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Protein

Small kinetochore-associated protein

Gene

Knstrn

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

Functioni

Essential component of the mitotic spindle required for faithful chromosome segregation and progression into anaphase. Promotes the metaphase-to-anaphase transition and is required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture. The astrin (SPAG5)-kinastrin (SKAP) complex promotes stable microtubule-kinetochore attachments. Required for kinetochore oscillations and dynamics of microtubule plus-ends during live cell mitosis, possibly by forming a link between spindle microtubule plus-ends and mitotic chromosomes to achieve faithful cell division.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Small kinetochore-associated protein
Short name:
SKAP
Alternative name(s):
Kinetochore-localized astrin-binding protein
Short name:
Kinastrin
Kinetochore-localized astrin/SPAG5-binding protein
TRAF4-associated factor 1
Gene namesi
Name:Knstrn
Synonyms:D2Ertd750e, Skap, Traf4af1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1289298. Knstrn.

Subcellular locationi

  • Nucleus By similarity
  • Chromosomecentromerekinetochore By similarity
  • Cytoplasmcytoskeletonspindle pole By similarity

  • Note: Colocalizes with microtubules around centrosomes in prophase and with the mitotic spindle at prometaphase and metaphase. From late prometaphase to anaphase, is highly concentrated on kinetochores. Located at the kinetochore-microtubule interface. The astrin (SPAG5)-kinastrin (SKAP) complex localizes to the microtubule plus ends.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 312312Small kinetochore-associated proteinPRO_0000274513Add
BLAST

Proteomic databases

EPDiQ9D9Z1.
MaxQBiQ9D9Z1.
PaxDbiQ9D9Z1.
PRIDEiQ9D9Z1.

PTM databases

PhosphoSiteiQ9D9Z1.

Expressioni

Gene expression databases

BgeeiQ9D9Z1.
CleanExiMM_D2ERTD750E.
ExpressionAtlasiQ9D9Z1. baseline and differential.
GenevisibleiQ9D9Z1. MM.

Interactioni

Subunit structurei

Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGOL2. Interacts with SPAG5. Directly binds to microtubules, although at relatively low affinity. Interacts with CENPE; this interaction greatly favors microtubule-binding. Interacts with DSN1/MIS13; leading to localization to kinetochores. Interacts with MAPRE1/EB1; leading to localization to the microtubule plus ends. Interacts with PRPF19.By similarity

Protein-protein interaction databases

BioGridi206280. 4 interactions.
IntActiQ9D9Z1. 4 interactions.
MINTiMINT-218986.
STRINGi10090.ENSMUSP00000115860.

Structurei

3D structure databases

ProteinModelPortaliQ9D9Z1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni156 – 312157Interaction with SPAG5By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili166 – 21045Sequence analysisAdd
BLAST
Coiled coili246 – 28742Sequence analysisAdd
BLAST

Domaini

The coiled coil regions mediate binding to kinetochores.By similarity

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IKUT. Eukaryota.
ENOG4111DW5. LUCA.
GeneTreeiENSGT00390000010376.
HOGENOMiHOG000246953.
HOVERGENiHBG083924.
InParanoidiQ9D9Z1.
OMAiLCNNQVN.
OrthoDBiEOG7N0C5M.
PhylomeDBiQ9D9Z1.
TreeFamiTF336302.

Family and domain databases

InterProiIPR033373. SKAP.
[Graphical view]
PANTHERiPTHR31940. PTHR31940. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9D9Z1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPEAEAQE TAFRTTGPPT DSEPRPFPPS SRKFPFESAA ADSNEDWAVA
60 70 80 90 100
AEHYLKGSGE NGGWEQPAPG VQPSHPATMA SAKTVCDAQP HSMPSCGLPA
110 120 130 140 150
DTQTRATSKL PVKSKEADLL RHLHPGGPEP DVTKVTKSRR ENGQVKAAET
160 170 180 190 200
ASRRNLRNSY KPFNKQKPEE ELKDKNELLE AVNKQLHQKL TETQGELKDL
210 220 230 240 250
TQKVELLEKF QDNCLALLES KGLNPGQETL ASKQEPTTDH TDSMLLLETL
260 270 280 290 300
KDELKVFNET AKKQMEELQA LKVKLKLKEE ESVQFLEQQT LCKDEASDFT
310
IILEEMEQLL EM
Length:312
Mass (Da):34,728
Last modified:February 6, 2007 - v2
Checksum:i6247C22DE714CDC6
GO

Sequence cautioni

The sequence AAH31709.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2101F → I in BAB24529 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006328 mRNA. Translation: BAB24529.1.
BC031709 mRNA. Translation: AAH31709.1. Different initiation.
CCDSiCCDS16585.1.
RefSeqiNP_080688.2. NM_026412.3.
UniGeneiMm.252695.

Genome annotation databases

EnsembliENSMUST00000134661; ENSMUSP00000115860; ENSMUSG00000027331.
GeneIDi51944.
KEGGimmu:51944.
UCSCiuc008lst.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006328 mRNA. Translation: BAB24529.1.
BC031709 mRNA. Translation: AAH31709.1. Different initiation.
CCDSiCCDS16585.1.
RefSeqiNP_080688.2. NM_026412.3.
UniGeneiMm.252695.

3D structure databases

ProteinModelPortaliQ9D9Z1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206280. 4 interactions.
IntActiQ9D9Z1. 4 interactions.
MINTiMINT-218986.
STRINGi10090.ENSMUSP00000115860.

PTM databases

PhosphoSiteiQ9D9Z1.

Proteomic databases

EPDiQ9D9Z1.
MaxQBiQ9D9Z1.
PaxDbiQ9D9Z1.
PRIDEiQ9D9Z1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000134661; ENSMUSP00000115860; ENSMUSG00000027331.
GeneIDi51944.
KEGGimmu:51944.
UCSCiuc008lst.2. mouse.

Organism-specific databases

CTDi90417.
MGIiMGI:1289298. Knstrn.

Phylogenomic databases

eggNOGiENOG410IKUT. Eukaryota.
ENOG4111DW5. LUCA.
GeneTreeiENSGT00390000010376.
HOGENOMiHOG000246953.
HOVERGENiHBG083924.
InParanoidiQ9D9Z1.
OMAiLCNNQVN.
OrthoDBiEOG7N0C5M.
PhylomeDBiQ9D9Z1.
TreeFamiTF336302.

Miscellaneous databases

NextBioi308268.
PROiQ9D9Z1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D9Z1.
CleanExiMM_D2ERTD750E.
ExpressionAtlasiQ9D9Z1. baseline and differential.
GenevisibleiQ9D9Z1. MM.

Family and domain databases

InterProiIPR033373. SKAP.
[Graphical view]
PANTHERiPTHR31940. PTHR31940. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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].
    Strain: C57BL/6J.
    Tissue: Testis.
  2. "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] OF 66-312.
    Strain: Czech II.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiSKAP_MOUSE
AccessioniPrimary (citable) accession number: Q9D9Z1
Secondary accession number(s): Q8K2D9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: May 11, 2016
This is version 84 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

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.