MPP10_HUMAN - dbPTM
MPP10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPP10_HUMAN
UniProt AC O00566
Protein Name U3 small nucleolar ribonucleoprotein protein MPP10
Gene Name MPHOSPH10
Organism Homo sapiens (Human).
Sequence Length 681
Subcellular Localization Nucleus, nucleolus . Chromosome . Fibrillar region of the nucleolus (PubMed:9450966). After dissolution of the nucleolus in early M phase becomes associated with chromosomes through metaphase and anaphase (PubMed:9450966). In telophase localized to s
Protein Description Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing..
Protein Sequence MAPQVWRRRTLERCLTEVGKATGRPECFLTIQEGLASKFTSLTKVLYDFNKILENGRIHGSPLQKLVIENFDDEQIWQQLELQNEPILQYFQNAVSETINDEDISLLPESEEQEREEDGSEIEADDKEDLEDLEEEEVSDMGNDDPEMGERAENSSKSDLRKSPVFSDEDSDLDFDISKLEQQSKVQNKGQGKPREKSIVDDKFFKLSEMEAYLENIEKEEERKDDNDEEEEDIDFFEDIDSDEDEGGLFGSKKLKSGKSSRNLKYKDFFDPVESDEDITNVHDDELDSNKEDDEIAEEEAEELSISETDEDDDLQENEDNKQHKESLKRVTFALPDDAETEDTGVLNVKKNSDEVKSSFEKRQEKMNEKIASLEKELLEKKPWQLQGEVTAQKRPENSLLEETLHFDHAVRMAPVITEETTLQLEDIIKQRIRDQAWDDVVRKEKPKEDAYEYKKRLTLDHEKSKLSLAEIYEQEYIKLNQQKTAEEENPEHVEIQKMMDSLFLKLDALSNFHFIPKPPVPEIKVVSNLPAITMEEVAPVSVSDAALLAPEEIKEKNKAGDIKTAAEKTATDKKRERRKKKYQKRMKIKEKEKRRKLLEKSSVDQAGKYSKTVASEKLKQLTKTGKASFIKDEGKDKALKSSQAFFSKLQDQVKMQINDAKKTEKKKKKRQDISVHKLKL
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
10PhosphorylationPQVWRRRTLERCLTE
CHHHHHHHHHHHHHH		31.0323882029
16PhosphorylationRTLERCLTEVGKATG
HHHHHHHHHHHHHCC		32.0523882029
22PhosphorylationLTEVGKATGRPECFL
HHHHHHHCCCCHHEE		36.8920068231
27GlutathionylationKATGRPECFLTIQEG
HHCCCCHHEEEECHH		3.6222555962
30PhosphorylationGRPECFLTIQEGLAS
CCCHHEEEECHHHHH		10.6020068231
37PhosphorylationTIQEGLASKFTSLTK
EECHHHHHHHHHHHH		33.0920068231
38UbiquitinationIQEGLASKFTSLTKV
ECHHHHHHHHHHHHH		47.2429967540
38AcetylationIQEGLASKFTSLTKV
ECHHHHHHHHHHHHH		47.2425953088
41PhosphorylationGLASKFTSLTKVLYD
HHHHHHHHHHHHHHC		36.8520068231
43PhosphorylationASKFTSLTKVLYDFN
HHHHHHHHHHHHCHH		20.9027251275
51UbiquitinationKVLYDFNKILENGRI
HHHHCHHHHHHCCCC		48.97-
61PhosphorylationENGRIHGSPLQKLVI
HCCCCCCCCCCEEEE		14.3125159151
120PhosphorylationQEREEDGSEIEADDK
HHCCCCCCCCCCCCH		47.9628355574
127AcetylationSEIEADDKEDLEDLE
CCCCCCCHHHHHHHH		54.3926051181
139PhosphorylationDLEEEEVSDMGNDDP
HHHHHHHHHCCCCCH		25.7628355574
158PhosphorylationRAENSSKSDLRKSPV
HHHCCCHHHHHCCCC		43.7721955146
163PhosphorylationSKSDLRKSPVFSDED
CHHHHHCCCCCCCCC		21.6229255136
167PhosphorylationLRKSPVFSDEDSDLD
HHCCCCCCCCCCCCC		40.0829255136
171PhosphorylationPVFSDEDSDLDFDIS
CCCCCCCCCCCCCHH		37.7229255136
178PhosphorylationSDLDFDISKLEQQSK
CCCCCCHHHHHHHHH		32.7923927012
184PhosphorylationISKLEQQSKVQNKGQ
HHHHHHHHHHCCCCC		34.1924732914
185SumoylationSKLEQQSKVQNKGQG
HHHHHHHHHCCCCCC		43.43-
185SumoylationSKLEQQSKVQNKGQG
HHHHHHHHHCCCCCC		43.43-
189AcetylationQQSKVQNKGQGKPRE
HHHHHCCCCCCCCCC		35.2021466224
193AcetylationVQNKGQGKPREKSIV
HCCCCCCCCCCCHHC		32.7721466224
197AcetylationGQGKPREKSIVDDKF
CCCCCCCCHHCCHHC		46.9225953088
198PhosphorylationQGKPREKSIVDDKFF
CCCCCCCHHCCHHCH		24.0827251275
203UbiquitinationEKSIVDDKFFKLSEM
CCHHCCHHCHHHHHH		48.5129967540
2032-HydroxyisobutyrylationEKSIVDDKFFKLSEM
CCHHCCHHCHHHHHH		48.51-
208PhosphorylationDDKFFKLSEMEAYLE
CHHCHHHHHHHHHHH		35.1719651622
242PhosphorylationDFFEDIDSDEDEGGL
CHHHCCCCCCCCCCC		43.1430266825
252PhosphorylationDEGGLFGSKKLKSGK
CCCCCCCCCCCCCCC		21.2023663014
257PhosphorylationFGSKKLKSGKSSRNL
CCCCCCCCCCCCCCC		62.9926074081
260PhosphorylationKKLKSGKSSRNLKYK
CCCCCCCCCCCCCCC		37.7526074081
261PhosphorylationKLKSGKSSRNLKYKD
CCCCCCCCCCCCCCH		28.7726074081
266PhosphorylationKSSRNLKYKDFFDPV
CCCCCCCCCHHCCCC		20.9626074081
275PhosphorylationDFFDPVESDEDITNV
HHCCCCCCCCCCCCC		46.6720164059
280PhosphorylationVESDEDITNVHDDEL
CCCCCCCCCCCHHHC		43.4420873877
289PhosphorylationVHDDELDSNKEDDEI
CCHHHCCCCCCCCHH		63.5320164059
305PhosphorylationEEEAEELSISETDED
HHHHHHCCCCCCCCC		27.6127362937
307PhosphorylationEAEELSISETDEDDD
HHHHCCCCCCCCCCC		30.9427362937
309PhosphorylationEELSISETDEDDDLQ
HHCCCCCCCCCCCCC		37.59-
332PhosphorylationKESLKRVTFALPDDA
HHHHHHHEEECCCCC		13.7628555341
341PhosphorylationALPDDAETEDTGVLN
ECCCCCCCCCCCEEE		40.6623312004
344PhosphorylationDDAETEDTGVLNVKK
CCCCCCCCCEEEECC		23.9823312004
350SumoylationDTGVLNVKKNSDEVK
CCCEEEECCCCHHHH		45.2028112733
373PhosphorylationKMNEKIASLEKELLE
HHHHHHHHHHHHHHH		40.3029214152
376UbiquitinationEKIASLEKELLEKKP
HHHHHHHHHHHHCCC		59.9829967540
382SumoylationEKELLEKKPWQLQGE
HHHHHHCCCCCCCCC		41.9628112733
382SumoylationEKELLEKKPWQLQGE
HHHHHHCCCCCCCCC		41.96-
382AcetylationEKELLEKKPWQLQGE
HHHHHHCCCCCCCCC		41.9626051181
394SumoylationQGEVTAQKRPENSLL
CCCEECCCCCCCCHH		68.4128112733
399PhosphorylationAQKRPENSLLEETLH
CCCCCCCCHHHHHHC		32.4420068231
404PhosphorylationENSLLEETLHFDHAV
CCCHHHHHHCCCHHH		19.0220068231
418PhosphorylationVRMAPVITEETTLQL
HHCCCCCCHHHHCCH		28.1820068231
421PhosphorylationAPVITEETTLQLEDI
CCCCCHHHHCCHHHH		26.9520068231
422PhosphorylationPVITEETTLQLEDII
CCCCHHHHCCHHHHH		18.7820068231
446AcetylationDDVVRKEKPKEDAYE
HHHHHCCCCCHHHHH		65.5125953088
448UbiquitinationVVRKEKPKEDAYEYK
HHHCCCCCHHHHHHH		78.3324816145
452PhosphorylationEKPKEDAYEYKKRLT
CCCCHHHHHHHHHHC		31.9222817900
454PhosphorylationPKEDAYEYKKRLTLD
CCHHHHHHHHHHCCC		14.7722817900
4552-HydroxyisobutyrylationKEDAYEYKKRLTLDH
CHHHHHHHHHHCCCH		21.34-
459PhosphorylationYEYKKRLTLDHEKSK
HHHHHHHCCCHHHHC		33.8920860994
4642-HydroxyisobutyrylationRLTLDHEKSKLSLAE
HHCCCHHHHCCCHHH		49.85-
466UbiquitinationTLDHEKSKLSLAEIY
CCCHHHHCCCHHHHH		53.8429967540
468PhosphorylationDHEKSKLSLAEIYEQ
CHHHHCCCHHHHHHH		29.3028555341
473PhosphorylationKLSLAEIYEQEYIKL
CCCHHHHHHHHHHHH		11.7627642862
477PhosphorylationAEIYEQEYIKLNQQK
HHHHHHHHHHHHHHC		11.75-
479UbiquitinationIYEQEYIKLNQQKTA
HHHHHHHHHHHHCCC		40.2522817900
484UbiquitinationYIKLNQQKTAEEENP
HHHHHHHCCCCHHCH		39.6822817900
498UbiquitinationPEHVEIQKMMDSLFL
HHHHHHHHHHHHHHH		41.6829967540
502PhosphorylationEIQKMMDSLFLKLDA
HHHHHHHHHHHHHHH		11.7920860994
518AcetylationSNFHFIPKPPVPEIK
CCCCCCCCCCCCCEE		58.0826051181
518UbiquitinationSNFHFIPKPPVPEIK
CCCCCCCCCCCCCEE		58.0823000965
555SumoylationLLAPEEIKEKNKAGD
HHCHHHHHHHCCCCC		66.9528112733
559AcetylationEEIKEKNKAGDIKTA
HHHHHHCCCCCHHHH		65.897708155
564AcetylationKNKAGDIKTAAEKTA
HCCCCCHHHHHHHHH		36.537708165
574AcetylationAEKTATDKKRERRKK
HHHHHHHHHHHHHHH		49.757708175
6012-HydroxyisobutyrylationKRRKLLEKSSVDQAG
HHHHHHHHCCHHHHH		48.26-
602PhosphorylationRRKLLEKSSVDQAGK
HHHHHHHCCHHHHHC		26.6420860994
603PhosphorylationRKLLEKSSVDQAGKY
HHHHHHCCHHHHHCH		40.5622210691
609AcetylationSSVDQAGKYSKTVAS
CCHHHHHCHHHHHHH		49.7419608861
6092-HydroxyisobutyrylationSSVDQAGKYSKTVAS
CCHHHHHCHHHHHHH		49.74-
610PhosphorylationSVDQAGKYSKTVASE
CHHHHHCHHHHHHHH		17.9322468782
611PhosphorylationVDQAGKYSKTVASEK
HHHHHCHHHHHHHHH		25.9022468782
613PhosphorylationQAGKYSKTVASEKLK
HHHCHHHHHHHHHHH		18.5022468782
616PhosphorylationKYSKTVASEKLKQLT
CHHHHHHHHHHHHHH		30.8120860994
618AcetylationSKTVASEKLKQLTKT
HHHHHHHHHHHHHHH		59.4925953088
6182-HydroxyisobutyrylationSKTVASEKLKQLTKT
HHHHHHHHHHHHHHH		59.49-
629PhosphorylationLTKTGKASFIKDEGK
HHHHCCCHHCCCCCH		30.8719691289
632SumoylationTGKASFIKDEGKDKA
HCCCHHCCCCCHHHH		47.9528112733
632SumoylationTGKASFIKDEGKDKA
HCCCHHCCCCCHHHH		47.95-
641MethylationEGKDKALKSSQAFFS
CCHHHHHHHHHHHHH		53.58115973209
649SumoylationSSQAFFSKLQDQVKM
HHHHHHHHHHHHHHH		45.0428112733
649AcetylationSSQAFFSKLQDQVKM
HHHHHHHHHHHHHHH		45.0426051181
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
332TPhosphorylationKinaseAURKBQ96GD4
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPP10_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 MPP10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX52_HUMANDDX52physical
26344197
DDX56_HUMANDDX56physical
26344197
DKC1_HUMANDKC1physical
26344197
IMP3_HUMANIMP3physical
26344197
IMP4_HUMANIMP4physical
26344197
NOL10_HUMANNOL10physical
26344197
NOL6_HUMANNOL6physical
26344197
RS7_HUMANRPS7physical
26344197
UT14A_HUMANUTP14Aphysical
26344197
UTP15_HUMANUTP15physical
26344197
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 MPP10_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-609, AND MASS SPECTROMETRY.
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-167; SER-171 ANDSER-242, AND MASS SPECTROMETRY.
"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-163; SER-167; SER-171AND SER-242, AND MASS SPECTROMETRY.
"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-120 AND SER-139, ANDMASS SPECTROMETRY.
"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-163; SER-167; SER-171;SER-242; SER-275 AND SER-289, AND MASS SPECTROMETRY.

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