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P49755

- TMEDA_HUMAN

UniProt

P49755 - TMEDA_HUMAN

Protein

Transmembrane emp24 domain-containing protein 10

Gene

TMED10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1 By similarity. In COPI vesicle-mediated retrograde transport involved in the biogenesis of COPI vesicles and vesicle coat recruitment. On Golgi membranes, acts as primary receptor for ARF1-GDP which is involved in COPI-vesicle formation. Increases coatomer-dependent GTPase-activating activity of ARFGAP2. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2LR1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent of modulation of gamma-secretase activity). As part of the presenilin-dependent gamma-secretase complex regulates gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40 (Abeta40). Involved in organization of the Golgi apparatus.By similarity7 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. beta-amyloid formation Source: UniProtKB
    2. cargo loading into vesicle Source: UniProtKB
    3. COPI-coated vesicle budding Source: UniProtKB
    4. COPI coating of Golgi vesicle Source: UniProtKB
    5. COPII vesicle coating Source: UniProtKB
    6. ER to Golgi vesicle-mediated transport Source: UniProtKB
    7. Golgi organization Source: Ensembl
    8. intracellular protein transport Source: UniProtKB
    9. kidney development Source: Ensembl
    10. protein oligomerization Source: Ensembl
    11. regulated secretory pathway Source: HGNC
    12. response to acid chemical Source: Ensembl
    13. response to alkaloid Source: Ensembl
    14. retrograde vesicle-mediated transport, Golgi to ER Source: UniProtKB
    15. vesicle targeting, to, from or within Golgi Source: HGNC

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transmembrane emp24 domain-containing protein 10
    Alternative name(s):
    21 kDa transmembrane-trafficking protein
    S31III125
    Short name:
    S31I125
    Tmp-21-I
    Transmembrane protein Tmp21
    p23
    p24 family protein delta-1
    Short name:
    p24delta1
    p24delta
    Gene namesi
    Name:TMED10
    Synonyms:TMP21
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:16998. TMED10.

    Subcellular locationi

    GO - Cellular componenti

    1. cis-Golgi network Source: HGNC
    2. COPI-coated vesicle Source: UniProtKB
    3. endoplasmic reticulum Source: UniProtKB
    4. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
    5. endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB-SubCell
    6. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    7. extracellular vesicular exosome Source: UniProt
    8. gamma-secretase complex Source: UniProtKB
    9. Golgi apparatus Source: UniProtKB
    10. Golgi membrane Source: GOC
    11. integral component of membrane Source: HGNC
    12. melanosome Source: UniProtKB-SubCell
    13. plasma membrane Source: UniProtKB
    14. secretory granule membrane Source: UniProtKB
    15. trans-Golgi network transport vesicle Source: UniProtKB
    16. transport vesicle membrane Source: UniProtKB-SubCell
    17. zymogen granule membrane Source: HGNC

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi211 – 2122FF → AA: Disrupts interaction with COPG1 and association with coatomer; when associated with 215-A-A-216.
    Mutagenesisi211 – 2122FF → AA: No decrease in binding to COPG1. Disrupts interaction with SEC23A.
    Mutagenesisi215 – 2162KK → AA: Disrupts interaction with COPG1 and association with coatomer; when associated with 211-A-A-212.
    Mutagenesisi215 – 2162KK → AA: Significant reduction in binding to COPG1.

    Organism-specific databases

    PharmGKBiPA128394579.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 31311 PublicationAdd
    BLAST
    Chaini32 – 219188Transmembrane emp24 domain-containing protein 10PRO_0000010399Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei171 – 1711Omega-N-methylated arginineBy similarity
    Modified residuei176 – 1761Omega-N-methylated arginineBy similarity
    Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein, Methylation

    Proteomic databases

    MaxQBiP49755.
    PaxDbiP49755.
    PeptideAtlasiP49755.
    PRIDEiP49755.

    PTM databases

    PhosphoSiteiP49755.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP49755.
    BgeeiP49755.
    CleanExiHS_TMED10.
    GenevestigatoriP49755.

    Organism-specific databases

    HPAiCAB034442.
    CAB037251.
    HPA047139.
    HPA050539.

    Interactioni

    Subunit structurei

    Predominantly homodimeric and to lesser extent monomeric in endoplasmic reticulum. Homodimer and monomer 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 TMED9. Interacts with TMED2. Associates with the COPI vesicle coat (coatomer); TMED10:TMED2 heterotetramers are proposed to be involved in coatomer association. Interacts (via C-terminus) with COPG1; the interaction involves dimeric TMED10. Interacts with ARF1 (GDP-bound); the interaction probably involves a TMED10 oligomer. Interacts with SEC23A; indicative for an association of TMED10 with the COPII vesicle coat. Interacts with CD59, SEC24B, SEC24C and SEC24D By similarity. Interacts with MPPE1/PGAP5. Interacts with F2LR1. Interacts with KDELR2; the interaction is disrupted by KDELR2 ligand By similarity. Found in a complex composed at least of SURF4, TMED2 and TMED10. Associates with the presenilin-dependent gamma-secretase complex. Interacts with STX17; the interaction is direct.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCSTNQ925425EBI-998422,EBI-998440
    PSEN1P497683EBI-998422,EBI-297277
    PSENENQ9NZ423EBI-998422,EBI-998468
    PTPN2P17706-15EBI-998422,EBI-4409481
    TMED2Q153637EBI-998422,EBI-998485

    Protein-protein interaction databases

    BioGridi116169. 31 interactions.
    IntActiP49755. 23 interactions.
    MINTiMINT-3017717.
    STRINGi9606.ENSP00000303145.

    Structurei

    3D structure databases

    ProteinModelPortaliP49755.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 185154LumenalSequence AnalysisAdd
    BLAST
    Topological domaini207 – 21913CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei186 – 20621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 193153GOLDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 142142Required for interaction with STX17Add
    BLAST
    Regioni147 – 17832Required for TMED10 and TMED2 cis-Golgi network localizationAdd
    BLAST
    Regioni204 – 21916Interaction with COPG1Add
    BLAST
    Regioni207 – 21913Interaction with ARF1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi211 – 2199COPI vesicle coat-binding
    Motifi211 – 2122COPII vesicle coat-binding

    Domaini

    The lumenal domain mediates localization to the plasma membrane by partially overriding the ER retention by the cytoplasmic domain.By similarity

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG323830.
    HOVERGENiHBG107275.
    InParanoidiP49755.
    OMAiILYAKED.
    OrthoDBiEOG7PZRZM.
    PhylomeDBiP49755.
    TreeFamiTF313729.

    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.

    P49755-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGLSGPPAR RGPFPLALLL LFLLGPRLVL AISFHLPINS RKCLREEIHK    50
    DLLVTGAYEI SDQSGGAGGL RSHLKITDSA GHILYSKEDA TKGKFAFTTE 100
    DYDMFEVCFE SKGTGRIPDQ LVILDMKHGV EAKNYEEIAK VEKLKPLEVE 150
    LRRLEDLSES IVNDFAYMKK REEEMRDTNE STNTRVLYFS IFSMFCLIGL 200
    ATWQVFYLRR FFKAKKLIE 219
    Length:219
    Mass (Da):24,976
    Last modified:December 15, 1998 - v2
    Checksum:i0A0486BE65C4DBBB
    GO

    Sequence cautioni

    The sequence AAC42003.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence CAD66561.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751K → R in CAD89913. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti64 – 641S → Y.
    Corresponds to variant rs4929 [ dbSNP | Ensembl ].
    VAR_012051
    Natural varianti152 – 1521R → G.
    Corresponds to variant rs17103066 [ dbSNP | Ensembl ].
    VAR_049111

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97442 mRNA. Translation: CAA66071.1.
    X97444 mRNA. Translation: CAA66073.1.
    U61734 Genomic DNA. Translation: AAB03625.1.
    L40397 mRNA. Translation: AAC42003.1. Frameshift.
    AJ004913 mRNA. Translation: CAA06213.1.
    BX248754 mRNA. Translation: CAD66561.1. Different initiation.
    AK312384 mRNA. Translation: BAG35302.1.
    AL832012 mRNA. Translation: CAD89913.1.
    AC007055 Genomic DNA. Translation: AAD31941.1.
    CH471061 Genomic DNA. Translation: EAW81223.1.
    BC001496 mRNA. Translation: AAH01496.1.
    BC001825 mRNA. Translation: AAH01825.1.
    CCDSiCCDS9840.1.
    PIRiG01159.
    RefSeqiNP_006818.3. NM_006827.5.
    UniGeneiHs.74137.

    Genome annotation databases

    EnsembliENST00000303575; ENSP00000303145; ENSG00000170348.
    GeneIDi10972.
    KEGGihsa:10972.
    UCSCiuc001xrm.1. human.

    Polymorphism databases

    DMDMi3915893.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97442 mRNA. Translation: CAA66071.1 .
    X97444 mRNA. Translation: CAA66073.1 .
    U61734 Genomic DNA. Translation: AAB03625.1 .
    L40397 mRNA. Translation: AAC42003.1 . Frameshift.
    AJ004913 mRNA. Translation: CAA06213.1 .
    BX248754 mRNA. Translation: CAD66561.1 . Different initiation.
    AK312384 mRNA. Translation: BAG35302.1 .
    AL832012 mRNA. Translation: CAD89913.1 .
    AC007055 Genomic DNA. Translation: AAD31941.1 .
    CH471061 Genomic DNA. Translation: EAW81223.1 .
    BC001496 mRNA. Translation: AAH01496.1 .
    BC001825 mRNA. Translation: AAH01825.1 .
    CCDSi CCDS9840.1.
    PIRi G01159.
    RefSeqi NP_006818.3. NM_006827.5.
    UniGenei Hs.74137.

    3D structure databases

    ProteinModelPortali P49755.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116169. 31 interactions.
    IntActi P49755. 23 interactions.
    MINTi MINT-3017717.
    STRINGi 9606.ENSP00000303145.

    PTM databases

    PhosphoSitei P49755.

    Polymorphism databases

    DMDMi 3915893.

    Proteomic databases

    MaxQBi P49755.
    PaxDbi P49755.
    PeptideAtlasi P49755.
    PRIDEi P49755.

    Protocols and materials databases

    DNASUi 10972.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303575 ; ENSP00000303145 ; ENSG00000170348 .
    GeneIDi 10972.
    KEGGi hsa:10972.
    UCSCi uc001xrm.1. human.

    Organism-specific databases

    CTDi 10972.
    GeneCardsi GC14M075598.
    HGNCi HGNC:16998. TMED10.
    HPAi CAB034442.
    CAB037251.
    HPA047139.
    HPA050539.
    MIMi 605406. gene.
    neXtProti NX_P49755.
    PharmGKBi PA128394579.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG323830.
    HOVERGENi HBG107275.
    InParanoidi P49755.
    OMAi ILYAKED.
    OrthoDBi EOG7PZRZM.
    PhylomeDBi P49755.
    TreeFami TF313729.

    Miscellaneous databases

    ChiTaRSi TMED10. human.
    GeneWikii TMED10.
    GenomeRNAii 10972.
    NextBioi 41690.
    PROi P49755.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49755.
    Bgeei P49755.
    CleanExi HS_TMED10.
    Genevestigatori P49755.

    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. "Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal membranes, are members of a protein family involved in vesicular trafficking."
      Blum R., Feick P., Puype M., Vandekerckhove J., Klengel R., Nastainczyk W., Schulz I.
      J. Biol. Chem. 271:17183-17189(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "New human gene, member of a large family implicated in protein trafficking."
      Sanseau P., Sherington R., Trower M.K., St George-Hyslop P.H., Dykes C.W.
      Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    4. "A comparative study of rat and human Tmp21 (p23) reveals the pseudogene-like features of human Tmp21-II."
      Hoerer J., Blum R., Feick P., Nastainczyk W., Schulz I.
      DNA Seq. 10:121-126(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pancreas.
    5. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Fetal brain.
    6. "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: Amygdala.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skeletal muscle.
    8. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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: Colon.
    11. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
      Xu G., Shin S.B., Jaffrey S.R.
      Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 32-42.
      Tissue: Leukemic T-cell.
    12. "gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer."
      Dominguez M., Dejgaard K., Fullekrug J., Dahan S., Fazel A., Paccaud J.P., Thomas D.Y., Bergeron J.J., Nilsson T.
      J. Cell Biol. 140:751-765(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH COPI AND COPII VESICLE COAT, MUTAGENESIS OF 211-PHE-PHE-212 AND 215-LYS-LYS-216.
    13. "Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors."
      Bremser M., Nickel W., Schweikert M., Ravazzola M., Amherdt M., Hughes C.A., Sollner T.H., Rothman J.E., Wieland F.T.
      Cell 96:495-506(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "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: SUBUNIT.
    15. "Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex."
      Goldberg J.
      Cell 100:671-679(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 211-PHE-PHE-212 AND 215-LYS-LYS-216.
    16. "Identification and characterization of novel isoforms of COP I subunits."
      Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.
      J. Biochem. 128:793-801(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COPG1, MUTAGENESIS OF 211-PHE-PHE-212 AND 215-LYS-LYS-216.
    17. "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: SUBCELLULAR LOCATION.
    18. "Recruitment to Golgi membranes of ADP-ribosylation factor 1 is mediated by the cytoplasmic domain of p23."
      Gommel D.U., Memon A.R., Heiss A., Lottspeich F., Pfannstiel J., Lechner J., Reinhard C., Helms J.B., Nickel W., Wieland F.T.
      EMBO J. 20:6751-6760(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ARF1.
    19. "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.
    20. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    21. "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.
    22. Cited for: FUNCTION, SUBUNIT.
    23. "Dual roles of the transmembrane protein p23/TMP21 in the modulation of amyloid precursor protein metabolism."
      Vetrivel K.S., Gong P., Bowen J.W., Cheng H., Chen Y., Carter M., Nguyen P.D., Placanica L., Wieland F.T., Li Y.M., Kounnas M.Z., Thinakaran G.
      Mol. Neurodegener. 2:4-4(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "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: IDENTIFICATION IN A COMPLEX WITH SURF4 AND TMED2.
    25. "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi."
      Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T.
      Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MPPE1.
    26. "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.
    27. "Selective export of human GPI-anchored proteins from the endoplasmic reticulum."
      Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.
      J. Cell Sci. 123:1705-1715(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "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.
    30. "Proteinase-activated receptors, nucleotide P2Y receptors, and mu-opioid receptor-1B are under the control of the type I transmembrane proteins p23 and p24A in post-Golgi trafficking."
      Luo W., Wang Y., Reiser G.
      J. Neurochem. 117:71-81(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH F2RL1.

    Entry informationi

    Entry nameiTMEDA_HUMAN
    AccessioniPrimary (citable) accession number: P49755
    Secondary accession number(s): B2R605
    , Q15602, Q16536, Q86TC2, Q86TS5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 141 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

    Miscellaneous

    Ectopic expression of TMED10 alone does not result in its proper cis-Golgi network localization. Coexpression of TMED2 is necessary, and coexpression of TMED3 and /or TMED9 is facilitating localization.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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