MS18B_HUMAN - dbPTM
MS18B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MS18B_HUMAN
UniProt AC O43482
Protein Name Protein Mis18-beta
Gene Name OIP5 {ECO:0000303|PubMed:9466265}
Organism Homo sapiens (Human).
Sequence Length 229
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 MAAQPLRHRSRCATPPRGDFCGGTERAIDQASFTTSMEWDTQVVKGSSPLGPAGLGAEEPAAGPQLPSWLQPERCAVFQCAQCHAVLADSVHLAWDLSRSLGAVVFSRVTNNVVLEAPFLVGIEGSLKGSTYNLLFCGSCGIPVGFHLYSTHAALAALRGHFCLSSDKMVCYLLKTKAIVNASEMDIQNVPLSEKIAELKEKIVLTHNRLKSLMKILSEVTPDQSKPEN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
7Methylation-MAAQPLRHRSRCAT
-CCCCCCCCCCCCCC		29.83115486003
10PhosphorylationAQPLRHRSRCATPPR
CCCCCCCCCCCCCCC		26.1126074081
14PhosphorylationRHRSRCATPPRGDFC
CCCCCCCCCCCCCCC		37.1323401153
24PhosphorylationRGDFCGGTERAIDQA
CCCCCCCCHHCCCCC		13.9526552605
47PhosphorylationDTQVVKGSSPLGPAG
EEEEEECCCCCCCCC		24.0623401153
48PhosphorylationTQVVKGSSPLGPAGL
EEEEECCCCCCCCCC		32.5830266825
68PhosphorylationAAGPQLPSWLQPERC
CCCCCCCCCCCHHHC		49.3529978859
175UbiquitinationKMVCYLLKTKAIVNA
HHHHHHHCCCEEECH		45.44-
195UbiquitinationQNVPLSEKIAELKEK
CCCCHHHHHHHHHHH		43.79-
202UbiquitinationKIAELKEKIVLTHNR
HHHHHHHHHHHCHHH		36.21-
212PhosphorylationLTHNRLKSLMKILSE
HCHHHHHHHHHHHHH		37.9824719451
215UbiquitinationNRLKSLMKILSEVTP
HHHHHHHHHHHHCCC		45.87-
215MethylationNRLKSLMKILSEVTP
HHHHHHHHHHHHCCC		45.87-
215"N6,N6-dimethyllysine"NRLKSLMKILSEVTP
HHHHHHHHHHHHCCC		45.87-
218PhosphorylationKSLMKILSEVTPDQS
HHHHHHHHHCCCCCC		33.2329255136
221PhosphorylationMKILSEVTPDQSKPE
HHHHHHCCCCCCCCC		19.6629255136
225PhosphorylationSEVTPDQSKPEN---
HHCCCCCCCCCC---		58.5223401153
226MethylationEVTPDQSKPEN----
HCCCCCCCCCC----		51.20-
226UbiquitinationEVTPDQSKPEN----
HCCCCCCCCCC----		51.2021906983
226"N6,N6-dimethyllysine"EVTPDQSKPEN----
HCCCCCCCCCC----		51.20-
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 MS18B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MS18B_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 MS18B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PEX19_HUMANPEX19physical
21988832
RARG_HUMANRARGphysical
21988832
TSSK3_HUMANTSSK3physical
21988832
KDM1A_HUMANKDM1Aphysical
23455924
NUP62_HUMANNUP62physical
25416956
TFP11_HUMANTFIP11physical
25416956
MS18A_HUMANMIS18Aphysical
25416956
4ET_HUMANEIF4ENIF1physical
25416956
GCC1_HUMANGCC1physical
25416956
CA094_HUMANC1orf94physical
25416956
CE170_HUMANCEP170physical
26186194
UBE2T_HUMANUBE2Tphysical
26186194
BRE1B_HUMANRNF40physical
26186194
QKI_HUMANQKIphysical
26186194
TRAF7_HUMANTRAF7physical
26186194
SNP47_HUMANSNAP47physical
26186194
PZRN3_HUMANPDZRN3physical
26186194
MS18A_HUMANMIS18Aphysical
26186194
CYH3_HUMANCYTH3physical
26186194
MED29_HUMANMED29physical
26186194
STX1A_HUMANSTX1Aphysical
26186194
M18BP_HUMANMIS18BP1physical
26186194
CUED1_HUMANCUEDC1physical
26186194
CI016_HUMANC9orf16physical
26186194
MS18A_HUMANMIS18Aphysical
21516116
MS18A_HUMANMIS18Aphysical
28514442
CE170_HUMANCEP170physical
28514442
STX1A_HUMANSTX1Aphysical
28514442
TRAF7_HUMANTRAF7physical
28514442
M18BP_HUMANMIS18BP1physical
28514442
MED29_HUMANMED29physical
28514442
PZRN3_HUMANPDZRN3physical
28514442
TACC3_HUMANTACC3physical
28514442
UBE2T_HUMANUBE2Tphysical
28514442
CI016_HUMANC9orf16physical
28514442
BRE1B_HUMANRNF40physical
28514442
CUED1_HUMANCUEDC1physical
28514442
CAPON_HUMANNOS1APphysical
28514442
CYH3_HUMANCYTH3physical
28514442
PKN3_HUMANPKN3physical
27173435
NCK5L_HUMANNCKAP5Lphysical
27173435
TFPT_HUMANTFPTphysical
27173435
CCHCR_HUMANCCHCR1physical
27173435
YETS4_HUMANYEATS4physical
27173435
TUFT1_HUMANTUFT1physical
27173435
GOGA5_HUMANGOLGA5physical
27173435
CLOCK_HUMANCLOCKphysical
27173435
PSMD9_HUMANPSMD9physical
27173435
VPS53_HUMANVPS53physical
27173435
DZIP3_HUMANDZIP3physical
27173435
GRAP1_HUMANGRIPAP1physical
27173435
RCOR1_HUMANRCOR1physical
27173435
VPS50_HUMANCCDC132physical
27173435
CCD93_HUMANCCDC93physical
27173435
PF21A_HUMANPHF21Aphysical
27173435
CAVN1_HUMANPTRFphysical
27173435
HAUS6_HUMANHAUS6physical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
BMAL1_HUMANARNTLphysical
27173435
RABX5_HUMANRABGEF1physical
27173435
NUF2_HUMANNUF2physical
27173435
THA11_HUMANTHAP11physical
27173435
KDM1A_HUMANKDM1Aphysical
27173435
VPS51_HUMANVPS51physical
27173435
EIPR1_HUMANTSSC1physical
27173435
JUN_HUMANJUNphysical
27173435
MS18B_HUMANOIP5physical
26942680
HJURP_HUMANHJURPphysical
26942680
CENPA_HUMANCENPAphysical
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 MS18B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-48; THR-221 AND SER-225,AND MASS SPECTROMETRY.

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