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P82979

- SARNP_HUMAN

UniProt

P82979 - SARNP_HUMAN

Protein

SAP domain-containing ribonucleoprotein

Gene

SARNP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single-stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production.3 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. mRNA export from nucleus Source: UniProtKB
    2. regulation of transcription, DNA-templated Source: UniProtKB-KW
    3. regulation of translation Source: UniProtKB-KW
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    mRNA transport, Transcription, Transcription regulation, Translation regulation, Transport

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SAP domain-containing ribonucleoprotein
    Alternative name(s):
    Cytokine-induced protein of 29 kDa
    Nuclear protein Hcc-1
    Proliferation-associated cytokine-inducible protein CIP29
    Gene namesi
    Name:SARNP
    Synonyms:HCC1
    ORF Names:HSPC316
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:24432. SARNP.

    Subcellular locationi

    GO - Cellular componenti

    1. intracellular membrane-bounded organelle Source: HPA
    2. nuclear speck Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. transcription export complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165513309.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 210209SAP domain-containing ribonucleoproteinPRO_0000083916Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei10 – 101N6-acetyllysineBy similarity
    Modified residuei142 – 1421N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP82979.
    PaxDbiP82979.
    PRIDEiP82979.

    PTM databases

    PhosphoSiteiP82979.

    Expressioni

    Tissue specificityi

    Low expression in spleen, liver, pancreas, testis, thymus, heart, and kidney. Increased levels are seen in hepatocellular carcinoma and pancreatic adenocarcinoma.1 Publication

    Inductioni

    By EPO/erythropoietin.

    Gene expression databases

    ArrayExpressiP82979.
    BgeeiP82979.
    GenevestigatoriP82979.

    Organism-specific databases

    HPAiHPA030902.
    HPA030903.

    Interactioni

    Subunit structurei

    Interacts with DDX39A. Interacts with FUS. Component of the transcription/export (TREX) complex at least composed of ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; TREX seems to have dynamic structure involving ATP-dependent remodeling; in the complex interacts directly with DDX39B in a ATP-dependent manner which bridges it to ALYREF/THOC4.2 Publications

    Protein-protein interaction databases

    BioGridi124049. 40 interactions.
    IntActiP82979. 5 interactions.
    MINTiMINT-5008704.
    STRINGi9606.ENSP00000337632.

    Structurei

    Secondary structure

    1
    210
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni8 – 103
    Helixi13 – 2311
    Helixi31 – 4414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DO1NMR-A6-47[»]
    ProteinModelPortaliP82979.
    SMRiP82979. Positions 6-47.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP82979.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 4235SAPPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 SAP domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG290157.
    HOGENOMiHOG000013054.
    InParanoidiP82979.
    OrthoDBiEOG7J9VRJ.
    PhylomeDBiP82979.
    TreeFamiTF319843.

    Family and domain databases

    Gene3Di1.10.720.30. 1 hit.
    InterProiIPR003034. SAP_dom.
    [Graphical view]
    PfamiPF02037. SAP. 1 hit.
    [Graphical view]
    SMARTiSM00513. SAP. 1 hit.
    [Graphical view]
    PROSITEiPS50800. SAP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P82979-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATETVELHK LKLAELKQEC LARGLETKGI KQDLIHRLQA YLEEHAEEEA    50
    NEEDVLGDET EEEETKPIEL PVKEEEPPEK TVDVAAEKKV VKITSEIPQT 100
    ERMQKRAERF NVPVSLESKK AARAARFGIS SVPTKGLSSD NKPMVNLDKL 150
    KERAQRFGLN VSSISRKSED DEKLKKRKER FGIVTSSAGT GTTEDTEAKK 200
    RKRAERFGIA 210
    Length:210
    Mass (Da):23,671
    Last modified:January 23, 2007 - v3
    Checksum:i96AFDD37EA328126
    GO

    Sequence cautioni

    The sequence AAF28994.1 differs from that shown. Reason: Frameshift at positions 134 and 149.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti127 – 1271F → V in AAF28994. (PubMed:11042152)Curated
    Sequence conflicti153 – 1575RAQRF → ELKDL in AAF28994. (PubMed:11042152)Curated
    Sequence conflicti199 – 21012KKRKR…RFGIA → RRGKEQSALGLP in AAF28994. (PubMed:11042152)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ409089 Genomic DNA. Translation: CAC37950.1.
    AF486281 mRNA. Translation: AAM09686.1.
    AF161434 mRNA. Translation: AAF28994.1. Sequence problems.
    AK290508 mRNA. Translation: BAF83197.1.
    CH471054 Genomic DNA. Translation: EAW96838.1.
    BC007099 mRNA. Translation: AAH07099.1.
    CCDSiCCDS8892.1.
    PIRiJC7830.
    RefSeqiNP_149073.1. NM_033082.3.
    UniGeneiHs.505676.

    Genome annotation databases

    EnsembliENST00000336133; ENSP00000337632; ENSG00000205323.
    ENST00000546604; ENSP00000449409; ENSG00000205323.
    GeneIDi84324.
    KEGGihsa:84324.
    UCSCiuc001sht.3. human.

    Polymorphism databases

    DMDMi18202440.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ409089 Genomic DNA. Translation: CAC37950.1 .
    AF486281 mRNA. Translation: AAM09686.1 .
    AF161434 mRNA. Translation: AAF28994.1 . Sequence problems.
    AK290508 mRNA. Translation: BAF83197.1 .
    CH471054 Genomic DNA. Translation: EAW96838.1 .
    BC007099 mRNA. Translation: AAH07099.1 .
    CCDSi CCDS8892.1.
    PIRi JC7830.
    RefSeqi NP_149073.1. NM_033082.3.
    UniGenei Hs.505676.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DO1 NMR - A 6-47 [» ]
    ProteinModelPortali P82979.
    SMRi P82979. Positions 6-47.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124049. 40 interactions.
    IntActi P82979. 5 interactions.
    MINTi MINT-5008704.
    STRINGi 9606.ENSP00000337632.

    PTM databases

    PhosphoSitei P82979.

    Polymorphism databases

    DMDMi 18202440.

    Proteomic databases

    MaxQBi P82979.
    PaxDbi P82979.
    PRIDEi P82979.

    Protocols and materials databases

    DNASUi 84324.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336133 ; ENSP00000337632 ; ENSG00000205323 .
    ENST00000546604 ; ENSP00000449409 ; ENSG00000205323 .
    GeneIDi 84324.
    KEGGi hsa:84324.
    UCSCi uc001sht.3. human.

    Organism-specific databases

    CTDi 84324.
    GeneCardsi GC12M056146.
    HGNCi HGNC:24432. SARNP.
    HPAi HPA030902.
    HPA030903.
    MIMi 610049. gene.
    neXtProti NX_P82979.
    PharmGKBi PA165513309.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG290157.
    HOGENOMi HOG000013054.
    InParanoidi P82979.
    OrthoDBi EOG7J9VRJ.
    PhylomeDBi P82979.
    TreeFami TF319843.

    Miscellaneous databases

    ChiTaRSi SARNP. human.
    EvolutionaryTracei P82979.
    GeneWikii CIP29.
    GenomeRNAii 84324.
    NextBioi 74056.
    PROi P82979.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P82979.
    Bgeei P82979.
    Genevestigatori P82979.

    Family and domain databases

    Gene3Di 1.10.720.30. 1 hit.
    InterProi IPR003034. SAP_dom.
    [Graphical view ]
    Pfami PF02037. SAP. 1 hit.
    [Graphical view ]
    SMARTi SM00513. SAP. 1 hit.
    [Graphical view ]
    PROSITEi PS50800. SAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "An integrated approach in the discovery and characterization of a novel nuclear protein over-expressed in liver and pancreatic tumors."
      Choong M.L., Tan L.K., Lo S.L., Ren E.-C., Ou K.L., Ong S.-E., Liang R.C.M.Y., Seow T.K., Chung M.C.M.
      FEBS Lett. 496:109-116(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 110-119; 157-167 AND 181-199, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Liver.
    2. "Cloning and characterization of a proliferation-associated cytokine-inducible protein, CIP29."
      Fukuda S., Wu D.W., Stark K., Pelus L.M.
      Biochem. Biophys. Res. Commun. 292:593-600(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary cancer.
    3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Umbilical cord blood.
    4. "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: Fetal brain.
    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].
      Tissue: Prostate.
    7. Bienvenut W.V., Potts A., Brablan J., Quadroni M.
      Submitted (JUL-2004) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10 AND 127-135, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    8. "Hcc-1 is a novel component of the nuclear matrix with growth inhibitory function."
      Leaw C.L., Ren E.C., Choong M.L.
      Cell. Mol. Life Sci. 61:2264-2273(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Intracellular characterization of DDX39, a novel growth-associated RNA helicase."
      Sugiura T., Sakurai K., Nagano Y.
      Exp. Cell Res. 313:782-790(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DDX39A AND FUS.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex."
      Dufu K., Livingstone M.J., Seebacher J., Gygi S.P., Wilson S.A., Reed R.
      Genes Dev. 24:2043-2053(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE TREX COMPLEX, INTERACTION WITH DDX39B.
    12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Solution structure of the SAP domain of human nuclear protein HCC-1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 6-47.

    Entry informationi

    Entry nameiSARNP_HUMAN
    AccessioniPrimary (citable) accession number: P82979
    Secondary accession number(s): A8K393, Q9P066
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 129 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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