P52272 (HNRPM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heterogeneous nuclear ribonucleoprotein M
Short name=hnRNP M

Gene names

Name:	HNRNPM
Synonyms:	HNRPM, NAGR1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	730 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Nucleus › nucleolus Ref.5.
Post-translational modification	Sumoylated. Ref.7
Sequence similarities	Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	alternative mRNA splicing, via spliceosome Inferred from mutant phenotype PubMed 19874820. Source: BHF-UCL
Cellular_component	catalytic step 2 spliceosome Inferred from direct assay Ref.6. Source: UniProtKB integral to plasma membrane Traceable author statement PubMed 8088785. Source: ProtInc nuclear matrix Inferred from direct assay PubMed 19874820. Source: BHF-UCL paraspeckles Inferred from direct assay PubMed 19874820. Source: BHF-UCL
Molecular_function	RNA binding Non-traceable author statement PubMed 9731529. Source: HGNC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 730

729

Heterogeneous nuclear ribonucleoprotein M

PRO_0000081864

Regions

Domain

71 – 149

79

RRM 1

Domain

204 – 281

78

RRM 2

Repeat

400 – 405

6

1

Repeat

407 – 412

6

2

Repeat

415 – 420

6

3

Repeat

426 – 431

6

4

Repeat

433 – 438

6

5

Repeat

440 – 445

6

6

Repeat

446 – 451

6

7

Repeat

453 – 458

6

8

Repeat

461 – 466

6

9

Repeat

468 – 473

6

10

Repeat

475 – 480

6

11

Repeat

482 – 487

6

12

Repeat

493 – 498

6

13

Repeat

500 – 505

6

14

Repeat

507 – 512

6

15

Repeat

514 – 519

6

16

Repeat

521 – 526

6

17

Repeat

528 – 533

6

18

Repeat

540 – 545

6

19

Repeat

547 – 552

6

20

Repeat

554 – 559

6

21

Repeat

562 – 567

6

22

Repeat

567 – 572

6

23

Repeat

575 – 580

6

24

Repeat

580 – 585

6

25

Repeat

588 – 593

6

26

Repeat

603 – 608

6

27

Domain

653 – 729

77

RRM 3

Region

400 – 608

209

27 X 6 AA repeats of [GEVSTPAN]-[ILMV]-[DE]-[RH]-[MLVI]-[GAV]

Compositional bias

390 – 396

7

Poly-Gly

Compositional bias

612 – 616

5

Poly-Gly

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.5

Modified residue

29

1

Phosphoserine Ref.15

Modified residue

277

1

N6-acetyllysine Ref.12

Modified residue

432

1

Phosphoserine Ref.15

Modified residue

446

1

Phosphoserine Ref.15

Modified residue

452

1

Phosphoserine Ref.15

Modified residue

468

1

Phosphoserine Ref.10

Modified residue

481

1

Phosphoserine Ref.15

Modified residue

528

1

Phosphoserine Ref.15

Modified residue

575

1

Phosphoserine Ref.9 Ref.13 Ref.15

Modified residue

588

1

Phosphoserine Ref.9 Ref.13 Ref.15

Modified residue

618

1

Phosphoserine Ref.8 Ref.9 Ref.11 Ref.13 Ref.15

Modified residue

633

1

Phosphoserine Ref.10

Modified residue

637

1

Phosphoserine Ref.10

Modified residue

698

1

N6-acetyllysine Ref.12

Modified residue

701

1

Phosphoserine Ref.8 Ref.9 Ref.13 Ref.15

Natural variations

Alternative sequence

160 – 198

39

Missing in isoform 2.

VSP_005845

Experimental info

Sequence conflict

24 – 34

11

APGVPSGNGAP → GPACERQRGS in AAA36192. Ref.1

Sequence conflict

34

1

P → S in AAC16002. Ref.3

Sequence conflict

51

1

E → V in AAA36192. Ref.1

Sequence conflict

152

1

H → C in AAC16002. Ref.3

Sequence conflict

527

1

L → P Ref.1

Sequence conflict

527

1

L → P Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

730

Helix Strand Turn

Details...

Beta strand

206 – 210

5

Helix

217 – 224

8

Turn

225 – 227

3

Beta strand

230 – 237

8

Beta strand

242 – 253

12

Helix

254 – 264

11

Beta strand

275 – 278

4

Beta strand

654 – 657

4

Helix

666 – 674

9

Beta strand

679 – 689

11

Beta strand

691 – 701

11

Helix

702 – 712

11

Beta strand

725 – 727

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (M4) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1A73DD35A3501861	FASTA	730	77,516
	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
	Isoform 2 (M1-M2) [UniParc]. Checksum: 028646C136D3CBD1	FASTA	691	73,621
	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 EHARRAMQKA GRLGSTVFVA NLDYKVGWKK 190 200 210 220 230 240 LKEVFSMAGV VVRADILEDK DGKSRGIGTV TFEQSIEAVQ AISMFNGQLL FDRPMHVKMD 250 260 270 280 290 300 ERALPKGDFF PPERPQQLPH GLGGIGMGLG PGGQPIDANH LNKGIGMGNI GPAGMGMEGI 310 320 330 340 350 360 GFGINKMGGM EGPFGGGMEN MGRFGSGMNM GRINEILSNA LKRGEIIAKQ GGGGGGGSVP 370 380 390 400 410 420 GIERMGPGID RLGGAGMERM GAGLGHGMDR VGSEIERMGL VMDRMGSVER MGSGIERMGP 430 440 450 460 470 480 LGLDHMASSI ERMGQTMERI GSGVERMGAG MGFGLERMAA PIDRVGQTIE RMGSGVERMG 490 500 510 520 530 540 PAIERMGLSM ERMVPAGMGA GLERMGPVMD RMATGLERMG ANNLERMGLE RMGANSLERM 550 560 570 580 590 600 GLERMGANSL ERMGPAMGPA LGAGIERMGL AMGGGGGASF DRAIEMERGN FGGSFAGSFG 610 620 630 640 650 660 GAGGHAPGVA RKACQIFVRN LPFDFTWKML KDKFNECGHV LYADIKMENG KSKGCGVVKF 670 680 690 ESPEVAERAC RMMNGMKLSG REIDVRIDRN A
	Isoform 3 (M3) (Sequence not available).		–	–

References

	« Hide 'large scale' referencesShow '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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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, MASS SPECTROMETRY.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"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-446; SER-452; SER-481; SER-528; SER-575; SER-588; SER-618 AND SER-701, MASS SPECTROMETRY.
[16]	"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.

IPI

IPI00171903.
IPI00383296.

PIR

S35532.

RefSeq

NP_005959.2. NM_005968.4.
NP_112480.2. NM_031203.3.

UniGene

Hs.465808.
Hs.666214.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DGV	NMR	-	A	652-729	[»]
2DH9	NMR	-	A	655-729	[»]
2DO0	NMR	-	A	196-295	[»]
2OT8	X-ray	3.10	C/D	41-70	[»]

ProteinModelPortal

P52272.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29336N.

IntAct

P52272. 22 interactions.

MINT

MINT-4999200.

STRING

9606.ENSP00000325376.

PTM databases

PhosphoSite

P52272.

Polymorphism databases

DMDM

55977747.

2D gel databases

REPRODUCTION-2DPAGE

IPI00383296.

UCD-2DPAGE

P52272.

Proteomic databases

PaxDb

P52272.

PRIDE

P52272.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000325495; ENSP00000325376; ENSG00000099783.
ENST00000348943; ENSP00000325732; ENSG00000099783.

GeneID

4670.

KEGG

hsa:4670.

UCSC

uc010dwd.3. human.
uc010dwe.3. human.

Organism-specific databases

CTD

4670.

GeneCards

GC19P008509.

H-InvDB

HIX0137462.

HGNC

HGNC:5046. HNRNPM.

HPA

CAB016113.
HPA024344.

MIM

160994. gene.

neXtProt

NX_P52272.

PharmGKB

PA29370.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0724.

HOGENOM

HOG000231932.

HOVERGEN

HBG054880.

InParanoid

P52272.

KO

K12887.

OMA

PGIERMA.

OrthoDB

EOG4RBQJN.

PhylomeDB

P52272.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P52272.

Bgee

P52272.

CleanEx

HS_HNRNPM.

Genevestigator

P52272.

GermOnline

ENSG00000099783. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 3 hits.

InterPro

IPR024667. HnRNP_M.
IPR024666. HnRNP_M_PY-NLS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

PANTHER

PTHR23003:SF6. PTHR23003:SF6. 1 hit.

Pfam

PF11532. HnRNP_M. 1 hit.
PF00076. RRM_1. 3 hits.
[Graphical view]

SMART

SM00360. RRM. 3 hits.
[Graphical view]

PROSITE

PS50102. RRM. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HNRNPM. human.

EvolutionaryTrace

P52272.

GenomeRNAi

4670.

NextBio

17994.

SOURCE

Search...

Entry information

Entry name

HNRPM_HUMAN

Accession

Primary (citable) accession number: P52272
Secondary accession number(s): Q15584 , Q8WZ44, Q96H56, Q9BWL9, Q9Y492

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 137 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.