SKAP_HUMAN - dbPTM
SKAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SKAP_HUMAN
UniProt AC Q9Y448
Protein Name Small kinetochore-associated protein {ECO:0000303|PubMed:19667759}
Gene Name KNSTRN {ECO:0000312|HGNC:HGNC:30767}
Organism Homo sapiens (Human).
Sequence Length 316
Subcellular Localization Nucleus . Chromosome, centromere, kinetochore . Cytoplasm, cytoskeleton, spindle pole . Colocalizes with microtubules around centrosomes in prophase and with the mitotic spindle at prometaphase and metaphase. From late prometaphase to anaphase, is hi
Protein Description Essential component of the mitotic spindle required for faithful chromosome segregation and progression into anaphase. [PubMed: 19667759 Promotes the metaphase-to-anaphase transition and is required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture]
Protein Sequence MAAPEAPPLDRVFRTTWLSTECDSHPLPPSYRKFLFETQAADLAGGTTVAAGNLLNESEKDCGQDRRAPGVQPCRLVTMTSVVKTVYSLQPPSALSGGQPADTQTRATSKSLLPVRSKEVDVSKQLHSGGPENDVTKITKLRRENGQMKATDTATRRNVRKGYKPLSKQKSEEELKDKNQLLEAVNKQLHQKLTETQGELKDLTQKVELLEKFRDNCLAILESKGLDPALGSETLASRQESTTDHMDSMLLLETLQEELKLFNETAKKQMEELQALKVKLEMKEERVRFLEQQTLCNNQVNDLTTALKEMEQLLEM
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
15PhosphorylationPLDRVFRTTWLSTEC
CCCCEEHHHCCCCCC		15.74-
16PhosphorylationLDRVFRTTWLSTECD
CCCEEHHHCCCCCCC		21.83-
20PhosphorylationFRTTWLSTECDSHPL
EHHHCCCCCCCCCCC		38.16-
78PhosphorylationVQPCRLVTMTSVVKT
CCCCEEEEECCCEEE		21.23-
85PhosphorylationTMTSVVKTVYSLQPP
EECCCEEEHHHCCCC		17.0521945579
87PhosphorylationTSVVKTVYSLQPPSA
CCCEEEHHHCCCCHH		14.6421945579
88PhosphorylationSVVKTVYSLQPPSAL
CCEEEHHHCCCCHHH		19.0521945579
93PhosphorylationVYSLQPPSALSGGQP
HHHCCCCHHHCCCCC		48.8321945579
96PhosphorylationLQPPSALSGGQPADT
CCCCHHHCCCCCCCC		40.3621945579
103PhosphorylationSGGQPADTQTRATSK
CCCCCCCCCCCCCCC		33.6722210691
105PhosphorylationGQPADTQTRATSKSL
CCCCCCCCCCCCCCC		25.1022210691
108PhosphorylationADTQTRATSKSLLPV
CCCCCCCCCCCCCCC		33.1420860994
109PhosphorylationDTQTRATSKSLLPVR
CCCCCCCCCCCCCCC		21.1829743597
110UbiquitinationTQTRATSKSLLPVRS
CCCCCCCCCCCCCCC		40.5429967540
110AcetylationTQTRATSKSLLPVRS
CCCCCCCCCCCCCCC		40.5425953088
111PhosphorylationQTRATSKSLLPVRSK
CCCCCCCCCCCCCCC		34.6029743597
117PhosphorylationKSLLPVRSKEVDVSK
CCCCCCCCCEEEHHH		33.1425159151
124UbiquitinationSKEVDVSKQLHSGGP
CCEEEHHHHHCCCCC		57.6429967540
128PhosphorylationDVSKQLHSGGPENDV
EHHHHHCCCCCCCCH		54.7825194279
137UbiquitinationGPENDVTKITKLRRE
CCCCCHHHHHHHHHH		48.5029967540
149UbiquitinationRRENGQMKATDTATR
HHHCCCCCCCCHHHH		40.0024816145
151PhosphorylationENGQMKATDTATRRN
HCCCCCCCCHHHHHH		28.50-
163PhosphorylationRRNVRKGYKPLSKQK
HHHHHCCCCCCCCCC		16.6829496907
171PhosphorylationKPLSKQKSEEELKDK
CCCCCCCCHHHHHHH		47.9826055452
178UbiquitinationSEEELKDKNQLLEAV
CHHHHHHHHHHHHHH		45.0329967540
187UbiquitinationQLLEAVNKQLHQKLT
HHHHHHHHHHHHHHH		47.8729967540
192UbiquitinationVNKQLHQKLTETQGE
HHHHHHHHHHHCHHH		46.7829967540
201UbiquitinationTETQGELKDLTQKVE
HHCHHHHHHHHHHHH		46.5233845483
206UbiquitinationELKDLTQKVELLEKF
HHHHHHHHHHHHHHH		32.2329967540
212UbiquitinationQKVELLEKFRDNCLA
HHHHHHHHHHHHHHH		45.7422817900
224UbiquitinationCLAILESKGLDPALG
HHHHHHHCCCCHHHC		54.8621963094
232PhosphorylationGLDPALGSETLASRQ
CCCHHHCCHHHHHCC		28.4025159151
234PhosphorylationDPALGSETLASRQES
CHHHCCHHHHHCCCC		29.3525159151
237PhosphorylationLGSETLASRQESTTD
HCCHHHHHCCCCCCC		37.2925159151
241PhosphorylationTLASRQESTTDHMDS
HHHHCCCCCCCHHHH		28.4125159151
242PhosphorylationLASRQESTTDHMDSM
HHHCCCCCCCHHHHH		35.1820068231
243PhosphorylationASRQESTTDHMDSML
HHCCCCCCCHHHHHH		32.9425159151
248PhosphorylationSTTDHMDSMLLLETL
CCCCHHHHHHHHHHH		12.0720068231
254PhosphorylationDSMLLLETLQEELKL
HHHHHHHHHHHHHHH		33.4420068231
268MethylationLFNETAKKQMEELQA
HHHHHHHHHHHHHHH		53.0323644510
268TrimethylationLFNETAKKQMEELQA
HHHHHHHHHHHHHHH		53.03-
270SulfoxidationNETAKKQMEELQALK
HHHHHHHHHHHHHHH		6.2421406390
279UbiquitinationELQALKVKLEMKEER
HHHHHHHHHHHHHHH		36.8229967540
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 SKAP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SKAP_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 SKAP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRP19_HUMANPRPF19physical
24718257
HSP7C_HUMANHSPA8physical
24718257
HSP76_HUMANHSPA6physical
24718257
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 SKAP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND MASSSPECTROMETRY.

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