Skip Header

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

M-phase phosphoprotein 6

Gene

MPHOSPH6

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

Functioni

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.1 Publication

GO - Molecular functioni

GO - Biological processi

  • maturation of 5.8S rRNA Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
M-phase phosphoprotein 6
Gene namesi
Name:MPHOSPH6
Synonyms:MPP6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:7214. MPHOSPH6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • exosome (RNase complex) Source: UniProtKB
  • nucleolus Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30920.

Polymorphism and mutation databases

BioMutaiMPHOSPH6.
DMDMi296438296.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 160160M-phase phosphoprotein 6PRO_0000122437Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101Phosphoserine1 Publication
Modified residuei147 – 1471Phosphothreonine5 Publications

Post-translational modificationi

Phosphorylated in M (mitotic) phase.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99547.
PaxDbiQ99547.
PRIDEiQ99547.

PTM databases

PhosphoSiteiQ99547.

Expressioni

Gene expression databases

BgeeiQ99547.
CleanExiHS_MPHOSPH6.
HS_MPP6.
ExpressionAtlasiQ99547. baseline and differential.
GenevestigatoriQ99547.

Organism-specific databases

HPAiCAB003674.
HPA026948.

Interactioni

Subunit structurei

Associates with the RNA exosome complex, probably mediated by EXOSC10. Interacts with ARHGAP18, EXOSC10 and SKIV2L2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EXOSC10Q017804EBI-373187,EBI-358236
EXOSC2Q138683EBI-373187,EBI-301735
SKIV2L2P422852EBI-373187,EBI-347612

Protein-protein interaction databases

BioGridi115495. 16 interactions.
DIPiDIP-31131N.
IntActiQ99547. 28 interactions.
MINTiMINT-1372240.
STRINGi9606.ENSP00000258169.

Structurei

3D structure databases

ProteinModelPortaliQ99547.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi116 – 13318Nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi32 – 354Poly-Glu

Sequence similaritiesi

Belongs to the MPP6 family.Curated

Phylogenomic databases

eggNOGiNOG256213.
GeneTreeiENSGT00390000009212.
HOGENOMiHOG000007728.
HOVERGENiHBG031714.
InParanoidiQ99547.
KOiK12593.
OMAiNGDITPI.
PhylomeDBiQ99547.
TreeFamiTF323810.

Family and domain databases

InterProiIPR019324. MPP6.
[Graphical view]
PANTHERiPTHR13582. PTHR13582. 1 hit.
PfamiPF10175. MPP6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99547-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAERKTRLS KNLLRMKFMQ RGLDSETKKQ LEEEEKKIIS EEHWYLDLPE
60 70 80 90 100
LKEKESFIIE EQSFLLCEDL LYGRMSFRGF NPEVEKLMLQ MNAKHKAEEV
110 120 130 140 150
EDETVELDVS DEEMARRYET LVGTIGKKFA RKRDHANYEE DENGDITPIK
160
AKKMFLKPQD
Length:160
Mass (Da):19,024
Last modified:May 18, 2010 - v2
Checksum:i506D5274C839BD7E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81R → K in CAA66916 (PubMed:8885239).Curated
Sequence conflicti8 – 81R → K in BAG36847 (PubMed:14702039).Curated
Sequence conflicti8 – 81R → K in AAH05242 (PubMed:15489334).Curated
Sequence conflicti8 – 81R → K in AAH11020 (PubMed:15489334).Curated
Sequence conflicti8 – 81R → K in AAH31017 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti58 – 581I → V.
Corresponds to variant rs2303267 [ dbSNP | Ensembl ].
VAR_056150

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10937.1.
RefSeqiNP_005783.2. NM_005792.2.
UniGeneiHs.344400.

Genome annotation databases

EnsembliENST00000258169; ENSP00000258169; ENSG00000135698.
GeneIDi10200.
KEGGihsa:10200.
UCSCiuc002fgw.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10937.1.
RefSeqiNP_005783.2. NM_005792.2.
UniGeneiHs.344400.

3D structure databases

ProteinModelPortaliQ99547.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115495. 16 interactions.
DIPiDIP-31131N.
IntActiQ99547. 28 interactions.
MINTiMINT-1372240.
STRINGi9606.ENSP00000258169.

PTM databases

PhosphoSiteiQ99547.

Polymorphism and mutation databases

BioMutaiMPHOSPH6.
DMDMi296438296.

Proteomic databases

MaxQBiQ99547.
PaxDbiQ99547.
PRIDEiQ99547.

Protocols and materials databases

DNASUi10200.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258169; ENSP00000258169; ENSG00000135698.
GeneIDi10200.
KEGGihsa:10200.
UCSCiuc002fgw.3. human.

Organism-specific databases

CTDi10200.
GeneCardsiGC16M082181.
H-InvDBHIX0013281.
HGNCiHGNC:7214. MPHOSPH6.
HPAiCAB003674.
HPA026948.
MIMi605500. gene.
neXtProtiNX_Q99547.
PharmGKBiPA30920.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG256213.
GeneTreeiENSGT00390000009212.
HOGENOMiHOG000007728.
HOVERGENiHBG031714.
InParanoidiQ99547.
KOiK12593.
OMAiNGDITPI.
PhylomeDBiQ99547.
TreeFamiTF323810.

Miscellaneous databases

GeneWikiiMPHOSPH6.
GenomeRNAii10200.
NextBioi38606.
PROiQ99547.
SOURCEiSearch...

Gene expression databases

BgeeiQ99547.
CleanExiHS_MPHOSPH6.
HS_MPP6.
ExpressionAtlasiQ99547. baseline and differential.
GenevestigatoriQ99547.

Family and domain databases

InterProiIPR019324. MPP6.
[Graphical view]
PANTHERiPTHR13582. PTHR13582. 1 hit.
PfamiPF10175. MPP6. 1 hit.
[Graphical view]
ProtoNetiSearch...

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].
    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: 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMPH6_HUMAN
AccessioniPrimary (citable) accession number: Q99547
Secondary accession number(s): B2RAF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 18, 2010
Last modified: April 29, 2015
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 16
    Human chromosome 16: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.