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Protein

Heterogeneous nuclear ribonucleoprotein M

Gene

Hnrnpm

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-6803529. FGFR2 alternative splicing.
R-MMU-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein M
Short name:
hnRNP M
Gene namesi
Name:Hnrnpm
Synonyms:Hnrpm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1926465. Hnrnpm.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 729728Heterogeneous nuclear ribonucleoprotein MPRO_0000081865Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Cross-linki17 – 17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei29 – 291PhosphoserineBy similarity
Cross-linki82 – 82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei133 – 1331N6-acetyllysineCombined sources
Cross-linki144 – 144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei276 – 2761N6-acetyllysineBy similarity
Modified residuei364 – 3641PhosphoserineBy similarity
Cross-linki387 – 387Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei396 – 3961PhosphoserineBy similarity
Modified residuei431 – 4311PhosphoserineBy similarity
Modified residuei451 – 4511PhosphoserineBy similarity
Modified residuei467 – 4671PhosphoserineBy similarity
Modified residuei480 – 4801PhosphoserineBy similarity
Modified residuei527 – 5271PhosphoserineBy similarity
Modified residuei574 – 5741PhosphoserineBy similarity
Modified residuei587 – 5871PhosphoserineBy similarity
Modified residuei617 – 6171PhosphoserineCombined sources
Modified residuei632 – 6321PhosphoserineBy similarity
Modified residuei636 – 6361PhosphoserineBy similarity
Modified residuei671 – 6711N6-acetyllysineCombined sources
Cross-linki684 – 684Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei697 – 6971N6-acetyllysine; alternateCombined sources
Cross-linki697 – 697Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei700 – 7001PhosphoserineCombined sources

Post-translational modificationi

Sumoylated.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9D0E1.
MaxQBiQ9D0E1.
PaxDbiQ9D0E1.
PRIDEiQ9D0E1.

PTM databases

iPTMnetiQ9D0E1.
PhosphoSiteiQ9D0E1.
SwissPalmiQ9D0E1.

Expressioni

Gene expression databases

BgeeiQ9D0E1.
ExpressionAtlasiQ9D0E1. baseline and differential.
GenevisibleiQ9D0E1. MM.

Interactioni

Subunit structurei

Identified in the spliceosome C complex.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi218411. 7 interactions.
IntActiQ9D0E1. 6 interactions.
MINTiMINT-1868359.
STRINGi10090.ENSMUSP00000120115.

Structurei

3D structure databases

ProteinModelPortaliQ9D0E1.
SMRiQ9D0E1. Positions 73-146, 195-295, 651-729.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 14879RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini203 – 28078RRM 2PROSITE-ProRule annotationAdd
BLAST
Repeati399 – 40461
Repeati406 – 41162
Repeati414 – 41963
Repeati425 – 43064
Repeati432 – 43765
Repeati439 – 44466
Repeati445 – 45067
Repeati452 – 45768
Repeati460 – 46569
Repeati467 – 472610
Repeati474 – 479611
Repeati481 – 486612
Repeati492 – 497613
Repeati499 – 504614
Repeati506 – 511615
Repeati513 – 518616
Repeati520 – 525617
Repeati527 – 532618
Repeati539 – 544619
Repeati546 – 551620
Repeati553 – 558621
Repeati561 – 566622
Repeati566 – 571623
Repeati574 – 579624
Repeati579 – 584625
Repeati587 – 592626
Repeati602 – 607627
Domaini652 – 72877RRM 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni399 – 60720927 X 6 AA repeats of [GEVSTPAN]-[ILMV]-[DE]-[RH]-[MLVI]-[GAV]Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi389 – 3957Poly-Gly

Sequence similaritiesi

Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4212. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00410000025635.
HOGENOMiHOG000231932.
HOVERGENiHBG054880.
InParanoidiQ9D0E1.
KOiK12887.
OMAiGMNKMGG.
OrthoDBiEOG7ZSHSK.
PhylomeDBiQ9D0E1.
TreeFamiTF313406.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR024667. HnRNP_M.
IPR024666. HnRNP_M_PY-NLS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR23003:SF6. PTHR23003:SF6. 3 hits.
PfamiPF11532. HnRNP_M. 1 hit.
PF00076. RRM_1. 3 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9D0E1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAGVEAAAE VAATEPKMEE ESGAPCVPSG NGAPGPKGEE RPTQNEKRKE
60 70 80 90 100
KNIKRGGNRF EPYSNPTKRY RAFITNIPFD VKWQSLKDLV KEKVGEVTYV
110 120 130 140 150
ELLMDAEGKS RGCAVVEFKM EESMKKAAEV LNKHSLSGRP LKVKEDPDGE
160 170 180 190 200
HARRAMQKVM ATTGGMGMGP GGPGMINIPP SILNNPNIPN EIIHALQAGR
210 220 230 240 250
LGSTVFVANL DYKVGWKKLK EVFSMAGVVV RADILEDKDG KSRGIGIVTF
260 270 280 290 300
EQSIEAVQAI SMFNGQLLFD RPMHVKMDER ALPKGDFFPP ERPQQLPHGL
310 320 330 340 350
GGIGMGLGPG GQPIDANHLS KGIGMGNLGP AGMGMEGIGF GINKIGGMEG
360 370 380 390 400
PFGGGMENMG RFGSGMNMGR INEILSNALK RGEIIAKQGG GGAGGSVPGI
410 420 430 440 450
ERMGPGIDRI SGAGMERMGA GLGHGMDRVG SEIERMGLVM DRMGSVERMG
460 470 480 490 500
SSIERMGPLG LDHMASSIER MGQTMERIGS GVERMGAGMG FGLERMAAPI
510 520 530 540 550
DRVGQTIERM GSGVERMGPA IERMGLSMDR MVPTGMGASL ERMGPVMDRM
560 570 580 590 600
ATGLERMGAN NLERMGLERM GANSLERMGL ERMGANSLER MGPAMGPALG
610 620 630 640 650
AGIERMGLAM GGAGGASFDR AIEMERGNFG GSFAGSFGGA GGHAPGVARK
660 670 680 690 700
ACQIFVRNLP FDFTWKMLKD KFNECGHVLY ADIKMENGKS KGCGVVKFES
710 720
PEVAERACRM MNGMKLSGRE IDVRIDRNA
Length:729
Mass (Da):77,649
Last modified:January 23, 2007 - v3
Checksum:iD42650B419362D6B
GO
Isoform 2 (identifier: Q9D0E1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     159-197: Missing.

Show »
Length:690
Mass (Da):73,741
Checksum:iC72B1AE0C8A5DE4F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti357 – 3571E → G in AAH05758 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei159 – 19739Missing in isoform 2. 1 PublicationVSP_011933Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011521 mRNA. Translation: BAB27675.1.
BC005758 mRNA. Translation: AAH05758.1.
BC065172 mRNA. Translation: AAH65172.1.
CCDSiCCDS37570.1. [Q9D0E1-1]
CCDS50068.1. [Q9D0E1-2]
RefSeqiNP_001103383.1. NM_001109913.1. [Q9D0E1-2]
NP_084080.1. NM_029804.3. [Q9D0E1-1]
UniGeneiMm.311439.

Genome annotation databases

EnsembliENSMUST00000087582; ENSMUSP00000084864; ENSMUSG00000059208. [Q9D0E1-2]
ENSMUST00000148178; ENSMUSP00000120115; ENSMUSG00000059208. [Q9D0E1-1]
GeneIDi76936.
KEGGimmu:76936.
UCSCiuc008bze.2. mouse. [Q9D0E1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011521 mRNA. Translation: BAB27675.1.
BC005758 mRNA. Translation: AAH05758.1.
BC065172 mRNA. Translation: AAH65172.1.
CCDSiCCDS37570.1. [Q9D0E1-1]
CCDS50068.1. [Q9D0E1-2]
RefSeqiNP_001103383.1. NM_001109913.1. [Q9D0E1-2]
NP_084080.1. NM_029804.3. [Q9D0E1-1]
UniGeneiMm.311439.

3D structure databases

ProteinModelPortaliQ9D0E1.
SMRiQ9D0E1. Positions 73-146, 195-295, 651-729.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi218411. 7 interactions.
IntActiQ9D0E1. 6 interactions.
MINTiMINT-1868359.
STRINGi10090.ENSMUSP00000120115.

PTM databases

iPTMnetiQ9D0E1.
PhosphoSiteiQ9D0E1.
SwissPalmiQ9D0E1.

Proteomic databases

EPDiQ9D0E1.
MaxQBiQ9D0E1.
PaxDbiQ9D0E1.
PRIDEiQ9D0E1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000087582; ENSMUSP00000084864; ENSMUSG00000059208. [Q9D0E1-2]
ENSMUST00000148178; ENSMUSP00000120115; ENSMUSG00000059208. [Q9D0E1-1]
GeneIDi76936.
KEGGimmu:76936.
UCSCiuc008bze.2. mouse. [Q9D0E1-1]

Organism-specific databases

CTDi4670.
MGIiMGI:1926465. Hnrnpm.

Phylogenomic databases

eggNOGiKOG4212. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00410000025635.
HOGENOMiHOG000231932.
HOVERGENiHBG054880.
InParanoidiQ9D0E1.
KOiK12887.
OMAiGMNKMGG.
OrthoDBiEOG7ZSHSK.
PhylomeDBiQ9D0E1.
TreeFamiTF313406.

Enzyme and pathway databases

ReactomeiR-MMU-6803529. FGFR2 alternative splicing.
R-MMU-72163. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiHnrnpm. mouse.
PROiQ9D0E1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0E1.
ExpressionAtlasiQ9D0E1. baseline and differential.
GenevisibleiQ9D0E1. MM.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR024667. HnRNP_M.
IPR024666. HnRNP_M_PY-NLS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR23003:SF6. PTHR23003:SF6. 3 hits.
PfamiPF11532. HnRNP_M. 1 hit.
PF00076. RRM_1. 3 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  2. "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] (ISOFORM 2).
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Mammary tumor.
  3. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 449-455, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-700, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-671 AND LYS-697, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiHNRPM_MOUSE
AccessioniPrimary (citable) accession number: Q9D0E1
Secondary accession number(s): Q6P1B2, Q99JQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.