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P49755

- TMEDA_HUMAN

UniProt

P49755 - TMEDA_HUMAN

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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

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. 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
Complete GO annotation...

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. extracellular vesicular exosome Source: UniProt
  6. gamma-secretase complex Source: UniProtKB
  7. Golgi apparatus Source: UniProtKB
  8. Golgi membrane Source: GOC
  9. integral component of membrane Source: HGNC
  10. plasma membrane Source: UniProtKB
  11. secretory granule membrane Source: UniProtKB
  12. trans-Golgi network transport vesicle Source: UniProtKB
  13. zymogen granule membrane Source: HGNC
Complete GO annotation...

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. 3 Publications
Mutagenesisi211 – 2122FF → AA: No decrease in binding to COPG1. Disrupts interaction with SEC23A. 3 Publications
Mutagenesisi215 – 2162KK → AA: Disrupts interaction with COPG1 and association with coatomer; when associated with 211-A-A-212. 3 Publications
Mutagenesisi215 – 2162KK → AA: Significant reduction in binding to COPG1. 3 Publications

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

BgeeiP49755.
CleanExiHS_TMED10.
ExpressionAtlasiP49755. baseline and differential.
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. 39 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.
GeneTreeiENSGT00550000074954.
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

        10         20         30         40         50
MSGLSGPPAR RGPFPLALLL LFLLGPRLVL AISFHLPINS RKCLREEIHK
60 70 80 90 100
DLLVTGAYEI SDQSGGAGGL RSHLKITDSA GHILYSKEDA TKGKFAFTTE
110 120 130 140 150
DYDMFEVCFE SKGTGRIPDQ LVILDMKHGV EAKNYEEIAK VEKLKPLEVE
160 170 180 190 200
LRRLEDLSES IVNDFAYMKK REEEMRDTNE STNTRVLYFS IFSMFCLIGL
210
ATWQVFYLRR FFKAKKLIE
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. 39 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.
GeneTreei ENSGT00550000074954.
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

Bgeei P49755.
CleanExi HS_TMED10.
ExpressionAtlasi P49755. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 142 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