Reviewed, UniProtKB/Swiss-Prot Q9CR46 (SKA2_MOUSE)

Names and origin

Protein names

Recommended name:
    Spindle and kinetochore-associated protein 2
Alternative name(s):
    Protein FAM33A

Gene names

Name:	Ska2
Synonyms:	Fam33a

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	120 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex, it is required for SKA1 localization By similarity.
Subunit structure	Component of the SKA1 complex, composed of SKA1, SKA2/FAM33A and RAMA1. Forms a heterodimer with SKA1; the heterodimer interacting with RAMA1. The core SKA1 complex is composed of 2 SKA1-SKA2 heterodimers, each heterodimer interacting with a molecule of the RAMA1 homodimer. The core SKA1 complex associates with microtubules and forms oligomeric assemblies. Interacts directly with SKA1. Binds directly to microtubules; but with a much lower affinity than SKA1 in vivo By similarity.
Subcellular location	Cytoplasm › cytoskeleton › spindle By similarity. Kinetochore By similarity. Note: Localizes to the outer kinetochore and spindle microtubules during mitosis in a NDC80 complex-dependent manner. Localizes to both the mitotic spindle and kinetochore-associated proteins By similarity.
Sequence similarities	Belongs to the SKA2 family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Kinetochore Microtubule
Gene Ontology (GO)
Biological process	cell division Inferred from sequence or structural similarity. Source: UniProtKB chromosome segregation Inferred from sequence or structural similarity. Source: UniProtKB mitotic anaphase Inferred from sequence or structural similarity. Source: UniProtKB regulation of microtubule polymerization or depolymerization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	outer kinetochore of condensed chromosome Inferred from sequence or structural similarity. Source: UniProtKB spindle microtubule Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	microtubule binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 120	120	Spindle and kinetochore-associated protein 2		PRO_0000273161

Sequences

	Sequence		Length	Mass (Da)
	Q9CR46-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 233FE4303B84C117	FASTA	120	13,725
	10 20 30 40 50 60 MEAEVDKLEL MFQKADSDLD YLQYRLEYEV KTNHPHSAGE KNAVTVLKEL SAIKSRYQAL 70 80 90 100 110 120 CARFKAVSVE QKETKSCICA TLNKTMTMIQ ELQKQTNLEL TLLTEEEKAA TEPLKSHMPD

References

[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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK003196 mRNA. Translation: BAB22634.1. AK013317 mRNA. Translation: BAB28787.1. AK013370 mRNA. Translation: BAB28814.1. AK017811 mRNA. Translation: BAB30948.1. AK162628 mRNA. Translation: BAE36998.1. AL713917 Genomic DNA. Translation: CAI25315.1. CU468043 Genomic DNA. Translation: CAQ51630.1. CH466556 Genomic DNA. Translation: EDL15809.1. BC117001 mRNA. Translation: AAI17002.1. BC119167 mRNA. Translation: AAI19168.1.
IPI	IPI00133130.
RefSeq	NP_079653.1.
UniGene	Mm.45008
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9CR46.
Proteomic databases
PRIDE	Q9CR46.
Genome annotation databases
Ensembl	ENSMUST00000020794; ENSMUSP00000020794; ENSMUSG00000020492; Mus musculus. [Genome view]
GeneID	66140.
KEGG	mmu:66140.
UCSC	uc007kti.1. mouse.
Organism-specific databases
CTD	66140.
MGI	MGI:1913390. 1110001A07Rik.
Phylogenomic databases
HOGENOM	HBG283940.
HOVERGEN	Q9CR46.
InParanoid	Q9CR46.
OMA	KPIAVEQ.
OrthoDB	EOG97H88V.
Gene expression databases
ArrayExpress	Q9CR46.
Bgee	Q9CR46.
CleanEx	MM_1110001A07RIK.
Genevestigator	Q9CR46.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	320746.
SOURCE	Search...

Entry information

Entry name

SKA2_MOUSE

Accession

Primary (citable) accession number: Q9CR46
Secondary accession number(s): B2KGY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	June 1, 2001
Last modified:	December 15, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)