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HNRPM_RAT
ID   HNRPM_RAT               Reviewed;         690 AA.
AC   Q62826; Q5M815;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   25-MAY-2022, entry version 154.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein M;
DE            Short=hnRNP M;
DE   AltName: Full=M4 protein;
GN   Name=Hnrnpm; Synonyms=Hnrpm;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAA83442.2}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver {ECO:0000312|EMBL:AAA83442.2};
RX   PubMed=11406629; DOI=10.1074/jbc.m104093200;
RA   Bajenova O.V., Zimmer R., Stolper E., Salisbury-Rowswell J., Nanji A.,
RA   Thomas P.;
RT   "Heterogeneous RNA-binding protein M4 is a receptor for carcinoembryonic
RT   antigen in Kupffer cells.";
RL   J. Biol. Chem. 276:31067-31073(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 55-68; 182-196; 245-260 AND 612-625.
RC   TISSUE=Liver {ECO:0000269|PubMed:10947964};
RX   PubMed=10947964; DOI=10.1042/bj3500495;
RA   Kafasla P., Patrinou-Georgoula M., Guialis A.;
RT   "The 72/74-kDa polypeptides of the 70-110 S large heterogeneous nuclear
RT   ribonucleoprotein complex (LH-nRNP) represent a discrete subset of the
RT   hnRNP M protein family.";
RL   Biochem. J. 350:495-503(2000).
RN   [4]
RP   PROTEIN SEQUENCE OF 60-68 AND 418-423, AND SUBCELLULAR LOCATION.
RC   TISSUE=Liver;
RX   PubMed=16128803; DOI=10.1111/j.1742-4658.2005.04847.x;
RA   Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K.,
RA   Watanabe Y., Furukawa K., Horigome T.;
RT   "Proteome analysis of a rat liver nuclear insoluble protein fraction and
RT   localization of a novel protein, ISP36, to compartments in the
RT   interchromatin space.";
RL   FEBS J. 272:4327-4338(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535; SER-548 AND SER-661, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Pre-mRNA binding protein, binds avidly to poly(G) and poly(U)
CC       RNA homopolymers. Involved in splicing. Acts as a receptor for
CC       carcinoembryonic antigen in Kupffer cells, may initiate a series of
CC       signaling events leading to tyrosine phosphorylation of proteins and
CC       induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha
CC       cytokines. {ECO:0000269|PubMed:11406629}.
CC   -!- SUBUNIT: Identified in the spliceosome C complex (By similarity).
CC       Interacts with PPIA/CYPA (By similarity).
CC       {ECO:0000250|UniProtKB:P52272}.
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:16128803}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:11406629};
CC         IsoId=Q62826-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q62826-2; Sequence=VSP_051766;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including liver,
CC       heart, lung, skeletal muscle, kidney, stomach, large intestine, small
CC       intestine, pancreas, spleen, peritoneal macrophage and thyroid.
CC       {ECO:0000269|PubMed:11406629}.
CC   -!- PTM: Sumoylated. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA83442.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U32577; AAA83442.2; ALT_INIT; mRNA.
DR   EMBL; BC088317; AAH88317.1; -; mRNA.
DR   RefSeq; NP_001103381.1; NM_001109911.1.
DR   RefSeq; NP_446328.2; NM_053876.2.
DR   AlphaFoldDB; Q62826; -.
DR   SMR; Q62826; -.
DR   BioGRID; 250540; 5.
DR   IntAct; Q62826; 3.
DR   MINT; Q62826; -.
DR   STRING; 10116.ENSRNOP00000032108; -.
DR   CarbonylDB; Q62826; -.
DR   iPTMnet; Q62826; -.
DR   PhosphoSitePlus; Q62826; -.
DR   jPOST; Q62826; -.
DR   PeptideAtlas; Q62826; -.
DR   PRIDE; Q62826; -.
DR   GeneID; 116655; -.
DR   KEGG; rno:116655; -.
DR   UCSC; RGD:620369; rat. [Q62826-1]
DR   CTD; 4670; -.
DR   RGD; 620369; Hnrnpm.
DR   eggNOG; KOG4212; Eukaryota.
DR   InParanoid; Q62826; -.
DR   OrthoDB; 1174365at2759; -.
DR   PhylomeDB; Q62826; -.
DR   Reactome; R-RNO-6803529; FGFR2 alternative splicing.
DR   Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR   PRO; PR:Q62826; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0042382; C:paraspeckles; ISO:RGD.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0005681; C:spliceosomal complex; ISO:RGD.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IDA:RGD.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:1990405; F:protein antigen binding; IDA:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR   GO; GO:0003723; F:RNA binding; TAS:RGD.
DR   GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISO:RGD.
DR   GO; GO:1990831; P:cellular response to carcinoembryonic antigen; IEP:RGD.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:1904591; P:positive regulation of protein import; IDA:RGD.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:RGD.
DR   GO; GO:2000815; P:regulation of mRNA stability involved in response to oxidative stress; IBA:GO_Central.
DR   CDD; cd12661; RRM3_hnRNPM; 1.
DR   Gene3D; 3.30.70.330; -; 3.
DR   InterPro; IPR024667; HnRNP_M.
DR   InterPro; IPR024666; HnRNP_M_PY-NLS.
DR   InterPro; IPR034990; hnRNPM_RRM3.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR23003:SF6; PTHR23003:SF6; 5.
DR   Pfam; PF11532; HnRNP_M_NLS; 1.
DR   Pfam; PF00076; RRM_1; 3.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   Isopeptide bond; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW   Spliceosome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CHAIN           2..690
FT                   /note="Heterogeneous nuclear ribonucleoprotein M"
FT                   /id="PRO_0000081866"
FT   DOMAIN          70..148
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          164..241
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REPEAT          360..365
FT                   /note="1"
FT   REPEAT          367..372
FT                   /note="2"
FT   REPEAT          375..380
FT                   /note="3"
FT   REPEAT          386..391
FT                   /note="4"
FT   REPEAT          393..398
FT                   /note="5"
FT   REPEAT          400..405
FT                   /note="6"
FT   REPEAT          406..411
FT                   /note="7"
FT   REPEAT          413..418
FT                   /note="8"
FT   REPEAT          421..426
FT                   /note="9"
FT   REPEAT          428..433
FT                   /note="10"
FT   REPEAT          435..440
FT                   /note="11"
FT   REPEAT          442..447
FT                   /note="12"
FT   REPEAT          453..458
FT                   /note="13"
FT   REPEAT          460..465
FT                   /note="14"
FT   REPEAT          467..472
FT                   /note="15"
FT   REPEAT          474..479
FT                   /note="16"
FT   REPEAT          481..486
FT                   /note="17"
FT   REPEAT          488..493
FT                   /note="18"
FT   REPEAT          500..505
FT                   /note="19"
FT   REPEAT          507..512
FT                   /note="20"
FT   REPEAT          514..519
FT                   /note="21"
FT   REPEAT          522..527
FT                   /note="22"
FT   REPEAT          528..532
FT                   /note="23"
FT   REPEAT          535..540
FT                   /note="24"
FT   REPEAT          541..545
FT                   /note="25"
FT   REPEAT          548..553
FT                   /note="26"
FT   REPEAT          563..568
FT                   /note="27"
FT   DOMAIN          613..689
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..568
FT                   /note="27 X 6 AA repeats of [GEVSTPAN]-[ILMV]-[DE]-[RH]-
FT                   [MLVI]-[GAV]"
FT   COMPBIAS        40..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         133
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D0E1"
FT   MOD_RES         164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         237
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         325
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         337
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         357
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         392
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         428
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         441
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         456
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         488
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         535
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         548
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         578
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         593
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         597
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         625
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         632
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D0E1"
FT   MOD_RES         658
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   MOD_RES         661
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CROSSLNK        17
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        37
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        68
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        82
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        87
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        126
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        133
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        142
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        144
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        181
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        237
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        245
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        305
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        341
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        348
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        611
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        627
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        645
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        652
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        658
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        658
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   CROSSLNK        676
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52272"
FT   VAR_SEQ         1..155
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_051766"
FT   CONFLICT        55
FT                   /note="R -> S (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        352
FT                   /note="S -> G (in Ref. 2; AAH88317)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        582
FT                   /note="T -> A (in Ref. 2; AAH88317)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        615
FT                   /note="I -> T (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   690 AA;  73782 MW;  4FF9B6D6BD9B1F43 CRC64;
     MAAGVEAAAE VAATEPKMEE ESGAPCVPSG NGAPVPKGEE RPTQNEKRKE KNIKRGGNRF
     EPYANPTKRY RAFITNIPFD VKWQSLKDLV KEKVGEVTYV ELLMDAEGKS RGCAVVEFKM
     EESMKKAAEV LNKHSLSGRP LKVKEDPDGE HARRAMQKAG RLGSTVFVAN LDYKVGWKKL
     KEVFSMAGVV VRADILEDKD GKSRGIGTVT FEQSIEAVQA ISMFNGQLLF DRPMHVKMDE
     RALPKGDFFP PERPQQLPHG LGGIGMGLGP GGQPIDANHL NKGIGMGNLG PAGMGMEGIG
     FGINKIGGME GPFGGGMENM GRFGSGMNMG RINEILSNAL KRGEIIAKQG GSGAGGSVPG
     IERMGPGIDR ISGAGMERMG AGLGHGMDRV GSEIERMGLV MDRMGSVERM GSGIERMGPL
     GLDHMASSIE RMGQTMERIG SGVERMGAGM GFGLERMAAP IDRVGQTIER MGSGVERMGP
     AIERMGLSMD RMVPTGMGAG LERMGPVMDR MATGLERMGA NNLERMGLER MGANSLERMG
     LERMGANSLE RMGPAMGPAL GAGIERMGLA MGGAGGASFD RTIEMERGNF GGSFAGSFGG
     AGGHAPGVAR KACQIFVRNL PFDFTWKMLK DKFNECGHVL YADIKMENGK SKGCGVVKFE
     SPEVAERACR MMNGMKLSGR EIDVRIDRNA
 
 
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