Details for: MPHOSPH10
Associated with
Other Information
Genular Protein ID: 1129112547
Symbol: MPP10_HUMAN
Name: U3 small nucleolar ribonucleoprotein protein MPP10
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 8885239
Title: Identification of novel M phase phosphoproteins by expression cloning.
PubMed ID: 8885239
DOI: 10.1091/mbc.7.9.1455
PubMed ID: 9450966
Title: M phase phosphoprotein 10 is a human U3 small nucleolar ribonucleoprotein component.
PubMed ID: 9450966
DOI: 10.1091/mbc.9.2.437
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 12429849
Title: Functional proteomic analysis of human nucleolus.
PubMed ID: 12429849
PubMed ID: 12655004
Title: The human Imp3 and Imp4 proteins form a ternary complex with hMpp10, which only interacts with the U3 snoRNA in 60-80S ribonucleoprotein complexes.
PubMed ID: 12655004
DOI: 10.1093/nar/gkg300
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 25755297
Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.
PubMed ID: 25755297
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 34516797
Title: Nucleolar maturation of the human small subunit processome.
PubMed ID: 34516797
Sequence Information:
- Length: 681
- Mass: 78864
- Checksum: EDF27859D735D4E2
- Sequence:
MAPQVWRRRT LERCLTEVGK ATGRPECFLT IQEGLASKFT SLTKVLYDFN KILENGRIHG SPLQKLVIEN FDDEQIWQQL ELQNEPILQY FQNAVSETIN DEDISLLPES EEQEREEDGS EIEADDKEDL EDLEEEEVSD MGNDDPEMGE RAENSSKSDL RKSPVFSDED SDLDFDISKL EQQSKVQNKG QGKPREKSIV DDKFFKLSEM EAYLENIEKE EERKDDNDEE EEDIDFFEDI DSDEDEGGLF GSKKLKSGKS SRNLKYKDFF DPVESDEDIT NVHDDELDSN KEDDEIAEEE AEELSISETD EDDDLQENED NKQHKESLKR VTFALPDDAE TEDTGVLNVK KNSDEVKSSF EKRQEKMNEK IASLEKELLE KKPWQLQGEV TAQKRPENSL LEETLHFDHA VRMAPVITEE TTLQLEDIIK QRIRDQAWDD VVRKEKPKED AYEYKKRLTL DHEKSKLSLA EIYEQEYIKL NQQKTAEEEN PEHVEIQKMM DSLFLKLDAL SNFHFIPKPP VPEIKVVSNL PAITMEEVAP VSVSDAALLA PEEIKEKNKA GDIKTAAEKT ATDKKRERRK KKYQKRMKIK EKEKRRKLLE KSSVDQAGKY SKTVASEKLK QLTKTGKASF IKDEGKDKAL KSSQAFFSKL QDQVKMQIND AKKTEKKKKK RQDISVHKLK L
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.