MEP50_HUMAN - dbPTM
MEP50_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MEP50_HUMAN
UniProt AC Q9BQA1
Protein Name Methylosome protein 50
Gene Name WDR77
Organism Homo sapiens (Human).
Sequence Length 342
Subcellular Localization Nucleus . Cytoplasm . Nuclear in Leydig cells and cytoplasmic in germ cells during fetal testicular development. In adult testis, predominantly nuclear. Subcellular location varies from nuclear to cytoplasmic in various tumors (PubMed:17437848).
Protein Description Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones. [PubMed: 11756452 This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage]
Protein Sequence MRKETPPPLVPPAAREWNLPPNAPACMERQLEAARYRSDGALLLGASSLSGRCWAGSLWLFKDPCAAPNEGFCSAGVQTEAGVADLTWVGERGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQVVLSSYRAHAAQVTCVAASPHKDSVFLSCSEDNRILLWDTRCPKPASQIGCSAPGYLPTSLAWHPQQSEVFVFGDENGTVSLVDTKSTSCVLSSAVHSQCVTGLVFSPHSVPFLASLSEDCSLAVLDSSLSELFRSQAHRDFVRDATWSPLNHSLLTTVGWDHQVVHHVVPTEPLPAPGPASVTE
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
3Ubiquitination-----MRKETPPPLV
-----CCCCCCCCCC		65.72-
3Ubiquitination-----MRKETPPPLV
-----CCCCCCCCCC		65.72-
5Phosphorylation---MRKETPPPLVPP
---CCCCCCCCCCCC		44.1029255136
38PhosphorylationLEAARYRSDGALLLG
HHHHHHHCCCCEEEC		31.3121712546
47PhosphorylationGALLLGASSLSGRCW
CCEEECCCCCCCCCC		29.9825850435
48PhosphorylationALLLGASSLSGRCWA
CEEECCCCCCCCCCC		26.4825850435
50PhosphorylationLLGASSLSGRCWAGS
EECCCCCCCCCCCCC		26.5825850435
115UbiquitinationLDENETLIVSKFCKY
CCCCCEEEEEECCCC		4.25-
121AcetylationLIVSKFCKYEHDDIV
EEEEECCCCCCCCCE		57.7327452117
121UbiquitinationLIVSKFCKYEHDDIV
EEEEECCCCCCCCCE		57.73-
132PhosphorylationDDIVSTVSVLSSGTQ
CCCEEEEEHHHCCCC		19.8923909892
135PhosphorylationVSTVSVLSSGTQAVS
EEEEEHHHCCCCCCC		25.2723909892
136PhosphorylationSTVSVLSSGTQAVSG
EEEEHHHCCCCCCCC		41.5223909892
137UbiquitinationTVSVLSSGTQAVSGS
EEEHHHCCCCCCCCC		20.62-
138PhosphorylationVSVLSSGTQAVSGSK
EEHHHCCCCCCCCCC		18.4623909892
142PhosphorylationSSGTQAVSGSKDICI
HCCCCCCCCCCEEEE		40.1223909892
144PhosphorylationGTQAVSGSKDICIKV
CCCCCCCCCEEEEEH		21.4623909892
145UbiquitinationTQAVSGSKDICIKVW
CCCCCCCCEEEEEHH		55.42-
171PhosphorylationRAHAAQVTCVAASPH
HHHHEEEEEEECCCC		6.81-
176PhosphorylationQVTCVAASPHKDSVF
EEEEEECCCCCCCEE		20.1425159151
179UbiquitinationCVAASPHKDSVFLSC
EEECCCCCCCEEEEE		55.90-
181PhosphorylationAASPHKDSVFLSCSE
ECCCCCCCEEEEECC		21.41-
197PhosphorylationNRILLWDTRCPKPAS
CCEEEEECCCCCCHH		23.6925690035
246O-linked_GlycosylationLVDTKSTSCVLSSAV
EEECCCCCEEECHHH		14.87OGP
264PhosphorylationCVTGLVFSPHSVPFL
CEEEECCCCCCHHHH		17.7720951943
306PhosphorylationFVRDATWSPLNHSLL
HHHHCCCCCCCCHHH		18.3620951943
339PhosphorylationLPAPGPASVTE----
CCCCCCCCCCC----		32.4826074081
341PhosphorylationAPGPASVTE------
CCCCCCCCC------		33.2226074081
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
5TPhosphorylationKinaseCDK4P11802
PSP
264SPhosphorylationKinaseCDK4P11802
PSP
306SPhosphorylationKinaseCDK4P11802
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MEP50_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 MEP50_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANM5_HUMANPRMT5physical
11756452
SMD1_HUMANSNRPD1physical
11756452
SMD2_HUMANSNRPD2physical
11756452
SMD3_HUMANSNRPD3physical
11756452
RUXE_HUMANSNRPEphysical
11756452
RSMB_HUMANSNRPBphysical
11756452
SUZ12_HUMANSUZ12physical
16712789
H2A2B_HUMANHIST2H2ABphysical
16712789
ANM5_HUMANPRMT5physical
21316606
ANM5_HUMANPRMT5physical
20951943
CCND1_HUMANCCND1physical
20951943
CDK4_HUMANCDK4physical
20951943
SMCA4_HUMANSMARCA4physical
20951943
ANM5_HUMANPRMT5physical
22169276
NKX31_HUMANNKX3-1physical
12972618
ANDR_HUMANARphysical
12972618
MEP50_HUMANWDR77physical
12972618
ANM5_HUMANPRMT5physical
12972618
RU1C_HUMANSNRPCphysical
22365833
SF3A1_HUMANSF3A1physical
22365833
SF3B4_HUMANSF3B4physical
22365833
SF01_HUMANSF1physical
22365833
RBM5_HUMANRBM5physical
22365833
LSM3_HUMANLSM3physical
22365833
PQBP1_HUMANPQBP1physical
22365833
PPIL1_HUMANPPIL1physical
22365833
AQR_HUMANAQRphysical
22365833
THOC1_HUMANTHOC1physical
22365833
ZN207_HUMANZNF207physical
22365833
PP1R8_HUMANPPP1R8physical
22365833
S30BP_HUMANSAP30BPphysical
22365833
ANM5_HUMANPRMT5physical
22365833
HNRPM_HUMANHNRNPMphysical
22365833
PCBP2_HUMANPCBP2physical
22365833
BAG2_HUMANBAG2physical
22365833
TOE1_HUMANTOE1physical
22365833
GPKOW_HUMANGPKOWphysical
22365833
QKI_HUMANQKIphysical
22365833
SMYD1_HUMANSMYD1physical
23455924
CSN4_HUMANCOPS4physical
22863883
ANM5_HUMANPRMT5physical
22863883
SMAD1_HUMANSMAD1physical
23734213
ANDR_HUMANARphysical
23734213
KGP2_HUMANPRKG2physical
23755100
KGP1_HUMANPRKG1physical
23755100
CDK8_HUMANCDK8physical
23749998
CDK19_HUMANCDK19physical
23749998
T22D2_HUMANTSC22D2physical
27337956
ANM5_HUMANPRMT5physical
26763441
TCPW_HUMANCCT6Bphysical
28514442
TCPB_HUMANCCT2physical
28514442
TCPA_HUMANTCP1physical
28514442
TCPD_HUMANCCT4physical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
TCPE_HUMANCCT5physical
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 MEP50_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND MASSSPECTROMETRY.
"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-5, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND MASSSPECTROMETRY.
"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 THR-5, AND MASSSPECTROMETRY.

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