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P52272 (HNRPM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein M

Short name=hnRNP M
Gene names
Name:HNRNPM
Synonyms:HNRPM, NAGR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length730 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

Identified in the spliceosome C complex. Ref.6

Subcellular location

Nucleusnucleolus Ref.5.

Post-translational modification

Sumoylated. Ref.7

Sequence similarities

Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement. Source: Reactome

alternative mRNA splicing, via spliceosome

Inferred from mutant phenotype PubMed 19874820. Source: BHF-UCL

gene expression

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Inferred by curator Ref.6. Source: UniProtKB

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.6. Source: UniProtKB

integral component of plasma membrane

Traceable author statement PubMed 8088785. Source: ProtInc

nuclear matrix

Inferred from direct assay PubMed 19874820. Source: BHF-UCL

nucleoplasm

Inferred from direct assay PubMed 19874820. Source: BHF-UCL

nucleus

Inferred from direct assay. Source: HPA

paraspeckles

Inferred from direct assay PubMed 19874820. Source: BHF-UCL

spliceosomal complex

Inferred from direct assay PubMed 9731529. Source: HGNC

   Molecular_functionRNA binding

Non-traceable author statement PubMed 9731529. Source: HGNC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20467437. Source: IntAct

protein domain specific binding

Inferred from physical interaction PubMed 11984006. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDC5LQ994597EBI-486809,EBI-374880
PLRG1O436605EBI-486809,EBI-1051504

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: P52272-1)

Also known as: M4;

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.
Isoform 2 (identifier: P52272-2)

Also known as: M1-M2;

The sequence of this isoform differs from the canonical sequence as follows:
     160-198: Missing.
Isoform 3 (identifier: P52272-3)

Also known as: M3;

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 730729Heterogeneous nuclear ribonucleoprotein M
PRO_0000081864

Regions

Domain71 – 14979RRM 1
Domain204 – 28178RRM 2
Repeat400 – 40561
Repeat407 – 41262
Repeat415 – 42063
Repeat426 – 43164
Repeat433 – 43865
Repeat440 – 44566
Repeat446 – 45167
Repeat453 – 45868
Repeat461 – 46669
Repeat468 – 473610
Repeat475 – 480611
Repeat482 – 487612
Repeat493 – 498613
Repeat500 – 505614
Repeat507 – 512615
Repeat514 – 519616
Repeat521 – 526617
Repeat528 – 533618
Repeat540 – 545619
Repeat547 – 552620
Repeat554 – 559621
Repeat562 – 567622
Repeat567 – 572623
Repeat575 – 580624
Repeat580 – 585625
Repeat588 – 593626
Repeat603 – 608627
Domain653 – 72977RRM 3
Region400 – 60820927 X 6 AA repeats of [GEVSTPAN]-[ILMV]-[DE]-[RH]-[MLVI]-[GAV]
Compositional bias390 – 3967Poly-Gly
Compositional bias612 – 6165Poly-Gly

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.11 Ref.17
Modified residue291Phosphoserine Ref.16
Modified residue1341N6-acetyllysine By similarity
Modified residue2771N6-acetyllysine Ref.13
Modified residue4321Phosphoserine Ref.16
Modified residue4521Phosphoserine Ref.16
Modified residue4681Phosphoserine Ref.10
Modified residue4811Phosphoserine Ref.16
Modified residue5281Phosphoserine Ref.16
Modified residue5751Phosphoserine Ref.9 Ref.14 Ref.16
Modified residue5881Phosphoserine Ref.9 Ref.14 Ref.16
Modified residue6181Phosphoserine Ref.8 Ref.9 Ref.12 Ref.14 Ref.16
Modified residue6331Phosphoserine Ref.10
Modified residue6371Phosphoserine Ref.10
Modified residue6721N6-acetyllysine By similarity
Modified residue6981N6-acetyllysine Ref.13
Modified residue7011Phosphoserine Ref.8 Ref.9 Ref.14 Ref.16

Natural variations

Alternative sequence160 – 19839Missing in isoform 2.
VSP_005845

Experimental info

Sequence conflict24 – 3411APGVPSGNGAP → GPACERQRGS in AAA36192. Ref.1
Sequence conflict341P → S in AAC16002. Ref.3
Sequence conflict511E → V in AAA36192. Ref.1
Sequence conflict1521H → C in AAC16002. Ref.3
Sequence conflict5271L → P Ref.1
Sequence conflict5271L → P Ref.3

Secondary structure

........................ 730
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (M4) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1A73DD35A3501861

FASTA73077,516
        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 

« Hide

Isoform 2 (M1-M2) [UniParc].

Checksum: 028646C136D3CBD1
Show »

FASTA69173,621
Isoform 3 (M3) (Sequence not available).

References

« Hide 'large scale' references
[1]"The human hnRNP M proteins: identification of a methionine/arginine-rich repeat motif in ribonucleoproteins."
Datar K.V., Dreyfuss G., Swanson M.S.
Nucleic Acids Res. 21:439-446(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
[2]"The human hnRNP-M proteins: structure and relation with early heat shock-induced splicing arrest and chromosome mapping."
Gattoni R., Mahe D., Mahl P., Fischer N., Mattei M.-G., Stevenin J., Fuchs J.-P.
Nucleic Acids Res. 24:2535-2542(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"A new human M4 protein with deletion."
Zhao Z., Huang X., Li N., Cao X.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[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] (ISOFORM 1).
Tissue: Brain, Lymph and Placenta.
[5]Bienvenut W.V.
Submitted (OCT-2004) to UniProtKB
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[6]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[7]"Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
Gocke C.B., Yu H., Kang J.
J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
[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 SER-618 AND SER-701, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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 SER-575; SER-588; SER-618 AND SER-701, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-633 AND SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-618, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-277 AND LYS-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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 SER-575; SER-588; SER-618 AND SER-701, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-432; SER-452; SER-481; SER-528; SER-575; SER-588; SER-618 AND SER-701, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Solution structure of the RNA binding domains of heterogeneous nuclear ribonucleoprotein M."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 196-296 AND 652-730.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L03532 mRNA. Translation: AAA36192.1.
L32611 mRNA. Translation: AAL31359.1.
AF061832 mRNA. Translation: AAC16002.1.
BC000138 mRNA. Translation: AAH00138.2.
BC008895 mRNA. Translation: AAH08895.2.
BC019580 mRNA. Translation: AAH19580.1.
CCDSCCDS12203.1. [P52272-1]
CCDS12204.1. [P52272-2]
PIRS35532.
RefSeqNP_005959.2. NM_005968.4. [P52272-1]
NP_112480.2. NM_031203.3. [P52272-2]
UniGeneHs.465808.
Hs.666214.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DGVNMR-A652-730[»]
2DH9NMR-A655-730[»]
2DO0NMR-A196-296[»]
2OT8X-ray3.10C/D41-70[»]
ProteinModelPortalP52272.
SMRP52272. Positions 74-147, 196-296, 652-730.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110751. 213 interactions.
DIPDIP-29336N.
IntActP52272. 39 interactions.
MINTMINT-4999200.
STRING9606.ENSP00000325376.

PTM databases

PhosphoSiteP52272.

Polymorphism databases

DMDM55977747.

2D gel databases

REPRODUCTION-2DPAGEIPI00383296.
UCD-2DPAGEP52272.

Proteomic databases

MaxQBP52272.
PaxDbP52272.
PRIDEP52272.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325495; ENSP00000325376; ENSG00000099783. [P52272-1]
ENST00000348943; ENSP00000325732; ENSG00000099783. [P52272-2]
GeneID4670.
KEGGhsa:4670.
UCSCuc010dwd.3. human. [P52272-2]
uc010dwe.3. human. [P52272-1]

Organism-specific databases

CTD4670.
GeneCardsGC19P008509.
H-InvDBHIX0137462.
HGNCHGNC:5046. HNRNPM.
HPACAB016113.
HPA024344.
MIM160994. gene.
neXtProtNX_P52272.
PharmGKBPA29370.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000231932.
HOVERGENHBG054880.
InParanoidP52272.
KOK12887.
OMAGSGMDRM.
OrthoDBEOG7ZSHSK.
PhylomeDBP52272.
TreeFamTF313406.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP52272.
BgeeP52272.
CleanExHS_HNRNPM.
GenevestigatorP52272.

Family and domain databases

Gene3D3.30.70.330. 3 hits.
InterProIPR024667. HnRNP_M.
IPR024666. HnRNP_M_PY-NLS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERPTHR23003:SF6. PTHR23003:SF6. 1 hit.
PfamPF11532. HnRNP_M. 1 hit.
PF00076. RRM_1. 3 hits.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPM. human.
EvolutionaryTraceP52272.
GenomeRNAi4670.
NextBio17994.
PROP52272.
SOURCESearch...

Entry information

Entry nameHNRPM_HUMAN
AccessionPrimary (citable) accession number: P52272
Secondary accession number(s): Q15584 expand/collapse secondary AC list , Q8WZ44, Q96H56, Q9BWL9, Q9Y492
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM