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P52272

- HNRPM_HUMAN

UniProt

P52272 - HNRPM_HUMAN

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Protein
Heterogeneous nuclear ribonucleoprotein M
Gene
HNRNPM, HNRPM, NAGR1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

GO - Molecular functioni

  1. RNA binding Source: HGNC
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. protein domain specific binding Source: UniProtKB

GO - Biological processi

  1. RNA splicing Source: Reactome
  2. alternative mRNA splicing, via spliceosome Source: BHF-UCL
  3. gene expression Source: Reactome
  4. mRNA splicing, via spliceosome Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein M
Short name:
hnRNP M
Gene namesi
Name:HNRNPM
Synonyms:HNRPM, NAGR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:5046. HNRNPM.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. integral component of plasma membrane Source: ProtInc
  3. nuclear matrix Source: BHF-UCL
  4. nucleoplasm Source: BHF-UCL
  5. nucleus Source: HPA
  6. paraspeckles Source: BHF-UCL
  7. spliceosomal complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29370.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 730729Heterogeneous nuclear ribonucleoprotein M
PRO_0000081864Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei29 – 291Phosphoserine1 Publication
Modified residuei134 – 1341N6-acetyllysine By similarity
Modified residuei277 – 2771N6-acetyllysine1 Publication
Modified residuei432 – 4321Phosphoserine1 Publication
Modified residuei452 – 4521Phosphoserine1 Publication
Modified residuei468 – 4681Phosphoserine1 Publication
Modified residuei481 – 4811Phosphoserine1 Publication
Modified residuei528 – 5281Phosphoserine1 Publication
Modified residuei575 – 5751Phosphoserine3 Publications
Modified residuei588 – 5881Phosphoserine3 Publications
Modified residuei618 – 6181Phosphoserine5 Publications
Modified residuei633 – 6331Phosphoserine1 Publication
Modified residuei637 – 6371Phosphoserine1 Publication
Modified residuei672 – 6721N6-acetyllysine By similarity
Modified residuei698 – 6981N6-acetyllysine1 Publication
Modified residuei701 – 7011Phosphoserine4 Publications

Post-translational modificationi

Sumoylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP52272.
PaxDbiP52272.
PRIDEiP52272.

2D gel databases

REPRODUCTION-2DPAGEIPI00383296.
UCD-2DPAGEP52272.

PTM databases

PhosphoSiteiP52272.

Expressioni

Gene expression databases

ArrayExpressiP52272.
BgeeiP52272.
CleanExiHS_HNRNPM.
GenevestigatoriP52272.

Organism-specific databases

HPAiCAB016113.
HPA024344.

Interactioni

Subunit structurei

Identified in the spliceosome C complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC5LQ994597EBI-486809,EBI-374880
PLRG1O436605EBI-486809,EBI-1051504

Protein-protein interaction databases

BioGridi110751. 210 interactions.
DIPiDIP-29336N.
IntActiP52272. 39 interactions.
MINTiMINT-4999200.
STRINGi9606.ENSP00000325376.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi206 – 2105
Helixi217 – 2248
Turni225 – 2273
Beta strandi230 – 2378
Beta strandi242 – 25312
Helixi254 – 26411
Beta strandi275 – 2784
Beta strandi654 – 6574
Helixi666 – 6749
Beta strandi679 – 68911
Beta strandi691 – 70111
Helixi702 – 71211
Beta strandi725 – 7273

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DGVNMR-A652-730[»]
2DH9NMR-A655-730[»]
2DO0NMR-A196-296[»]
2OT8X-ray3.10C/D41-70[»]
ProteinModelPortaliP52272.
SMRiP52272. Positions 74-147, 196-296, 652-730.

Miscellaneous databases

EvolutionaryTraceiP52272.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini71 – 14979RRM 1
Add
BLAST
Domaini204 – 28178RRM 2
Add
BLAST
Repeati400 – 40561
Repeati407 – 41262
Repeati415 – 42063
Repeati426 – 43164
Repeati433 – 43865
Repeati440 – 44566
Repeati446 – 45167
Repeati453 – 45868
Repeati461 – 46669
Repeati468 – 473610
Repeati475 – 480611
Repeati482 – 487612
Repeati493 – 498613
Repeati500 – 505614
Repeati507 – 512615
Repeati514 – 519616
Repeati521 – 526617
Repeati528 – 533618
Repeati540 – 545619
Repeati547 – 552620
Repeati554 – 559621
Repeati562 – 567622
Repeati567 – 572623
Repeati575 – 580624
Repeati580 – 585625
Repeati588 – 593626
Repeati603 – 608627
Domaini653 – 72977RRM 3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni400 – 60820927 X 6 AA repeats of [GEVSTPAN]-[ILMV]-[DE]-[RH]-[MLVI]-[GAV]
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi390 – 3967Poly-Gly
Compositional biasi612 – 6165Poly-Gly

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
HOGENOMiHOG000231932.
HOVERGENiHBG054880.
InParanoidiP52272.
KOiK12887.
OMAiGSGMDRM.
OrthoDBiEOG7ZSHSK.
PhylomeDBiP52272.
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. 1 hit.
PfamiPF11532. HnRNP_M. 1 hit.
PF00076. RRM_1. 3 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: P52272-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAAGVEAAAE VAATEIKMEE ESGAPGVPSG NGAPGPKGEG ERPAQNEKRK    50
EKNIKRGGNR FEPYANPTKR YRAFITNIPF DVKWQSLKDL VKEKVGEVTY 100
VELLMDAEGK SRGCAVVEFK MEESMKKAAE VLNKHSLSGR PLKVKEDPDG 150
EHARRAMQKV MATTGGMGMG PGGPGMITIP PSILNNPNIP NEIIHALQAG 200
RLGSTVFVAN LDYKVGWKKL KEVFSMAGVV VRADILEDKD GKSRGIGTVT 250
FEQSIEAVQA ISMFNGQLLF DRPMHVKMDE RALPKGDFFP PERPQQLPHG 300
LGGIGMGLGP GGQPIDANHL NKGIGMGNIG PAGMGMEGIG FGINKMGGME 350
GPFGGGMENM GRFGSGMNMG RINEILSNAL KRGEIIAKQG GGGGGGSVPG 400
IERMGPGIDR LGGAGMERMG AGLGHGMDRV GSEIERMGLV MDRMGSVERM 450
GSGIERMGPL GLDHMASSIE RMGQTMERIG SGVERMGAGM GFGLERMAAP 500
IDRVGQTIER MGSGVERMGP AIERMGLSME RMVPAGMGAG LERMGPVMDR 550
MATGLERMGA NNLERMGLER MGANSLERMG LERMGANSLE RMGPAMGPAL 600
GAGIERMGLA MGGGGGASFD RAIEMERGNF GGSFAGSFGG AGGHAPGVAR 650
KACQIFVRNL PFDFTWKMLK DKFNECGHVL YADIKMENGK SKGCGVVKFE 700
SPEVAERACR MMNGMKLSGR EIDVRIDRNA 730
Length:730
Mass (Da):77,516
Last modified:January 23, 2007 - v3
Checksum:i1A73DD35A3501861
GO
Isoform 2 (identifier: P52272-2) [UniParc]FASTAAdd to Basket

Also known as: M1-M2

The sequence of this isoform differs from the canonical sequence as follows:
     160-198: Missing.

Show »
Length:691
Mass (Da):73,621
Checksum:i028646C136D3CBD1
GO
Isoform 3 (identifier: P52272-3)

Also known as: M3

Sequence is not available
Length:
Mass (Da):

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei160 – 19839Missing in isoform 2.
VSP_005845Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 3411APGVPSGNGAP → GPACERQRGS in AAA36192. 1 Publication
Add
BLAST
Sequence conflicti34 – 341P → S in AAC16002. 1 Publication
Sequence conflicti51 – 511E → V in AAA36192. 1 Publication
Sequence conflicti152 – 1521H → C in AAC16002. 1 Publication
Sequence conflicti527 – 5271L → P1 Publication
Sequence conflicti527 – 5271L → P1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS12203.1. [P52272-1]
CCDS12204.1. [P52272-2]
PIRiS35532.
RefSeqiNP_005959.2. NM_005968.4. [P52272-1]
NP_112480.2. NM_031203.3. [P52272-2]
UniGeneiHs.465808.
Hs.666214.

Genome annotation databases

EnsembliENST00000325495; ENSP00000325376; ENSG00000099783. [P52272-1]
ENST00000348943; ENSP00000325732; ENSG00000099783. [P52272-2]
GeneIDi4670.
KEGGihsa:4670.
UCSCiuc010dwd.3. human. [P52272-2]
uc010dwe.3. human. [P52272-1]

Polymorphism databases

DMDMi55977747.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS12203.1. [P52272-1 ]
CCDS12204.1. [P52272-2 ]
PIRi S35532.
RefSeqi NP_005959.2. NM_005968.4. [P52272-1 ]
NP_112480.2. NM_031203.3. [P52272-2 ]
UniGenei Hs.465808.
Hs.666214.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DGV NMR - A 652-730 [» ]
2DH9 NMR - A 655-730 [» ]
2DO0 NMR - A 196-296 [» ]
2OT8 X-ray 3.10 C/D 41-70 [» ]
ProteinModelPortali P52272.
SMRi P52272. Positions 74-147, 196-296, 652-730.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110751. 210 interactions.
DIPi DIP-29336N.
IntActi P52272. 39 interactions.
MINTi MINT-4999200.
STRINGi 9606.ENSP00000325376.

PTM databases

PhosphoSitei P52272.

Polymorphism databases

DMDMi 55977747.

2D gel databases

REPRODUCTION-2DPAGE IPI00383296.
UCD-2DPAGE P52272.

Proteomic databases

MaxQBi P52272.
PaxDbi P52272.
PRIDEi P52272.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000325495 ; ENSP00000325376 ; ENSG00000099783 . [P52272-1 ]
ENST00000348943 ; ENSP00000325732 ; ENSG00000099783 . [P52272-2 ]
GeneIDi 4670.
KEGGi hsa:4670.
UCSCi uc010dwd.3. human. [P52272-2 ]
uc010dwe.3. human. [P52272-1 ]

Organism-specific databases

CTDi 4670.
GeneCardsi GC19P008509.
H-InvDB HIX0137462.
HGNCi HGNC:5046. HNRNPM.
HPAi CAB016113.
HPA024344.
MIMi 160994. gene.
neXtProti NX_P52272.
PharmGKBi PA29370.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
HOGENOMi HOG000231932.
HOVERGENi HBG054880.
InParanoidi P52272.
KOi K12887.
OMAi GSGMDRM.
OrthoDBi EOG7ZSHSK.
PhylomeDBi P52272.
TreeFami TF313406.

Enzyme and pathway databases

Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi HNRNPM. human.
EvolutionaryTracei P52272.
GenomeRNAii 4670.
NextBioi 17994.
PROi P52272.
SOURCEi Search...

Gene expression databases

ArrayExpressi P52272.
Bgeei P52272.
CleanExi HS_HNRNPM.
Genevestigatori P52272.

Family and domain databases

Gene3Di 3.30.70.330. 3 hits.
InterProi IPR024667. HnRNP_M.
IPR024666. HnRNP_M_PY-NLS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
PANTHERi PTHR23003:SF6. PTHR23003:SF6. 1 hit.
Pfami PF11532. HnRNP_M. 1 hit.
PF00076. RRM_1. 3 hits.
[Graphical view ]
SMARTi SM00360. RRM. 3 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiHNRPM_HUMAN
AccessioniPrimary (citable) accession number: P52272
Secondary accession number(s): Q15584
, Q8WZ44, Q96H56, Q9BWL9, Q9Y492
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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