dbPTM

MS18A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MS18A_HUMAN
UniProt AC	Q9NYP9
Protein Name	Protein Mis18-alpha
Gene Name	MIS18A
Organism	Homo sapiens (Human).
Sequence Length	233
Subcellular Localization	Nucleus . Chromosome . Chromosome, centromere . Associated with centromeres in interphase cells, from late anaphase to the G1 phase. Not detected on centromeres during earlier phases of mitosis. Associated with chromatin.
Protein Description	Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis..
Protein Sequence	MAGVRSLRCSRGCAGGCECGDKGKCSDSSLLGKRLSEDSSRHQLLQKWASMWSSMSEDASVADMERAQLEEEAAAAEERPLVFLCSGCRRPLGDSLSWVASQEDTNCILLRCVSCNVSVDKEQKLSKREKENGCVLETLCCAGCSLNLGYVYRCTPKNLDYKRDLFCLSVEAIESYVLGSSEKQIVSEDKELFNLESRVEIEKSLTQMEDVLKALQMKLWEAESKLSFATCKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MAGVRSLRCSRGC --CCCCCCCCCCCCC	20.12	24719451
10	Phosphorylation	GVRSLRCSRGCAGGC CCCCCCCCCCCCCCC	25.85	28985074
24	Ubiquitination	CECGDKGKCSDSSLL CCCCCCCCCCCHHHH	35.98	32015554
26	Phosphorylation	CGDKGKCSDSSLLGK CCCCCCCCCHHHHCC	43.97	28450419
28	Phosphorylation	DKGKCSDSSLLGKRL CCCCCCCHHHHCCCC	13.44	25159151
29	Phosphorylation	KGKCSDSSLLGKRLS CCCCCCHHHHCCCCC	32.38	25159151
33	Acetylation	SDSSLLGKRLSEDSS CCHHHHCCCCCCCHH	50.57	25953088
33	Ubiquitination	SDSSLLGKRLSEDSS CCHHHHCCCCCCCHH	50.57	22505724
34	Methylation	DSSLLGKRLSEDSSR CHHHHCCCCCCCHHH	41.47	24384671
36	Phosphorylation	SLLGKRLSEDSSRHQ HHHCCCCCCCHHHHH	43.31	22617229
39	Phosphorylation	GKRLSEDSSRHQLLQ CCCCCCCHHHHHHHH	25.81	22617229
40	Phosphorylation	KRLSEDSSRHQLLQK CCCCCCHHHHHHHHH	46.21	22617229
50	Phosphorylation	QLLQKWASMWSSMSE HHHHHHHHHHHHHCC	21.48	23186163
53	Phosphorylation	QKWASMWSSMSEDAS HHHHHHHHHHCCCCC	13.92	24719451
54	Phosphorylation	KWASMWSSMSEDASV HHHHHHHHHCCCCCH	15.71	23186163
56	Phosphorylation	ASMWSSMSEDASVAD HHHHHHHCCCCCHHH	33.98	23186163
114	O-linked_Glycosylation	CILLRCVSCNVSVDK EEEEEEHHCCCCCCH	12.00	23301498
118	O-linked_Glycosylation	RCVSCNVSVDKEQKL EEHHCCCCCCHHHHH	15.59	23301498
121	Ubiquitination	SCNVSVDKEQKLSKR HCCCCCCHHHHHCHH	60.95	-
124	Ubiquitination	VSVDKEQKLSKREKE CCCCHHHHHCHHHHH	56.68	-
130	Ubiquitination	QKLSKREKENGCVLE HHHCHHHHHCCCCHH	61.59	-
157	Ubiquitination	YVYRCTPKNLDYKRD EEEECCCCCCCCCCC	52.57	-
162	Sumoylation	TPKNLDYKRDLFCLS CCCCCCCCCCEEEEE	38.82	-
162	Sumoylation	TPKNLDYKRDLFCLS CCCCCCCCCCEEEEE	38.82	28112733
190	Ubiquitination	KQIVSEDKELFNLES CEECCCCHHHHCHHH	52.87	23000965
203	Ubiquitination	ESRVEIEKSLTQMED HHHHHHHHHHHHHHH	57.32	32015554
213	Ubiquitination	TQMEDVLKALQMKLW HHHHHHHHHHHHHHH	47.07	23000965
218	Ubiquitination	VLKALQMKLWEAESK HHHHHHHHHHHHHHH	37.17	23000965
225	Ubiquitination	KLWEAESKLSFATCK HHHHHHHHHCCHHCC	39.39	29967540
227	Phosphorylation	WEAESKLSFATCKS- HHHHHHHCCHHCCC-	19.30	30266825
230	Phosphorylation	ESKLSFATCKS---- HHHHCCHHCCC----	20.61	30266825
232	Ubiquitination	KLSFATCKS------ HHCCHHCCC------	55.64	33845483
233	Phosphorylation	LSFATCKS------- HCCHHCCC-------	47.83	25159151

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
36	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24658274

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MS18A_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 MS18A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZN471_HUMAN	ZNF471	physical	25416956
CCD96_HUMAN	CCDC96	physical	28514442
M18BP_HUMAN	MIS18BP1	physical	28514442
CP135_HUMAN	CEP135	physical	28514442
HOME1_HUMAN	HOMER1	physical	28514442
BICD2_HUMAN	BICD2	physical	28514442
PCM1_HUMAN	PCM1	physical	28514442
PCNT_HUMAN	PCNT	physical	28514442
SYBU_HUMAN	SYBU	physical	28514442
TXLNG_HUMAN	TXLNG	physical	28514442
OFD1_HUMAN	OFD1	physical	28514442
BFSP1_HUMAN	BFSP1	physical	28514442
DCTN5_HUMAN	DCTN5	physical	28514442
CC170_HUMAN	CCDC170	physical	28514442
TXLNA_HUMAN	TXLNA	physical	28514442
UACA_HUMAN	UACA	physical	28514442
SENP5_HUMAN	SENP5	physical	28514442
DCTN3_HUMAN	DCTN3	physical	28514442
ARP10_HUMAN	ACTR10	physical	28514442
OSBL6_HUMAN	OSBPL6	physical	28514442
DCTN6_HUMAN	DCTN6	physical	28514442
DCTN2_HUMAN	DCTN2	physical	28514442
DCTN4_HUMAN	DCTN4	physical	28514442
ACTY_HUMAN	ACTR1B	physical	28514442
ACTZ_HUMAN	ACTR1A	physical	28514442
MS18B_HUMAN	OIP5	physical	26921242
MS18B_HUMAN	OIP5	physical	26942680
MS18A_HUMAN	MIS18A	physical	26942680
HJURP_HUMAN	HJURP	physical	26942680
CENPA_HUMAN	CENPA	physical	26942680

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 MS18A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-233, AND MASSSPECTROMETRY.	18669648 [Abstract]