Q99547 (MPH6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
M-phase phosphoprotein 6

Gene names

Name:	MPHOSPH6
Synonyms:	MPP6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	160 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleolus. 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 process	rRNA processing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	M phase of mitotic cell cycle Traceable author statement Ref.1. Source: ProtInc maturation of 5.8S rRNA Inferred from mutant phenotype Ref.9. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA exosome (RNase complex) Inferred from direct assay Ref.14. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EXOSC10	Q01780	4	EBI-373187,EBI-358236
EXOSC2	Q13868	3	EBI-373187,EBI-301735
SKIV2L2	P42285	2	EBI-373187,EBI-347612

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 160	160	M-phase phosphoprotein 6		PRO_0000122437
Regions
	Motif	116 – 133	18	Nuclear localization signal Potential
	Compositional bias	32 – 35	4	Poly-Glu
Amino acid modifications
	Modified residue	110	1	Phosphoserine Ref.12
	Modified residue	147	1	Phosphothreonine Ref.8 Ref.10 Ref.11 Ref.12 Ref.15
Natural variations
	Natural variant	58	1	I → V. Corresponds to variant rs2303267 [ dbSNP | Ensembl ].		VAR_056150
Experimental info
	Sequence conflict	8	1	R → K in CAA66916. Ref.1
	Sequence conflict	8	1	R → K in BAG36847. Ref.2
	Sequence conflict	8	1	R → K in AAH05242. Ref.4
	Sequence conflict	8	1	R → K in AAH11020. Ref.4
	Sequence conflict	8	1	R → K in AAH31017. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q99547 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 506D5274C839BD7E	FASTA	160	19,024
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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: MASS SPECTROMETRY, ASSOCIATION WITH THE RNA EXOSOME COMPLEX.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, 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, MASS SPECTROMETRY. 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.
IPI	IPI00016074.
RefSeq	NP_005783.2. NM_005792.2.
UniGene	Hs.344400.
3D structure databases
ProteinModelPortal	Q99547.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99547. 26 interactions.
MINT	MINT-1372240.
STRING	9606.ENSP00000258169.
PTM databases
PhosphoSite	Q99547.
Polymorphism databases
DMDM	296438296.
Proteomic databases
PaxDb	Q99547.
PRIDE	Q99547.
Protocols and materials databases
DNASU	10200.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000258169; ENSP00000258169; ENSG00000135698.
GeneID	10200.
KEGG	hsa:10200.
UCSC	uc002fgw.3. human.
Organism-specific databases
CTD	10200.
GeneCards	GC16M082181.
H-InvDB	HIX0013281.
HGNC	HGNC:7214. MPHOSPH6.
HPA	CAB003674. HPA026948.
MIM	605500. gene.
neXtProt	NX_Q99547.
PharmGKB	PA30920.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG256213.
HOGENOM	HOG000007728.
HOVERGEN	HBG031714.
InParanoid	Q99547.
KO	K12593.
OMA	EEMALRY.
OrthoDB	EOG4QZ7NB.
PhylomeDB	Q99547.
Gene expression databases
ArrayExpress	Q99547.
Bgee	Q99547.
CleanEx	HS_MPHOSPH6. HS_MPP6.
Genevestigator	Q99547.
GermOnline	ENSG00000135698. Homo sapiens.
Family and domain databases
InterPro	IPR019324. MPP6. [Graphical view]
PANTHER	PTHR13582. PTHR13582. 1 hit.
Pfam	PF10175. MPP6. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10200.
NextBio	38606.
SOURCE	Search...

Entry information

Entry name

MPH6_HUMAN

Accession

Primary (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 3, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.