Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O00566

- MPP10_HUMAN

UniProt

O00566 - MPP10_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

U3 small nucleolar ribonucleoprotein protein MPP10

Gene

MPHOSPH10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of phosphatase activity Source: UniProtKB
  2. RNA processing Source: UniProtKB
  3. RNA splicing Source: UniProtKB
  4. RNA splicing, via transesterification reactions Source: UniProtKB
  5. rRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
U3 small nucleolar ribonucleoprotein protein MPP10
Alternative name(s):
M phase phosphoprotein 10
Gene namesi
Name:MPHOSPH10
Synonyms:MPP10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:7213. MPHOSPH10.

Subcellular locationi

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.

GO - Cellular componenti

  1. chromosome Source: UniProtKB-KW
  2. nucleolus Source: UniProtKB
  3. small nucleolar ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30919.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 681681U3 small nucleolar ribonucleoprotein protein MPP10PRO_0000121535Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611PhosphoserineSequence Analysis
Modified residuei120 – 1201Phosphoserine2 Publications
Modified residuei139 – 1391Phosphoserine2 Publications
Modified residuei163 – 1631Phosphoserine4 Publications
Modified residuei167 – 1671Phosphoserine5 Publications
Modified residuei171 – 1711Phosphoserine5 Publications
Modified residuei242 – 2421Phosphoserine5 Publications
Modified residuei275 – 2751Phosphoserine2 Publications
Modified residuei289 – 2891Phosphoserine2 Publications
Modified residuei609 – 6091N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated in M (mitotic) phase.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO00566.
PaxDbiO00566.
PeptideAtlasiO00566.
PRIDEiO00566.

2D gel databases

SWISS-2DPAGEO00566.

PTM databases

PhosphoSiteiO00566.

Miscellaneous databases

PMAP-CutDBO00566.

Expressioni

Gene expression databases

BgeeiO00566.
CleanExiHS_MPHOSPH10.
ExpressionAtlasiO00566. baseline and differential.
GenevestigatoriO00566.

Organism-specific databases

HPAiHPA035059.
HPA035060.
HPA049907.

Interactioni

Subunit structurei

Component of a heterotrimeric complex containing IMP3, IMP4 and MPHOSPH10. Interacts with IMP3 and IMP4.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP1CAP621362EBI-5235884,EBI-357253

Protein-protein interaction databases

BioGridi115494. 13 interactions.
IntActiO00566. 2 interactions.
MINTiMINT-1192399.
STRINGi9606.ENSP00000244230.

Structurei

3D structure databases

ProteinModelPortaliO00566.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili109 – 13830Sequence AnalysisAdd
BLAST
Coiled coili205 – 23935Sequence AnalysisAdd
BLAST
Coiled coili284 – 32441Sequence AnalysisAdd
BLAST
Coiled coili348 – 38235Sequence AnalysisAdd
BLAST
Coiled coili469 – 49022Sequence AnalysisAdd
BLAST
Coiled coili574 – 60431Sequence AnalysisAdd
BLAST
Coiled coili648 – 67023Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi134 – 1374Poly-Glu
Compositional biasi229 – 2324Poly-Glu
Compositional biasi666 – 6705Poly-Lys

Sequence similaritiesi

Belongs to the MPP10 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5384.
GeneTreeiENSGT00390000011359.
HOGENOMiHOG000046317.
HOVERGENiHBG052502.
InParanoidiO00566.
KOiK14559.
OMAiRSRPQNS.
OrthoDBiEOG7VDXPQ.
PhylomeDBiO00566.
TreeFamiTF105794.

Family and domain databases

InterProiIPR007151. Mpp10.
IPR012173. snoRNP_Mpp10.
[Graphical view]
PANTHERiPTHR17039. PTHR17039. 1 hit.
PfamiPF04006. Mpp10. 1 hit.
[Graphical view]
PIRSFiPIRSF017300. snoRNP_Mpp10. 1 hit.

Sequencei

Sequence statusi: Complete.

O00566-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPQVWRRRT LERCLTEVGK ATGRPECFLT IQEGLASKFT SLTKVLYDFN
60 70 80 90 100
KILENGRIHG SPLQKLVIEN FDDEQIWQQL ELQNEPILQY FQNAVSETIN
110 120 130 140 150
DEDISLLPES EEQEREEDGS EIEADDKEDL EDLEEEEVSD MGNDDPEMGE
160 170 180 190 200
RAENSSKSDL RKSPVFSDED SDLDFDISKL EQQSKVQNKG QGKPREKSIV
210 220 230 240 250
DDKFFKLSEM EAYLENIEKE EERKDDNDEE EEDIDFFEDI DSDEDEGGLF
260 270 280 290 300
GSKKLKSGKS SRNLKYKDFF DPVESDEDIT NVHDDELDSN KEDDEIAEEE
310 320 330 340 350
AEELSISETD EDDDLQENED NKQHKESLKR VTFALPDDAE TEDTGVLNVK
360 370 380 390 400
KNSDEVKSSF EKRQEKMNEK IASLEKELLE KKPWQLQGEV TAQKRPENSL
410 420 430 440 450
LEETLHFDHA VRMAPVITEE TTLQLEDIIK QRIRDQAWDD VVRKEKPKED
460 470 480 490 500
AYEYKKRLTL DHEKSKLSLA EIYEQEYIKL NQQKTAEEEN PEHVEIQKMM
510 520 530 540 550
DSLFLKLDAL SNFHFIPKPP VPEIKVVSNL PAITMEEVAP VSVSDAALLA
560 570 580 590 600
PEEIKEKNKA GDIKTAAEKT ATDKKRERRK KKYQKRMKIK EKEKRRKLLE
610 620 630 640 650
KSSVDQAGKY SKTVASEKLK QLTKTGKASF IKDEGKDKAL KSSQAFFSKL
660 670 680
QDQVKMQIND AKKTEKKKKK RQDISVHKLK L
Length:681
Mass (Da):78,864
Last modified:May 30, 2000 - v2
Checksum:iEDF27859D735D4E2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti69 – 691E → A.
Corresponds to variant rs10199088 [ dbSNP | Ensembl ].
VAR_053511
Natural varianti115 – 1151R → H.
Corresponds to variant rs13010513 [ dbSNP | Ensembl ].
VAR_053512
Natural varianti140 – 1401D → N.
Corresponds to variant rs10175940 [ dbSNP | Ensembl ].
VAR_053513
Natural varianti229 – 2291E → D.
Corresponds to variant rs1813160 [ dbSNP | Ensembl ].
VAR_024539
Natural varianti425 – 4251L → M.
Corresponds to variant rs3732240 [ dbSNP | Ensembl ].
VAR_022000
Natural varianti634 – 6341E → K.
Corresponds to variant rs6574 [ dbSNP | Ensembl ].
VAR_014470
Natural varianti639 – 6391A → T.
Corresponds to variant rs4852764 [ dbSNP | Ensembl ].
VAR_053514

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98494 mRNA. Translation: CAA67120.1.
BC126389 mRNA. Translation: AAI26390.1.
CCDSiCCDS1916.1.
RefSeqiNP_005782.1. NM_005791.2.
UniGeneiHs.656208.

Genome annotation databases

EnsembliENST00000244230; ENSP00000244230; ENSG00000124383.
GeneIDi10199.
KEGGihsa:10199.
UCSCiuc002sht.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98494 mRNA. Translation: CAA67120.1 .
BC126389 mRNA. Translation: AAI26390.1 .
CCDSi CCDS1916.1.
RefSeqi NP_005782.1. NM_005791.2.
UniGenei Hs.656208.

3D structure databases

ProteinModelPortali O00566.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115494. 13 interactions.
IntActi O00566. 2 interactions.
MINTi MINT-1192399.
STRINGi 9606.ENSP00000244230.

PTM databases

PhosphoSitei O00566.

2D gel databases

SWISS-2DPAGE O00566.

Proteomic databases

MaxQBi O00566.
PaxDbi O00566.
PeptideAtlasi O00566.
PRIDEi O00566.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000244230 ; ENSP00000244230 ; ENSG00000124383 .
GeneIDi 10199.
KEGGi hsa:10199.
UCSCi uc002sht.2. human.

Organism-specific databases

CTDi 10199.
GeneCardsi GC02P071358.
HGNCi HGNC:7213. MPHOSPH10.
HPAi HPA035059.
HPA035060.
HPA049907.
MIMi 605503. gene.
neXtProti NX_O00566.
PharmGKBi PA30919.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5384.
GeneTreei ENSGT00390000011359.
HOGENOMi HOG000046317.
HOVERGENi HBG052502.
InParanoidi O00566.
KOi K14559.
OMAi RSRPQNS.
OrthoDBi EOG7VDXPQ.
PhylomeDBi O00566.
TreeFami TF105794.

Miscellaneous databases

ChiTaRSi MPHOSPH10. human.
GeneWikii MPHOSPH10.
GenomeRNAii 10199.
NextBioi 38602.
PMAP-CutDB O00566.
PROi O00566.
SOURCEi Search...

Gene expression databases

Bgeei O00566.
CleanExi HS_MPHOSPH10.
ExpressionAtlasi O00566. baseline and differential.
Genevestigatori O00566.

Family and domain databases

InterProi IPR007151. Mpp10.
IPR012173. snoRNP_Mpp10.
[Graphical view ]
PANTHERi PTHR17039. PTHR17039. 1 hit.
Pfami PF04006. Mpp10. 1 hit.
[Graphical view ]
PIRSFi PIRSF017300. snoRNP_Mpp10. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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].

Entry informationi

Entry nameiMPP10_HUMAN
AccessioniPrimary (citable) accession number: O00566
Secondary accession number(s): A0AVJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: October 29, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3