dbPTM

KI10A_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KI10A_DROME
UniProt AC	Q960Z0
Protein Name	Kinesin-like protein Klp10A
Gene Name	Klp10A
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	805
Subcellular Localization	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Chromosome, centromere. Localizes to mitotic centrosomes, spindle poles and centromeres through metaphase. However, the centromeric localizatio
Protein Description	Required during anaphase to drive sister chromatid separation to promote flux by actively depolymerizing kinetochore microtubules at their pole-associated minus ends, thereby moving chromatids through a "poleward flux". [PubMed: 14681690]
Protein Sequence	MDMITVGQSVKIKRTDGRVHMAVVAVINQSGKCITVEWYERGETKGKEVELDAILTLNPELMQDTVEQHAAPEPKKQATAPMNLSRNPTQSAIGGNLTSRMTMAGNMLNKIQESQSIPNPIVSSNSVNTNSNSNTTAGGGGGTTTSTTTGLQRPRYSQAATGQQQTRIASAVPNNTLPNPSAAASAGPAAQGVATAATTQGAGGASTRRSHALKEVERLKENREKRRARQAEMKEEKVALMNQDPGNPNWETAQMIREYQSTLEFVPLLDGQAVDDHQITVCVRKRPISRKEVNRKEIDVISVPRKDMLIVHEPRSKVDLTKFLENHKFRFDYAFNDTCDNAMVYKYTAKPLVKTIFEGGMATCFAYGQTGSGKTHTMGGEFNGKVQDCKNGIYAMAAKDVFVTLNMPRYRAMNLVVSASFFEIYSGKVFDLLSDKQKLRVLEDGKQQVQVVGLTEKVVDGVEEVLKLIQHGNAARTSGQTSANSNSSRSHAVFQIVLRPQGSTKIHGKFSFIDLAGNERGVDTSSADRQTRMEGAEINKSLLALKECIRALGKQSAHLPFRVSKLTQVLRDSFIGEKSKTCMIAMISPGLSSCEHTLNTLRYADRVKELVVKDIVEVCPGGDTEPIEITDDEEEEELNMVHPHSHQLHPNSHAPASQSNNQRAPASHHSGAVIHNNNNNNNKNGNAGNMDLAMLSSLSEHEMSDELIVQHQAIDDLQQTEEMVVEYHRTVNATLETFLAESKALYNLTNYVDYDQDSYCKRGESMFSQLLDIAIQCRDMMAEYRAKLAKEEMLSCSFNSPNGKR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
85	Phosphorylation	ATAPMNLSRNPTQSA CCCCCCCCCCCCCCC	25.63	21082442
89	Phosphorylation	MNLSRNPTQSAIGGN CCCCCCCCCCCCCCC	38.41	19429919
91	Phosphorylation	LSRNPTQSAIGGNLT CCCCCCCCCCCCCHH	25.08	19429919
99	Phosphorylation	AIGGNLTSRMTMAGN CCCCCHHHHCHHHHH	24.18	21082442
102	Phosphorylation	GNLTSRMTMAGNMLN CCHHHHCHHHHHHHH	11.62	18511481
156	Phosphorylation	TGLQRPRYSQAATGQ CCCCCCCCCCCCCCC	14.07	18511481
157	Phosphorylation	GLQRPRYSQAATGQQ CCCCCCCCCCCCCCC	18.02	19060867
210	Phosphorylation	GGASTRRSHALKEVE CCHHHHHHHHHHHHH	15.15	18511481
630	Phosphorylation	DTEPIEITDDEEEEE CCCCCEECCCHHHHH	25.30	22817900
652	Phosphorylation	SHQLHPNSHAPASQS CCCCCCCCCCCCCCC	26.02	22668510
659	Phosphorylation	SHAPASQSNNQRAPA CCCCCCCCCCCCCCC	34.94	22668510
670	Phosphorylation	RAPASHHSGAVIHNN CCCCCCCCCCEEECC	24.03	21082442
751	Phosphorylation	ALYNLTNYVDYDQDS HHHHHCCCCCCCCCC	6.89	19429919
795	Phosphorylation	LAKEEMLSCSFNSPN HHHHHHHHCCCCCCC	13.35	22817900
797	Phosphorylation	KEEMLSCSFNSPNGK HHHHHHCCCCCCCCC	24.88	22817900
800	Phosphorylation	MLSCSFNSPNGKR-- HHHCCCCCCCCCC--	20.10	29892262

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 KI10A_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KI10A_DROME !!

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 KI10A_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of KI10A_DROME !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KI10A_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-630; SER-795;SER-797 AND SER-800, AND MASS SPECTROMETRY.	18327897 [Abstract]
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797, AND MASSSPECTROMETRY.	17372656 [Abstract]