dbPTM

KIF3A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KIF3A_HUMAN
UniProt AC	Q9Y496
Protein Name	Kinesin-like protein KIF3A
Gene Name	KIF3A
Organism	Homo sapiens (Human).
Sequence Length	699
Subcellular Localization	Cytoplasm, cytoskeleton . Cell projection, cilium . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Localizes to the subdistal appendage region of the centriole.
Protein Description	Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation. Plays a role in centriole cohesion and subdistal appendage organization and function. Regulates the formation of the subdistal appendage via recruitement of DCTN1 to the centriole. Also required for ciliary basal feet formation and microtubule anchoring to mother centriole..
Protein Sequence	MPINKSEKPESCDNVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNGTIFAYGQTGTGKTFTMEGVRAIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMHVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDETISTLRYANRAKNIKNKARINEDPKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQLSRELRLQMLIIDNFIPRDYQEMIENYVHWNEDIGEWQLKCVAYTGNNMRKQTPVPDKKEKDPFEVDLSHVYLAYTEESLRQSLMKLERPRTSKGKARPKTGRRKRSAKPETVIDSLLQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Acetylation	PESCDNVKVVVRCRP CCCCCCEEEEEEECC	35.25	25953088
30	Phosphorylation	PLNEREKSMCYKQAV CCCHHHHCCHHEECC	14.88	29978859
33	Phosphorylation	EREKSMCYKQAVSVD HHHHCCHHEECCCHH	9.48	29978859
34	Acetylation	REKSMCYKQAVSVDE HHHCCHHEECCCHHH	27.18	25953088
38	Phosphorylation	MCYKQAVSVDEMRGT CHHEECCCHHHCCCE	27.20	29978859
45	Phosphorylation	SVDEMRGTITVHKTD CHHHCCCEEEEEECC	11.78	22617229
47	Phosphorylation	DEMRGTITVHKTDSS HHCCCEEEEEECCCC	19.18	22617229
51	Phosphorylation	GTITVHKTDSSNEPP CEEEEEECCCCCCCC	26.66	22617229
92	Phosphorylation	IDSVLEGYNGTIFAY HHHHHCCCCCEEEEE	10.88	22210691
95	Phosphorylation	VLEGYNGTIFAYGQT HHCCCCCEEEEECCC	14.86	22210691
163	Ubiquitination	EVRDLLGKDQTQRLE HHHHHCCCCCCCCCE	46.78	-
207	Phosphorylation	TLGHKNRSVGATNMN HHCCCCCCCCCCCCC	34.01	22210691
211	Phosphorylation	KNRSVGATNMNEHSS CCCCCCCCCCCCCCC	29.13	22210691
217	Phosphorylation	ATNMNEHSSRSHAIF CCCCCCCCCCCEEEE	22.67	22210691
218	Phosphorylation	TNMNEHSSRSHAIFT CCCCCCCCCCEEEEE	39.44	22210691
271	Phosphorylation	GQRLKEATKINLSLS CHHHHHHHHCCCCHH	33.28	22210691
278	Phosphorylation	TKINLSLSTLGNVIS HHCCCCHHHHHHHHH	20.43	22210691
297	Phosphorylation	GKSTHVPYRNSKLTR CCCCCCCCCCCHHHH	22.72	22210691
316	Phosphorylation	SLGGNSKTMMCANIG HCCCCCCEEEECEEC	15.23	-
327	Phosphorylation	ANIGPADYNYDETIS CEECCCCCCHHHHHH	20.09	-
329	Phosphorylation	IGPADYNYDETISTL ECCCCCCHHHHHHHH	14.66	-
338	Phosphorylation	ETISTLRYANRAKNI HHHHHHHHHHHHHCC	16.02	-
346	Acetylation	ANRAKNIKNKARINE HHHHHCCCCCCCCCC	62.89	11925903
348	Acetylation	RAKNIKNKARINEDP HHHCCCCCCCCCCCH	33.76	11925913
356	Ubiquitination	ARINEDPKDALLRQF CCCCCCHHHHHHHHH	68.87	-
356	Acetylation	ARINEDPKDALLRQF CCCCCCHHHHHHHHH	68.87	20167786
365	Acetylation	ALLRQFQKEIEELKK HHHHHHHHHHHHHHH	63.05	20167786
381	Phosphorylation	LEEGEEISGSDISGS HHCCCCCCCCCCCCC	35.21	20363803
383	Phosphorylation	EGEEISGSDISGSEE CCCCCCCCCCCCCCC	25.61	20363803
386	Phosphorylation	EISGSDISGSEEDDD CCCCCCCCCCCCCCC	41.06	20363803
388	Phosphorylation	SGSDISGSEEDDDEE CCCCCCCCCCCCCCC	30.90	20363803
415	Phosphorylation	RRGKKKVSPDKMIEM HCCCCCCCHHHHHHH	35.94	27422710
467	Phosphorylation	KAQQEHQSLLEKLSA HHHHHHHHHHHHHHH	36.51	24719451
473	Phosphorylation	QSLLEKLSALEKKVI HHHHHHHHHHHHHEE	41.70	21964256
477	2-Hydroxyisobutyrylation	EKLSALEKKVIVGGV HHHHHHHHHEEECHH	53.87	-
477	Acetylation	EKLSALEKKVIVGGV HHHHHHHHHEEECHH	53.87	11921635
478	Acetylation	KLSALEKKVIVGGVD HHHHHHHHEEECHHH	28.02	11921645
495	Acetylation	AKAEEQEKLLEESNM HHHHHHHHHHHHHCH	59.05	11921655
498	Ubiquitination	EEQEKLLEESNMELE HHHHHHHHHHCHHHH	70.57	-
500	Phosphorylation	QEKLLEESNMELEER HHHHHHHHCHHHHHH	31.91	28355574
502	Sulfoxidation	KLLEESNMELEERRK HHHHHHCHHHHHHHH	9.65	21406390
505	Ubiquitination	EESNMELEERRKRAE HHHCHHHHHHHHHHH	35.83	-
509	Ubiquitination	MELEERRKRAEQLRR HHHHHHHHHHHHHHH	63.28	-
532	Phosphorylation	RLDIEEKYTSLQEEA HCCHHHHHHHHHHHH	12.58	29759185
533	Phosphorylation	LDIEEKYTSLQEEAQ CCHHHHHHHHHHHHC	33.75	28796482
534	Phosphorylation	DIEEKYTSLQEEAQG CHHHHHHHHHHHHCC	25.60	29759185
543	Phosphorylation	QEEAQGKTKKLKKVW HHHHCCCCHHHHHHH	39.99	29759185
558	Ubiquitination	TMLMAAKSEMADLQQ HHHHHHHHHHHHHHH	28.07	-
560	Sulfoxidation	LMAAKSEMADLQQEH HHHHHHHHHHHHHHH	4.54	21406390
569	Ubiquitination	DLQQEHQREIEGLLE HHHHHHHHHHHHHHH	49.09	-
589	Sulfoxidation	SRELRLQMLIIDNFI HHHHHHHHHHHCCCC	3.25	21406390
624	Phosphorylation	WQLKCVAYTGNNMRK EEEEEEEEECCCCCC	8.52	-
633	Phosphorylation	GNNMRKQTPVPDKKE CCCCCCCCCCCCCCC	29.32	26657352
660	Phosphorylation	LAYTEESLRQSLMKL HHCCHHHHHHHHHHC	6.99	-
672	Phosphorylation	MKLERPRTSKGKARP HHCCCCCCCCCCCCC	37.16	28102081
673	Phosphorylation	KLERPRTSKGKARPK HCCCCCCCCCCCCCC	40.46	28102081
687	Phosphorylation	KTGRRKRSAKPETVI CCCCCCCCCCCHHHH	43.62	29255136
690	Phosphorylation	RRKRSAKPETVIDSL CCCCCCCCHHHHHHH	42.05	18669648
692	Phosphorylation	KRSAKPETVIDSLLQ CCCCCCHHHHHHHHC	31.15	29255136
693	Ubiquitination	RSAKPETVIDSLLQ- CCCCCHHHHHHHHC-	4.34	-
696	Phosphorylation	KPETVIDSLLQ---- CCHHHHHHHHC----	21.61	23927012
699	Phosphorylation	TVIDSLLQ------- HHHHHHHC-------	57.47	-
714	Phosphorylation	---------------------- ----------------------		15345747
716	Ubiquitination	------------------------ ------------------------		-
719	Phosphorylation	--------------------------- ---------------------------		-

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
672	T	Phosphorylation	Kinase	ICK	Q9UPZ9	PSP
687	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KIF3A_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 KIF3A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
M3K10_HUMAN	MAP3K10	physical	9427749
KIF3B_HUMAN	KIF3B	physical	17825299
KIFA3_HUMAN	KIFAP3	physical	17825299
A4_HUMAN	APP	physical	21832049
RAN_HUMAN	RAN	physical	26496610
KIF3B_HUMAN	KIF3B	physical	26496610
DHX34_HUMAN	DHX34	physical	26496610
KIFA3_HUMAN	KIFAP3	physical	26496610
CTBL1_HUMAN	CTNNBL1	physical	26496610
F192A_HUMAN	FAM192A	physical	26496610
SSH2_HUMAN	SSH2	physical	26496610
KIF3B_HUMAN	KIF3B	physical	28514442
KIF3C_HUMAN	KIF3C	physical	28514442
LYPA2_HUMAN	LYPLA2	physical	28514442
HPHL1_HUMAN	HEPHL1	physical	28514442
ATG9B_HUMAN	ATG9B	physical	28514442
PKP3_HUMAN	PKP3	physical	28514442
DUS14_HUMAN	DUSP14	physical	28514442
PADI3_HUMAN	PADI3	physical	28514442
MFHA1_HUMAN	MFHAS1	physical	28514442
SBP1_HUMAN	SELENBP1	physical	28514442
LYG2_HUMAN	LYG2	physical	28514442
MP3B2_HUMAN	MAP1LC3B2	physical	28514442
TRI29_HUMAN	TRIM29	physical	28514442
FA26D_HUMAN	FAM26D	physical	28514442
PLCD1_HUMAN	PLCD1	physical	28514442
PPAP_HUMAN	ACPP	physical	28514442
ANXA8_HUMAN	ANXA8	physical	28514442
ARL8A_HUMAN	ARL8A	physical	28514442
P4K2A_HUMAN	PI4K2A	physical	28514442
LRC15_HUMAN	LRRC15	physical	28514442
PPCE_HUMAN	PREP	physical	28514442
DSG4_HUMAN	DSG4	physical	28514442
SPB5_HUMAN	SERPINB5	physical	28514442
PKP1_HUMAN	PKP1	physical	28514442
NHRF2_HUMAN	SLC9A3R2	physical	27173435
CE170_HUMAN	CEP170	physical	27173435

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 KIF3A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687, AND MASSSPECTROMETRY.	18669648 [Abstract]