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P31943

- HNRH1_HUMAN

UniProt

P31943 - HNRH1_HUMAN

Protein

Heterogeneous nuclear ribonucleoprotein H

Gene

HNRNPH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA alternative splicing regulation. Inhibits, together with CUGBP1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Binds to the IR RNA. Binds poly(RG).2 Publications

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. poly(U) RNA binding Source: ProtInc
    4. protein binding Source: UniProtKB
    5. RNA binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA splicing, via spliceosome Source: UniProtKB
    3. regulation of RNA splicing Source: UniProtKB
    4. RNA processing Source: ProtInc
    5. 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 H
    Short name:
    hnRNP H
    Cleaved into the following chain:
    Gene namesi
    Name:HNRNPH1
    Synonyms:HNRPH, HNRPH1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:5041. HNRNPH1.

    Subcellular locationi

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. membrane Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti99861. Precursor T-cell acute lymphoblastic leukemia.
    PharmGKBiPA162391284.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 449449Heterogeneous nuclear ribonucleoprotein HPRO_0000367119Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate3 Publications
    Chaini2 – 449448Heterogeneous nuclear ribonucleoprotein H, N-terminally processedPRO_0000081857Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein H; alternate3 Publications
    Modified residuei2 – 21N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein H, N-terminally processed4 Publications
    Modified residuei23 – 231Phosphoserine1 Publication
    Modified residuei63 – 631Phosphoserine6 Publications
    Modified residuei233 – 2331Dimethylated arginine; alternate1 Publication
    Modified residuei233 – 2331Omega-N-methylarginine; alternate1 Publication
    Modified residuei246 – 2461Phosphotyrosine1 Publication
    Modified residuei310 – 3101PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP31943.
    PaxDbiP31943.
    PRIDEiP31943.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00013881.
    P31943.

    PTM databases

    PhosphoSiteiP31943.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously.

    Inductioni

    Up-regulated in myotonic dystrophy pathophysiology (DM).1 Publication

    Gene expression databases

    ArrayExpressiP31943.
    BgeeiP31943.
    CleanExiHS_HNRNPH1.
    GenevestigatoriP31943.

    Organism-specific databases

    HPAiHPA001359.
    HPA016884.

    Interactioni

    Subunit structurei

    Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and HNRNPH1. Identified in the spliceosome C complex. Interacts with IGF2BP1. Interacts with CUGBP1; the interaction is RNA-dependent. Interacts with MBNL1; the interaction in RNA-independent.4 Publications

    Protein-protein interaction databases

    BioGridi109428. 137 interactions.
    IntActiP31943. 55 interactions.
    MINTiMINT-1160934.
    STRINGi9606.ENSP00000349168.

    Structurei

    Secondary structure

    1
    449
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 179
    Helixi24 – 307
    Turni31 – 333
    Helixi39 – 413
    Beta strandi42 – 476
    Beta strandi51 – 6212
    Helixi64 – 718
    Turni72 – 754
    Beta strandi84 – 885
    Helixi90 – 989

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LXUNMR-A7-111[»]
    ProteinModelPortaliP31943.
    SMRiP31943. Positions 7-193, 283-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 9080RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini111 – 18878RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati234 – 249161-1Add
    BLAST
    Domaini289 – 36476RRM 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati354 – 372192-1Add
    BLAST
    Repeati374 – 392192-2Add
    BLAST
    Repeati418 – 433161-2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni234 – 4332002 X 16 AA Gly-rich approximate repeatsAdd
    BLAST
    Regioni354 – 392392 X 19 AA perfect repeatsAdd
    BLAST

    Domaini

    Each quasi-RRM repeat bound poly(RG), while only the N-terminal QRRM bound poly(RC) and poly(RU). None of the repeats bound detectable amounts of poly(RA).

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG262593.
    HOGENOMiHOG000220896.
    HOVERGENiHBG055557.
    KOiK12898.
    OrthoDBiEOG7BS4BZ.
    PhylomeDBiP31943.
    TreeFamiTF316157.

    Family and domain databases

    Gene3Di3.30.70.330. 3 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR012996. Znf_CHHC.
    [Graphical view]
    PfamiPF08080. zf-RNPHF. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 3 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P31943-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMLGTEGGEG FVVKVRGLPW SCSADEVQRF FSDCKIQNGA QGIRFIYTRE    50
    GRPSGEAFVE LESEDEVKLA LKKDRETMGH RYVEVFKSNN VEMDWVLKHT 100
    GPNSPDTAND GFVRLRGLPF GCSKEEIVQF FSGLEIVPNG ITLPVDFQGR 150
    STGEAFVQFA SQEIAEKALK KHKERIGHRY IEIFKSSRAE VRTHYDPPRK 200
    LMAMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY GGYDDYNGYN 250
    DGYGFGSDRF GRDLNYCFSG MSDHRYGDGG STFQSTTGHC VHMRGLPYRA 300
    TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHED AVAAMSKDKA 350
    NMQHRYVELF LNSTAGASGG AYEHRYVELF LNSTAGASGG AYGSQMMGGM 400
    GLSNQSSYGG PASQQLSGGY GGGYGGQSSM SGYDQVLQEN SSDFQSNIA 449
    Length:449
    Mass (Da):49,229
    Last modified:January 23, 2007 - v4
    Checksum:i4ECF7A075C2526FF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1881R → G in CAG33059. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22009 mRNA. Translation: AAA91346.1.
    CR456778 mRNA. Translation: CAG33059.1.
    AK124530 mRNA. Translation: BAG54048.1.
    CH471165 Genomic DNA. Translation: EAW53807.1.
    CH471165 Genomic DNA. Translation: EAW53808.1.
    BC001348 mRNA. Translation: AAH01348.1.
    CCDSiCCDS4446.1.
    PIRiI39358.
    RefSeqiNP_001244222.1. NM_001257293.1.
    NP_005511.1. NM_005520.2.
    UniGeneiHs.604001.

    Genome annotation databases

    EnsembliENST00000356731; ENSP00000349168; ENSG00000169045.
    ENST00000393432; ENSP00000377082; ENSG00000169045.
    ENST00000442819; ENSP00000397797; ENSG00000169045.
    GeneIDi3187.
    KEGGihsa:3187.
    UCSCiuc003mke.4. human.

    Polymorphism databases

    DMDMi1710632.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22009 mRNA. Translation: AAA91346.1 .
    CR456778 mRNA. Translation: CAG33059.1 .
    AK124530 mRNA. Translation: BAG54048.1 .
    CH471165 Genomic DNA. Translation: EAW53807.1 .
    CH471165 Genomic DNA. Translation: EAW53808.1 .
    BC001348 mRNA. Translation: AAH01348.1 .
    CCDSi CCDS4446.1.
    PIRi I39358.
    RefSeqi NP_001244222.1. NM_001257293.1.
    NP_005511.1. NM_005520.2.
    UniGenei Hs.604001.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LXU NMR - A 7-111 [» ]
    ProteinModelPortali P31943.
    SMRi P31943. Positions 7-193, 283-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109428. 137 interactions.
    IntActi P31943. 55 interactions.
    MINTi MINT-1160934.
    STRINGi 9606.ENSP00000349168.

    PTM databases

    PhosphoSitei P31943.

    Polymorphism databases

    DMDMi 1710632.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00013881.
    P31943.

    Proteomic databases

    MaxQBi P31943.
    PaxDbi P31943.
    PRIDEi P31943.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356731 ; ENSP00000349168 ; ENSG00000169045 .
    ENST00000393432 ; ENSP00000377082 ; ENSG00000169045 .
    ENST00000442819 ; ENSP00000397797 ; ENSG00000169045 .
    GeneIDi 3187.
    KEGGi hsa:3187.
    UCSCi uc003mke.4. human.

    Organism-specific databases

    CTDi 3187.
    GeneCardsi GC05M179043.
    HGNCi HGNC:5041. HNRNPH1.
    HPAi HPA001359.
    HPA016884.
    MIMi 601035. gene.
    neXtProti NX_P31943.
    Orphaneti 99861. Precursor T-cell acute lymphoblastic leukemia.
    PharmGKBi PA162391284.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262593.
    HOGENOMi HOG000220896.
    HOVERGENi HBG055557.
    KOi K12898.
    OrthoDBi EOG7BS4BZ.
    PhylomeDBi P31943.
    TreeFami TF316157.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi HNRNPH1. human.
    GeneWikii HNRPH1.
    GenomeRNAii 3187.
    NextBioi 12670.
    PROi P31943.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31943.
    Bgeei P31943.
    CleanExi HS_HNRNPH1.
    Genevestigatori P31943.

    Family and domain databases

    Gene3Di 3.30.70.330. 3 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR012996. Znf_CHHC.
    [Graphical view ]
    Pfami PF08080. zf-RNPHF. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 3 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Heterogeneous nuclear ribonucleoproteins H, H', and F are members of a ubiquitously expressed subfamily of related but distinct proteins encoded by genes mapping to different chromosomes."
      Honore B., Rasmussen H.H., Vorum H., Dejgaard K., Liu X., Gromov P., Madsen P., Gesser B., Tommerup N., Celis J.E.
      J. Biol. Chem. 270:28780-28789(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 180-184; 193-197 AND 200-230.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cerebellum.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Muscle.
    6. Cited for: PROTEIN SEQUENCE OF 1-14; 17-44; 50-68; 82-114; 151-167; 180-185; 233-259; 276-294; 300-347 AND 356-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND MET-2, METHYLATION AT ARG-233, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma, Cervix carcinoma, Hepatoma, Lung carcinoma, Mammary carcinoma and Ovarian carcinoma.
    7. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-14; 17-29; 88-114; 151-167; 263-275; 300-347; 344-375; 377-386; 418-432; 473-483 AND 542-553, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    8. "The hnRNP F protein: unique primary structure, nucleic acid-binding properties, and subcellular localization."
      Matunis M.J., Xing J., Dreyfuss G.
      Nucleic Acids Res. 22:1059-1067(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 127-135 AND 153-163.
    9. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 200-230.
      Tissue: Keratinocyte.
    10. "Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein."
      Markovtsov V., Nikolic J.M., Goldman J.A., Turck C.W., Chou M.-Y., Black D.L.
      Mol. Cell. Biol. 20:7463-7479(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PTBP1; PTBP2 AND FUBP2.
    11. "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.
    12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Interaction of muscleblind, CUG-BP1 and hnRNP H proteins in DM1-associated aberrant IR splicing."
      Paul S., Dansithong W., Kim D., Rossi J., Webster N.J., Comai L., Reddy S.
      EMBO J. 25:4271-4283(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CUGBP1 AND MBNL1, RNA-BINDING, INDUCTION.
    15. Cited for: INTERACTION WITH IGF2BP1.
    16. "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-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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 MET-1 AND MET-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-23 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "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-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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 MET-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHNRH1_HUMAN
    AccessioniPrimary (citable) accession number: P31943
    Secondary accession number(s): B3KW86, D3DWQ2, Q6IBM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 164 of the entry and version 4 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 5
      Human chromosome 5: 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