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Q99547 (MPH6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. 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:
M-phase phosphoprotein 6
Gene names
Name:MPHOSPH6
Synonyms:MPP6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

RNA-binding protein that associates with the RNA exosome complex. Involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA and may play a role in recruiting the RNA exosome complex to pre-rRNA; this function may include C1D. Ref.9

Subunit structure

Associates with the RNA exosome complex, probably mediated by EXOSC10. Interacts with ARHGAP18, EXOSC10 and SKIV2L2. Ref.6 Ref.9

Subcellular location

Nucleusnucleolus. Cytoplasm. Note: Cytoplasmic in M phase. Ref.7 Ref.9 Ref.13

Post-translational modification

Phosphorylated in M (mitotic) phase.

Sequence similarities

Belongs to the MPP6 family.

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmaturation of 5.8S rRNA

Inferred from mutant phenotype Ref.9. Source: UniProtKB

mitotic M phase

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

exosome (RNase complex)

Inferred from direct assay Ref.14. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 160160M-phase phosphoprotein 6
PRO_0000122437

Regions

Motif116 – 13318Nuclear localization signal Potential
Compositional bias32 – 354Poly-Glu

Amino acid modifications

Modified residue1101Phosphoserine Ref.12
Modified residue1471Phosphothreonine Ref.8 Ref.10 Ref.11 Ref.12 Ref.15

Natural variations

Natural variant581I → V.
Corresponds to variant rs2303267 [ dbSNP | Ensembl ].
VAR_056150

Experimental info

Sequence conflict81R → K in CAA66916. Ref.1
Sequence conflict81R → K in BAG36847. Ref.2
Sequence conflict81R → K in AAH05242. Ref.4
Sequence conflict81R → K in AAH11020. Ref.4
Sequence conflict81R → K in AAH31017. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q99547 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 506D5274C839BD7E

FASTA16019,024
        10         20         30         40         50         60 
MAAERKTRLS KNLLRMKFMQ RGLDSETKKQ LEEEEKKIIS EEHWYLDLPE LKEKESFIIE 

        70         80         90        100        110        120 
EQSFLLCEDL LYGRMSFRGF NPEVEKLMLQ MNAKHKAEEV EDETVELDVS DEEMARRYET 

       130        140        150        160 
LVGTIGKKFA RKRDHANYEE DENGDITPIK AKKMFLKPQD 

« 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].
Tissue: Lymphoblast.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle.
[3]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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, Lung and Urinary bladder.
[5]"AU binding proteins recruit the exosome to degrade ARE-containing mRNAs."
Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R., Pruijn G.J.M., Stoecklin G., Moroni C., Mann M., Karin M.
Cell 107:451-464(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"A protein interaction framework for human mRNA degradation."
Lehner B., Sanderson C.M.
Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGAP18.
[7]"MPP6 is an exosome-associated RNA-binding protein involved in 5.8S rRNA maturation."
Schilders G., Raijmakers R., Raats J.M., Pruijn G.J.
Nucleic Acids Res. 33:6795-6804(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH THE RNA EXOSOME COMPLEX, RNA-BINDING, SUBCELLULAR LOCATION.
[8]"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 THR-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"C1D and hMtr4p associate with the human exosome subunit PM/Scl-100 and are involved in pre-rRNA processing."
Schilders G., van Dijk E., Pruijn G.J.M.
Nucleic Acids Res. 35:2564-2572(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EXOSC10 AND SKIV2L2.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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 THR-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-110 AND THR-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"The human core exosome interacts with differentially localized processive RNases: hDIS3 and hDIS3L."
Tomecki R., Kristiansen M.S., Lykke-Andersen S., Chlebowski A., Larsen K.M., Szczesny R.J., Drazkowska K., Pastula A., Andersen J.S., Stepien P.P., Dziembowski A., Jensen T.H.
EMBO J. 29:2342-2357(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH THE RNA EXOSOME COMPLEX, SUBCELLULAR LOCATION.
[14]"Dis3-like 1: a novel exoribonuclease associated with the human exosome."
Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G., Heck A.J., Raijmakers R., Pruijn G.J.
EMBO J. 29:2358-2367(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"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 THR-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98263 mRNA. Translation: CAA66916.1.
AK314163 mRNA. Translation: BAG36847.1.
AC138304 Genomic DNA. No translation available.
BC005242 mRNA. Translation: AAH05242.1.
BC011020 mRNA. Translation: AAH11020.1.
BC031017 mRNA. Translation: AAH31017.1.
RefSeqNP_005783.2. NM_005792.2.
UniGeneHs.344400.

3D structure databases

ProteinModelPortalQ99547.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115495. 14 interactions.
IntActQ99547. 27 interactions.
MINTMINT-1372240.
STRING9606.ENSP00000258169.

PTM databases

PhosphoSiteQ99547.

Polymorphism databases

DMDM296438296.

Proteomic databases

PaxDbQ99547.
PRIDEQ99547.

Protocols and materials databases

DNASU10200.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258169; ENSP00000258169; ENSG00000135698.
GeneID10200.
KEGGhsa:10200.
UCSCuc002fgw.3. human.

Organism-specific databases

CTD10200.
GeneCardsGC16M082181.
H-InvDBHIX0013281.
HGNCHGNC:7214. MPHOSPH6.
HPACAB003674.
HPA026948.
MIM605500. gene.
neXtProtNX_Q99547.
PharmGKBPA30920.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG256213.
HOGENOMHOG000007728.
HOVERGENHBG031714.
InParanoidQ99547.
KOK12593.
OMANGDITPI.
PhylomeDBQ99547.
TreeFamTF323810.

Gene expression databases

ArrayExpressQ99547.
BgeeQ99547.
CleanExHS_MPHOSPH6.
HS_MPP6.
GenevestigatorQ99547.

Family and domain databases

InterProIPR019324. MPP6.
[Graphical view]
PANTHERPTHR13582. PTHR13582. 1 hit.
PfamPF10175. MPP6. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMPHOSPH6.
GenomeRNAi10200.
NextBio38606.
PROQ99547.
SOURCESearch...

Entry information

Entry nameMPH6_HUMAN
AccessionPrimary (citable) accession number: Q99547
Secondary accession number(s): B2RAF0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 121 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 16

Human chromosome 16: entries, gene names and cross-references to MIM