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Q07666

- KHDR1_HUMAN

UniProt

Q07666 - KHDR1_HUMAN

Protein

KH domain-containing, RNA-binding, signal transduction-associated protein 1

Gene

KHDRBS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824).1 Publication
    Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase.1 Publication

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. poly(A) binding Source: MGI
    3. poly(A) RNA binding Source: UniProtKB
    4. poly(U) RNA binding Source: MGI
    5. protein binding Source: UniProtKB
    6. RNA binding Source: UniProtKB
    7. SH3/SH2 adaptor activity Source: UniProtKB

    GO - Biological processi

    1. cell cycle arrest Source: ProtInc
    2. cell proliferation Source: ProtInc
    3. cell surface receptor signaling pathway Source: UniProtKB
    4. G2/M transition of mitotic cell cycle Source: UniProtKB
    5. mRNA processing Source: ProtInc
    6. negative regulation of transcription, DNA-templated Source: UniProtKB
    7. positive regulation of RNA export from nucleus Source: UniProtKB
    8. positive regulation of signal transduction Source: GOC
    9. positive regulation of translational initiation Source: UniProtKB
    10. regulation of RNA export from nucleus Source: UniProtKB
    11. signal transduction Source: ProtInc
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    SignaLinkiQ07666.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    KH domain-containing, RNA-binding, signal transduction-associated protein 1
    Alternative name(s):
    GAP-associated tyrosine phosphoprotein p62
    Src-associated in mitosis 68 kDa protein
    Short name:
    Sam68
    p21 Ras GTPase-activating protein-associated p62
    p68
    Gene namesi
    Name:KHDRBS1Imported
    Synonyms:SAM681 Publication
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:18116. KHDRBS1.

    Subcellular locationi

    Nucleus 1 Publication. Membrane 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. Grb2-Sos complex Source: Ensembl
    3. membrane Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi435 – 4351Y → F: No effect on the nuclear localization. 1 Publication
    Mutagenesisi440 – 4401Y → F: Completely blocks nuclear localization. 1 Publication
    Mutagenesisi443 – 4431Y → F: No effect on the nuclear localization. 1 Publication

    Organism-specific databases

    PharmGKBiPA30092.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 443443KH domain-containing, RNA-binding, signal transduction-associated protein 1PRO_0000050124Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201Phosphoserine2 Publications
    Modified residuei29 – 291Phosphoserine1 Publication
    Modified residuei45 – 451Asymmetric dimethylarginine; by PRMT12 Publications
    Modified residuei52 – 521Asymmetric dimethylarginine; partial; by PRMT12 Publications
    Modified residuei58 – 581Phosphoserine1 Publication
    Modified residuei113 – 1131PhosphoserineBy similarity
    Modified residuei175 – 1751N6-acetyllysine2 Publications
    Modified residuei304 – 3041Asymmetric dimethylarginine; by PRMT12 Publications
    Modified residuei310 – 3101Omega-N-methylarginine; by PRMT12 Publications
    Modified residuei315 – 3151Omega-N-methylarginine; by PRMT12 Publications
    Modified residuei320 – 3201Dimethylated arginine; in A2780 ovarian carcinoma cell line3 Publications
    Modified residuei320 – 3201Omega-N-methylarginine; by PRMT13 Publications
    Modified residuei325 – 3251Omega-N-methylarginine; by PRMT13 Publications
    Modified residuei331 – 3311Dimethylated arginine; in A2780 ovarian carcinoma cell line2 Publications
    Modified residuei331 – 3311Omega-N-methylated arginine; by PRMT13 Publications
    Modified residuei340 – 3401Omega-N-methylarginine; by PRMT13 Publications
    Modified residuei435 – 4351Phosphotyrosine; by PTK61 Publication
    Modified residuei440 – 4401Phosphotyrosine; by PTK61 Publication
    Modified residuei443 – 4431Phosphotyrosine; by PTK61 Publication

    Post-translational modificationi

    Tyrosine phosphorylated by several non-receptor tyrosine kinases, LCK, FYN and JAK3. Negatively correlates with ability to bind RNA but required for many interactions with proteins. Phosphorylation by PTK6 negatively regulates its RNA binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the nulear localization of KHDRBS1.5 Publications
    Acetylated. Positively correlates with ability to bind RNA.2 Publications
    Arginine methylation is required for nuclear localization. Also can affect interaction with other proteins. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 AND FNBP4/FBP30.4 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ07666.
    PaxDbiQ07666.
    PRIDEiQ07666.

    PTM databases

    PhosphoSiteiQ07666.

    Miscellaneous databases

    PMAP-CutDBQ07666.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in all tissue examined. Isoform 1 is expressed at lower levels in brain, skeletal muscle, and liver whereas isoform 3 is intensified in skeletal muscle and in liver.1 Publication

    Developmental stagei

    Isoform 3 is only expressed in growth-arrested cells.1 Publication

    Gene expression databases

    ArrayExpressiQ07666.
    BgeeiQ07666.
    CleanExiHS_KHDRBS1.
    GenevestigatoriQ07666.

    Organism-specific databases

    HPAiCAB005355.
    HPA051280.
    HPA056813.

    Interactioni

    Subunit structurei

    Self-associates to form homooligomers when bound to RNA, oligomerization appears to be limited when binding to proteins. Interacts with CBL, KHDRBS3, LCK, GRB2, JAK3, PIK3R1, PLCG1, PTPN6, RASA1, RBMY1A1 and STAT3. Interacts with PRMT1. Binds the WW domains of WBP4/FBP21, FNBP4/FBP30 and the SH3 domain of FYN through the Arg/Gly-rich-flanked Pro-rich regions By similarity. Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA. Interacts with PTK6 (via SH3 and SH2 domains). Does not interact with TPR.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FYNP062414EBI-1364,EBI-515315
    GRB2P629938EBI-1364,EBI-401755
    HCKP086314EBI-1364,EBI-346340
    HNRNPA1P096512EBI-1364,EBI-352662
    JAK3P523332EBI-1364,EBI-518246
    LCKP062395EBI-1364,EBI-1348
    LckP062402EBI-1364,EBI-1401From a different organism.
    PIK3R1P237272EBI-1364,EBI-520244From a different organism.
    PLCG1P191742EBI-1364,EBI-79387
    SMARCA2P515312EBI-1364,EBI-679562
    SRCP129313EBI-1364,EBI-621482
    STAT3P407632EBI-1364,EBI-518675
    VAV1P154983EBI-1364,EBI-625518

    Protein-protein interaction databases

    BioGridi115900. 135 interactions.
    DIPiDIP-29007N.
    IntActiQ07666. 65 interactions.
    MINTiMINT-102826.
    STRINGi9606.ENSP00000313829.

    Structurei

    Secondary structure

    1
    443
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi100 – 11314
    Helixi119 – 13416

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XA6NMR-A/B97-135[»]
    3QHEX-ray2.40B/D365-419[»]
    ProteinModelPortaliQ07666.
    SMRiQ07666. Positions 98-276.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07666.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini171 – 19727KHPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi34 – 418Pro-richSequence Analysis
    Compositional biasi44 – 5512DMA/Gly-richSequence AnalysisAdd
    BLAST
    Compositional biasi59 – 8931Pro-richSequence AnalysisAdd
    BLAST
    Compositional biasi282 – 29211DMA/Gly-richSequence AnalysisAdd
    BLAST
    Compositional biasi295 – 3017Pro-richSequence Analysis
    Compositional biasi302 – 33231Arg/Gly-richSequence AnalysisAdd
    BLAST
    Compositional biasi334 – 36330Pro-richSequence AnalysisAdd
    BLAST

    Domaini

    The KH domain is required for binding to RNA.By similarity
    The Pro-rich domains are flanked by Arg/Gly-rich motifs which can be asymmetric dimethylated on arginine residues to give the DMA/Gly-rich regions. Selective methylation on these motifs can modulate protein-protein interactions By similarity.By similarity

    Sequence similaritiesi

    Belongs to the KHDRBS family.Sequence Analysis
    Contains 1 KH domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3-binding

    Phylogenomic databases

    eggNOGiCOG5176.
    HOGENOMiHOG000230771.
    HOVERGENiHBG079164.
    InParanoidiQ07666.
    KOiK13198.
    OMAiFMELSYL.
    OrthoDBiEOG75MVX3.
    PhylomeDBiQ07666.
    TreeFamiTF314878.

    Family and domain databases

    Gene3Di3.30.1370.10. 1 hit.
    InterProiIPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    [Graphical view]
    PfamiPF00013. KH_1. 1 hit.
    [Graphical view]
    SMARTiSM00322. KH. 1 hit.
    [Graphical view]
    SUPFAMiSSF54791. SSF54791. 1 hit.
    PROSITEiPS50084. KH_TYPE_1. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q07666-1) [UniParc]FASTAAdd to Basket

    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

    MQRRDDPAAR MSRSSGRSGS MDPSGAHPSV RQTPSRQPPL PHRSRGGGGG    50
    SRGGARASPA TQPPPLLPPS ATGPDATVGG PAPTPLLPPS ATASVKMEPE 100
    NKYLPELMAE KDSLDPSFTH AMQLLTAEIE KIQKGDSKKD DEENYLDLFS 150
    HKNMKLKERV LIPVKQYPKF NFVGKILGPQ GNTIKRLQEE TGAKISVLGK 200
    GSMRDKAKEE ELRKGGDPKY AHLNMDLHVF IEVFGPPCEA YALMAHAMEE 250
    VKKFLVPDMM DDICQEQFLE LSYLNGVPEP SRGRGVPVRG RGAAPPPPPV 300
    PRGRGVGPPR GALVRGTPVR GAITRGATVT RGVPPPPTVR GAPAPRARTA 350
    GIQRIPLPPP PAPETYEEYG YDDTYAEQSY EGYEGYYSQS QGDSEYYDYG 400
    HGEVQDSYEA YGQDDWNGTR PSLKAPPARP VKGAYREHPY GRY 443
    Length:443
    Mass (Da):48,227
    Last modified:November 1, 1996 - v1
    Checksum:i59FB4DB6FB4DBE98
    GO
    Isoform 2Curated (identifier: Q07666-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         37-61: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:418
    Mass (Da):45,861
    Checksum:i36B5B877E35D9A2C
    GO
    Isoform 31 Publication (identifier: Q07666-3) [UniParc]FASTAAdd to Basket

    Also known as: DeltaKH1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         169-207: Missing.

    Show »
    Length:404
    Mass (Da):44,027
    Checksum:i0E6334E3447CCA5F
    GO

    Sequence cautioni

    The sequence AAH10132.1 differs from that shown. Reason: Intron retention.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei37 – 6125Missing in isoform 2. 1 PublicationVSP_051719Add
    BLAST
    Alternative sequencei169 – 20739Missing in isoform 3. 1 PublicationVSP_051720Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88108 mRNA. Translation: AAA59990.1.
    U78971 mRNA. Translation: AAB47504.1.
    AK091346 mRNA. Translation: BAC03643.1.
    AL139249, AL445248 Genomic DNA. Translation: CAI21971.1.
    AL139249, AL445248 Genomic DNA. Translation: CAI21972.1.
    AL445248, AL139249 Genomic DNA. Translation: CAH71944.1.
    AL445248, AL139249 Genomic DNA. Translation: CAH71945.1.
    CH471059 Genomic DNA. Translation: EAX07576.1.
    CH471059 Genomic DNA. Translation: EAX07577.1.
    BC000717 mRNA. Translation: AAH00717.1.
    BC010132 mRNA. Translation: AAH10132.1. Sequence problems.
    BC019109 mRNA. Translation: AAH19109.1.
    CCDSiCCDS350.1. [Q07666-1]
    CCDS60067.1. [Q07666-3]
    PIRiA38219.
    RefSeqiNP_001258807.1. NM_001271878.1. [Q07666-3]
    NP_006550.1. NM_006559.2. [Q07666-1]
    UniGeneiHs.445893.

    Genome annotation databases

    EnsembliENST00000327300; ENSP00000313829; ENSG00000121774. [Q07666-1]
    ENST00000492989; ENSP00000417731; ENSG00000121774. [Q07666-3]
    GeneIDi10657.
    KEGGihsa:10657.
    UCSCiuc001bua.2. human. [Q07666-3]
    uc001bub.4. human. [Q07666-1]

    Polymorphism databases

    DMDMi62511098.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88108 mRNA. Translation: AAA59990.1 .
    U78971 mRNA. Translation: AAB47504.1 .
    AK091346 mRNA. Translation: BAC03643.1 .
    AL139249 , AL445248 Genomic DNA. Translation: CAI21971.1 .
    AL139249 , AL445248 Genomic DNA. Translation: CAI21972.1 .
    AL445248 , AL139249 Genomic DNA. Translation: CAH71944.1 .
    AL445248 , AL139249 Genomic DNA. Translation: CAH71945.1 .
    CH471059 Genomic DNA. Translation: EAX07576.1 .
    CH471059 Genomic DNA. Translation: EAX07577.1 .
    BC000717 mRNA. Translation: AAH00717.1 .
    BC010132 mRNA. Translation: AAH10132.1 . Sequence problems.
    BC019109 mRNA. Translation: AAH19109.1 .
    CCDSi CCDS350.1. [Q07666-1 ]
    CCDS60067.1. [Q07666-3 ]
    PIRi A38219.
    RefSeqi NP_001258807.1. NM_001271878.1. [Q07666-3 ]
    NP_006550.1. NM_006559.2. [Q07666-1 ]
    UniGenei Hs.445893.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XA6 NMR - A/B 97-135 [» ]
    3QHE X-ray 2.40 B/D 365-419 [» ]
    ProteinModelPortali Q07666.
    SMRi Q07666. Positions 98-276.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115900. 135 interactions.
    DIPi DIP-29007N.
    IntActi Q07666. 65 interactions.
    MINTi MINT-102826.
    STRINGi 9606.ENSP00000313829.

    Chemistry

    BindingDBi Q07666.
    ChEMBLi CHEMBL1795190.

    PTM databases

    PhosphoSitei Q07666.

    Polymorphism databases

    DMDMi 62511098.

    Proteomic databases

    MaxQBi Q07666.
    PaxDbi Q07666.
    PRIDEi Q07666.

    Protocols and materials databases

    DNASUi 10657.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327300 ; ENSP00000313829 ; ENSG00000121774 . [Q07666-1 ]
    ENST00000492989 ; ENSP00000417731 ; ENSG00000121774 . [Q07666-3 ]
    GeneIDi 10657.
    KEGGi hsa:10657.
    UCSCi uc001bua.2. human. [Q07666-3 ]
    uc001bub.4. human. [Q07666-1 ]

    Organism-specific databases

    CTDi 10657.
    GeneCardsi GC01P032479.
    HGNCi HGNC:18116. KHDRBS1.
    HPAi CAB005355.
    HPA051280.
    HPA056813.
    MIMi 602489. gene.
    neXtProti NX_Q07666.
    PharmGKBi PA30092.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5176.
    HOGENOMi HOG000230771.
    HOVERGENi HBG079164.
    InParanoidi Q07666.
    KOi K13198.
    OMAi FMELSYL.
    OrthoDBi EOG75MVX3.
    PhylomeDBi Q07666.
    TreeFami TF314878.

    Enzyme and pathway databases

    SignaLinki Q07666.

    Miscellaneous databases

    ChiTaRSi KHDRBS1. human.
    EvolutionaryTracei Q07666.
    GeneWikii KHDRBS1.
    GenomeRNAii 10657.
    NextBioi 40517.
    PMAP-CutDB Q07666.
    PROi Q07666.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q07666.
    Bgeei Q07666.
    CleanExi HS_KHDRBS1.
    Genevestigatori Q07666.

    Family and domain databases

    Gene3Di 3.30.1370.10. 1 hit.
    InterProi IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    [Graphical view ]
    Pfami PF00013. KH_1. 1 hit.
    [Graphical view ]
    SMARTi SM00322. KH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54791. SSF54791. 1 hit.
    PROSITEi PS50084. KH_TYPE_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62."
      Wong G., Muller O., Clark R., Conroy L., Moran M.F., Polakis P., McCormick F.
      Cell 69:551-558(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, RNA-BINDING, METHYLATION, INTERACTION WITH RASA1.
      Tissue: Fetal brainImported.
    2. "A role for Sam68 in cell cycle progression antagonized by a spliced variant within the KH domain."
      Barlat I., Maurier F., Duchesne M., Guitard E., Tocque B., Schweighoffer F.
      J. Biol. Chem. 272:3129-3132(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Placenta1 Publication.
    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] (ISOFORM 2).
      Tissue: BrainImported.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: LymphImported and PlacentaImported.
    7. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 18-31; 57-96; 103-131; 139-152; 176-185; 292-302 AND 316-340, METHYLATION AT ARG-320; ARG-331 AND ARG-340, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    8. "Interaction between Sam68 and Src family tyrosine kinases, Fyn and Lck, in T cell receptor signaling."
      Fusaki N., Iwamatsu A., Iwashima M., Fujisawa J.
      J. Biol. Chem. 272:6214-6219(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 102-110 AND 169-175 (ISOFORMS 1/2), FUNCTION, PHOSPHORYLATION, INTERACTION WITH LCK; FYN; PTPN6; PLCG1; GRB2; CBL; JAK3 AND PIK3R1.
    9. "T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-binding protein implicated in spermatogenesis."
      Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B., Wu J., Cooke H.J., Artzt K., Eperon I.C.
      Hum. Mol. Genet. 8:959-969(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KHDRBS3.
      Tissue: Testis1 Publication.
    10. "Sik (BRK) phosphorylates Sam68 in the nucleus and negatively regulates its RNA binding ability."
      Derry J.J., Richard S., Valderrama Carvajal H., Ye X., Vasioukhin V., Cochrane A.W., Chen T., Tyner A.L.
      Mol. Cell. Biol. 20:6114-6126(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PTK6.
    11. "Human leptin signaling in human peripheral blood mononuclear cells: activation of the JAK-STAT pathway."
      Sanchez-Margalet V., Martin-Romero C.
      Cell. Immunol. 211:30-36(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH STAT3.
    12. "Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1."
      Cote J., Boisvert F.-M., Boulanger M.-C., Bedford M.T., Richard S.
      Mol. Biol. Cell 14:274-287(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-45; ARG-52; ARG-304; ARG-310; ARG-315; ARG-320 AND ARG-325, SUBCELLULAR LOCATION.
    13. "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC."
      Ong S.E., Mittler G., Mann M.
      Nat. Methods 1:119-126(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "The RNA binding protein Sam68 is acetylated in tumor cell lines, and its acetylation correlates with enhanced RNA binding activity."
      Babic I., Jakymiw A., Fujita D.J.
      Oncogene 23:3781-3789(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION, INTERACTION WITH RNA.
    15. "Tyrosine phosphorylation of sam68 by breast tumor kinase regulates intranuclear localization and cell cycle progression."
      Lukong K.E., Larocque D., Tyner A.L., Richard S.
      J. Biol. Chem. 280:38639-38647(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-435; TYR-440 AND TYR-443, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-435; TYR-440 AND TYR-443.
    16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G."
      Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.
      Biochim. Biophys. Acta 1774:1339-1350(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; RBMX; NCOA5 AND PPP1CA.
    18. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "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-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "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-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "The Tpr protein regulates export of mRNAs with retained introns that traffic through the Nxf1 pathway."
      Coyle J.H., Bor Y.C., Rekosh D., Hammarskjold M.L.
      RNA 17:1344-1356(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    27. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA."
      Rajanala K., Nandicoori V.K.
      PLoS ONE 7:E29921-E29921(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABSENCE OF FUNCTION IN UNSPLICED RNA EXPORT, ABSENCE OF INTERACTION WITH TPR.

    Entry informationi

    Entry nameiKHDR1_HUMAN
    AccessioniPrimary (citable) accession number: Q07666
    Secondary accession number(s): D3DPP3
    , Q6PJX7, Q8NB97, Q99760
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 147 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 1
      Human chromosome 1: 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