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KIF3A (human)

Overview KIF3A Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation. Heterodimer of KIF3A and KIF3B. Interacts with PIFO/C1orf88. Interacts with CLN3. Belongs to the kinesin-like protein family. Kinesin II subfamily. Note: This description may include information from UniProtKB. Protein type: Microtubule binding protein; Motor protein Cellular Component: centrosome; spindle microtubule; kinesin II complex; cytosol; photoreceptor connecting cilium Molecular Function: protein binding; plus-end-directed microtubule motor activity; ATP binding Biological Process: anterior/posterior pattern formation; smoothened signaling pathway; in utero embryonic development; organelle organization and biogenesis; heart development; antigen processing and presentation of exogenous peptide antigen via MHC class II; cilium biogenesis; blood coagulation; kidney development; determination of left/right symmetry; microtubule-based movement; dorsoventral neural tube patterning Reference #:  Q9Y496 (UniProtKB) Alt. Names/Synonyms: KIF3; KIF3A; kinesin family member 3A; kinesin family protein 3A; Kinesin-like protein KIF3A; Microtubule plus end-directed kinesin motor 3A Gene Symbols: KIF3A Molecular weight: 80,041 Da Basal Isoelectric point: 6.16  Predict pI for various phosphorylation states CST Pathways:  Hedgehog Signaling Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below KIF3A

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	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		K245	NMHVRMGKLHLVDLA
0	1		K259	AGSERQAKTGATGQR
0	1		T316-p	SLGGNSKtMMCANIG
0	1		Y327-p	ANIGPADyNyDETIS
0	1		Y329-p	IGPADyNyDETISTL
0	1		Y338-p	ETISTLRyANRAKNI
0	1		K346-a	ANRAKNIkNkARINE
0	1		K348-a	RAKNIkNkARINEDP
0	1		K356-a	ARINEDPkDALLRQF
0	1		K365-a	ALLRQFQkEIEELkk
0	1		K371-a	QkEIEELkkKLEEGE
0	1		K372-a	kEIEELkkKLEEGEE
0	1		S381-p	LEEGEEIsGsDIsGs
0	1		S383-p	EGEEIsGsDIsGsEE
0	1		S386-p	EIsGsDIsGsEEDDD
0	1		S388-p	sGsDIsGsEEDDDEE
0	12		S415-p	RRGKKKVsPDKMIEM
0	1		K431-a	AKIDEERkALETKLD
0	2		K477-a	EKLSALEkkVIVGGV
0	2		K478-a	KLSALEkkVIVGGVD
0	2		K495-a	AKAEEQEkLLEESNM
0	1		T551	KKLKKVWTMLMAAKS
0	39		Y624-p	WQLKCVAyTGNNMRK
0	1		T633	GNNMRKQTPVPDKKE
0	13		S687-p	KTGRRKRsAKPETVI

	mouse
K245-a	NMHVRMGkLHLVDLA
K259-a	AGSERQAkTGATGQR
T316	SLGGNSKTMMCANIG
Y327	ANIGPADYNYDETIS
Y329	IGPADYNYDETISTL
Y338	ETISTLRYANRAKNI
K346	ANRAKNIKNKARINE
K348	RAKNIKNKARINEDP
K356	ARINEDPKDALLRQF
K365	ALLRQFQKEIEELkk
K371-a	QKEIEELkkKLEEGE
K372-a	KEIEELkkKLEEGEE
S381	LEEGEEVSGSDISGS
S383	EGEEVSGSDISGSEE
S386	EVSGSDISGSEEDDE
S388	SGSDISGSEEDDEEG
S417-p	QAGKKKVsPDKMVEM
K433-a	AKIDEERkALETKLD
K479	EKLSALEKKVIVGGV
K480	KLSALEKKVIVGGVD
K497	AKAEEQEKLLEESNM
T553-p	KKLKKVWtMLMAAKS
Y626	WQLKCVAYTGNNMRK
T635-p	GNNMRKQtPVPDKKE
S689-p	KMGRRKRsAKPETVI

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