Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P52272

- HNRPM_HUMAN

UniProt

P52272 - HNRPM_HUMAN

Protein

Heterogeneous nuclear ribonucleoprotein M

Gene

HNRNPM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

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

    GO - Biological processi

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

    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. membrane Source: UniProtKB
    4. nuclear matrix Source: BHF-UCL
    5. nucleoplasm Source: BHF-UCL
    6. nucleus Source: HPA
    7. paraspeckles Source: BHF-UCL
    8. spliceosomal complex Source: HGNC

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29370.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 730729Heterogeneous nuclear ribonucleoprotein MPRO_0000081864Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei29 – 291Phosphoserine1 Publication
    Modified residuei134 – 1341N6-acetyllysineBy 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-acetyllysineBy 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
    EBNA-LPQ8AZK72EBI-486809,EBI-1185167From a different organism.
    PLRG1O436605EBI-486809,EBI-1051504

    Protein-protein interaction databases

    BioGridi110751. 210 interactions.
    DIPiDIP-29336N.
    IntActiP52272. 40 interactions.
    MINTiMINT-4999200.
    STRINGi9606.ENSP00000325376.

    Structurei

    Secondary structure

    1
    730
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52272.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini71 – 14979RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini204 – 28178RRM 2PROSITE-ProRule annotationAdd
    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 3PROSITE-ProRule annotationAdd
    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

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

    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):

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 3411APGVPSGNGAP → GPACERQRGS in AAA36192. (PubMed:8441656)CuratedAdd
    BLAST
    Sequence conflicti34 – 341P → S in AAC16002. 1 PublicationCurated
    Sequence conflicti51 – 511E → V in AAA36192. (PubMed:8441656)Curated
    Sequence conflicti152 – 1521H → C in AAC16002. 1 PublicationCurated
    Sequence conflicti527 – 5271L → P(PubMed:8441656)Curated
    Sequence conflicti527 – 5271L → P1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei160 – 19839Missing in isoform 2. 3 PublicationsVSP_005845Add
    BLAST

    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. 40 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

    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: October 1, 2014
    This is version 151 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