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O00566 (MPP10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
U3 small nucleolar ribonucleoprotein protein MPP10
Alternative name(s):
M phase phosphoprotein 10
Gene names
Name:MPHOSPH10
Synonyms:MPP10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length681 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing.

Subunit structure

Component of a heterotrimeric complex containing IMP3, IMP4 and MPHOSPH10. Interacts with IMP3 and IMP4. Ref.5

Subcellular location

Nucleusnucleolus. Chromosome. Note: Fibrillar region of the nucleolus. After dissolution of the nucleolus in early M phase becomes associated with chromosomes through metaphase and anaphase. In telophase localized to small cellular prenucleolar bodies that not always contain fibrillarin. The reassociation with nucleolus is preceeded by the arrival of fibrillarin. Ref.4 Ref.5

Post-translational modification

Phosphorylated in M (mitotic) phase.

Sequence similarities

Belongs to the MPP10 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PPP1CAP621362EBI-5235884,EBI-357253

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 681681U3 small nucleolar ribonucleoprotein protein MPP10
PRO_0000121535

Regions

Coiled coil109 – 13830 Potential
Coiled coil205 – 23935 Potential
Coiled coil284 – 32441 Potential
Coiled coil348 – 38235 Potential
Coiled coil469 – 49022 Potential
Coiled coil574 – 60431 Potential
Coiled coil648 – 67023 Potential
Compositional bias134 – 1374Poly-Glu
Compositional bias229 – 2324Poly-Glu
Compositional bias666 – 6705Poly-Lys

Amino acid modifications

Modified residue611Phosphoserine Potential
Modified residue1201Phosphoserine Ref.10 Ref.11
Modified residue1391Phosphoserine Ref.10 Ref.11
Modified residue1631Phosphoserine Ref.6 Ref.7 Ref.10 Ref.11
Modified residue1671Phosphoserine Ref.6 Ref.7 Ref.8 Ref.10 Ref.11
Modified residue1711Phosphoserine Ref.6 Ref.7 Ref.8 Ref.10 Ref.11
Modified residue2421Phosphoserine Ref.6 Ref.7 Ref.8 Ref.10 Ref.11
Modified residue2751Phosphoserine Ref.6 Ref.11
Modified residue2891Phosphoserine Ref.6 Ref.11
Modified residue6091N6-acetyllysine Ref.9

Natural variations

Natural variant691E → A.
Corresponds to variant rs10199088 [ dbSNP | Ensembl ].
VAR_053511
Natural variant1151R → H.
Corresponds to variant rs13010513 [ dbSNP | Ensembl ].
VAR_053512
Natural variant1401D → N.
Corresponds to variant rs10175940 [ dbSNP | Ensembl ].
VAR_053513
Natural variant2291E → D.
Corresponds to variant rs1813160 [ dbSNP | Ensembl ].
VAR_024539
Natural variant4251L → M.
Corresponds to variant rs3732240 [ dbSNP | Ensembl ].
VAR_022000
Natural variant6341E → K.
Corresponds to variant rs6574 [ dbSNP | Ensembl ].
VAR_014470
Natural variant6391A → T.
Corresponds to variant rs4852764 [ dbSNP | Ensembl ].
VAR_053514

Sequences

Sequence LengthMass (Da)Tools
O00566 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: EDF27859D735D4E2

FASTA68178,864
        10         20         30         40         50         60 
MAPQVWRRRT LERCLTEVGK ATGRPECFLT IQEGLASKFT SLTKVLYDFN KILENGRIHG 

        70         80         90        100        110        120 
SPLQKLVIEN FDDEQIWQQL ELQNEPILQY FQNAVSETIN DEDISLLPES EEQEREEDGS 

       130        140        150        160        170        180 
EIEADDKEDL EDLEEEEVSD MGNDDPEMGE RAENSSKSDL RKSPVFSDED SDLDFDISKL 

       190        200        210        220        230        240 
EQQSKVQNKG QGKPREKSIV DDKFFKLSEM EAYLENIEKE EERKDDNDEE EEDIDFFEDI 

       250        260        270        280        290        300 
DSDEDEGGLF GSKKLKSGKS SRNLKYKDFF DPVESDEDIT NVHDDELDSN KEDDEIAEEE 

       310        320        330        340        350        360 
AEELSISETD EDDDLQENED NKQHKESLKR VTFALPDDAE TEDTGVLNVK KNSDEVKSSF 

       370        380        390        400        410        420 
EKRQEKMNEK IASLEKELLE KKPWQLQGEV TAQKRPENSL LEETLHFDHA VRMAPVITEE 

       430        440        450        460        470        480 
TTLQLEDIIK QRIRDQAWDD VVRKEKPKED AYEYKKRLTL DHEKSKLSLA EIYEQEYIKL 

       490        500        510        520        530        540 
NQQKTAEEEN PEHVEIQKMM DSLFLKLDAL SNFHFIPKPP VPEIKVVSNL PAITMEEVAP 

       550        560        570        580        590        600 
VSVSDAALLA PEEIKEKNKA GDIKTAAEKT ATDKKRERRK KKYQKRMKIK EKEKRRKLLE 

       610        620        630        640        650        660 
KSSVDQAGKY SKTVASEKLK QLTKTGKASF IKDEGKDKAL KSSQAFFSKL QDQVKMQIND 

       670        680 
AKKTEKKKKK RQDISVHKLK L 

« Hide

References

« Hide 'large scale' references
[1]"Identification of novel M phase phosphoproteins by expression cloning."
Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.
Mol. Biol. Cell 7:1455-1469(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-681.
Tissue: Blood.
[2]"M phase phosphoprotein 10 is a human U3 small nucleolar ribonucleoprotein component."
Westendorf J.M., Konstantinov K.N., Wormsley S., Shu M.-D., Matsumoto-Taniura N., Pirollet F., Klier F.G., Gerace L., Baserga S.J.
Mol. Biol. Cell 9:437-449(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary cancer and Placenta.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"The human Imp3 and Imp4 proteins form a ternary complex with hMpp10, which only interacts with the U3 snoRNA in 60-80S ribonucleoprotein complexes."
Granneman S., Gallagher J.E.G., Vogelzangs J., Horstman W., van Venrooij W.J., Baserga S.J., Pruijn G.J.M.
Nucleic Acids Res. 31:1877-1887(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH IMP3 AND IMP4.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-167; SER-171; SER-242; SER-275 AND SER-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-167; SER-171 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-171 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-609, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-139; SER-163; SER-167; SER-171 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-139; SER-163; SER-167; SER-171; SER-242; SER-275 AND SER-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98494 mRNA. Translation: CAA67120.1.
BC126389 mRNA. Translation: AAI26390.1.
CCDSCCDS1916.1.
RefSeqNP_005782.1. NM_005791.2.
UniGeneHs.656208.

3D structure databases

ProteinModelPortalO00566.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115494. 10 interactions.
IntActO00566. 2 interactions.
MINTMINT-1192399.
STRING9606.ENSP00000244230.

PTM databases

PhosphoSiteO00566.

2D gel databases

SWISS-2DPAGEO00566.

Proteomic databases

MaxQBO00566.
PaxDbO00566.
PeptideAtlasO00566.
PRIDEO00566.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244230; ENSP00000244230; ENSG00000124383.
GeneID10199.
KEGGhsa:10199.
UCSCuc002sht.2. human.

Organism-specific databases

CTD10199.
GeneCardsGC02P071358.
HGNCHGNC:7213. MPHOSPH10.
HPAHPA035059.
HPA035060.
HPA049907.
MIM605503. gene.
neXtProtNX_O00566.
PharmGKBPA30919.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5384.
HOGENOMHOG000046317.
HOVERGENHBG052502.
InParanoidO00566.
KOK14559.
OMARSRPQNS.
OrthoDBEOG7VDXPQ.
PhylomeDBO00566.
TreeFamTF105794.

Gene expression databases

ArrayExpressO00566.
BgeeO00566.
CleanExHS_MPHOSPH10.
GenevestigatorO00566.

Family and domain databases

InterProIPR007151. Mpp10.
IPR012173. snoRNP_Mpp10.
[Graphical view]
PANTHERPTHR17039. PTHR17039. 1 hit.
PfamPF04006. Mpp10. 1 hit.
[Graphical view]
PIRSFPIRSF017300. snoRNP_Mpp10. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMPHOSPH10. human.
GeneWikiMPHOSPH10.
GenomeRNAi10199.
NextBio38602.
PMAP-CutDBO00566.
PROO00566.
SOURCESearch...

Entry information

Entry nameMPP10_HUMAN
AccessionPrimary (citable) accession number: O00566
Secondary accession number(s): A0AVJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM