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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