Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P57678

- GEMI4_HUMAN

UniProt

P57678 - GEMI4_HUMAN

Protein

Gem-associated protein 4

Gene

GEMIN4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (08 Feb 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. ncRNA metabolic process Source: Reactome
    3. RNA metabolic process Source: Reactome
    4. rRNA processing Source: ProtInc
    5. spliceosomal snRNP assembly Source: UniProtKB

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Enzyme and pathway databases

    ReactomeiREACT_11066. snRNP Assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gem-associated protein 4
    Short name:
    Gemin-4
    Alternative name(s):
    Component of gems 4
    p97
    Gene namesi
    Name:GEMIN4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:15717. GEMIN4.

    Subcellular locationi

    Cytoplasm. Nucleus. Nucleusnucleolus. Nucleusgem
    Note: Localized in subnuclear structures next to coiled bodies, called gems, which are highly enriched in spliceosomal snRNPs and in the nucleolus.

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. Gemini of coiled bodies Source: UniProtKB-SubCell
    5. membrane Source: UniProtKB
    6. nucleolus Source: ProtInc
    7. nucleoplasm Source: Reactome
    8. small nuclear ribonucleoprotein complex Source: ProtInc
    9. SMN complex Source: UniProtKB
    10. SMN-Sm protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10581058Gem-associated protein 4PRO_0000087459Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei205 – 2051Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP57678.
    PaxDbiP57678.
    PRIDEiP57678.

    PTM databases

    PhosphoSiteiP57678.

    Expressioni

    Gene expression databases

    ArrayExpressiP57678.
    BgeeiP57678.
    CleanExiHS_GEMIN4.
    GenevestigatoriP57678.

    Interactioni

    Subunit structurei

    Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN3 and with several snRNP SM core proteins, including SNRPB, SNRPD1, SNRPD2, SNRPD3 and SNRPE. Interacts with PPP4R2.2 Publications

    Protein-protein interaction databases

    BioGridi119102. 61 interactions.
    IntActiP57678. 22 interactions.
    MINTiMINT-124789.
    STRINGi9606.ENSP00000321706.

    Structurei

    3D structure databases

    ProteinModelPortaliP57678.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni714 – 73522Leucine-zipperSequence AnalysisAdd
    BLAST

    Phylogenomic databases

    eggNOGiNOG81539.
    HOGENOMiHOG000143409.
    HOVERGENiHBG051720.
    InParanoidiP57678.
    KOiK13132.
    OMAiYIFASEK.
    OrthoDBiEOG7MKW5F.
    PhylomeDBiP57678.
    TreeFamiTF329445.

    Sequencei

    Sequence statusi: Complete.

    P57678-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLGPLNICE EMTILHGGFL LAEQLFHPKA LAELTKSDWE RVGRPIVEAL     50
    REISSAAAHS QPFAWKKKAL IIIWAKVLQP HPVTPSDTET RWQEDLFFSV 100
    GNMIPTINHT ILFELLKSLE ASGLFIQLLM ALPTTICHAE LERFLEHVTV 150
    DTSAEDVAFF LDVWWEVMKH KGHPQDPLLS QFSAMAHKYL PALDEFPHPP 200
    KRLRSDPDAC PTMPLLAMLL RGLTQIQSRI LGPGRKCCAL ANLADMLTVF 250
    ALTEDDPQEV SATVYLDKLA TVISVWNSDT QNPYHQQALA EKVKEAERDV 300
    SLTSLAKLPS ETIFVGCEFL HHLLREWGEE LQAVLRSSQG TSYDSYRLCD 350
    SLTSFSQNAT LYLNRTSLSK EDRQVVSELA ECVRDFLRKT STVLKNRALE 400
    DITASIAMAV IQQKMDRHME VCYIFASEKK WAFSDEWVAC LGSNRALFRQ 450
    PDLVLRLLET VIDVSTADRA IPESQIRQVI HLILECYADL SLPGKNKVLA 500
    GILRSWGRKG LSEKLLAYVE GFQEDLNTTF NQLTQSASEQ GLAKAVASVA 550
    RLVIVHPEVT VKKMCSLAVV NLGTHKFLAQ ILTAFPALRF VEEQGPNSSA 600
    TFMVSCLKET VWMKFSTPKE EKQFLELLNC LMSPVKPQGI PVAALLEPDE 650
    VLKEFVLPFL RLDVEEVDLS LRIFIQTLEA NACREEYWLQ TCSPFPLLFS 700
    LCQLLDRFSK YWQLPKEKRC LSLDRKDLAI HILELLCEIV SANAETFSPD 750
    VWIKSLSWLH RKLEQLDWTV GLRLKSFFEG HFKCEVPATL FEICKLSEDE 800
    WTSQAHPGYG AGTGLLAWME CCCVSSGISE RMLSLLVVDV GNPEEVRLFS 850
    KGFLVALVQV MPWCSPQEWQ RLHQLTRRLL EKQLLHVPYS LEYIQFVPLL 900
    NLKPFAQELQ LSVLFLRTFQ FLCSHSCRDW LPLEGWNHVV KLLCGSLTRL 950
    LDSVRAIQAA GPWVQGPEQD LTQEALFVYT QVFCHALHIM AMLHPEVCEP 1000
    LYVLALETLT CYETLSKTNP SVSSLLQRAH EQRFLKSIAE GIGPEERRQT 1050
    LLQKMSSF 1058
    Length:1,058
    Mass (Da):120,037
    Last modified:February 8, 2011 - v2
    Checksum:iACEC60EC19EF5081
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti163 – 1631V → I in AAF35283. (PubMed:10725331)Curated
    Sequence conflicti450 – 4501Q → E in AAF35283. (PubMed:10725331)Curated
    Sequence conflicti450 – 4501Q → E in CAB45743. (PubMed:11230166)Curated
    Sequence conflicti593 – 5931E → V in AAF35283. (PubMed:10725331)Curated
    Sequence conflicti593 – 5931E → V in CAB45743. (PubMed:11230166)Curated
    Sequence conflicti713 – 7131Q → P in AAF35283. (PubMed:10725331)Curated
    Sequence conflicti929 – 9291D → N in AAF35283. (PubMed:10725331)Curated
    Sequence conflicti929 – 9291D → N in CAB45755. (PubMed:11230166)Curated
    Sequence conflicti929 – 9291D → N in CAB45743. (PubMed:11230166)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti182 – 1821F → L.
    Corresponds to variant rs34604548 [ dbSNP | Ensembl ].
    VAR_056891
    Natural varianti502 – 5021I → V.
    Corresponds to variant rs34616851 [ dbSNP | Ensembl ].
    VAR_056892
    Natural varianti579 – 5791A → G.
    Corresponds to variant rs910925 [ dbSNP | Ensembl ].
    VAR_024317
    Natural varianti684 – 6841R → Q.
    Corresponds to variant rs3744741 [ dbSNP | Ensembl ].
    VAR_021971
    Natural varianti739 – 7391I → T.
    Corresponds to variant rs1062923 [ dbSNP | Ensembl ].
    VAR_056893
    Natural varianti749 – 7491P → L.
    Corresponds to variant rs8078660 [ dbSNP | Ensembl ].
    VAR_056894
    Natural varianti782 – 7821F → L.
    Corresponds to variant rs34452716 [ dbSNP | Ensembl ].
    VAR_056895
    Natural varianti824 – 8241V → F.
    Corresponds to variant rs34936176 [ dbSNP | Ensembl ].
    VAR_056896
    Natural varianti913 – 9131V → I.
    Corresponds to variant rs34610323 [ dbSNP | Ensembl ].
    VAR_056897
    Natural varianti1033 – 10331R → C.
    Corresponds to variant rs7813 [ dbSNP | Ensembl ].
    VAR_020390

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF173856 mRNA. Translation: AAF35283.1.
    AC087392 Genomic DNA. No translation available.
    AL080150 mRNA. Translation: CAB45743.3.
    AL080167 mRNA. Translation: CAB45755.1.
    CCDSiCCDS45559.1.
    PIRiT12535.
    RefSeqiNP_056536.2. NM_015721.2.
    UniGeneiHs.499620.

    Genome annotation databases

    EnsembliENST00000319004; ENSP00000321706; ENSG00000179409.
    GeneIDi50628.
    KEGGihsa:50628.
    UCSCiuc002frs.1. human.

    Polymorphism databases

    DMDMi322510030.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF173856 mRNA. Translation: AAF35283.1 .
    AC087392 Genomic DNA. No translation available.
    AL080150 mRNA. Translation: CAB45743.3 .
    AL080167 mRNA. Translation: CAB45755.1 .
    CCDSi CCDS45559.1.
    PIRi T12535.
    RefSeqi NP_056536.2. NM_015721.2.
    UniGenei Hs.499620.

    3D structure databases

    ProteinModelPortali P57678.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119102. 61 interactions.
    IntActi P57678. 22 interactions.
    MINTi MINT-124789.
    STRINGi 9606.ENSP00000321706.

    PTM databases

    PhosphoSitei P57678.

    Polymorphism databases

    DMDMi 322510030.

    Proteomic databases

    MaxQBi P57678.
    PaxDbi P57678.
    PRIDEi P57678.

    Protocols and materials databases

    DNASUi 50628.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319004 ; ENSP00000321706 ; ENSG00000179409 .
    GeneIDi 50628.
    KEGGi hsa:50628.
    UCSCi uc002frs.1. human.

    Organism-specific databases

    CTDi 50628.
    GeneCardsi GC17M000693.
    H-InvDB HIX0013389.
    HGNCi HGNC:15717. GEMIN4.
    MIMi 606969. gene.
    neXtProti NX_P57678.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG81539.
    HOGENOMi HOG000143409.
    HOVERGENi HBG051720.
    InParanoidi P57678.
    KOi K13132.
    OMAi YIFASEK.
    OrthoDBi EOG7MKW5F.
    PhylomeDBi P57678.
    TreeFami TF329445.

    Enzyme and pathway databases

    Reactomei REACT_11066. snRNP Assembly.

    Miscellaneous databases

    GeneWikii GEMIN4.
    GenomeRNAii 50628.
    NextBioi 53160.
    PROi P57678.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P57678.
    Bgeei P57678.
    CleanExi HS_GEMIN4.
    Genevestigatori P57678.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Gemin4: a novel component of the SMN complex that is found in both gems and nucleoli."
      Charroux B., Pellizzoni L., Perkinson R.A., Yong J., Shevchenko A., Mann M., Dreyfuss G.
      J. Cell Biol. 148:1177-1186(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY.
    2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 186-1058.
      Tissue: Testis.
    4. "Protein phosphatase 4 interacts with the survival of motor neurons complex and enhances the temporal localisation of snRNPs."
      Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W., Philp A., Lamond A.I., Cohen P.T.W.
      J. Cell Sci. 116:1905-1913(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP4R2.
    5. "An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
      Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
      Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN SMN-SM COMPLEX.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGEMI4_HUMAN
    AccessioniPrimary (citable) accession number: P57678
    Secondary accession number(s): Q9NZS7, Q9UG32, Q9Y4Q2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 118 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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

    External Data

    Dasty 3