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Q9BVK6

- TMED9_HUMAN

UniProt

Q9BVK6 - TMED9_HUMAN

Protein

Transmembrane emp24 domain-containing protein 9

Gene

TMED9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Appears to be involved in vesicular protein trafficking, mainly in the early secretory pathway. In COPI vesicle-mediated retrograde transport involved in the coatomer recruitment to membranes of the early secretory pathway. Increases coatomer-dependent activity of ARFGAP2. Thought to play a crucial role in the specific retention of p24 complexes in cis-Golgi membranes; specifically contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. May be involved in organization of intracellular membranes, such as of the ER-Golgi intermediate compartment and the Golgi apparatus. Involved in ER localization of PTPN2 isoform PTPB.5 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. syntaxin binding Source: UniProtKB

    GO - Biological processi

    1. COPI coating of Golgi vesicle Source: UniProtKB
    2. Golgi organization Source: UniProtKB
    3. positive regulation of organelle organization Source: UniProtKB
    4. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transmembrane emp24 domain-containing protein 9
    Alternative name(s):
    GMP25
    Glycoprotein 25L2
    p24 family protein alpha-2
    Short name:
    p24alpha2
    p25
    Gene namesi
    Name:TMED9
    Synonyms:GP25L2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:24878. TMED9.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
    3. endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB-SubCell
    4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi apparatus Source: UniProtKB
    7. Golgi membrane Source: GOC
    8. integral component of membrane Source: UniProtKB-KW
    9. trans-Golgi network transport vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi232 – 2332KK → SS: Localization to plasma membrane and endocytosis. 1 Publication

    Organism-specific databases

    PharmGKBiPA134881976.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3737By similarityAdd
    BLAST
    Chaini38 – 235198Transmembrane emp24 domain-containing protein 9PRO_0000010396Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi125 – 1251N-linked (GlcNAc...)3 Publications
    Modified residuei160 – 1601N6-acetyllysineBy similarity

    Post-translational modificationi

    N-linked glycosylated containing high mannose.3 Publications

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    MaxQBiQ9BVK6.
    PaxDbiQ9BVK6.
    PRIDEiQ9BVK6.

    PTM databases

    PhosphoSiteiQ9BVK6.

    Expressioni

    Gene expression databases

    BgeeiQ9BVK6.
    CleanExiHS_TMED9.
    GenevestigatoriQ9BVK6.

    Organism-specific databases

    HPAiHPA014650.

    Interactioni

    Subunit structurei

    Monomer and homodimer in endoplasmic reticulum. Predominantly monomeric and to lesser extent homodimeric in endoplasmic reticulum-Golgi intermediate compartment and cis-Golgi network. Probably oligomerizes with other members of the EMP24/GP25L family such as TMED2, TMED7 and TMED10. Interacts with TMED5. Interacts (via C-terminus) with COPG1; the interaction involves dimeric TMED9. Interacts with PTPN2 and SPAST. Interacts with STX17; the interaction is direct.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PTPN2P17706-15EBI-1056827,EBI-4409481

    Protein-protein interaction databases

    BioGridi120115. 36 interactions.
    IntActiQ9BVK6. 20 interactions.
    MINTiMINT-5001958.
    STRINGi9606.ENSP00000330945.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BVK6.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini38 – 202165LumenalSequence AnalysisAdd
    BLAST
    Topological domaini223 – 23513CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei203 – 22220HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini47 – 14599GOLDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni121 – 16040Required for interaction with STX17Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili154 – 18431Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi228 – 2358COPI vesicle coat-bindingSequence Analysis
    Motifi228 – 2292COPII vesicle coat-bindingSequence Analysis

    Sequence similaritiesi

    Belongs to the EMP24/GP25L family.Curated
    Contains 1 GOLD domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG323830.
    HOGENOMiHOG000160228.
    HOVERGENiHBG105357.
    InParanoidiQ9BVK6.
    OMAiVLWWSIV.
    OrthoDBiEOG74BJT2.
    PhylomeDBiQ9BVK6.
    TreeFamiTF314123.

    Family and domain databases

    InterProiIPR009038. GOLD.
    IPR015720. TMP21-related.
    [Graphical view]
    PANTHERiPTHR22811. PTHR22811. 1 hit.
    PfamiPF01105. EMP24_GP25L. 1 hit.
    [Graphical view]
    PROSITEiPS50866. GOLD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9BVK6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVELGVLLV RPRPGTGLGR VMRTLLLVLW LATRGSALYF HIGETEKKCF    50
    IEEIPDETMV IGNYRTQLYD KQREEYQPAT PGLGMFVEVK DPEDKVILAR 100
    QYGSEGRFTF TSHTPGEHQI CLHSNSTKFS LFAGGMLRVH LDIQVGEHAN 150
    DYAEIAAKDK LSELQLRVRQ LVEQVEQIQK EQNYQRWREE RFRQTSESTN 200
    QRVLWWSILQ TLILVAIGVW QMRHLKSFFE AKKLV 235
    Length:235
    Mass (Da):27,277
    Last modified:June 16, 2009 - v2
    Checksum:i9B6D2D517D9E77D8
    GO

    Sequence cautioni

    The sequence AAL35268.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA62380.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 831L → F in CAA62380. (PubMed:15489334)Curated
    Sequence conflicti86 – 861F → C in CAA62380. (PubMed:15489334)Curated
    Sequence conflicti101 – 1011Q → E in CAA62380. (PubMed:15489334)Curated
    Sequence conflicti102 – 1021Y → C in AAL35268. 1 PublicationCurated
    Sequence conflicti156 – 1561A → P in CAA62380. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161T → S.
    Corresponds to variant rs57960711 [ dbSNP | Ensembl ].
    VAR_061178

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC139795 Genomic DNA. No translation available.
    BC001123 mRNA. Translation: AAH01123.2.
    X90872 mRNA. Translation: CAA62380.1. Different initiation.
    AF441399 mRNA. Translation: AAL35268.1. Different initiation.
    CCDSiCCDS4428.1.
    RefSeqiNP_059980.2. NM_017510.4.
    UniGeneiHs.279929.

    Genome annotation databases

    EnsembliENST00000332598; ENSP00000330945; ENSG00000184840.
    GeneIDi54732.
    KEGGihsa:54732.
    UCSCiuc003mhx.3. human.

    Polymorphism databases

    DMDMi239938724.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC139795 Genomic DNA. No translation available.
    BC001123 mRNA. Translation: AAH01123.2 .
    X90872 mRNA. Translation: CAA62380.1 . Different initiation.
    AF441399 mRNA. Translation: AAL35268.1 . Different initiation.
    CCDSi CCDS4428.1.
    RefSeqi NP_059980.2. NM_017510.4.
    UniGenei Hs.279929.

    3D structure databases

    ProteinModelPortali Q9BVK6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120115. 36 interactions.
    IntActi Q9BVK6. 20 interactions.
    MINTi MINT-5001958.
    STRINGi 9606.ENSP00000330945.

    PTM databases

    PhosphoSitei Q9BVK6.

    Polymorphism databases

    DMDMi 239938724.

    Proteomic databases

    MaxQBi Q9BVK6.
    PaxDbi Q9BVK6.
    PRIDEi Q9BVK6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000332598 ; ENSP00000330945 ; ENSG00000184840 .
    GeneIDi 54732.
    KEGGi hsa:54732.
    UCSCi uc003mhx.3. human.

    Organism-specific databases

    CTDi 54732.
    GeneCardsi GC05P177019.
    H-InvDB HIX0005470.
    HGNCi HGNC:24878. TMED9.
    HPAi HPA014650.
    neXtProti NX_Q9BVK6.
    PharmGKBi PA134881976.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG323830.
    HOGENOMi HOG000160228.
    HOVERGENi HBG105357.
    InParanoidi Q9BVK6.
    OMAi VLWWSIV.
    OrthoDBi EOG74BJT2.
    PhylomeDBi Q9BVK6.
    TreeFami TF314123.

    Miscellaneous databases

    ChiTaRSi TMED9. human.
    GenomeRNAii 54732.
    NextBioi 57312.
    PROi Q9BVK6.

    Gene expression databases

    Bgeei Q9BVK6.
    CleanExi HS_TMED9.
    Genevestigatori Q9BVK6.

    Family and domain databases

    InterProi IPR009038. GOLD.
    IPR015720. TMP21-related.
    [Graphical view ]
    PANTHERi PTHR22811. PTHR22811. 1 hit.
    Pfami PF01105. EMP24_GP25L. 1 hit.
    [Graphical view ]
    PROSITEi PS50866. GOLD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "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: Skin.
    3. Dominguez M., Fazel A., Parlati F., Bell A.W., Thomas D.Y., Bergeron J.J.M.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-235.
      Tissue: Liver.
    4. "A novel human cDNA that shares sequence homology with Homo sapiens mRNAs LOC96645 and gp25L2."
      Wang C., Li Y.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-235.
    5. Bienvenut W.V.
      Submitted (MAR-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 129-138 AND 170-180, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    6. "Localization and recycling of gp27 (hp24gamma3): complex formation with other p24 family members."
      Fullekrug J., Suganuma T., Tang B.L., Hong W., Storrie B., Nilsson T.
      Mol. Biol. Cell 10:1939-1955(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, SUBUNIT.
    7. "Coupled transport of p24 family members."
      Emery G., Rojo M., Gruenberg J.
      J. Cell Sci. 113:2507-2516(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Oligomeric state and stoichiometry of p24 proteins in the early secretory pathway."
      Jenne N., Frey K., Brugger B., Wieland F.T.
      J. Biol. Chem. 277:46504-46511(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT.
    9. "The trans-membrane protein p25 forms highly specialized domains that regulate membrane composition and dynamics."
      Emery G., Parton R.G., Rojo M., Gruenberg J.
      J. Cell Sci. 116:4821-4832(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 232-LYS-LYS-233.
    10. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
      Zhang H., Li X.-J., Martin D.B., Aebersold R.
      Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-125.
    11. "The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B."
      Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E., Sanderson C.M.
      Hum. Mol. Genet. 14:19-38(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPAST.
    12. "Evidence for a role of transmembrane protein p25 in localization of protein tyrosine phosphatase TC48 to the ER."
      Gupta V., Swarup G.
      J. Cell Sci. 119:1703-1714(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PTPN2.
    13. "Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins."
      Bethune J., Kol M., Hoffmann J., Reckmann I., Brugger B., Wieland F.
      Mol. Cell. Biol. 26:8011-8021(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COPG1.
    14. "The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53, and p25 are required to maintain the architecture of ERGIC and Golgi."
      Mitrovic S., Ben-Tekaya H., Koegler E., Gruenberg J., Hauri H.-P.
      Mol. Biol. Cell 19:1976-1990(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Arf GAP2 is positively regulated by coatomer and cargo."
      Luo R., Ha V.L., Hayashi R., Randazzo P.A.
      Cell. Signal. 21:1169-1179(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125.
      Tissue: Liver.
    17. "p28, a novel ERGIC/cis Golgi protein, required for Golgi ribbon formation."
      Koegler E., Bonnon C., Waldmeier L., Mitrovic S., Halbeisen R., Hauri H.P.
      Traffic 11:70-89(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMED5.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Syntaxin 17 cycles between the ER and ERGIC and is required to maintain the architecture of ERGIC and Golgi."
      Muppirala M., Gupta V., Swarup G.
      Biol. Cell 103:333-350(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STX17.

    Entry informationi

    Entry nameiTMED9_HUMAN
    AccessioniPrimary (citable) accession number: Q9BVK6
    Secondary accession number(s): Q14437, Q8WZ61
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 111 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3