQLS QIEQAIENTD LDSAKKLQGQ FKCSFISTEN
210 220 230 240 250
YHSCLSLVAS QSGTFASKTS VIIGGTGSCA FSKWEPDSTK KEMSLKNFVG
260 270 280 290 300
TDIIKGAKSF QLIDNLLFVL DTDNVLSLWD AYTLTPVWNW PSLPVEQFVL
310 320 330 340 350
TTEADSPSSV TWQGITNLKL VTLTATAKEK MRSLIIYSLP SMETLYSLEV
360 370 380 390 400
SSVSSLVQTG ISTDTIYLLE GIHKNDPNLC EDSVSDLVLR YLTEVLPENR
410 420 430 440 450
LSRLLHKHRF AEAESFAIQF GLDVELVYKV KSNDMLEKLA LISSDKSEQS
460 470 480 490 500
KWQQLVDEAK ENLCKIQDDD FVVNFCLKAQ WVTYETTQEM LSYAKTRLMK
510 520 530 540 550
KEDRALPASS DAFMEVLKAH AKLTTFYGAF GPEKFSGSSW IEFLNNEDDL
560 570 580 590 600
RDVFLQLSEG NFACAQYLWL RHRADFESKF DVKMLENLLN SISTQFPLEN
610 620 630 640 650
LCSWFKNEVI PFVRRIVPEG QNILAKWLEQ ASRNLELTDK ANWPENGLQL
660 670 680 690 700
AEVFFTAEKT DRFGFASSWH WISLDYQNTE EVRQLRTLVS KLRELIILHR
710 720 730 740 750
KYNCKLALSD FEKENATTVV FRMFDRVSAP ELIPSVLEKS VRVYIREQNL
760 770 780 790 800
QEEELLLLYI EDLLKRCSSK SMTLFDTAWE AKAMAVIRCL SDTDLIFDAV
810 820 830 840 850
LKIMYKAVVP WSAAVEQLVK QHLEMDHPKV KLLQESYKLM EMKKLLRGYG
860 870 880 890 900
IREVNLLNKE IMRVIRYILK QDIPSSLEDA LKVAQGYRLS DDEIYSLRII
910 920 930 940 950
DLIDREQGGD CLLLLKSLPA AEAEKTAERV IIWARLALQE EPDGSEEDKA
960 970 980 990 1000
WRISVAKTSV DILKILCDIR KDNLQKKDES EEFLKRFQMV ASLQENFEVF
1010 1020 1030 1040 1050
LPFEDYSNTA LVAGLREQYI KAQEAAQAEH KHRGPPGPTP ARGTHLSIKS
1060 1070 1080 1090 1100
KLHRQALALQ VSEQELEAEL TLRALKDGKV VAALSKCRDL LKHYCNADTG
1110 1120 1130 1140 1150
RLLFVVCQKL CQMLADDVPM VAPGGLSLPS EIHDLACHAV TICSPDYLLD
1160 1170 1180 1190 1200
VLELSKYTLT AVELCRQCQM DDCGMLMKAA LGTHKDPYEE WSFSDFFSED
1210 1220 1230 1240 1250
GIVLESQVVL PVIYELISSV MPPAESKRHP LDSISLPYCS TSEGENRILP
1260 1270 1280 1290 1300
LVSSISALLR SLQECSQWEL ALRFVVGSFG TCLQHSMSNV MSISLSKQLL
1310 1320 1330 1340 1350
GKNTLANSRH IIMELKEKSI TFIRENATTL LHKVFNCRVV DLDLALAYCT
1360 1370 1380 1390 1400
LLPQKDVFDN LWKFIDKAWQ NYDKILALSL VGSQLANLYQ DIETGLWFHE
1410 1420 1430 1440 1450
LSIDAKWGIR LGKLGISFQP AFRQNFLTKK DLIKALVNNI DMDTSLILEY
1460 1470 1480 1490 1500
CSTFQLDSDA ALRLFIETLL RNTSSQSQGD AAPESTKHQH SKLLAKATEL
1510 1520 1530 1540 1550
VPLLKNTKDL VISLSEILYK LDPYDYEMID VVLKVLEQAN EKITSVNINQ
1560 1570 1580 1590 1600
ALNLLRHLKS YRRISPPVDH EYQYALEHMI TLPPAAHTRL PFHLILFGTA
1610 1620 1630 1640 1650
QNFWKILSSE LSEESLPTLL LIAKLMKFSL DTLYVSTAKH LFEKNLKPKL
1660 1670 1680 1690 1700
LKSAQARSST LMSKEVDKLM QTLESYLLSI VNPEWAVAIA ISLTQEVPEG
1710 1720 1730 1740 1750
PFKMSSLKFC LYLAERWLQN IPPQDETCEK AKALQKKLCL QVRLSGTEAV
1760 1770 1780 1790 1800
LIAHKLNDQE YLRVIGKPAH LIVSLYEHPS ISERLCTTSG KDYPDIHTAA
1810 1820 1830 1840 1850
KEIAEVNEVN LEKIWDMLLE KWLCPSTVPS EKASEFFELE EDEVLHRVVY
1860 1870 1880 1890 1900
LLQARPVDYC SRMLFVFATS ATSTLGMRQL TFAHKARALQ CLLYLADKET
1910 1920 1930 1940 1950
IESLFKKPIK EMKSYLKCIT FLASFETLNI PITYELFCNS PKEGMIKGLW
1960 1970 1980 1990 2000
KNHSHEPMAV RLVAELCLEY KIYDLQLWNG LLQKLLGFNM IPYLRKVLSC
2010 2020 2030 2040 2050
ISSIHSLWQV PYFSKAWQRV IQIPLLSASC PLRPSQLADC CDSLVAILEC
2060 2070 2080 2090 2100
PVSDDLDMMG VAKQYVQLDL PAFALTCLTL MPHSEKRHQQ IKNFLNSCDA
2110 2120 2130 2140 2150
RIILQQIEEH MNTGQLAGFS HQIGSLVLNH VVNKKEFGIL AKTKYFQLLK
2160 2170 2180 2190 2200
CHVINTGNVT ELVNYLANDF SVDEASALIN EYSKHCGKPV PADAAPCEIL

QTFLGGS
Length:2,207
Mass (Da):250,358
Last modified:November 8, 2005 - v2
Checksum:iCE217F32714D83D0
GO

Sequence cautioni

The sequence BAD32183.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2187 – 21871G → E in BAC39211 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK172905 mRNA. Translation: BAD32183.1. Different initiation.
AK084529 mRNA. Translation: BAC39211.1.
CCDSiCCDS39274.1.
RefSeqiNP_001035886.1. NM_001042421.1.
UniGeneiMm.441089.

Genome annotation databases

EnsembliENSMUST00000031366; ENSMUSP00000031366; ENSMUSG00000029414.
GeneIDi208628.
KEGGimmu:208628.
UCSCiuc008zoo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK172905 mRNA. Translation: BAD32183.1. Different initiation.
AK084529 mRNA. Translation: BAC39211.1.
CCDSiCCDS39274.1.
RefSeqiNP_001035886.1. NM_001042421.1.
UniGeneiMm.441089.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228995. 2 interactions.
IntActiQ8C3Y4. 2 interactions.
MINTiMINT-8178482.
STRINGi10090.ENSMUSP00000031366.

PTM databases

iPTMnetiQ8C3Y4.
PhosphoSiteiQ8C3Y4.

Proteomic databases

EPDiQ8C3Y4.
MaxQBiQ8C3Y4.
PaxDbiQ8C3Y4.
PeptideAtlasiQ8C3Y4.
PRIDEiQ8C3Y4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031366; ENSMUSP00000031366; ENSMUSG00000029414.
GeneIDi208628.
KEGGimmu:208628.
UCSCiuc008zoo.1. mouse.

Organism-specific databases

CTDi9735.
MGIiMGI:2673709. Kntc1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG4256. Eukaryota.
ENOG410YKFS. LUCA.
GeneTreeiENSGT00390000007883.
HOGENOMiHOG000001565.
HOVERGENiHBG052269.
InParanoidiQ8C3Y4.
KOiK11577.
OMAiREQGEDC.
OrthoDBiEOG7QNVK5.
PhylomeDBiQ8C3Y4.
TreeFamiTF101176.

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

PROiQ8C3Y4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C3Y4.
CleanExiMM_KNTC1.
ExpressionAtlasiQ8C3Y4. baseline and differential.
GenevisibleiQ8C3Y4. MM.

Family and domain databases

InterProiIPR019527. RZZ-complex_KNTC1/ROD_C.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF10493. Rod_C. 1 hit.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic intestine.
  2. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 839-843 AND 1650-1657, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  3. "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] OF 1484-2207.
    Strain: C57BL/6J.
    Tissue: Heart.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiKNTC1_MOUSE
AccessioniPrimary (citable) accession number: Q8C3Y4
Secondary accession number(s): Q6A0B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 8, 2005
Last modified: July 6, 2016
This is version 103 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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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.