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[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
DOI=10.1093/nar/21.3.439; PubMed=8441656 [NCBI, ExPASy, EBI, Israel, Japan]
Datar K.V.,
Dreyfuss G.,
Swanson M.S.;
"The human hnRNP M proteins: identification of a methionine/arginine-rich repeat motif in ribonucleoproteins.";
Nucleic Acids Res. 21:439-446(1993).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
DOI=10.1093/nar/24.13.2535; PubMed=8692693 [NCBI, ExPASy, EBI, Israel, Japan]
Gattoni R.,
Mahe D.,
Mahl P.,
Fischer N.,
Mattei M.-G.,
Stevenin J.,
Fuchs J.-P.;
"The human hnRNP-M proteins: structure and relation with early heat shock-induced splicing arrest and chromosome mapping.";
Nucleic Acids Res. 24:2535-2542(1996).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Zhao Z.,
Huang X.,
Li N.,
Cao X.;
"A new human M4 protein with deletion.";
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, Lymph, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[5]
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PROTEIN SEQUENCE OF 2-17; 73-83; 222-232; 372-381; 404-410; 497-503; 518-524 AND 628-650, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V.;
Submitted (OCT-2004) to UniProtKB.
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[6]
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IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
DOI=10.1017/S1355838202021088; PubMed=11991638 [NCBI, ExPASy, EBI, Israel, Japan]
Jurica M.S.,
Licklider L.J.,
Gygi S.P.,
Grigorieff N.,
Moore M.J.;
"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.";
RNA 8:426-439(2002).
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[7]
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IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUMOYLATION.
DOI=10.1074/jbc.M404201200; PubMed=15175327 [NCBI, ExPASy, EBI, Israel, Japan]
Vertegaal A.C.O.,
Ogg S.C.,
Jaffray E.,
Rodriguez M.S.,
Hay R.T.,
Andersen J.S.,
Mann M.,
Lamond A.I.;
"A proteomic study of SUMO-2 target proteins.";
J. Biol. Chem. 279:33791-33798(2004).
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[8]
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SUMOYLATION.
DOI=10.1074/jbc.M411718200; PubMed=15561718 [NCBI, ExPASy, EBI, Israel, Japan]
Gocke C.B.,
Yu H.,
Kang J.;
"Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates.";
J. Biol. Chem. 280:5004-5012(2005).
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[9]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-618 AND SER-701, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V.,
Blagoev B.,
Gnad F.,
Macek B.,
Kumar C.,
Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
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[10]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A.,
Villen J.,
Gerber S.A.,
Rush J.,
Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
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[11]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588; SER-618 AND SER-701, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H.,
Olsen J.V.,
Bairlein M.,
Gnad F.,
Oppermann F.S.,
Korner R.,
Greff Z.,
Keri G.,
Stemmann O.,
Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
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[12]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432; SER-468; SER-528; SER-588; SER-618; SER-633; SER-637 AND SER-701, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N.,
Zhou C.,
Villen J.,
Beausoleil S.A.,
Bakalarski C.E.,
Elledge S.J.,
Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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[13]
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IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J.,
Superti-Furga G.,
Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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[14]
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STRUCTURE BY NMR OF 196-296 AND 652-730.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the RNA binding domains of heterogeneous nuclear ribonucleoprotein M.";
Submitted (OCT-2006) to the PDB data bank.
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- FUNCTION: Pre-mRNA binding protein in vivo, binds avidly to poly(G) and poly(U) RNA homopolymers in vitro. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines.
- SUBUNIT: Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRNPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8.
- INTERACTION:
P48634:BAT2; NbExp=1; IntAct=EBI-486809, EBI-347545;
Q9Y2Q3:GSTK1; NbExp=1; IntAct=EBI-486809, EBI-1053767;
Q9Y5J5:PHLDA3; NbExp=1; IntAct=EBI-486809, EBI-1055859;
O75365:PTP4A3; NbExp=1; IntAct=EBI-486809, EBI-1043866;
O14593:RFXANK; NbExp=1; IntAct=EBI-486809, EBI-1057665;
Q15714:TSC22D1; NbExp=1; IntAct=EBI-486809, EBI-712609;
- SUBCELLULAR LOCATION: Nucleus, nucleolus.
- ALTERNATIVE PRODUCTS:
3 named isoforms [FASTA] produced by alternative splicing. Experimental confirmation may be lacking for some isoforms.
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| Name | 2 |
| Synonyms | M1-M2 |
| Isoform ID | P52272-2 |
| Features which should be applied to build the isoform sequence: VSP_005845. |
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| Name | 3 |
| Synonyms | M3 |
| Isoform ID | P52272-3 |
| The sequence of this isoform is not described. |
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- PTM: Sumoylated.
- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 730 AA [This is the length of the unprocessed precursor] |
Molecular weight: 77516 Da [This is the MW of the unprocessed precursor] |
CRC64: 1A73DD35A3501861 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAAGVEAAAE VAATEIKMEE ESGAPGVPSG NGAPGPKGEG ERPAQNEKRK EKNIKRGGNR
70 80 90 100 110 120
FEPYANPTKR YRAFITNIPF DVKWQSLKDL VKEKVGEVTY VELLMDAEGK SRGCAVVEFK
130 140 150 160 170 180
MEESMKKAAE VLNKHSLSGR PLKVKEDPDG EHARRAMQKV MATTGGMGMG PGGPGMITIP
190 200 210 220 230 240
PSILNNPNIP NEIIHALQAG RLGSTVFVAN LDYKVGWKKL KEVFSMAGVV VRADILEDKD
250 260 270 280 290 300
GKSRGIGTVT FEQSIEAVQA ISMFNGQLLF DRPMHVKMDE RALPKGDFFP PERPQQLPHG
310 320 330 340 350 360
LGGIGMGLGP GGQPIDANHL NKGIGMGNIG PAGMGMEGIG FGINKMGGME GPFGGGMENM
370 380 390 400 410 420
GRFGSGMNMG RINEILSNAL KRGEIIAKQG GGGGGGSVPG IERMGPGIDR LGGAGMERMG
430 440 450 460 470 480
AGLGHGMDRV GSEIERMGLV MDRMGSVERM GSGIERMGPL GLDHMASSIE RMGQTMERIG
490 500 510 520 530 540
SGVERMGAGM GFGLERMAAP IDRVGQTIER MGSGVERMGP AIERMGLSME RMVPAGMGAG
550 560 570 580 590 600
LERMGPVMDR MATGLERMGA NNLERMGLER MGANSLERMG LERMGANSLE RMGPAMGPAL
610 620 630 640 650 660
GAGIERMGLA MGGGGGASFD RAIEMERGNF GGSFAGSFGG AGGHAPGVAR KACQIFVRNL
670 680 690 700 710 720
PFDFTWKMLK DKFNECGHVL YADIKMENGK SKGCGVVKFE SPEVAERACR MMNGMKLSGR
730
EIDVRIDRNA
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P52272 in FASTA format |
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