Publication for HAUS6 and NEDD1

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
hsa	HAUS6	HAUS augmin like complex subunit 6	54801			[link]
hsa	NEDD1	NEDD1 gamma-tubulin ring complex targeting factor	121441

Pubmed ID	Priority	Text
19029337	0.98	FAM29A (unpublished data), recruitment of NEDD1 to spindle MTs is under the control of FAM29A (Fig. 4 A).
	0.98	FAM29A almost quantitatively removed NEDD1 from spindle MTs without affecting its localization to centrosomes (Fig. 4, A and B).
	0.97	FAM29A did not alter the level of the NEDD1 protein (Fig. S4 B).
	0.97	FAM29A-NEDD1-gamma-tubulin complex peaked in mitosis and was reduced as cells exited into G1 (Fig. 5 C).
	0.97	FAM29A-NEDD1-gamma-tubulin complex amplifies MTs in the spindle, thereby efficiently increasing the MT mass for timely formation of the bipolar spindle.
	0.97	NEDD1 was efficiently targeted to chromatin foci in both control and FAM29A-depleted cells (Fig. 6 D).
	0.97	FAM29A interacts with the NEDD1-gamma-tubulin complex.
	0.96	FAM29A recruits NEDD1 onto spindle MTs.
	0.96	NEDD1 was cotransfected with GFP-FAM29A or GFP in HeLa cells.
	0.96	FAM29A promotes MT amplification through the recruitment of the NEDD1-gamma-tubulin complex to the mitotic spindle in a manner independent of centrosomes and chromatin.
	0.96	FAM29A-NEDD1 pathway is under active regulation, either through post-translational modifications or through an involvement of other uncharacterized factors.
	0.95	FAM29A cells transfected with siRNAs and stained for NEDD1 (green), beta-tubulin (red), and DNA (blue) (A).
	0.95	FAM29A promotes the nucleation of MTs from the spindle through recruitment of NEDD1 and gamma-tubulin, and that loss of this nucleation activity leads to a reduction of the MT density and an aberrant mitotic spindle.
	0.95	FAM29A and NEDD1 proteins are present throughout the cell cycle, they only interact in mitosis (Fig. 5).
	0.94	FAM29A-NEDD1 pathway controls the MT-dependent MT polymerization, a process important for the assembly of the spindle, for the maturation of k-MTs, and for normal progression of mitosis in mammalian cells.
	0.94	FAM29A with the NEDD1-gamma-tubulin complex is cell cycle regulated.
	0.91	FAM29A recruits NEDD1 to spindle MTs
	0.91	FAM29A is specifically required for the association of NEDD1 with spindle MTs, but not for its localization to centrosomes.
	0.91	FAM29A does not interfere with initial recruitment of NEDD1 to centrosomes and chromatin, but prevents the association of NEDD1 with newly synthesized MTs.
	0.90	FAM29A and NEDD1 colocalized on the entire mitotic spindle.
	0.87	FAM29A recruits the NEDD1-gamma-tubulin complex to MTs derived from centrosomes and chromatin to promote their amplification (IIIa and IIIb, respectively).
	0.81	FAM29A localization on NEDD1.
	0.79	NEDD1 and FAM29A in the cell cycle (Fig. S4 A, available at http://www.jcb.org/cgi/content/full/jcb.200807046/DC1).
	0.78	NEDD1 is still mostly on centrosomes, FAM29A becomes associated with newly polymerized MTs.
	0.78	FAM29A acts upstream of NEDD1 to promote its recruitment to the mitotic spindle.
	0.76	NEDD1 and FAM29A interact with each other.
	0.58	FAM29A and NEDD1 interact, we investigated the physiological forms of the FAM29A and NEDD1 proteins in mitosis by centrifugation of lysates of mitotic cells through a sucrose-density gradient.
	0.58	FAM29A and NEDD1 colocalized to the central spindle at anaphase (Fig. 1 B; Fig. S4 A).
22800182	0.98	HAUS6/FAM29A, which in turn binds the gamma-TuRC via NEDD1.
29514869	0.96	HAUS6 subunit to the recruitment factor NEDD1.
31455158	0.95	NEDD1, HAUS6), kinetochore function (e.g. SKA3, CENP-X), proteolysis (e.g. the 26S proteasome components PSMC3/4/5/7) and cytokinesis/abscission (e.g. CHMP1A/B) (figure 8a,b).
28351835	0.93	HAUS6 (FAM29A) subunit has been shown to associate with NEDD1, part of the MT nucleating gamma-Tubulin ring complex (gamma-TuRC).
21364642	0.50	FAM29A, one of these complex proteins, has been shown to interact with NEDD1 and recruits this protein and therefore also gamma-tubulin to the centrosome and mitotic spindle.