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Q9BUJ2

- HNRL1_HUMAN

UniProt

Q9BUJ2 - HNRL1_HUMAN

Protein

Heterogeneous nuclear ribonucleoprotein U-like protein 1

Gene

HNRNPUL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (21 Mar 2006)
      Previous versions | rss
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    Functioni

    Acts as a basic transcriptional regulator. Represses basic transcription driven by several virus and cellular promoters. When associated with BRD7, activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation. Plays also a role in mRNA processing and transport. Binds avidly to poly(G) and poly(C) RNA homopolymers in vitro.2 Publications

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. RNA binding Source: ProtInc

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA splicing, via spliceosome Source: Reactome
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. response to virus Source: ProtInc
    5. RNA processing Source: ProtInc
    6. RNA splicing Source: Reactome
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor, Ribonucleoprotein

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heterogeneous nuclear ribonucleoprotein U-like protein 1
    Alternative name(s):
    Adenovirus early region 1B-associated protein 5
    E1B-55 kDa-associated protein 5
    Short name:
    E1B-AP5
    Gene namesi
    Name:HNRNPUL1
    Synonyms:E1BAP5, HNRPUL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:17011. HNRNPUL1.

    Subcellular locationi

    Nucleus 3 Publications

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: UniProtKB
    3. ribonucleoprotein complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162391519.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 856856Heterogeneous nuclear ribonucleoprotein U-like protein 1PRO_0000227555Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei194 – 1941Phosphoserine5 Publications
    Modified residuei512 – 5121Phosphoserine3 Publications
    Modified residuei718 – 7181Phosphoserine1 Publication

    Post-translational modificationi

    Methylated.2 Publications

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BUJ2.
    PaxDbiQ9BUJ2.
    PRIDEiQ9BUJ2.

    PTM databases

    PhosphoSiteiQ9BUJ2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BUJ2.
    BgeeiQ9BUJ2.
    CleanExiHS_HNRNPUL1.
    GenevestigatoriQ9BUJ2.

    Organism-specific databases

    HPAiCAB046477.
    HPA046290.
    HPA049475.

    Interactioni

    Subunit structurei

    Interacts with the adenovirus type 5 (Ad5) E1B-55 kDa, BRD7, PRMT2, TP53 and NXF1. Associates with histones and BRD7.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRD7Q9NPI15EBI-1018153,EBI-711221

    Protein-protein interaction databases

    BioGridi116281. 93 interactions.
    DIPiDIP-39419N.
    IntActiQ9BUJ2. 49 interactions.
    MINTiMINT-121512.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BUJ2.
    SMRiQ9BUJ2. Positions 1-37, 243-384.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 3735SAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini191 – 388198B30.2/SPRYPROSITE-ProRule annotationAdd
    BLAST
    Repeati612 – 61431-1
    Repeati620 – 62231-2
    Repeati639 – 64131-3
    Repeati645 – 64731-4
    Repeati656 – 65831-5

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 103103Necessary for interaction with HRMT1L1Add
    BLAST
    Regioni213 – 856644Necessary for interaction with TP53Add
    BLAST
    Regioni456 – 594139Necessary for interaction with BRD7 and transcriptional activationAdd
    BLAST
    Regioni612 – 658475 X 3 AA repeats of R-G-GAdd
    BLAST
    Regioni612 – 65847Necessary for transcription repressionAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi613 – 66654Gly-richAdd
    BLAST
    Compositional biasi670 – 68920Asn-richAdd
    BLAST
    Compositional biasi692 – 811120Pro-richAdd
    BLAST
    Compositional biasi757 – 84589Tyr-richAdd
    BLAST
    Compositional biasi806 – 83227Gln-richAdd
    BLAST

    Domaini

    The RGG-box domain is methylated.

    Sequence similaritiesi

    Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
    Contains 1 SAP domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG297571.
    HOVERGENiHBG061101.
    InParanoidiQ9BUJ2.
    KOiK15047.
    OMAiSGPDGHY.
    OrthoDBiEOG79CZ07.
    PhylomeDBiQ9BUJ2.
    TreeFamiTF317301.

    Family and domain databases

    Gene3Di1.10.720.30. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR001870. B30.2/SPRY.
    IPR008985. ConA-like_lec_gl_sf.
    IPR027025. hnRNP_U_like_1.
    IPR027417. P-loop_NTPase.
    IPR003034. SAP_dom.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    [Graphical view]
    PANTHERiPTHR12381:SF41. PTHR12381:SF41. 1 hit.
    PfamiPF02037. SAP. 1 hit.
    PF00622. SPRY. 1 hit.
    [Graphical view]
    SMARTiSM00513. SAP. 1 hit.
    SM00449. SPRY. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS50188. B302_SPRY. 1 hit.
    PS50800. SAP. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BUJ2-1) [UniParc]FASTAAdd to Basket

    Also known as: Isoform a

    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

    MDVRRLKVNE LREELQRRGL DTRGLKAELA ERLQAALEAE EPDDERELDA    50
    DDEPGRPGHI NEEVETEGGS ELEGTAQPPP PGLQPHAEPG GYSGPDGHYA 100
    MDNITRQNQF YDTQVIKQEN ESGYERRPLE MEQQQAYRPE MKTEMKQGAP 150
    TSFLPPEASQ LKPDRQQFQS RKRPYEENRG RGYFEHREDR RGRSPQPPAE 200
    EDEDDFDDTL VAIDTYNCDL HFKVARDRSS GYPLTIEGFA YLWSGARASY 250
    GVRRGRVCFE MKINEEISVK HLPSTEPDPH VVRIGWSLDS CSTQLGEEPF 300
    SYGYGGTGKK STNSRFENYG DKFAENDVIG CFADFECGND VELSFTKNGK 350
    WMGIAFRIQK EALGGQALYP HVLVKNCAVE FNFGQRAEPY CSVLPGFTFI 400
    QHLPLSERIR GTVGPKSKAE CEILMMVGLP AAGKTTWAIK HAASNPSKKY 450
    NILGTNAIMD KMRVMGLRRQ RNYAGRWDVL IQQATQCLNR LIQIAARKKR 500
    NYILDQTNVY GSAQRRKMRP FEGFQRKAIV ICPTDEDLKD RTIKRTDEEG 550
    KDVPDHAVLE MKANFTLPDV GDFLDEVLFI ELQREEADKL VRQYNEEGRK 600
    AGPPPEKRFD NRGGGGFRGR GGGGGFQRYE NRGPPGGNRG GFQNRGGGSG 650
    GGGNYRGGFN RSGGGGYSQN RWGNNNRDNN NSNNRGSYNR APQQQPPPQQ 700
    PPPPQPPPQQ PPPPPSYSPA RNPPGASTYN KNSNIPGSSA NTSTPTVSSY 750
    SPPQPSYSQP PYNQGGYSQG YTAPPPPPPP PPAYNYGSYG GYNPAPYTPP 800
    PPPTAQTYPQ PSYNQYQQYA QQWNQYYQNQ GQWPPYYGNY DYGSYSGNTQ 850
    GGTSTQ 856
    Length:856
    Mass (Da):95,739
    Last modified:March 21, 2006 - v2
    Checksum:i6E57C0271E5F3A77
    GO
    Isoform 2 (identifier: Q9BUJ2-2) [UniParc]FASTAAdd to Basket

    Also known as: Isoform b

    The sequence of this isoform differs from the canonical sequence as follows:
         755-806: Missing.

    Show »
    Length:804
    Mass (Da):90,292
    Checksum:i05950AF9FAFD192F
    GO
    Isoform 3 (identifier: Q9BUJ2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         35-77: Missing.
         263-333: Missing.
         754-754: Q → QSFGFFPSTFQ

    Show »
    Length:752
    Mass (Da):84,500
    Checksum:i207A6A67EFFFA299
    GO
    Isoform 4 (identifier: Q9BUJ2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-100: Missing.

    Show »
    Length:756
    Mass (Da):84,794
    Checksum:iB16C6EC86B997FFA
    GO
    Isoform 5 (identifier: Q9BUJ2-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-460: Missing.
         461-562: KMRVMGLRRQ...VPDHAVLEMK → MGFCHVGQAG...CSLWGTSFLL
         754-754: Q → QSFGFFPSTFQ

    Note: May be due to intron retention. No experimental confirmation available.

    Show »
    Length:390
    Mass (Da):42,189
    Checksum:iA86E13953F84279F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271A → T in CAA07548. (PubMed:9733834)Curated
    Sequence conflicti508 – 5081N → S in BAC86806. (PubMed:14702039)Curated
    Sequence conflicti619 – 6191G → A in CAA07548. (PubMed:9733834)Curated
    Sequence conflicti625 – 6251G → A in CAA07548. (PubMed:9733834)Curated
    Sequence conflicti662 – 6621S → N in CAA07548. (PubMed:9733834)Curated
    Sequence conflicti691 – 6911A → S in BAC86806. (PubMed:14702039)Curated
    Sequence conflicti773 – 7731A → G in CAA07548. (PubMed:9733834)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti91 – 911G → C.1 Publication
    Corresponds to variant rs17849624 [ dbSNP | Ensembl ].
    VAR_025606

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 460460Missing in isoform 5. 1 PublicationVSP_017546Add
    BLAST
    Alternative sequencei1 – 100100Missing in isoform 4. 1 PublicationVSP_017547Add
    BLAST
    Alternative sequencei35 – 7743Missing in isoform 3. 1 PublicationVSP_017548Add
    BLAST
    Alternative sequencei263 – 33371Missing in isoform 3. 1 PublicationVSP_017549Add
    BLAST
    Alternative sequencei461 – 562102KMRVM…VLEMK → MGFCHVGQAGLELLTSGDPP ASASQSAGITGVSHRARPSV FVFLIHYSSFLHLLPSGRPL FWVEGTRLQKVLTSSSCSLW GTSFLL in isoform 5. 1 PublicationVSP_017550Add
    BLAST
    Alternative sequencei754 – 7541Q → QSFGFFPSTFQ in isoform 3 and isoform 5. 1 PublicationVSP_017551
    Alternative sequencei755 – 80652Missing in isoform 2. 1 PublicationVSP_017552Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007509 mRNA. Translation: CAA07548.1.
    AK021455 mRNA. Translation: BAB13831.1.
    AK022863 mRNA. Translation: BAG51129.1.
    AK127057 mRNA. Translation: BAC86806.1.
    AC011462 Genomic DNA. No translation available.
    AC011510 Genomic DNA. No translation available.
    CH471126 Genomic DNA. Translation: EAW57025.1.
    BC002564 mRNA. Translation: AAH02564.1.
    BC009988 mRNA. Translation: AAH09988.2.
    BC014232 mRNA. Translation: AAH14232.1.
    BC027713 mRNA. Translation: AAH27713.1.
    AL050146 mRNA. Translation: CAB43291.1.
    CCDSiCCDS12576.1. [Q9BUJ2-1]
    CCDS12577.1. [Q9BUJ2-4]
    PIRiT08776.
    T13159.
    RefSeqiNP_008971.2. NM_007040.3. [Q9BUJ2-1]
    NP_653333.1. NM_144732.2. [Q9BUJ2-4]
    XP_005258523.1. XM_005258466.1. [Q9BUJ2-4]
    UniGeneiHs.155218.
    Hs.718642.

    Genome annotation databases

    EnsembliENST00000378215; ENSP00000367460; ENSG00000105323. [Q9BUJ2-3]
    ENST00000392006; ENSP00000375863; ENSG00000105323. [Q9BUJ2-1]
    ENST00000593587; ENSP00000472629; ENSG00000105323. [Q9BUJ2-4]
    ENST00000595018; ENSP00000473132; ENSG00000105323. [Q9BUJ2-4]
    ENST00000602130; ENSP00000470687; ENSG00000105323. [Q9BUJ2-2]
    GeneIDi11100.
    KEGGihsa:11100.
    UCSCiuc002opz.4. human. [Q9BUJ2-1]
    uc002oqc.4. human. [Q9BUJ2-3]
    uc002oqf.4. human. [Q9BUJ2-5]
    uc010ehl.1. human. [Q9BUJ2-4]
    uc010ehm.3. human. [Q9BUJ2-2]

    Polymorphism databases

    DMDMi90101344.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007509 mRNA. Translation: CAA07548.1 .
    AK021455 mRNA. Translation: BAB13831.1 .
    AK022863 mRNA. Translation: BAG51129.1 .
    AK127057 mRNA. Translation: BAC86806.1 .
    AC011462 Genomic DNA. No translation available.
    AC011510 Genomic DNA. No translation available.
    CH471126 Genomic DNA. Translation: EAW57025.1 .
    BC002564 mRNA. Translation: AAH02564.1 .
    BC009988 mRNA. Translation: AAH09988.2 .
    BC014232 mRNA. Translation: AAH14232.1 .
    BC027713 mRNA. Translation: AAH27713.1 .
    AL050146 mRNA. Translation: CAB43291.1 .
    CCDSi CCDS12576.1. [Q9BUJ2-1 ]
    CCDS12577.1. [Q9BUJ2-4 ]
    PIRi T08776.
    T13159.
    RefSeqi NP_008971.2. NM_007040.3. [Q9BUJ2-1 ]
    NP_653333.1. NM_144732.2. [Q9BUJ2-4 ]
    XP_005258523.1. XM_005258466.1. [Q9BUJ2-4 ]
    UniGenei Hs.155218.
    Hs.718642.

    3D structure databases

    ProteinModelPortali Q9BUJ2.
    SMRi Q9BUJ2. Positions 1-37, 243-384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116281. 93 interactions.
    DIPi DIP-39419N.
    IntActi Q9BUJ2. 49 interactions.
    MINTi MINT-121512.

    PTM databases

    PhosphoSitei Q9BUJ2.

    Polymorphism databases

    DMDMi 90101344.

    Proteomic databases

    MaxQBi Q9BUJ2.
    PaxDbi Q9BUJ2.
    PRIDEi Q9BUJ2.

    Protocols and materials databases

    DNASUi 11100.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378215 ; ENSP00000367460 ; ENSG00000105323 . [Q9BUJ2-3 ]
    ENST00000392006 ; ENSP00000375863 ; ENSG00000105323 . [Q9BUJ2-1 ]
    ENST00000593587 ; ENSP00000472629 ; ENSG00000105323 . [Q9BUJ2-4 ]
    ENST00000595018 ; ENSP00000473132 ; ENSG00000105323 . [Q9BUJ2-4 ]
    ENST00000602130 ; ENSP00000470687 ; ENSG00000105323 . [Q9BUJ2-2 ]
    GeneIDi 11100.
    KEGGi hsa:11100.
    UCSCi uc002opz.4. human. [Q9BUJ2-1 ]
    uc002oqc.4. human. [Q9BUJ2-3 ]
    uc002oqf.4. human. [Q9BUJ2-5 ]
    uc010ehl.1. human. [Q9BUJ2-4 ]
    uc010ehm.3. human. [Q9BUJ2-2 ]

    Organism-specific databases

    CTDi 11100.
    GeneCardsi GC19P041768.
    HGNCi HGNC:17011. HNRNPUL1.
    HPAi CAB046477.
    HPA046290.
    HPA049475.
    MIMi 605800. gene.
    neXtProti NX_Q9BUJ2.
    PharmGKBi PA162391519.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG297571.
    HOVERGENi HBG061101.
    InParanoidi Q9BUJ2.
    KOi K15047.
    OMAi SGPDGHY.
    OrthoDBi EOG79CZ07.
    PhylomeDBi Q9BUJ2.
    TreeFami TF317301.

    Enzyme and pathway databases

    Reactomei REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi HNRNPUL1. human.
    GeneWikii HNRPUL1.
    GenomeRNAii 11100.
    NextBioi 42198.
    PROi Q9BUJ2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BUJ2.
    Bgeei Q9BUJ2.
    CleanExi HS_HNRNPUL1.
    Genevestigatori Q9BUJ2.

    Family and domain databases

    Gene3Di 1.10.720.30. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR001870. B30.2/SPRY.
    IPR008985. ConA-like_lec_gl_sf.
    IPR027025. hnRNP_U_like_1.
    IPR027417. P-loop_NTPase.
    IPR003034. SAP_dom.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    [Graphical view ]
    PANTHERi PTHR12381:SF41. PTHR12381:SF41. 1 hit.
    Pfami PF02037. SAP. 1 hit.
    PF00622. SPRY. 1 hit.
    [Graphical view ]
    SMARTi SM00513. SAP. 1 hit.
    SM00449. SPRY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50188. B302_SPRY. 1 hit.
    PS50800. SAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "E1B-55kilodalton-associated protein: a cellular protein with RNA-binding activity implicated in nucleocytoplasmic transport of adenovirus and cellular mRNAs."
      Gabler S., Schuett H., Groitl P., Wolf H., Shenk T., Dobner T.
      J. Virol. 72:7960-7971(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN MRNA PROCESSING, INTERACTION WITH ADENOVIRUS 5 E1B-55 KDA, RNA-BINDING, SUBCELLULAR LOCATION.
      Tissue: Cervix carcinoma.
    2. "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] (ISOFORMS 1; 3 AND 5).
      Tissue: Brain and Embryo.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1; 2 AND 4), VARIANT CYS-91.
      Tissue: Brain, Eye, Muscle and Placenta.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 355-856.
      Tissue: Uterus.
    7. "The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates."
      Bachi A., Braun I.C., Rodrigues J.P., Pante N., Ribbeck K., von Kobbe C., Kutay U., Wilm M., Goerlich D., Carmo-Fonseca M., Izaurralde E.
      RNA 6:136-158(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NXF1.
    8. "Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1."
      Kzhyshkowska J., Schuett H., Liss M., Kremmer E., Stauber R., Wolf H., Dobner T.
      Biochem. J. 358:305-314(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION, INTERACTION WITH PRMT2, SUBCELLULAR LOCATION.
    9. "Regulation of transcription by the heterogeneous nuclear ribonucleoprotein E1B-AP5 is mediated by complex formation with the novel bromodomain-containing protein BRD7."
      Kzhyshkowska J.G., Rusch A., Wolf H., Dobner T.
      Biochem. J. 371:385-393(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH BRD7, ASSOCIATION WITH HISTONES AND BRD7, SUBCELLULAR LOCATION.
    10. "Protein arginine methylation during lytic adenovirus infection."
      Kzhyshkowska J., Kremmer E., Hofmann M., Wolf H., Dobner T.
      Biochem. J. 383:259-265(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION DURING ADENOVIRAL INFECTION.
    11. Cited for: INTERACTION WITH TP53.
    12. "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-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
      Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
      Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    15. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: 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-194 AND SER-512, 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-512, 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-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHNRL1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BUJ2
    Secondary accession number(s): B3KMW7
    , O76022, Q6ZSZ0, Q7L8P4, Q8N6Z4, Q96G37, Q9HAL3, Q9UG75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: March 21, 2006
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 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

    Miscellaneous

    Its methylation is enhanced in the late phase of adenoviral infection.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3