SKA1_HUMAN - dbPTM
SKA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SKA1_HUMAN
UniProt AC Q96BD8
Protein Name Spindle and kinetochore-associated protein 1
Gene Name SKA1
Organism Homo sapiens (Human).
Sequence Length 255
Subcellular Localization Cytoplasm, cytoskeleton, spindle . Chromosome, centromere, kinetochore . 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 kinet
Protein Description Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. [PubMed: 17093495]
Protein Sequence MASSDLEQLCSHVNEKIGNIKKTLSLRNCGQEPTLKTVLNKIGDEIIVINELLNKLELEIQYQEQTNNSLKELCESLEEDYKDIEHLKENVPSHLPQVTVTQSCVKGSDLDPEEPIKVEEPEPVKKPPKEQRSIKEMPFITCDEFNGVPSYMKSRLTYNQINDVIKEINKAVISKYKILHQPKKSMNSVTRNLYHRFIDEETKDTKGRYFIVEADIKEFTTLKADKKFHVLLNILRHCRRLSEVRGGGLTRYVIT
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MASSDLEQL
------CCCHHHHHH		20.1019413330
4Phosphorylation----MASSDLEQLCS
----CCCHHHHHHHH		36.35-
11PhosphorylationSDLEQLCSHVNEKIG
HHHHHHHHHHHHHHC		38.78-
25PhosphorylationGNIKKTLSLRNCGQE
CHHHHHHCCCCCCCC		30.4325159151
36UbiquitinationCGQEPTLKTVLNKIG
CCCCCCHHHHHHHHC		38.78-
76PhosphorylationSLKELCESLEEDYKD
HHHHHHHHHHHHHHH		39.8325159151
81PhosphorylationCESLEEDYKDIEHLK
HHHHHHHHHHHHHHH		17.5328796482
117UbiquitinationLDPEEPIKVEEPEPV
CCCCCCCCCCCCCCC		55.07-
117SumoylationLDPEEPIKVEEPEPV
CCCCCCCCCCCCCCC		55.07-
117SumoylationLDPEEPIKVEEPEPV
CCCCCCCCCCCCCCC		55.07-
135UbiquitinationPKEQRSIKEMPFITC
CHHHCCCCCCCCEEE		49.56-
153UbiquitinationNGVPSYMKSRLTYNQ
CCCCHHHHHCCCHHH		24.96-
157PhosphorylationSYMKSRLTYNQINDV
HHHHHCCCHHHHHHH		21.2218491316
158PhosphorylationYMKSRLTYNQINDVI
HHHHCCCHHHHHHHH		15.0629496907
166UbiquitinationNQINDVIKEINKAVI
HHHHHHHHHHHHHHH		53.00-
170UbiquitinationDVIKEINKAVISKYK
HHHHHHHHHHHHHHH		50.09-
175UbiquitinationINKAVISKYKILHQP
HHHHHHHHHHHHCCC		39.16-
176PhosphorylationNKAVISKYKILHQPK
HHHHHHHHHHHCCCC		9.11-
177UbiquitinationKAVISKYKILHQPKK
HHHHHHHHHHCCCCC		42.39-
183UbiquitinationYKILHQPKKSMNSVT
HHHHCCCCCCCCHHH		51.41-
184UbiquitinationKILHQPKKSMNSVTR
HHHCCCCCCCCHHHH		62.71-
185PhosphorylationILHQPKKSMNSVTRN
HHCCCCCCCCHHHHH		29.3521406692
188PhosphorylationQPKKSMNSVTRNLYH
CCCCCCCHHHHHHHH		19.0721406692
190PhosphorylationKKSMNSVTRNLYHRF
CCCCCHHHHHHHHHH		17.4121406692
194PhosphorylationNSVTRNLYHRFIDEE
CHHHHHHHHHHCCCC		8.4229759185
202PhosphorylationHRFIDEETKDTKGRY
HHHCCCCCCCCCCCE		31.9729759185
203UbiquitinationRFIDEETKDTKGRYF
HHCCCCCCCCCCCEE		67.68-
205PhosphorylationIDEETKDTKGRYFIV
CCCCCCCCCCCEEEE		36.6329759185
206UbiquitinationDEETKDTKGRYFIVE
CCCCCCCCCCEEEEE		52.07-
242PhosphorylationLRHCRRLSEVRGGGL
HHHHHHHHHHCCCCC		32.0320860994
245MethylationCRRLSEVRGGGLTRY
HHHHHHHCCCCCCEE		33.71115917013
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SKA1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SKA1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SKA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MIS12_HUMANMIS12physical
22371557
SKA2_HUMANSKA2physical
22371557
NDC80_HUMANNDC80physical
22371557
SPC24_HUMANSPC24physical
22371557
SKA2_HUMANSKA2physical
17093495
DSC2_HUMANDSC2physical
26496610
ACSL3_HUMANACSL3physical
26496610
GMDS_HUMANGMDSphysical
26496610
KIF2A_HUMANKIF2Aphysical
26496610
PRS4_HUMANPSMC1physical
26496610
PRS8_HUMANPSMC5physical
26496610
WASL_HUMANWASLphysical
26496610
SNP29_HUMANSNAP29physical
26496610
ILVBL_HUMANILVBLphysical
26496610
NUDT5_HUMANNUDT5physical
26496610
MYCB2_HUMANMYCBP2physical
26496610
SYNEM_HUMANSYNMphysical
26496610
INT1_HUMANINTS1physical
26496610
PKN3_HUMANPKN3physical
26496610
ASCC1_HUMANASCC1physical
26496610
CCHCR_HUMANCCHCR1physical
26496610
THA11_HUMANTHAP11physical
26496610
SRGP1_HUMANSRGAP1physical
26496610
BEGIN_HUMANBEGAINphysical
26496610
ZMYM1_HUMANZMYM1physical
26496610
RFT1_HUMANRFT1physical
26496610
RRFM_HUMANMRRFphysical
26496610
BTBD9_HUMANBTBD9physical
26496610
LENG8_HUMANLENG8physical
26496610
SKA3_HUMANSKA3physical
26496610
SKA2_HUMANSKA2physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SKA1_HUMAN

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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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