dbPTM

MK67I_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MK67I_HUMAN
UniProt AC	Q9BYG3
Protein Name	MKI67 FHA domain-interacting nucleolar phosphoprotein
Gene Name	NIFK
Organism	Homo sapiens (Human).
Sequence Length	293
Subcellular Localization	Nucleus, nucleolus. Chromosome. Localizes to mitotic chromosomes in conjunction with MKI67.
Protein Description
Protein Sequence	MATFSGPAGPILSLNPQEDVEFQKEVAQVRKRITQRKKQEQLTPGVVYVRHLPNLLDETQIFSYFSQFGTVTRFRLSRSKRTGNSKGYAFVEFESEDVAKIVAETMNNYLFGERLLECHFMPPEKVHKELFKDWNIPFKQPSYPSVKRYNRNRTLTQKLRMEERFKKKERLLRKKLAKKGIDYDFPSLILQKTESISKTNRQTSTKGQVLRKKKKKVSGTLDTPEKTVDSQGPTPVCTPTFLERRKSQVAELNDDDKDDEIVFKQPISCVKEEIQETQTPTHSRKKRRRSSNQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATFSGPAG ------CCCCCCCCC	19.83	22223895
38	Ubiquitination	KRITQRKKQEQLTPG HHHHHHHHHHHCCCC	62.35	24816145
38	Sumoylation	KRITQRKKQEQLTPG HHHHHHHHHHHCCCC	62.35	28112733
38	Sumoylation	KRITQRKKQEQLTPG HHHHHHHHHHHCCCC	62.35	-
82	Phosphorylation	RLSRSKRTGNSKGYA EEECCCCCCCCCCEE	44.44	-
88	Phosphorylation	RTGNSKGYAFVEFES CCCCCCCEEEEEECC	10.70	-
109	Phosphorylation	VAETMNNYLFGERLL HHHHHHHHHHCCHHH	9.82	23663014
114	Methylation	NNYLFGERLLECHFM HHHHHCCHHHCCCCC	44.97	26529540
128	Ubiquitination	MPPEKVHKELFKDWN CCHHHHHHHHHHCCC	60.13	29967540
139	Sumoylation	KDWNIPFKQPSYPSV HCCCCCCCCCCCHHH	56.81	-
139	Ubiquitination	KDWNIPFKQPSYPSV HCCCCCCCCCCCHHH	56.81	23000965
139	Sumoylation	KDWNIPFKQPSYPSV HCCCCCCCCCCCHHH	56.81	28112733
139	Methylation	KDWNIPFKQPSYPSV HCCCCCCCCCCCHHH	56.81	44496799
142	Phosphorylation	NIPFKQPSYPSVKRY CCCCCCCCCHHHHHH	47.37	28152594
143	Phosphorylation	IPFKQPSYPSVKRYN CCCCCCCCHHHHHHC	13.25	28152594
145	Phosphorylation	FKQPSYPSVKRYNRN CCCCCCHHHHHHCCC	31.85	28152594
154	Phosphorylation	KRYNRNRTLTQKLRM HHHCCCCCHHHHHHH	37.39	-
156	Phosphorylation	YNRNRTLTQKLRMEE HCCCCCHHHHHHHHH	24.05	-
158	Ubiquitination	RNRTLTQKLRMEERF CCCCHHHHHHHHHHH	32.59	27667366
179	Ubiquitination	LRKKLAKKGIDYDFP HHHHHHHCCCCCCCH	56.33	33845483
179	Sumoylation	LRKKLAKKGIDYDFP HHHHHHHCCCCCCCH	56.33	28112733
179	Methylation	LRKKLAKKGIDYDFP HHHHHHHCCCCCCCH	56.33	23748837
179	Acetylation	LRKKLAKKGIDYDFP HHHHHHHCCCCCCCH	56.33	27452117
183	Phosphorylation	LAKKGIDYDFPSLIL HHHCCCCCCCHHHHH	19.98	28796482
187	Phosphorylation	GIDYDFPSLILQKTE CCCCCCHHHHHHHHH	28.21	27642862
192	Acetylation	FPSLILQKTESISKT CHHHHHHHHHCCCCC	51.30	26051181
192	Ubiquitination	FPSLILQKTESISKT CHHHHHHHHHCCCCC	51.30	29967540
192	Sumoylation	FPSLILQKTESISKT CHHHHHHHHHCCCCC	51.30	28112733
198	2-Hydroxyisobutyrylation	QKTESISKTNRQTST HHHHCCCCCCCCCCC	48.42	-
199	Phosphorylation	KTESISKTNRQTSTK HHHCCCCCCCCCCCH	28.92	-
204	Phosphorylation	SKTNRQTSTKGQVLR CCCCCCCCCHHHHHH	21.56	28857561
206	Ubiquitination	TNRQTSTKGQVLRKK CCCCCCCHHHHHHHH	47.30	29967540
218	Phosphorylation	RKKKKKVSGTLDTPE HHHHCCCCCCCCCCC	34.63	29255136
220	Phosphorylation	KKKKVSGTLDTPEKT HHCCCCCCCCCCCCC	17.60	29255136
223	Phosphorylation	KVSGTLDTPEKTVDS CCCCCCCCCCCCCCC	36.14	19664994
226	Acetylation	GTLDTPEKTVDSQGP CCCCCCCCCCCCCCC	55.86	26051181
227	Phosphorylation	TLDTPEKTVDSQGPT CCCCCCCCCCCCCCC	28.08	29255136
230	Phosphorylation	TPEKTVDSQGPTPVC CCCCCCCCCCCCCCC	32.47	29255136
234	Phosphorylation	TVDSQGPTPVCTPTF CCCCCCCCCCCCHHH	34.87	29255136
237	Glutathionylation	SQGPTPVCTPTFLER CCCCCCCCCHHHHHH	3.87	22555962
238	Phosphorylation	QGPTPVCTPTFLERR CCCCCCCCHHHHHHH	26.12	29255136
240	Phosphorylation	PTPVCTPTFLERRKS CCCCCCHHHHHHHHH	23.77	29255136
244	Methylation	CTPTFLERRKSQVAE CCHHHHHHHHHHHHC	54.17	26529540
245	Methylation	TPTFLERRKSQVAEL CHHHHHHHHHHHHCC	33.33	26529540
247	Phosphorylation	TFLERRKSQVAELND HHHHHHHHHHHCCCC	28.24	29255136
257	Acetylation	AELNDDDKDDEIVFK HCCCCCCCCCCEEEC	74.25	26051181
264	Acetylation	KDDEIVFKQPISCVK CCCCEEECCCCHHHH	44.25	26051181
268	Phosphorylation	IVFKQPISCVKEEIQ EEECCCCHHHHHHHH	21.38	28102081
271	Acetylation	KQPISCVKEEIQETQ CCCCHHHHHHHHHCC	54.69	26051181
271	Sumoylation	KQPISCVKEEIQETQ CCCCHHHHHHHHHCC	54.69	-
271	Sumoylation	KQPISCVKEEIQETQ CCCCHHHHHHHHHCC	54.69	25114211
277	Phosphorylation	VKEEIQETQTPTHSR HHHHHHHCCCCCCHH	22.74	29255136
279	Phosphorylation	EEIQETQTPTHSRKK HHHHHCCCCCCHHHH	37.26	29255136
281	Phosphorylation	IQETQTPTHSRKKRR HHHCCCCCCHHHHHH	35.55	29255136
283	Phosphorylation	ETQTPTHSRKKRRRS HCCCCCCHHHHHHHC	48.55	29255136
284	Methylation	TQTPTHSRKKRRRSS CCCCCCHHHHHHHCC	40.69	26529540
290	Phosphorylation	SRKKRRRSSNQ---- HHHHHHHCCCC----	31.65	-
291	Phosphorylation	RKKRRRSSNQ----- HHHHHHCCCC-----	37.12	-

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
230	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
230	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
234	T	Phosphorylation	Kinase	GSK3A	P49840	PSP
234	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
238	T	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
230	S	Phosphorylation	16244663
Likewise, phosphorylation at Ser-230 requires that Thr-234 and Thr-238 are phosphorylated.
230	S	Phosphorylation	16244663
Sequentially phosphorylated on Thr-238, Thr-234 and Ser-230.
234	T	Phosphorylation	11342549
Likewise, phosphorylation at Ser-230 requires that Thr-234 and Thr-238 are phosphorylated.
234	T	Phosphorylation	11342549
Sequentially phosphorylated on Thr-238, Thr-234 and Ser-230.
234	T	Phosphorylation	11342549
Thr-234 is phosphorylated only when Thr-238 is phosphorylated.
238	T	Phosphorylation	11342549
Likewise, phosphorylation at Ser-230 requires that Thr-234 and Thr-238 are phosphorylated.
238	T	Phosphorylation	11342549
Sequentially phosphorylated on Thr-238, Thr-234 and Ser-230.
238	T	Phosphorylation	11342549
Thr-234 is phosphorylated only when Thr-238 is phosphorylated.

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 MK67I_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NOP58_HUMAN	NOP58	physical	22939629
RL19_HUMAN	RPL19	physical	22939629
RRS1_HUMAN	RRS1	physical	22939629
RL18A_HUMAN	RPL18A	physical	22939629
RL30_HUMAN	RPL30	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL23_HUMAN	RPL23	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
SPB1_HUMAN	FTSJ3	physical	22939629
RL11_HUMAN	RPL11	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RL15_HUMAN	RPL15	physical	22939629
NH2L1_HUMAN	NHP2L1	physical	22939629
NOP2_HUMAN	NOP2	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
LARP7_HUMAN	LARP7	physical	26186194
RL26L_HUMAN	RPL26L1	physical	26186194
RPF1_HUMAN	RPF1	physical	26186194
YBOX2_HUMAN	YBX2	physical	26186194
RBM28_HUMAN	RBM28	physical	26186194
YTDC2_HUMAN	YTHDC2	physical	26186194
SRRM1_HUMAN	SRRM1	physical	26186194
POP1_HUMAN	POP1	physical	26186194
DDX24_HUMAN	DDX24	physical	26186194
RT26_HUMAN	MRPS26	physical	26186194
SPB1_HUMAN	FTSJ3	physical	26186194
PRP4B_HUMAN	PRPF4B	physical	26186194
RRS1_HUMAN	RRS1	physical	26186194
ZN574_HUMAN	ZNF574	physical	26186194
ZNF7_HUMAN	ZNF7	physical	26186194
TAF1A_HUMAN	TAF1A	physical	26186194
UTP18_HUMAN	UTP18	physical	26186194
PTCD3_HUMAN	PTCD3	physical	26186194
RENT1_HUMAN	UPF1	physical	26186194
STAU2_HUMAN	STAU2	physical	26186194
NCBP3_HUMAN	C17orf85	physical	26186194
SRP72_HUMAN	SRP72	physical	26186194
DDX27_HUMAN	DDX27	physical	26186194
RL1D1_HUMAN	RSL1D1	physical	26186194
DDX31_HUMAN	DDX31	physical	26186194
MBB1A_HUMAN	MYBBP1A	physical	26186194
RBM19_HUMAN	RBM19	physical	26186194
RS3A_HUMAN	RPS3A	physical	26186194
WDR12_HUMAN	WDR12	physical	26186194
RM48_HUMAN	MRPL48	physical	26186194
RRP8_HUMAN	RRP8	physical	26186194
ZCCHV_HUMAN	ZC3HAV1	physical	26186194
TTF1_HUMAN	TTF1	physical	26186194
ZCHC3_HUMAN	ZCCHC3	physical	26186194
SFR19_HUMAN	SCAF1	physical	26186194
NKRF_HUMAN	NKRF	physical	26186194
NPM_HUMAN	NPM1	physical	26186194
NOG1_HUMAN	GTPBP4	physical	26186194
LARP1_HUMAN	LARP1	physical	26186194
LAR1B_HUMAN	LARP1B	physical	26186194
NOP2_HUMAN	NOP2	physical	26186194
SRP68_HUMAN	SRP68	physical	26186194
NOG2_HUMAN	GNL2	physical	26186194
BMS1_HUMAN	BMS1	physical	26186194
RBBP6_HUMAN	RBBP6	physical	26186194
LN28B_HUMAN	LIN28B	physical	26186194
KRR1_HUMAN	KRR1	physical	26186194
RS8_HUMAN	RPS8	physical	26186194
BRX1_HUMAN	BRIX1	physical	26186194
DDX54_HUMAN	DDX54	physical	26186194
PK1IP_HUMAN	PAK1IP1	physical	26186194
NOP9_HUMAN	NOP9	physical	26186194
ZCHC9_HUMAN	ZCCHC9	physical	26186194
PUM3_HUMAN	KIAA0020	physical	26186194
RM47_HUMAN	MRPL47	physical	26186194
NOC4L_HUMAN	NOC4L	physical	26186194
PAPD5_HUMAN	PAPD5	physical	26186194
ZN770_HUMAN	ZNF770	physical	26186194
PESC_HUMAN	PES1	physical	26186194
CENPN_HUMAN	CENPN	physical	26186194
PHAX_HUMAN	PHAX	physical	26186194
ZBT11_HUMAN	ZBTB11	physical	26186194
RL7L_HUMAN	RPL7L1	physical	26186194
RL13A_HUMAN	RPL13A	physical	26186194
RFC1_HUMAN	RFC1	physical	26186194
RL37A_HUMAN	RPL37A	physical	26186194
RPF2_HUMAN	RPF2	physical	26186194
BUD13_HUMAN	BUD13	physical	26186194
ARGL1_HUMAN	ARGLU1	physical	26186194
H2A2B_HUMAN	HIST2H2AB	physical	26186194
DHX37_HUMAN	DHX37	physical	26186194
IMP3_HUMAN	IMP3	physical	26186194
G45IP_HUMAN	GADD45GIP1	physical	26186194
BBX_HUMAN	BBX	physical	26186194
SPT2_HUMAN	SPTY2D1	physical	26186194
CENPC_HUMAN	CENPC	physical	26186194
ZNF70_HUMAN	ZNF70	physical	26186194
NLE1_HUMAN	NLE1	physical	26186194
TDIF2_HUMAN	DNTTIP2	physical	26186194
SREK1_HUMAN	SREK1	physical	26186194
TOE1_HUMAN	TOE1	physical	26186194
TAF1B_HUMAN	TAF1B	physical	26186194
TOPRS_HUMAN	TOPORS	physical	26186194
ZN689_HUMAN	ZNF689	physical	26186194
ZNF48_HUMAN	ZNF48	physical	26186194
PRR3_HUMAN	PRR3	physical	26186194
MKRN2_HUMAN	MKRN2	physical	26186194
NSA2_HUMAN	NSA2	physical	26344197
RBM28_HUMAN	RBM28	physical	26344197
RPF2_HUMAN	RPF2	physical	26344197
TBL3_HUMAN	TBL3	physical	26344197
YBOX2_HUMAN	YBX2	physical	28514442
CENPI_HUMAN	CENPI	physical	28514442
ARGL1_HUMAN	ARGLU1	physical	28514442
CENPC_HUMAN	CENPC	physical	28514442
RBM19_HUMAN	RBM19	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
ZNF7_HUMAN	ZNF7	physical	28514442
TOPRS_HUMAN	TOPORS	physical	28514442
RENT1_HUMAN	UPF1	physical	28514442
NOG2_HUMAN	GNL2	physical	28514442
SPT2_HUMAN	SPTY2D1	physical	28514442
SREK1_HUMAN	SREK1	physical	28514442
DDX54_HUMAN	DDX54	physical	28514442
TDIF2_HUMAN	DNTTIP2	physical	28514442
TAF1B_HUMAN	TAF1B	physical	28514442
SFR19_HUMAN	SCAF1	physical	28514442
ZCHC9_HUMAN	ZCCHC9	physical	28514442
POP1_HUMAN	POP1	physical	28514442
BBX_HUMAN	BBX	physical	28514442
NCBP3_HUMAN	C17orf85	physical	28514442
LARP1_HUMAN	LARP1	physical	28514442
NLE1_HUMAN	NLE1	physical	28514442
PUM3_HUMAN	KIAA0020	physical	28514442
RPF2_HUMAN	RPF2	physical	28514442
LAR1B_HUMAN	LARP1B	physical	28514442
SRRM1_HUMAN	SRRM1	physical	28514442
CENPN_HUMAN	CENPN	physical	28514442
ZNF48_HUMAN	ZNF48	physical	28514442
ZN689_HUMAN	ZNF689	physical	28514442
ZCHC3_HUMAN	ZCCHC3	physical	28514442
RPF1_HUMAN	RPF1	physical	28514442
ZN574_HUMAN	ZNF574	physical	28514442
RBM34_HUMAN	RBM34	physical	28514442
NOG1_HUMAN	GTPBP4	physical	28514442
RM48_HUMAN	MRPL48	physical	28514442
ZNF70_HUMAN	ZNF70	physical	28514442
BUD13_HUMAN	BUD13	physical	28514442
RBM28_HUMAN	RBM28	physical	28514442
RS3A_HUMAN	RPS3A	physical	28514442
PRR3_HUMAN	PRR3	physical	28514442
DDX31_HUMAN	DDX31	physical	28514442
STAU2_HUMAN	STAU2	physical	28514442
WDR12_HUMAN	WDR12	physical	28514442
ZN770_HUMAN	ZNF770	physical	28514442
BRX1_HUMAN	BRIX1	physical	28514442
RS8_HUMAN	RPS8	physical	28514442
NOC4L_HUMAN	NOC4L	physical	28514442
SRP68_HUMAN	SRP68	physical	28514442
RRP8_HUMAN	RRP8	physical	28514442
RRP12_HUMAN	RRP12	physical	28514442
RL7L_HUMAN	RPL7L1	physical	28514442
DDX24_HUMAN	DDX24	physical	28514442
ZCCHV_HUMAN	ZC3HAV1	physical	28514442
DDX21_HUMAN	DDX21	physical	28514442

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 MK67I_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-223; THR-234 AND THR-238, AND MASSSPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Sequential phosphorylation and multisite interactions characterizespecific target recognition by the FHA domain of Ki67."; Byeon I.-J., Li H., Song H., Gronenborn A.M., Tsai M.-D.; Nat. Struct. Mol. Biol. 12:987-993(2005). Cited for: STRUCTURE BY NMR OF 226-269 IN COMPLEX WITH MKI67, MASS SPECTROMETRY,MUTAGENESIS OF SER-230; THR-234; PRO-235; THR-238 AND PRO-239, ANDPHOSPHORYLATION AT SER-230; THR-234 AND THR-238.	16244663 [Abstract]
"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 THR-234; THR-238; SER-247AND THR-279, AND MASS SPECTROMETRY.	18669648 [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 SER-218; THR-220; THR-223;SER-230; THR-234; SER-247 AND THR-279, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234; THR-240 ANDSER-247, AND MASS SPECTROMETRY.	17287340 [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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-223; THR-234 AND THR-238, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-238, AND MASSSPECTROMETRY.	18220336 [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-234, AND MASSSPECTROMETRY.	16565220 [Abstract]
"Structure of human Ki67 FHA domain and its binding to aphosphoprotein fragment from hNIFK reveal unique recognition sites andnew views to the structural basis of FHA domain functions."; Li H., Byeon I.-J., Ju Y., Tsai M.-D.; J. Mol. Biol. 335:371-381(2004). Cited for: PHOSPHORYLATION AT THR-234, AND INTERACTION WITH MKI67.	14659764 [Abstract]

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