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Q8TAD8

- SNIP1_HUMAN

UniProt

Q8TAD8 - SNIP1_HUMAN

Protein

Smad nuclear-interacting protein 1

Gene

SNIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Down-regulates NF-kappa-B signaling by competing with RELA for CREBBP/EP300 binding. Involved in the microRNA (miRNA) biogenesis. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA.4 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    2. production of miRNAs involved in gene silencing by miRNA Source: UniProtKB
    3. regulation of transcription, DNA-templated Source: Ensembl

    Keywords - Biological processi

    RNA-mediated gene silencing

    Enzyme and pathway databases

    SignaLinkiQ8TAD8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Smad nuclear-interacting protein 1
    Alternative name(s):
    FHA domain-containing protein SNIP1
    Gene namesi
    Name:SNIP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:30587. SNIP1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Psychomotor retardation, epilepsy, and craniofacial dysmorphism (PMRED) [MIM:614501]: A disease characterized by severe psychomotor retardation, intractable seizures, dysmorphic features, and a lumpy skull surface. Patients are hypotonic and have poor feeding in the neonatal period.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti366 – 3661E → G in PMRED. 1 Publication
    VAR_067542

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi30 – 301K → R: Abolishes sumoylation. 1 Publication

    Keywords - Diseasei

    Disease mutation, Epilepsy

    Organism-specific databases

    MIMi614501. phenotype.
    PharmGKBiPA142670893.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 396396Smad nuclear-interacting protein 1PRO_0000072009Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki30 – 30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei35 – 351Phosphoserine3 Publications
    Modified residuei49 – 491Phosphoserine1 Publication
    Modified residuei52 – 521Phosphoserine2 Publications
    Modified residuei54 – 541Phosphoserine2 Publications
    Modified residuei394 – 3941Phosphoserine1 Publication

    Post-translational modificationi

    Degraded by the proteasome upon binding to the SMAD1/OAZ1/PSMB4 complex.

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8TAD8.
    PaxDbiQ8TAD8.
    PRIDEiQ8TAD8.

    PTM databases

    PhosphoSiteiQ8TAD8.

    Expressioni

    Tissue specificityi

    Ubiquitous, with highest expression in heart and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ8TAD8.
    BgeeiQ8TAD8.
    CleanExiHS_SNIP1.
    GenevestigatoriQ8TAD8.

    Organism-specific databases

    HPAiHPA036896.

    Interactioni

    Subunit structurei

    Binds SMAD4 and CREBBP/EP300. Binds the SMAD1/OAZ1/PSMB4 complex. Interacts with DROSHA and SMARCA4. Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IKQ131232EBI-749336,EBI-713456
    MYCP011069EBI-749336,EBI-447544
    SNW1Q135737EBI-749336,EBI-632715

    Protein-protein interaction databases

    BioGridi122864. 27 interactions.
    DIPiDIP-38956N.
    IntActiQ8TAD8. 41 interactions.
    MINTiMINT-1181692.
    STRINGi9606.ENSP00000296215.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TAD8.
    SMRiQ8TAD8. Positions 246-374.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini281 – 34464FHAPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili165 – 19632Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi62 – 192131Arg-richAdd
    BLAST
    Compositional biasi385 – 3928Poly-Glu

    Sequence similaritiesi

    Contains 1 FHA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG271234.
    HOGENOMiHOG000264922.
    HOVERGENiHBG056615.
    InParanoidiQ8TAD8.
    KOiK13108.
    OMAiGQEHRRA.
    OrthoDBiEOG7P02K5.
    PhylomeDBiQ8TAD8.
    TreeFamiTF312797.

    Family and domain databases

    Gene3Di2.60.200.20. 1 hit.
    InterProiIPR000253. FHA_dom.
    IPR008984. SMAD_FHA_domain.
    [Graphical view]
    PfamiPF00498. FHA. 1 hit.
    [Graphical view]
    SMARTiSM00240. FHA. 1 hit.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.
    PROSITEiPS50006. FHA_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8TAD8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKAVKSERER GSRRRHRDGD VVLPAGVVVK QERLSPEVAP PAHRRPDHSG    50
    GSPSPPTSEP ARSGHRGNRA RGVSRSPPKK KNKASGRRSK SPRSKRNRSP 100
    HHSTVKVKQE REDHPRRGRE DRQHREPSEQ EHRRARNSDR DRHRGHSHQR 150
    RTSNERPGSG QGQGRDRDTQ NLQAQEEERE FYNARRREHR QRNDVGGGGS 200
    ESQELVPRPG GNNKEKEVPA KEKPSFELSG ALLEDTNTFR GVVIKYSEPP 250
    EARIPKKRWR LYPFKNDEVL PVMYIHRQSA YLLGRHRRIA DIPIDHPSCS 300
    KQHAVFQYRL VEYTRADGTV GRRVKPYIID LGSGNGTFLN NKRIEPQRYY 350
    ELKEKDVLKF GFSSREYVLL HESSDTSEID RKDDEDEEEE EEVSDS 396
    Length:396
    Mass (Da):45,778
    Last modified:June 1, 2002 - v1
    Checksum:iB183F83EC3184676
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti181 – 1811F → S in BAB55241. (PubMed:14702039)Curated
    Sequence conflicti364 – 3641S → I in BAB14134. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti366 – 3661E → G in PMRED. 1 Publication
    VAR_067542

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY081909 mRNA. Translation: AAL91140.1.
    AK022615 mRNA. Translation: BAB14134.1.
    AK027622 mRNA. Translation: BAB55241.1.
    BC027040 mRNA. Translation: AAH27040.1.
    CCDSiCCDS419.1.
    RefSeqiNP_078976.2. NM_024700.3.
    UniGeneiHs.47232.

    Genome annotation databases

    EnsembliENST00000296215; ENSP00000296215; ENSG00000163877.
    GeneIDi79753.
    KEGGihsa:79753.
    UCSCiuc001cbi.4. human.

    Polymorphism databases

    DMDMi48428655.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY081909 mRNA. Translation: AAL91140.1 .
    AK022615 mRNA. Translation: BAB14134.1 .
    AK027622 mRNA. Translation: BAB55241.1 .
    BC027040 mRNA. Translation: AAH27040.1 .
    CCDSi CCDS419.1.
    RefSeqi NP_078976.2. NM_024700.3.
    UniGenei Hs.47232.

    3D structure databases

    ProteinModelPortali Q8TAD8.
    SMRi Q8TAD8. Positions 246-374.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122864. 27 interactions.
    DIPi DIP-38956N.
    IntActi Q8TAD8. 41 interactions.
    MINTi MINT-1181692.
    STRINGi 9606.ENSP00000296215.

    PTM databases

    PhosphoSitei Q8TAD8.

    Polymorphism databases

    DMDMi 48428655.

    Proteomic databases

    MaxQBi Q8TAD8.
    PaxDbi Q8TAD8.
    PRIDEi Q8TAD8.

    Protocols and materials databases

    DNASUi 79753.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296215 ; ENSP00000296215 ; ENSG00000163877 .
    GeneIDi 79753.
    KEGGi hsa:79753.
    UCSCi uc001cbi.4. human.

    Organism-specific databases

    CTDi 79753.
    GeneCardsi GC01M038002.
    HGNCi HGNC:30587. SNIP1.
    HPAi HPA036896.
    MIMi 608241. gene.
    614501. phenotype.
    neXtProti NX_Q8TAD8.
    PharmGKBi PA142670893.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271234.
    HOGENOMi HOG000264922.
    HOVERGENi HBG056615.
    InParanoidi Q8TAD8.
    KOi K13108.
    OMAi GQEHRRA.
    OrthoDBi EOG7P02K5.
    PhylomeDBi Q8TAD8.
    TreeFami TF312797.

    Enzyme and pathway databases

    SignaLinki Q8TAD8.

    Miscellaneous databases

    ChiTaRSi SNIP1. human.
    GeneWikii SNIP1.
    GenomeRNAii 79753.
    NextBioi 69203.
    PROi Q8TAD8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TAD8.
    Bgeei Q8TAD8.
    CleanExi HS_SNIP1.
    Genevestigatori Q8TAD8.

    Family and domain databases

    Gene3Di 2.60.200.20. 1 hit.
    InterProi IPR000253. FHA_dom.
    IPR008984. SMAD_FHA_domain.
    [Graphical view ]
    Pfami PF00498. FHA. 1 hit.
    [Graphical view ]
    SMARTi SM00240. FHA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    PROSITEi PS50006. FHA_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel Smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-beta signal transduction."
      Kim R.H., Wang D., Tsang M., Martin J., Huff C., de Caestecker M.P., Parks T.W., Meng X., Lechleider R.J., Wang T., Roberts A.B.
      Genes Dev. 14:1605-1616(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SMAD4 AND CREBBP/EP300, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Embryonic kidney.
    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].
      Tissue: Teratocarcinoma.
    3. "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: Testis.
    4. "SNIP1 inhibits NF-kappa B signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators."
      Kim R.H., Flanders K.C., Birkey Reffey S., Anderson L.A., Duckett C.S., Perkins N.D., Roberts A.B.
      J. Biol. Chem. 276:46297-46304(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CREBBP AND EP300.
    5. "A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs)."
      Lin Y., Martin J., Gruendler C., Farley J., Meng X., Li B.-Y., Lechleider R., Huff C., Kim R.H., Grasser W.A., Paralkar V., Wang T.
      BMC Cell Biol. 3:15-15(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THE SMAD1/OAZ1/PSMB4 COMPLEX, DEGRADATION BY THE PROTEASOME.
    6. "The FHA domain protein SNIP1 is a regulator of the cell cycle and cyclin D1 expression."
      Roche K.C., Wiechens N., Owen-Hughes T., Perkins N.D.
      Oncogene 23:8185-8195(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SMARCA4.
    7. "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-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: SUMOYLATION AT LYS-30, MUTAGENESIS OF LYS-30.
    9. Cited for: FUNCTION, IDENTIFICATION IN THE SNARP COMPLEX.
    10. "The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act in small RNA biogenesis."
      Yu B., Bi L., Zheng B., Ji L., Chevalier D., Agarwal M., Ramachandran V., Li W., Lagrange T., Walker J.C., Chen X.
      Proc. Natl. Acad. Sci. U.S.A. 105:10073-10078(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DROSHA.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-52 AND SER-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "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-35 AND SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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-35 AND SER-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: VARIANT PMRED GLY-366.

    Entry informationi

    Entry nameiSNIP1_HUMAN
    AccessioniPrimary (citable) accession number: Q8TAD8
    Secondary accession number(s): Q96SP9, Q9H9T7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 108 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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