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Protein

Spindle and kinetochore-associated protein 1

Gene

SKA1

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: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). In the complex, it mediates the interaction with microtubules (PubMed:19289083, 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

BioCyciZFISH:ENSG00000154839-MONOMER.
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 1
Gene namesi
Name:SKA1
Synonyms:C18orf24
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:28109. SKA1.

Subcellular locationi

  • Cytoplasmcytoskeletonspindle 1 Publication
  • Chromosomecentromerekinetochore 1 Publication

  • Note: Localizes to the outer kinetochore and spindle microtubules during mitosis in a NDC80 complex-dependent manner (PubMed:17093495). Localizes to both the mitotic spindle and kinetochore-associated proteins (PubMed:17093495). Associates with kinetochores following microtubule attachment from prometaphase, through mid-anaphase and then vanishes in telophase (PubMed:17093495).1 Publication

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi155R → A: Abolishes microtubule binding; when associated with A-236 and A-245. 1 Publication1
Mutagenesisi185S → D: Phosphomimetic mutant which strongly reduces microtubule binding; when associated with D-242. 1 Publication1
Mutagenesisi236R → A: Abolishes microtubule binding; when associated with A-155 and A-245. 1 Publication1
Mutagenesisi242S → D: Phosphomimetic mutant which strongly reduces microtubule binding; when associated with D-185. 1 Publication1
Mutagenesisi245R → A: Abolishes microtubule binding; when associated with A-155 and A-236. 1 Publication1

Organism-specific databases

DisGeNETi220134.
OpenTargetsiENSG00000154839.
ENSG00000262634.
PharmGKBiPA165429102.

Polymorphism and mutation databases

BioMutaiSKA1.
DMDMi74731226.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002731552 – 255Spindle and kinetochore-associated protein 1Add BLAST254

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ96BD8.
MaxQBiQ96BD8.
PaxDbiQ96BD8.
PeptideAtlasiQ96BD8.
PRIDEiQ96BD8.

PTM databases

iPTMnetiQ96BD8.
PhosphoSitePlusiQ96BD8.

Expressioni

Gene expression databases

BgeeiENSG00000154839.
CleanExiHS_C18orf24.
ExpressionAtlasiQ96BD8. baseline and differential.
GenevisibleiQ96BD8. HS.

Organism-specific databases

HPAiHPA045495.

Interactioni

Subunit structurei

Component of the SKA1 complex, composed of SKA1, SKA2 and SKA3 (PubMed:17093495). Forms a heterodimer with SKA2; the heterodimer interacting with SKA3 (PubMed:17093495, PubMed:19289083, PubMed:23085020). The core SKA1 complex is composed of 2 SKA1-SKA2 heterodimers, each heterodimer interacting with a molecule of the SKA3 homodimer (PubMed:19289083). The core SKA1 complex associates with microtubules and forms oligomeric assemblies (PubMed:17093495, PubMed:19289083). Interacts with microtubules; the interaction is direct (PubMed:19289083, PubMed:23085020). Interacts with SKA2 (PubMed:19289083). Interacts with SKA3 (PubMed:19289083, PubMed:23085020).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BLOC1S6Q9UL456EBI-741854,EBI-465781
PSMC5P621953EBI-741854,EBI-357745
SKA2Q8WVK711EBI-741854,EBI-1773994
SYCE1Q8N0S23EBI-741854,EBI-6872807

GO - Molecular functioni

  • microtubule binding Source: UniProtKB

Protein-protein interaction databases

BioGridi128632. 45 interactors.
IntActiQ96BD8. 39 interactors.
MINTiMINT-2813709.
STRINGi9606.ENSP00000285116.

Structurei

Secondary structure

1255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 31Combined sources27
Helixi33 – 79Combined sources47
Helixi82 – 88Combined sources7
Helixi142 – 146Combined sources5
Helixi150 – 153Combined sources4
Helixi158 – 179Combined sources22
Helixi183 – 185Combined sources3
Helixi188 – 200Combined sources13
Turni203 – 207Combined sources5
Beta strandi210 – 212Combined sources3
Helixi213 – 219Combined sources7
Helixi226 – 237Combined sources12
Beta strandi240 – 244Combined sources5
Beta strandi251 – 254Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AJ5X-ray3.32A/B/C/D/E/F/G/H/I/J1-91[»]
4C9YX-ray2.01A/B133-255[»]
4CA0X-ray2.26A/B133-255[»]
ProteinModelPortaliQ96BD8.
SMRiQ96BD8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni132 – 255Microtubule binding1 PublicationAdd BLAST124

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili49 – 91Sequence analysisAdd BLAST43

Sequence similaritiesi

Belongs to the SKA1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4832. Eukaryota.
ENOG4111IBI. LUCA.
GeneTreeiENSGT00390000011654.
HOGENOMiHOG000154331.
HOVERGENiHBG082236.
InParanoidiQ96BD8.
OMAiIKEMLFI.
OrthoDBiEOG091G0R18.
PhylomeDBiQ96BD8.
TreeFamiTF324442.

Family and domain databases

InterProiIPR009829. SKA1.
[Graphical view]
PANTHERiPTHR28573:SF1. PTHR28573:SF1. 1 hit.
PfamiPF07160. SKA1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: Q96BD8-1) [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
MASSDLEQLC SHVNEKIGNI KKTLSLRNCG QEPTLKTVLN KIGDEIIVIN
60 70 80 90 100
ELLNKLELEI QYQEQTNNSL KELCESLEED YKDIEHLKEN VPSHLPQVTV
110 120 130 140 150
TQSCVKGSDL DPEEPIKVEE PEPVKKPPKE QRSIKEMPFI TCDEFNGVPS
160 170 180 190 200
YMKSRLTYNQ INDVIKEINK AVISKYKILH QPKKSMNSVT RNLYHRFIDE
210 220 230 240 250
ETKDTKGRYF IVEADIKEFT TLKADKKFHV LLNILRHCRR LSEVRGGGLT

RYVIT
Length:255
Mass (Da):29,484
Last modified:December 1, 2001 - v1
Checksum:i40F578B0B6D9B64D
GO
Isoform 2 (identifier: Q96BD8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     104-150: CVKGSDLDPEEPIKVEEPEPVKKPPKEQRSIKEMPFITCDEFNGVPS → W

Note: No experimental confirmation available.
Show »
Length:209
Mass (Da):24,390
Checksum:i754BCEB9A8705B39
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03009191V → I.1 PublicationCorresponds to variant rs6507992dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_037250104 – 150CVKGS…NGVPS → W in isoform 2. 1 PublicationAdd BLAST47

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK303464 mRNA. Translation: BAG64506.1.
AK313968 mRNA. Translation: BAG36683.1.
CH471096 Genomic DNA. Translation: EAW62971.1.
BC015706 mRNA. Translation: AAH15706.1.
CCDSiCCDS11946.1. [Q96BD8-1]
RefSeqiNP_001034624.1. NM_001039535.2. [Q96BD8-1]
NP_659497.1. NM_145060.3. [Q96BD8-1]
UniGeneiHs.134726.

Genome annotation databases

EnsembliENST00000285116; ENSP00000285116; ENSG00000154839. [Q96BD8-1]
ENST00000398452; ENSP00000381470; ENSG00000154839. [Q96BD8-1]
ENST00000417656; ENSP00000397222; ENSG00000154839. [Q96BD8-2]
ENST00000571751; ENSP00000458992; ENSG00000262634. [Q96BD8-1]
ENST00000616604; ENSP00000478259; ENSG00000262634. [Q96BD8-1]
ENST00000633940; ENSP00000488815; ENSG00000262634. [Q96BD8-2]
GeneIDi220134.
KEGGihsa:220134.
UCSCiuc002let.4. human. [Q96BD8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK303464 mRNA. Translation: BAG64506.1.
AK313968 mRNA. Translation: BAG36683.1.
CH471096 Genomic DNA. Translation: EAW62971.1.
BC015706 mRNA. Translation: AAH15706.1.
CCDSiCCDS11946.1. [Q96BD8-1]
RefSeqiNP_001034624.1. NM_001039535.2. [Q96BD8-1]
NP_659497.1. NM_145060.3. [Q96BD8-1]
UniGeneiHs.134726.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AJ5X-ray3.32A/B/C/D/E/F/G/H/I/J1-91[»]
4C9YX-ray2.01A/B133-255[»]
4CA0X-ray2.26A/B133-255[»]
ProteinModelPortaliQ96BD8.
SMRiQ96BD8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128632. 45 interactors.
IntActiQ96BD8. 39 interactors.
MINTiMINT-2813709.
STRINGi9606.ENSP00000285116.

PTM databases

iPTMnetiQ96BD8.
PhosphoSitePlusiQ96BD8.

Polymorphism and mutation databases

BioMutaiSKA1.
DMDMi74731226.

Proteomic databases

EPDiQ96BD8.
MaxQBiQ96BD8.
PaxDbiQ96BD8.
PeptideAtlasiQ96BD8.
PRIDEiQ96BD8.

Protocols and materials databases

DNASUi220134.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285116; ENSP00000285116; ENSG00000154839. [Q96BD8-1]
ENST00000398452; ENSP00000381470; ENSG00000154839. [Q96BD8-1]
ENST00000417656; ENSP00000397222; ENSG00000154839. [Q96BD8-2]
ENST00000571751; ENSP00000458992; ENSG00000262634. [Q96BD8-1]
ENST00000616604; ENSP00000478259; ENSG00000262634. [Q96BD8-1]
ENST00000633940; ENSP00000488815; ENSG00000262634. [Q96BD8-2]
GeneIDi220134.
KEGGihsa:220134.
UCSCiuc002let.4. human. [Q96BD8-1]

Organism-specific databases

CTDi220134.
DisGeNETi220134.
GeneCardsiSKA1.
H-InvDBHIX0022882.
HGNCiHGNC:28109. SKA1.
HPAiHPA045495.
MIMi616673. gene.
neXtProtiNX_Q96BD8.
OpenTargetsiENSG00000154839.
ENSG00000262634.
PharmGKBiPA165429102.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4832. Eukaryota.
ENOG4111IBI. LUCA.
GeneTreeiENSGT00390000011654.
HOGENOMiHOG000154331.
HOVERGENiHBG082236.
InParanoidiQ96BD8.
OMAiIKEMLFI.
OrthoDBiEOG091G0R18.
PhylomeDBiQ96BD8.
TreeFamiTF324442.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000154839-MONOMER.
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

ChiTaRSiSKA1. human.
GenomeRNAii220134.
PROiQ96BD8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000154839.
CleanExiHS_C18orf24.
ExpressionAtlasiQ96BD8. baseline and differential.
GenevisibleiQ96BD8. HS.

Family and domain databases

InterProiIPR009829. SKA1.
[Graphical view]
PANTHERiPTHR28573:SF1. PTHR28573:SF1. 1 hit.
PfamiPF07160. SKA1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSKA1_HUMAN
AccessioniPrimary (citable) accession number: Q96BD8
Secondary accession number(s): B2R9Y6, B4E0P4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 112 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 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.