Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Spindle and kinetochore-associated protein 2

Gene

SKA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation (PubMed:17093495, PubMed:19289083, PubMed:23085020). Required for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint (PubMed:17093495). The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies (PubMed:19289083). The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner (PubMed:17093495, PubMed:19289083). In the complex, it is required for SKA1 localization (PubMed:19289083). Affinity for microtubules is synergistically enhanced in the presence of the ndc-80 complex and may allow the ndc-80 complex to track depolymerizing microtubules (PubMed:23085020).3 Publications

GO - Molecular functioni

  • microtubule binding Source: UniProtKB

GO - Biological processi

  • cell division Source: UniProtKB
  • chromosome segregation Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB
  • regulation of microtubule polymerization or depolymerization Source: UniProtKB
  • sister chromatid cohesion Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Spindle and kinetochore-associated protein 2
Alternative name(s):
Protein FAM33A
Gene namesi
Name:SKA2
Synonyms:FAM33A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:28006. SKA2.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome outer kinetochore Source: UniProtKB
  • cytosol Source: Reactome
  • spindle microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165432792.

Polymorphism and mutation databases

BioMutaiSKA2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 121121Spindle and kinetochore-associated protein 2PRO_0000266035Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8WVK7.
MaxQBiQ8WVK7.
PaxDbiQ8WVK7.
PRIDEiQ8WVK7.

PTM databases

iPTMnetiQ8WVK7.
PhosphoSiteiQ8WVK7.

Expressioni

Gene expression databases

BgeeiQ8WVK7.
CleanExiHS_FAM33A.
ExpressionAtlasiQ8WVK7. baseline and differential.
GenevisibleiQ8WVK7. HS.

Organism-specific databases

HPAiHPA059235.

Interactioni

Subunit structurei

Component of the SKA1 complex, composed of SKA1, SKA2 and SKA3. Forms a heterodimer with SKA1; the heterodimer interacting with SKA3. The core SKA1 complex is composed of 2 SKA1-SKA2 heterodimers, each heterodimer interacting with a molecule of the SKA3 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. May interact with NR3C1; the relevance of such interaction remains unclear in vivo.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SKA1Q96BD811EBI-1773994,EBI-741854

GO - Molecular functioni

  • microtubule binding Source: UniProtKB

Protein-protein interaction databases

BioGridi131515. 13 interactions.
IntActiQ8WVK7. 9 interactions.
MINTiMINT-3391298.
STRINGi9606.ENSP00000333433.

Structurei

Secondary structure

1
121
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 3231Combined sources
Helixi44 – 9653Combined sources
Helixi104 – 1129Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AJ5X-ray3.32K/L/M/N/O/P/Q/R/S/T1-121[»]
ProteinModelPortaliQ8WVK7.
SMRiQ8WVK7. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SKA2 family.Curated

Phylogenomic databases

eggNOGiENOG410IZYA. Eukaryota.
ENOG4111NBU. LUCA.
GeneTreeiENSGT00390000009588.
HOGENOMiHOG000154333.
HOVERGENiHBG093956.
InParanoidiQ8WVK7.
OMAiSRYQTLH.
OrthoDBiEOG776SS0.
PhylomeDBiQ8WVK7.
TreeFamiTF332958.

Family and domain databases

InterProiIPR026762. Ska2.
[Graphical view]
PANTHERiPTHR32017:SF3. PTHR32017:SF3. 1 hit.
PfamiPF16740. SKA2. 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: Q8WVK7-1) [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
MEAEVDKLEL MFQKAESDLD YIQYRLEYEI KTNHPDSASE KNPVTLLKEL
60 70 80 90 100
SVIKSRYQTL YARFKPVAVE QKESKSRICA TVKKTMNMIQ KLQKQTDLEL
110 120
SPLTKEEKTA AEQFKFHMPD L
Length:121
Mass (Da):14,188
Last modified:March 1, 2002 - v1
Checksum:iD079F77E5BD4D7B0
GO
Isoform 2 (identifier: Q8WVK7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: MEAEVDKLEL...PVAVEQKESK → MASEVGHNLE...ILIQQVSCHH
     76-121: Missing.

Note: No experimental confirmation available.
Show »
Length:75
Mass (Da):8,282
Checksum:iBE3925745EDDA06B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7575MEAEV…QKESK → MASEVGHNLESPETPGGGGW TRVEFPPPAPKGAATVWCLN RLGSRKLSLIWITFNTGWNM KSRLIILIQQVSCHH in isoform 2. 1 PublicationVSP_047348Add
BLAST
Alternative sequencei76 – 12146Missing in isoform 2. 1 PublicationVSP_047349Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK056473 mRNA. Translation: BAG51725.1.
AC099850 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94420.1.
BC017873 mRNA. Translation: AAH17873.1.
BC106003 mRNA. Translation: AAI06004.1.
BI835364 mRNA. No translation available.
CCDSiCCDS45747.1. [Q8WVK7-1]
CCDS45748.1. [Q8WVK7-2]
RefSeqiNP_001094065.1. NM_001100595.1. [Q8WVK7-2]
NP_872426.1. NM_182620.3. [Q8WVK7-1]
UniGeneiHs.463607.

Genome annotation databases

EnsembliENST00000330137; ENSP00000333433; ENSG00000182628. [Q8WVK7-1]
ENST00000437036; ENSP00000411231; ENSG00000182628. [Q8WVK7-2]
GeneIDi348235.
KEGGihsa:348235.
UCSCiuc002ixd.3. human. [Q8WVK7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK056473 mRNA. Translation: BAG51725.1.
AC099850 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94420.1.
BC017873 mRNA. Translation: AAH17873.1.
BC106003 mRNA. Translation: AAI06004.1.
BI835364 mRNA. No translation available.
CCDSiCCDS45747.1. [Q8WVK7-1]
CCDS45748.1. [Q8WVK7-2]
RefSeqiNP_001094065.1. NM_001100595.1. [Q8WVK7-2]
NP_872426.1. NM_182620.3. [Q8WVK7-1]
UniGeneiHs.463607.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AJ5X-ray3.32K/L/M/N/O/P/Q/R/S/T1-121[»]
ProteinModelPortaliQ8WVK7.
SMRiQ8WVK7. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131515. 13 interactions.
IntActiQ8WVK7. 9 interactions.
MINTiMINT-3391298.
STRINGi9606.ENSP00000333433.

PTM databases

iPTMnetiQ8WVK7.
PhosphoSiteiQ8WVK7.

Polymorphism and mutation databases

BioMutaiSKA2.

Proteomic databases

EPDiQ8WVK7.
MaxQBiQ8WVK7.
PaxDbiQ8WVK7.
PRIDEiQ8WVK7.

Protocols and materials databases

DNASUi348235.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330137; ENSP00000333433; ENSG00000182628. [Q8WVK7-1]
ENST00000437036; ENSP00000411231; ENSG00000182628. [Q8WVK7-2]
GeneIDi348235.
KEGGihsa:348235.
UCSCiuc002ixd.3. human. [Q8WVK7-1]

Organism-specific databases

CTDi348235.
GeneCardsiSKA2.
HGNCiHGNC:28006. SKA2.
HPAiHPA059235.
MIMi616674. gene.
neXtProtiNX_Q8WVK7.
PharmGKBiPA165432792.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IZYA. Eukaryota.
ENOG4111NBU. LUCA.
GeneTreeiENSGT00390000009588.
HOGENOMiHOG000154333.
HOVERGENiHBG093956.
InParanoidiQ8WVK7.
OMAiSRYQTLH.
OrthoDBiEOG776SS0.
PhylomeDBiQ8WVK7.
TreeFamiTF332958.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiSKA2. human.
GenomeRNAii348235.
PROiQ8WVK7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WVK7.
CleanExiHS_FAM33A.
ExpressionAtlasiQ8WVK7. baseline and differential.
GenevisibleiQ8WVK7. HS.

Family and domain databases

InterProiIPR026762. Ska2.
[Graphical view]
PANTHERiPTHR32017:SF3. PTHR32017:SF3. 1 hit.
PfamiPF16740. SKA2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Teratocarcinoma.
  2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Eye and Lung.
  5. "Timely anaphase onset requires a novel spindle and kinetochore complex comprising Ska1 and Ska2."
    Hanisch A., Sillje H.H.W., Nigg E.A.
    EMBO J. 25:5504-5515(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SKA1.
  6. "Identification and functional analysis of SKA2 interaction with the glucocorticoid receptor."
    Rice L., Waters C.E., Eccles J., Garside H., Sommer P., Kay P., Blackhall F.H., Zeef L., Telfer B., Stratford I., Clarke R., Singh D., Stevens A., White A., Ray D.W.
    J. Endocrinol. 198:499-509(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INTERACTION WITH NR3C1.
  7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "The human kinetochore Ska1 complex facilitates microtubule depolymerization-coupled motility."
    Welburn J.P.I., Grishchuk E.L., Backer C.B., Wilson-Kubalek E.M., Yates J.R. III, Cheeseman I.M.
    Dev. Cell 16:374-385(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SKA1 COMPLEX, INTERACTION WITH MICROTUBULES AND SKA1.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "The kinetochore-bound Ska1 complex tracks depolymerizing microtubules and binds to curved protofilaments."
    Schmidt J.C., Arthanari H., Boeszoermenyi A., Dashkevich N.M., Wilson-Kubalek E.M., Monnier N., Markus M., Oberer M., Milligan R.A., Bathe M., Wagner G., Grishchuk E.L., Cheeseman I.M.
    Dev. Cell 23:968-980(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiSKA2_HUMAN
AccessioniPrimary (citable) accession number: Q8WVK7
Secondary accession number(s): A6NIL3, B3KPL3, E9PCB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.