dbPTM

KIF11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KIF11_HUMAN
UniProt AC	P52732
Protein Name	Kinesin-like protein KIF11
Gene Name	KIF11
Organism	Homo sapiens (Human).
Sequence Length	1056
Subcellular Localization	Cytoplasm . Cytoplasm, cytoskeleton, spindle pole .
Protein Description	Motor protein required for establishing a bipolar spindle during mitosis. [PubMed: 19001501 Required in non-mitotic cells for transport of secretory proteins from the Golgi complex to the cell surface]
Protein Sequence	MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADKSSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSPNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSERLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFSVTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNILNKPEVNQKLTKKALIKEYTEEIERLKRDLAAAREKNGVYISEENFRVMSGKLTVQEEQIVELIEKIGAVEEELNRVTELFMDNKNELDQCKSDLQNKTQELETTQKHLQETKLQLVKEEYITSALESTEEKLHDAASKLLNTVEETTKDVSGLHSKLDRKKAVDQHNAEAQDIFGKNLNSLFNNMEELIKDGSSKQKAMLEVHKTLFGNLLSSSVSALDTITTVALGSLTSIPENVSTHVSQIFNMILKEQSLAAESKTVLQELINVLKTDLLSSLEMILSPTVVSILKINSQLKHIFKTSLTVADKIEDQKKELDGFLSILCNNLHELQENTICSLVESQKQCGNLTEDLKTIKQTHSQELCKLMNLWTERFCALEEKCENIQKPLSSVQENIQQKSKDIVNKMTFHSQKFCADSDGFSQELRNFNQEGTKLVEESVKHSDKLNGNLEKISQETEQRCESLNTRTVYFSEQWVSSLNEREQELHNLLEVVSQCCEASSSDITEKSDGRKAAHEKQHNIFLDQMTIDEDKLIAQNLELNETIKIGLTKLNCFLEQDLKLDIPTGTTPQRKSYLYPSTLVRTEPREHLLDQLKRKQPELLMMLNCSENNKEETIPDVDVEEAVLGQYTEEPLSQEPSVDAGVDCSSIGGVPFFQHKKSHGKDKENRGINTLERSKVEETTEHLVTKSRLPLRAQINL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASQPNSSAK -----CCCCCCCCCC	59.01	25072903
7	Phosphorylation	-MASQPNSSAKKKEE -CCCCCCCCCCCHHH	38.05	25072903
8	Phosphorylation	MASQPNSSAKKKEEK CCCCCCCCCCCHHHC	51.23	25072903
34	Ubiquitination	PFNLAERKASAHSIV CCCHHHCCCCCCCCE	37.89	-
36	Phosphorylation	NLAERKASAHSIVEC CHHHCCCCCCCCEEC	29.56	20873877
39	Phosphorylation	ERKASAHSIVECDPV HCCCCCCCCEECCCC	28.22	20873877
51	Phosphorylation	DPVRKEVSVRTGGLA CCCCCEEEEECCCCC	13.63	29496963
60	Acetylation	RTGGLADKSSRKTYT ECCCCCCCCCCCEEE	44.73	25953088
60	Ubiquitination	RTGGLADKSSRKTYT ECCCCCCCCCCCEEE	44.73	27667366
62	Phosphorylation	GGLADKSSRKTYTFD CCCCCCCCCCEEEEE	43.46	17081983
75	Phosphorylation	FDMVFGASTKQIDVY EEEEECCCCCHHEEH	36.19	28355574
82	Phosphorylation	STKQIDVYRSVVCPI CCCHHEEHHHCHHHH	8.07	28787133
114	Phosphorylation	TGTGKTFTMEGERSP CCCCCEEEECCCCCC	21.39	-
120	Phosphorylation	FTMEGERSPNEEYTW EEECCCCCCCCCCCC	27.98	25106551
125	Phosphorylation	ERSPNEEYTWEEDPL CCCCCCCCCCCCCCH	15.80	28796482
126	Phosphorylation	RSPNEEYTWEEDPLA CCCCCCCCCCCCCHH	29.67	25106551
146	Acetylation	TLHQIFEKLTDNGTE HHHHHHHHHCCCCCE	46.03	19608861
197	Ubiquitination	NKRGVIIKGLEEITV CCCCEEEECCCEEEE	46.44	29967540
207	Ubiquitination	EEITVHNKDEVYQIL CEEEECCHHHHHHHH	40.15	29967540
211	Phosphorylation	VHNKDEVYQILEKGA ECCHHHHHHHHHHCC	6.44	27642862
216	Ubiquitination	EVYQILEKGAAKRTT HHHHHHHHCCCCHHH	50.86	29967540
222	Phosphorylation	EKGAAKRTTAATLMN HHCCCCHHHHHHHHH	21.78	24505115
223	Phosphorylation	KGAAKRTTAATLMNA HCCCCHHHHHHHHHH	20.51	20860994
226	Phosphorylation	AKRTTAATLMNAYSS CCHHHHHHHHHHHHC	24.87	20860994
231	Phosphorylation	AATLMNAYSSRSHSV HHHHHHHHHCCCCCE	11.37	20166139
232	Phosphorylation	ATLMNAYSSRSHSVF HHHHHHHHCCCCCEE	19.50	20166139
233	Phosphorylation	TLMNAYSSRSHSVFS HHHHHHHCCCCCEEE	25.73	20166139
240	Phosphorylation	SRSHSVFSVTIHMKE CCCCCEEEEEEEEEE	19.05	-
257	Ubiquitination	IDGEELVKIGKLNLV ECHHHHEEEECCCEE	59.36	29967540
260	Ubiquitination	EELVKIGKLNLVDLA HHHEEEECCCEEECC	37.36	29967540
291	Phosphorylation	EAGNINQSLLTLGRV HCCCCCHHHHHHHHH	22.36	-
294	Phosphorylation	NINQSLLTLGRVITA CCCHHHHHHHHHHHH	32.24	-
306	Phosphorylation	ITALVERTPHVPYRE HHHHHHCCCCCCCCH	12.30	28555341
323	Phosphorylation	LTRILQDSLGGRTRT HHHHHHHHCCCCCCC	18.89	21406692
357	Ubiquitination	LEYAHRAKNILNKPE HHHHHHHHHHCCCHH	44.47	29967540
362	Acetylation	RAKNILNKPEVNQKL HHHHHCCCHHHHHHH	38.83	26051181
362	Ubiquitination	RAKNILNKPEVNQKL HHHHHCCCHHHHHHH	38.83	29967540
372	Acetylation	VNQKLTKKALIKEYT HHHHHHHHHHHHHHH	43.09	18527761
376	Acetylation	LTKKALIKEYTEEIE HHHHHHHHHHHHHHH	45.58	18527769
376	Ubiquitination	LTKKALIKEYTEEIE HHHHHHHHHHHHHHH	45.58	29967540
395	Ubiquitination	DLAAAREKNGVYISE HHHHHHHHCCEEECC	54.14	29967540
399	Phosphorylation	AREKNGVYISEENFR HHHHCCEEECCCCEE	10.50	28796482
401	Phosphorylation	EKNGVYISEENFRVM HHCCEEECCCCEEEE	22.59	29978859
441	Sulfoxidation	NRVTELFMDNKNELD HHHHHHHHCCHHHHH	9.67	21406390
444	Ubiquitination	TELFMDNKNELDQCK HHHHHCCHHHHHHHH	47.75	29967540
451	Ubiquitination	KNELDQCKSDLQNKT HHHHHHHHHHHHHHH	41.18	29967540
457	Ubiquitination	CKSDLQNKTQELETT HHHHHHHHHHHHHHH	38.33	32015554
458	Phosphorylation	KSDLQNKTQELETTQ HHHHHHHHHHHHHHH	34.52	17525332
463	Phosphorylation	NKTQELETTQKHLQE HHHHHHHHHHHHHHH	47.34	-
464	Phosphorylation	KTQELETTQKHLQET HHHHHHHHHHHHHHH	26.67	-
466	Ubiquitination	QELETTQKHLQETKL HHHHHHHHHHHHHHH	44.16	29967540
472	Ubiquitination	QKHLQETKLQLVKEE HHHHHHHHHHHHHHH	33.22	29967540
477	Sumoylation	ETKLQLVKEEYITSA HHHHHHHHHHHHHHH	54.11	28112733
477	Ubiquitination	ETKLQLVKEEYITSA HHHHHHHHHHHHHHH	54.11	29967540
480	Phosphorylation	LQLVKEEYITSALES HHHHHHHHHHHHHHC	15.59	28796482
482	Phosphorylation	LVKEEYITSALESTE HHHHHHHHHHHHCHH	13.67	21406692
483	Phosphorylation	VKEEYITSALESTEE HHHHHHHHHHHCHHH	22.69	21406692
487	Phosphorylation	YITSALESTEEKLHD HHHHHHHCHHHHHHH	41.80	21406692
488	Phosphorylation	ITSALESTEEKLHDA HHHHHHCHHHHHHHH	38.50	21406692
491	Ubiquitination	ALESTEEKLHDAASK HHHCHHHHHHHHHHH	44.91	29967540
498	Ubiquitination	KLHDAASKLLNTVEE HHHHHHHHHHHHHHH	52.87	29967540
502	Phosphorylation	AASKLLNTVEETTKD HHHHHHHHHHHHHCC	29.30	20068231
506	Phosphorylation	LLNTVEETTKDVSGL HHHHHHHHHCCCCHH	26.16	20068231
507	Phosphorylation	LNTVEETTKDVSGLH HHHHHHHHCCCCHHH	28.64	20068231
508	Ubiquitination	NTVEETTKDVSGLHS HHHHHHHCCCCHHHH	64.65	29967540
516	Ubiquitination	DVSGLHSKLDRKKAV CCCHHHHHHCHHHHH	43.59	29967540
521	Ubiquitination	HSKLDRKKAVDQHNA HHHHCHHHHHHHHCH	55.31	29967540
536	Ubiquitination	EAQDIFGKNLNSLFN HHHHHHHHHHHHHHH	47.73	29967540
540	Phosphorylation	IFGKNLNSLFNNMEE HHHHHHHHHHHCHHH	37.19	28355574
550	Ubiquitination	NNMEELIKDGSSKQK HCHHHHHHCCCHHHH	69.53	21906983
555	Ubiquitination	LIKDGSSKQKAMLEV HHHCCCHHHHHHHHH	58.47	22817900
618	Ubiquitination	QSLAAESKTVLQELI HCHHHCCHHHHHHHH	33.87	29967540
643	Phosphorylation	LEMILSPTVVSILKI HHHHHCHHHHHHHHH	30.11	-
646	Phosphorylation	ILSPTVVSILKINSQ HHCHHHHHHHHHHHH	20.19	24719451
652	Phosphorylation	VSILKINSQLKHIFK HHHHHHHHHHHHHHH	40.12	-
655	Ubiquitination	LKINSQLKHIFKTSL HHHHHHHHHHHHHCC	27.32	29967540
659	Ubiquitination	SQLKHIFKTSLTVAD HHHHHHHHHCCHHHH	36.28	29967540
663	Phosphorylation	HIFKTSLTVADKIED HHHHHCCHHHHHHHH	17.26	-
667	Ubiquitination	TSLTVADKIEDQKKE HCCHHHHHHHHHHHH	37.95	29967540
672	Ubiquitination	ADKIEDQKKELDGFL HHHHHHHHHHHHHHH	61.61	-
712	Ubiquitination	GNLTEDLKTIKQTHS CCCHHHHHHHHHHHH	61.60	32015554
715	Acetylation	TEDLKTIKQTHSQEL HHHHHHHHHHHHHHH	55.14	25953088
715	Ubiquitination	TEDLKTIKQTHSQEL HHHHHHHHHHHHHHH	55.14	29967540
724	Ubiquitination	THSQELCKLMNLWTE HHHHHHHHHHHHHHH	64.49	29967540
739	Ubiquitination	RFCALEEKCENIQKP HHHHHHHHHHHCHHH	37.16	29967540
745	Ubiquitination	EKCENIQKPLSSVQE HHHHHCHHHHHHHHH	44.09	29967540
757	Ubiquitination	VQENIQQKSKDIVNK HHHHHHHHHHHHHHH	43.00	29967540
764	Ubiquitination	KSKDIVNKMTFHSQK HHHHHHHHHHHCCHH	28.55	29967540
771	Ubiquitination	KMTFHSQKFCADSDG HHHHCCHHCCCCCCC	45.48	29967540
784	Methylation	DGFSQELRNFNQEGT CCHHHHHHCCCHHHH	44.96	115481109
792	Ubiquitination	NFNQEGTKLVEESVK CCCHHHHHHHHHHHH	62.48	29967540
803	Acetylation	ESVKHSDKLNGNLEK HHHHCHHHCCCCHHH	47.03	19413330
803	Ubiquitination	ESVKHSDKLNGNLEK HHHHCHHHCCCCHHH	47.03	19413330
810	Ubiquitination	KLNGNLEKISQETEQ HCCCCHHHHHHHHHH	51.31	29967540
821	Phosphorylation	ETEQRCESLNTRTVY HHHHHHHHCCCCEEE	30.46	24245541
852	Phosphorylation	HNLLEVVSQCCEASS HHHHHHHHHHHHHCC	23.75	-
858	Phosphorylation	VSQCCEASSSDITEK HHHHHHHCCCCCCCC	14.21	-
875	Ubiquitination	GRKAAHEKQHNIFLD CCCHHHHHHHCCCCC	47.17	29967540
890	Ubiquitination	QMTIDEDKLIAQNLE CCCCCHHHHHHHHCC	39.48	29967540
903	Ubiquitination	LELNETIKIGLTKLN CCCCCCEEECCHHHH	37.83	22817900
908	Acetylation	TIKIGLTKLNCFLEQ CEEECCHHHHHHHHC	42.62	25953088
908	Ubiquitination	TIKIGLTKLNCFLEQ CEEECCHHHHHHHHC	42.62	21963094
918	Ubiquitination	CFLEQDLKLDIPTGT HHHHCCCCCCCCCCC	53.02	29967540
923	Phosphorylation	DLKLDIPTGTTPQRK CCCCCCCCCCCCCCC	47.71	16964243
925	Phosphorylation	KLDIPTGTTPQRKSY CCCCCCCCCCCCCCC	37.47	29255136
926	Phosphorylation	LDIPTGTTPQRKSYL CCCCCCCCCCCCCCC	20.83	19664994
930	Ubiquitination	TGTTPQRKSYLYPST CCCCCCCCCCCCCCC	37.90	29967540
931	Phosphorylation	GTTPQRKSYLYPSTL CCCCCCCCCCCCCCE	23.66	25159151
932	Phosphorylation	TTPQRKSYLYPSTLV CCCCCCCCCCCCCEE	17.19	21712546
934	Phosphorylation	PQRKSYLYPSTLVRT CCCCCCCCCCCEECC	6.21	27174698
936	Phosphorylation	RKSYLYPSTLVRTEP CCCCCCCCCEECCCC	22.33	27174698
937	Phosphorylation	KSYLYPSTLVRTEPR CCCCCCCCEECCCCC	25.43	27174698
952	Ubiquitination	EHLLDQLKRKQPELL HHHHHHHHHHCCCHH	52.49	32015554
965	Phosphorylation	LLMMLNCSENNKEET HHHHEECCCCCCCCC	42.14	28674419
1025	Methylation	HGKDKENRGINTLER CCCCCCCCCCCHHHH	48.76	115481101
1029	Phosphorylation	KENRGINTLERSKVE CCCCCCCHHHHHHHC	28.24	30576142
1033	Phosphorylation	GINTLERSKVEETTE CCCHHHHHHHCHHHH	31.51	25159151
1034	Ubiquitination	INTLERSKVEETTEH CCHHHHHHHCHHHHH	60.94	23000965
1038	Phosphorylation	ERSKVEETTEHLVTK HHHHHCHHHHHHHHH	24.79	29978859
1039	Phosphorylation	RSKVEETTEHLVTKS HHHHCHHHHHHHHHC	25.37	29978859
1044	Phosphorylation	ETTEHLVTKSRLPLR HHHHHHHHHCCCCCC	29.66	24719451
1045	Acetylation	TTEHLVTKSRLPLRA HHHHHHHHCCCCCCE	26.54	25953088
1045	Ubiquitination	TTEHLVTKSRLPLRA HHHHHHHHCCCCCCE	26.54	23000965

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
125	Y	Phosphorylation	Kinase	SRC	P12931	PSP
211	Y	Phosphorylation	Kinase	SRC	P12931	PSP
231	Y	Phosphorylation	Kinase	SRC	P12931	PSP
926	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
926	T	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
926	T	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
1033	S	Phosphorylation	Kinase	NEK6	Q9HC98	Uniprot
1033	S	Phosphorylation	Kinase	NEK7	Q8TDX7	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
926	T	Phosphorylation		8548803
Phosphorylated exclusively on serine during S phase, but on both serine and Thr-926 during mitosis, so controlling the association of KIF11 with the spindle apparatus (probably during early prophase).

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 KIF11_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DCTN1_HUMAN	DCTN1	physical	9235942
KIF11_HUMAN	KIF11	physical	9235942
KIF5A_HUMAN	KIF5A	physical	22939629
P4K2A_HUMAN	PI4K2A	physical	26344197
RU17_HUMAN	SNRNP70	physical	26344197
RED2_HUMAN	ADARB2	physical	26496610
AP2A2_HUMAN	AP2A2	physical	26496610
ANK3_HUMAN	ANK3	physical	26496610
ANXA1_HUMAN	ANXA1	physical	26496610
ANXA7_HUMAN	ANXA7	physical	26496610
CALD1_HUMAN	CALD1	physical	26496610
CETN2_HUMAN	CETN2	physical	26496610
DECR_HUMAN	DECR1	physical	26496610
ACSL3_HUMAN	ACSL3	physical	26496610
FAS_HUMAN	FASN	physical	26496610
H33_HUMAN	H3F3A	physical	26496610
VIGLN_HUMAN	HDLBP	physical	26496610
LAMB1_HUMAN	LAMB1	physical	26496610
LDHA_HUMAN	LDHA	physical	26496610
MAP4_HUMAN	MAP4	physical	26496610
KMT2A_HUMAN	KMT2A	physical	26496610
MYO1C_HUMAN	MYO1C	physical	26496610
ORC2_HUMAN	ORC2	physical	26496610
PDE3A_HUMAN	PDE3A	physical	26496610
PFKAM_HUMAN	PFKM	physical	26496610
KPCA_HUMAN	PRKCA	physical	26496610
RL23A_HUMAN	RPL23A	physical	26496610
RL28_HUMAN	RPL28	physical	26496610
RL32_HUMAN	RPL32	physical	26496610
RL36L_HUMAN	RPL36AL	physical	26496610
RL37A_HUMAN	RPL37A	physical	26496610
RS3A_HUMAN	RPS3A	physical	26496610
RS6_HUMAN	RPS6	physical	26496610
RS23_HUMAN	RPS23	physical	26496610
SMD3_HUMAN	SNRPD3	physical	26496610
SUV91_HUMAN	SUV39H1	physical	26496610
TLN1_HUMAN	TLN1	physical	26496610
ZKSC8_HUMAN	ZKSCAN8	physical	26496610
LUZP1_HUMAN	LUZP1	physical	26496610
BRPF1_HUMAN	BRPF1	physical	26496610
H31_HUMAN	HIST1H3A	physical	26496610
DUS11_HUMAN	DUSP11	physical	26496610
EIF3A_HUMAN	EIF3A	physical	26496610
EIF3I_HUMAN	EIF3I	physical	26496610
NOLC1_HUMAN	NOLC1	physical	26496610
MED14_HUMAN	MED14	physical	26496610
TRIP4_HUMAN	TRIP4	physical	26496610
CE350_HUMAN	CEP350	physical	26496610
ILVBL_HUMAN	ILVBL	physical	26496610
ANKL2_HUMAN	ANKLE2	physical	26496610
T131L_HUMAN	KIAA0922	physical	26496610
NOG1_HUMAN	GTPBP4	physical	26496610
EDC4_HUMAN	EDC4	physical	26496610
HSPB8_HUMAN	HSPB8	physical	26496610
AP3M1_HUMAN	AP3M1	physical	26496610
PNMA3_HUMAN	PNMA3	physical	26496610
IRAK4_HUMAN	IRAK4	physical	26496610
RM27_HUMAN	MRPL27	physical	26496610
NOL7_HUMAN	NOL7	physical	26496610
NT5D3_HUMAN	NT5DC3	physical	26496610
MET13_HUMAN	METTL13	physical	26496610
ACSL5_HUMAN	ACSL5	physical	26496610
ARI4B_HUMAN	ARID4B	physical	26496610
PKHA5_HUMAN	PLEKHA5	physical	26496610
DGCR8_HUMAN	DGCR8	physical	26496610
RBM28_HUMAN	RBM28	physical	26496610
ZGRF1_HUMAN	ZGRF1	physical	26496610
PCID2_HUMAN	PCID2	physical	26496610
ARP10_HUMAN	ACTR10	physical	26496610
MTUS1_HUMAN	MTUS1	physical	26496610
LST8_HUMAN	MLST8	physical	26496610
SPAS2_HUMAN	SPATS2	physical	26496610
PRR3_HUMAN	PRR3	physical	26496610
DLRB1_HUMAN	DYNLRB1	physical	26496610
FWCH1_HUMAN	FLYWCH1	physical	26496610
SPIR2_HUMAN	SPIRE2	physical	26496610
CE295_HUMAN	CEP295	physical	26496610
F122A_HUMAN	FAM122A	physical	26496610
RBM45_HUMAN	RBM45	physical	26496610
DHR13_HUMAN	DHRS13	physical	26496610
ANKS6_HUMAN	ANKS6	physical	26496610
CB069_HUMAN	C2orf69	physical	26496610
DDX51_HUMAN	DDX51	physical	26496610
H3C_HUMAN	H3F3C	physical	26496610
BRE1A_HUMAN	RNF20	physical	27557628
BRE1B_HUMAN	RNF40	physical	27557628

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
152950	Microcephaly with or without chorioretinopathy, lymphedema, or mental retardation (MCLMR)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KIF11_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-146, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novelsite necessary for mitotic spindle formation."; Rapley J., Nicolas M., Groen A., Regue L., Bertran M.T., Caelles C.,Avruch J., Roig J.; J. Cell Sci. 121:3912-3921(2008). Cited for: FUNCTION, INTERACTION WITH NEK6, SUBCELLULAR LOCATION, PHOSPHORYLATIONAT THR-926 AND SER-1033, AND MUTAGENESIS OF THR-926 AND SER-1033.	19001501 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-926; THR-1029 ANDSER-1033, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-926 AND SER-931, ANDMASS SPECTROMETRY.	16565220 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-926, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-926, AND MASSSPECTROMETRY.	19413330 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-458, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Phosphorylation by p34cdc2 regulates spindle association of humanEg5, a kinesin-related motor essential for bipolar spindle formationin vivo."; Blangy A., Lane H.A., D'Herin P., Harper M., Kress M., Nigg E.A.; Cell 83:1159-1169(1995). Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-926, ANDMUTAGENESIS.	8548803 [Abstract]

show