Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Spindle and kinetochore-associated protein 1  

UniProtKB / Swiss-Prot ID :  SKA1_HUMAN

Gene Name (Synonyms) : 
SKA1, C18orf24  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. 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 p 

Protein 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 mediates the interaction with microtubules. 

Protein Sequence MASSDLEQLCSHVNEKIGNIKKTLSLRNCGQEPTLKTVLNKIGDEIIVINELLNKLELEIQYQEQTNNSL...
Predicted Secondary Structure CCCCHHHHHHHHHHHHHHHHHHHHHHHHHCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
91V -> I (in dbSNP:rs6507992). VAR_030091
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MASSDL
---CCCCHH
20.10UniProtKB
Link
157PhosphothreonineKSRLTYNQI
HHCCCHHHH
21.22HPRD
Link-
157PhosphothreonineKSRLTYNQI
HHCCCHHHH
21.22Phosphositeplus
Link-
157PhosphothreonineKSRLTYNQI
HHCCCHHHH
21.22SysPTM
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NDC80_HUMANcolocalizationMINT-3391245MINT17093495
TBA4A_HUMANcolocalizationMINT-3391222MINT17093495
CENPE_HUMANcolocalizationMINT-3391266MINT17093495
SKA2_HUMANdirect interactionMINT-3391375MINT17093495
SKA2_HUMANdirect interactionMINT-3391398MINT17093495
SKA2_HUMANdirect interactionMINT-3391334MINT17093495
SKA2_HUMANdirect interactionMINT-3391357MINT17093495
SKA2_HUMANphysical interactionMINT-3391311MINT17093495
SKA2_HUMANphysical interactionMINT-4051212MINT17093495
SKA2_HUMANcolocalizationMINT-3391284MINT17093495
CN048_HUMANphysical interactionEBI-758521
intact16189514
PLDN_HUMANyeast 2-hybridHPRD:12689HPRD16189514
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures