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)

P55795

- HNRH2_HUMAN

UniProt

P55795 - HNRH2_HUMAN

Protein

Heterogeneous nuclear ribonucleoprotein H2

Gene

HNRNPH2

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 158 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Binds poly(RG).

    GO - Molecular functioni

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

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA splicing, via spliceosome Source: Reactome
    3. RNA splicing Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein

    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 H2
    Short name:
    hnRNP H2
    Alternative name(s):
    FTP-3
    Heterogeneous nuclear ribonucleoprotein H'
    Short name:
    hnRNP H'
    Cleaved into the following chain:
    Gene namesi
    Name:HNRNPH2
    Synonyms:FTP3, HNRPH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:5042. HNRNPH2.

    Subcellular locationi

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: ProtInc
    4. ribonucleoprotein complex Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162391316.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 449449Heterogeneous nuclear ribonucleoprotein H2PRO_0000081859Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 449448Heterogeneous nuclear ribonucleoprotein H2, N-terminally processedPRO_0000423273Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine4 Publications
    Modified residuei2 – 21N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein H2, N-terminally processedBy similarity
    Modified residuei23 – 231PhosphoserineBy similarity
    Modified residuei63 – 631PhosphoserineBy similarity
    Modified residuei233 – 2331Dimethylated arginine; alternateBy similarity
    Modified residuei233 – 2331Omega-N-methylarginine; alternateBy similarity
    Modified residuei246 – 2461PhosphotyrosineBy similarity
    Modified residuei310 – 3101Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP55795.
    PaxDbiP55795.
    PeptideAtlasiP55795.
    PRIDEiP55795.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00026230.

    PTM databases

    PhosphoSiteiP55795.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously.

    Gene expression databases

    BgeeiP55795.
    CleanExiHS_HNRNPH2.
    GenevestigatoriP55795.

    Organism-specific databases

    HPAiCAB004436.
    HPA001359.
    HPA016884.

    Interactioni

    Subunit structurei

    Interacts with TXNL4/DIM1.1 Publication

    Protein-protein interaction databases

    BioGridi109429. 58 interactions.
    IntActiP55795. 52 interactions.
    MINTiMINT-2804293.
    STRINGi9606.ENSP00000361927.

    Structurei

    Secondary structure

    1
    449
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi112 – 1176
    Helixi124 – 1307
    Turni131 – 1333
    Beta strandi136 – 1427
    Beta strandi147 – 1493
    Beta strandi153 – 1619
    Helixi162 – 1698
    Turni170 – 1734
    Beta strandi176 – 1794
    Beta strandi182 – 1865
    Turni188 – 1903
    Beta strandi286 – 2883
    Beta strandi290 – 2956
    Helixi302 – 3076
    Beta strandi315 – 32511
    Beta strandi327 – 3348
    Beta strandi336 – 3383
    Helixi339 – 3457
    Beta strandi352 – 3554
    Beta strandi358 – 3625

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WEZNMR-A281-369[»]
    1WG5NMR-A103-193[»]
    ProteinModelPortaliP55795.
    SMRiP55795. Positions 4-193, 277-401.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55795.

    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

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG262593.
    HOGENOMiHOG000220896.
    HOVERGENiHBG055557.
    InParanoidiP55795.
    KOiK12898.
    OMAiPPRKLMT.
    OrthoDBiEOG7BS4BZ.
    PhylomeDBiP55795.
    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.

    P55795-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMLSTEGREG FVVKVRGLPW SCSADEVMRF FSDCKIQNGT SGIRFIYTRE    50
    GRPSGEAFVE LESEEEVKLA LKKDRETMGH RYVEVFKSNS VEMDWVLKHT 100
    GPNSPDTAND GFVRLRGLPF GCSKEEIVQF FSGLEIVPNG MTLPVDFQGR 150
    STGEAFVQFA SQEIAEKALK KHKERIGHRY IEIFKSSRAE VRTHYDPPRK 200
    LMAMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY GGYDDYGGYN 250
    DGYGFGSDRF GRDLNYCFSG MSDHRYGDGG SSFQSTTGHC VHMRGLPYRA 300
    TENDIYNFFS PLNPMRVHIE IGPDGRVTGE ADVEFATHED AVAAMAKDKA 350
    NMQHRYVELF LNSTAGTSGG AYDHSYVELF LNSTAGASGG AYGSQMMGGM 400
    GLSNQSSYGG PASQQLSGGY GGGYGGQSSM SGYDQVLQEN SSDYQSNLA 449
    Length:449
    Mass (Da):49,264
    Last modified:November 1, 1997 - v1
    Checksum:iC892523A638F07C7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01923 mRNA. No translation available.
    U78027 Genomic DNA. Translation: AAB64202.1.
    AL035422 Genomic DNA. Translation: CAB55879.2.
    CH471115 Genomic DNA. Translation: EAX02864.1.
    BC130343 mRNA. Translation: AAI30344.1.
    BC130345 mRNA. Translation: AAI30346.1.
    CCDSiCCDS14485.1.
    RefSeqiNP_001027565.1. NM_001032393.2.
    NP_062543.1. NM_019597.4.
    UniGeneiHs.432485.

    Genome annotation databases

    EnsembliENST00000316594; ENSP00000361927; ENSG00000126945.
    GeneIDi3188.
    KEGGihsa:3188.
    UCSCiuc004ehm.3. human.

    Polymorphism databases

    DMDMi2500576.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01923 mRNA. No translation available.
    U78027 Genomic DNA. Translation: AAB64202.1 .
    AL035422 Genomic DNA. Translation: CAB55879.2 .
    CH471115 Genomic DNA. Translation: EAX02864.1 .
    BC130343 mRNA. Translation: AAI30344.1 .
    BC130345 mRNA. Translation: AAI30346.1 .
    CCDSi CCDS14485.1.
    RefSeqi NP_001027565.1. NM_001032393.2.
    NP_062543.1. NM_019597.4.
    UniGenei Hs.432485.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WEZ NMR - A 281-369 [» ]
    1WG5 NMR - A 103-193 [» ]
    ProteinModelPortali P55795.
    SMRi P55795. Positions 4-193, 277-401.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109429. 58 interactions.
    IntActi P55795. 52 interactions.
    MINTi MINT-2804293.
    STRINGi 9606.ENSP00000361927.

    PTM databases

    PhosphoSitei P55795.

    Polymorphism databases

    DMDMi 2500576.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00026230.

    Proteomic databases

    MaxQBi P55795.
    PaxDbi P55795.
    PeptideAtlasi P55795.
    PRIDEi P55795.

    Protocols and materials databases

    DNASUi 3188.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316594 ; ENSP00000361927 ; ENSG00000126945 .
    GeneIDi 3188.
    KEGGi hsa:3188.
    UCSCi uc004ehm.3. human.

    Organism-specific databases

    CTDi 3188.
    GeneCardsi GC0XP100663.
    HGNCi HGNC:5042. HNRNPH2.
    HPAi CAB004436.
    HPA001359.
    HPA016884.
    MIMi 300610. gene.
    neXtProti NX_P55795.
    PharmGKBi PA162391316.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262593.
    HOGENOMi HOG000220896.
    HOVERGENi HBG055557.
    InParanoidi P55795.
    KOi K12898.
    OMAi PPRKLMT.
    OrthoDBi EOG7BS4BZ.
    PhylomeDBi P55795.
    TreeFami TF316157.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTracei P55795.
    GeneWikii HNRPH2.
    GenomeRNAii 3188.
    NextBioi 12674.
    PROi P55795.
    SOURCEi Search...

    Gene expression databases

    Bgeei P55795.
    CleanExi HS_HNRNPH2.
    Genevestigatori P55795.

    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. "Isolation of cosmid and cDNA clones in the region surrounding the BTK gene at Xq21.3-q22."
      Vorechovsky I., Vetrie D., Holland J., Bentley D.R., Thomas K., Zhou J.N., Notarangelo L.D., Plebani A., Fontan G., Ochs H.D.
      Genomics 21:517-524(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Large-scale comparative sequence analysis of the human and murine Bruton's tyrosine kinase loci reveals conserved regulatory domains."
      Oeltjen J.C., Malley T.M., Muzny D.M., Miller W., Gibbs R.A., Belmont J.W.
      Genome Res. 7:315-329(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
    6. "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: Brain.
    7. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-8; 88-114; 151-167; 276-294 AND 300-326, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    8. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 17-29; 36-44; 88-98; 151-167; 263-275; 300-316 AND 327-347, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    9. "Evidence that Dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for Dim1 interactions with hnRNP F and Npw38/PQBP-1."
      Zhang Y.-Z., Lindblom T., Chang A., Sudol M., Sluder A.E., Golemis E.A.
      Gene 257:33-43(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TXNL4.
    10. "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-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Solution structure of RRM domains in heterogeneous nuclear ribonucleoprotein H."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 103-193 AND 280-369.

    Entry informationi

    Entry nameiHNRH2_HUMAN
    AccessioniPrimary (citable) accession number: P55795
    Secondary accession number(s): A1L400, Q9HHA7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 158 of the entry and version 1 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 X
      Human chromosome X: 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