dbPTM

MAK16_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MAK16_HUMAN
UniProt AC	Q9BXY0
Protein Name	Protein MAK16 homolog
Gene Name	MAK16
Organism	Homo sapiens (Human).
Sequence Length	300
Subcellular Localization	Nucleus, nucleolus .
Protein Description
Protein Sequence	MQSDDVIWDTLGNKQFCSFKIRTKTQSFCRNEYSLTGLCNRSSCPLANSQYATIKEEKGQCYLYMKVIERAAFPRRLWERVRLSKNYEKALEQIDENLIYWPRFIRHKCKQRFTKITQYLIRIRKLTLKRQRKLVPLSKKVERREKRREEKALIAAQLDNAIEKELLERLKQDTYGDIYNFPIHAFDKALEQQEAESDSSDTEEKDDDDDDEEDVGKREFVEDGEVDESDISDFEDMDKLDASSDEDQDGKSSSEEEEEKALSAKHKGKMPLRGPLQRKRAYVEIEYEQETEPVAKAKTT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MQSDDVIW -------CCCCCCEE	8.53	22223895
3	Phosphorylation	-----MQSDDVIWDT -----CCCCCCEEEC	34.18	21406692
10	Phosphorylation	SDDVIWDTLGNKQFC CCCCEEECCCCCEEE	22.90	21406692
20	Acetylation	NKQFCSFKIRTKTQS CCEEEEEEEEECCCC	18.25	26051181
25	Phosphorylation	SFKIRTKTQSFCRNE EEEEEECCCCHHCCC	28.91	28450419
27	Phosphorylation	KIRTKTQSFCRNEYS EEEECCCCHHCCCCC	31.39	30576142
33	Phosphorylation	QSFCRNEYSLTGLCN CCHHCCCCCCHHCCC	16.72	25884760
34	Phosphorylation	SFCRNEYSLTGLCNR CHHCCCCCCHHCCCC	17.18	28152594
43	Phosphorylation	TGLCNRSSCPLANSQ HHCCCCCCCCCCCCC	19.27	28555341
53	Phosphorylation	LANSQYATIKEEKGQ CCCCCCEEEEECCCC	27.87	22210691
55	Sumoylation	NSQYATIKEEKGQCY CCCCEEEEECCCCEE	56.30	28112733
55	Ubiquitination	NSQYATIKEEKGQCY CCCCEEEEECCCCEE	56.30	33845483
55	Acetylation	NSQYATIKEEKGQCY CCCCEEEEECCCCEE	56.30	26051181
62	Phosphorylation	KEEKGQCYLYMKVIE EECCCCEEEEEEHHH	7.93	22817900
66	Acetylation	GQCYLYMKVIERAAF CCEEEEEEHHHHHCC	26.89	26051181
100	Phosphorylation	QIDENLIYWPRFIRH HHHHHHCHHHHHHHH	16.72	-
110	Ubiquitination	RFIRHKCKQRFTKIT HHHHHHHHHHHHHHH	49.68	22817900
115	Ubiquitination	KCKQRFTKITQYLIR HHHHHHHHHHHHHHH	40.83	21890473
115	Ubiquitination	KCKQRFTKITQYLIR HHHHHHHHHHHHHHH	40.83	22817900
115	Acetylation	KCKQRFTKITQYLIR HHHHHHHHHHHHHHH	40.83	25953088
117	Phosphorylation	KQRFTKITQYLIRIR HHHHHHHHHHHHHHH	16.84	21406692
119	Phosphorylation	RFTKITQYLIRIRKL HHHHHHHHHHHHHHH	8.75	28152594
127	Phosphorylation	LIRIRKLTLKRQRKL HHHHHHHHHHCHHHH	33.01	24719451
138	Phosphorylation	QRKLVPLSKKVERRE HHHHHCCHHHHHHHH	25.10	24114839
140	Ubiquitination	KLVPLSKKVERREKR HHHCCHHHHHHHHHH	46.05	24816145
151	2-Hydroxyisobutyrylation	REKRREEKALIAAQL HHHHHHHHHHHHHHH	43.68	-
151	Sumoylation	REKRREEKALIAAQL HHHHHHHHHHHHHHH	43.68	-
151	Sumoylation	REKRREEKALIAAQL HHHHHHHHHHHHHHH	43.68	28112733
164	Acetylation	QLDNAIEKELLERLK HHHHHHHHHHHHHHH	47.77	26051181
164	Ubiquitination	QLDNAIEKELLERLK HHHHHHHHHHHHHHH	47.77	29967540
171	Acetylation	KELLERLKQDTYGDI HHHHHHHHCCCCCHH	52.96	26051181
171	Sumoylation	KELLERLKQDTYGDI HHHHHHHHCCCCCHH	52.96	-
171	Ubiquitination	KELLERLKQDTYGDI HHHHHHHHCCCCCHH	52.96	29967540
171	Sumoylation	KELLERLKQDTYGDI HHHHHHHHCCCCCHH	52.96	-
174	Phosphorylation	LERLKQDTYGDIYNF HHHHHCCCCCHHHHC	27.23	28152594
175	Phosphorylation	ERLKQDTYGDIYNFP HHHHCCCCCHHHHCH	22.53	28152594
179	Phosphorylation	QDTYGDIYNFPIHAF CCCCCHHHHCHHHHH	18.58	28152594
197	Phosphorylation	LEQQEAESDSSDTEE HHHHHHHCCCCCCCC	50.25	23927012
199	Phosphorylation	QQEAESDSSDTEEKD HHHHHCCCCCCCCCC	39.12	25159151
200	Phosphorylation	QEAESDSSDTEEKDD HHHHCCCCCCCCCCC	54.25	23927012
202	Phosphorylation	AESDSSDTEEKDDDD HHCCCCCCCCCCCCC	48.25	30278072
229	Phosphorylation	EDGEVDESDISDFED HCCCCCHHHCCCCCC	35.46	26503892
232	Phosphorylation	EVDESDISDFEDMDK CCCHHHCCCCCCHHH	41.03	26503892
243	Phosphorylation	DMDKLDASSDEDQDG CHHHCCCCCCCCCCC	37.68	20363803
244	Phosphorylation	MDKLDASSDEDQDGK HHHCCCCCCCCCCCC	46.90	20363803
252	Phosphorylation	DEDQDGKSSSEEEEE CCCCCCCCCCHHHHH	44.63	20363803
253	Phosphorylation	EDQDGKSSSEEEEEK CCCCCCCCCHHHHHH	45.30	20363803
254	Phosphorylation	DQDGKSSSEEEEEKA CCCCCCCCHHHHHHH	57.00	20363803
282	Phosphorylation	PLQRKRAYVEIEYEQ CCCCCCEEEEEEEEE	11.58	27642862
287	Phosphorylation	RAYVEIEYEQETEPV CEEEEEEEEECCCCC	28.68	28796482
291	Phosphorylation	EIEYEQETEPVAKAK EEEEEECCCCCCCCC	45.33	-

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
Oops, there are no upstream regulatory protein records of MAK16_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MAK16_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 MAK16_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BRX1_HUMAN	BRIX1	physical	26344197
FRMD6_HUMAN	FRMD6	physical	28514442
WDR74_HUMAN	WDR74	physical	28514442
RRP1_HUMAN	RRP1	physical	28514442
NOC2L_HUMAN	NOC2L	physical	28514442
NOC3L_HUMAN	NOC3L	physical	28514442
RS27A_HUMAN	RPS27A	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
CEBPZ_HUMAN	CEBPZ	physical	28514442
RL32_HUMAN	RPL32	physical	28514442
NVL_HUMAN	NVL	physical	28514442
PUM3_HUMAN	KIAA0020	physical	28514442
DDX27_HUMAN	DDX27	physical	28514442
RBM34_HUMAN	RBM34	physical	28514442
KNOP1_HUMAN	KNOP1	physical	28514442
RRP8_HUMAN	RRP8	physical	28514442
SPB1_HUMAN	FTSJ3	physical	28514442
RL4_HUMAN	RPL4	physical	28514442
ZCHC9_HUMAN	ZCCHC9	physical	28514442
RBM28_HUMAN	RBM28	physical	28514442
NOP2_HUMAN	NOP2	physical	28514442
RL30_HUMAN	RPL30	physical	28514442
RL3_HUMAN	RPL3	physical	28514442
RPF2_HUMAN	RPF2	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
GAR1_HUMAN	GAR1	physical	28514442
RL5_HUMAN	RPL5	physical	28514442
RS15_HUMAN	RPS15	physical	28514442
DKC1_HUMAN	DKC1	physical	28514442
NSA2_HUMAN	NSA2	physical	28514442
RLP24_HUMAN	RSL24D1	physical	28514442
BRX1_HUMAN	BRIX1	physical	28514442
DDX24_HUMAN	DDX24	physical	28514442
KRR1_HUMAN	KRR1	physical	28514442
EBP2_HUMAN	EBNA1BP2	physical	28514442
RL7A_HUMAN	RPL7A	physical	28514442
MDM2_HUMAN	MDM2	physical	28514442
NOL12_HUMAN	NOL12	physical	28514442
ZCCHV_HUMAN	ZC3HAV1	physical	28514442
NOG1_HUMAN	GTPBP4	physical	28514442
SURF6_HUMAN	SURF6	physical	28514442
ZCRB1_HUMAN	ZCRB1	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 MAK16_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-197 AND SER-200, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-197 AND SER-200, AND MASS SPECTROMETRY.	19413330 [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 SER-197; SER-199; SER-200AND THR-202, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-200; SER-229AND SER-232, AND MASS SPECTROMETRY.	17081983 [Abstract]