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P49755 (TMEDA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TMED10
Synonyms:TMP21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length219 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13 Ref.18 Ref.22 Ref.23 Ref.26 Ref.27 Ref.30

Subunit structure

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. Ref.14 Ref.16 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24 Ref.25 Ref.29 Ref.30

Subcellular location

Golgi apparatuscis-Golgi network membrane; Single-pass type I membrane protein. Melanosome. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Cytoplasmic vesiclesecretory vesicle membrane; Single-pass type I membrane protein By similarity. Cell membrane By similarity. Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein By similarity. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Cycles between compartments of the early secretatory pathway. Ref.12 Ref.17 Ref.19 Ref.20

Tissue specificity

Ubiquitous.

Domain

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

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.

Sequence similarities

Belongs to the EMP24/GP25L family.

Contains 1 GOLD domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processER-Golgi transport
Protein transport
Transport
   Cellular componentCell membrane
Cytoplasmic vesicle
Endoplasmic reticulum
Golgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Methylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCOPI coating of Golgi vesicle

Traceable author statement Ref.15. Source: UniProtKB

COPI-coated vesicle budding

Inferred from direct assay Ref.13. Source: UniProtKB

COPII vesicle coating

Traceable author statement Ref.27. Source: UniProtKB

ER to Golgi vesicle-mediated transport

Traceable author statement Ref.27. Source: UniProtKB

Golgi organization

Inferred from electronic annotation. Source: Ensembl

beta-amyloid formation

Inferred from mutant phenotype Ref.22. Source: UniProtKB

cargo loading into vesicle

Traceable author statement Ref.27. Source: UniProtKB

intracellular protein transport

Inferred from direct assay Ref.27. Source: UniProtKB

kidney development

Inferred from electronic annotation. Source: Ensembl

protein oligomerization

Inferred from electronic annotation. Source: Ensembl

regulated secretory pathway

Inferred from sequence or structural similarity. Source: HGNC

response to acid

Inferred from electronic annotation. Source: Ensembl

response to alkaloid

Inferred from electronic annotation. Source: Ensembl

retrograde vesicle-mediated transport, Golgi to ER

Inferred from sequence or structural similarity. Source: UniProtKB

vesicle targeting, to, from or within Golgi

Inferred from sequence or structural similarity. Source: HGNC

   Cellular_componentCOPI-coated vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi apparatus

Inferred from direct assay Ref.19. Source: UniProtKB

Golgi membrane

Inferred from direct assay Ref.13. Source: GOC

cis-Golgi network

Inferred from sequence or structural similarity. Source: HGNC

endoplasmic reticulum

Inferred from direct assay Ref.19. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum-Golgi intermediate compartment

Inferred from direct assay Ref.19. Source: UniProtKB

endoplasmic reticulum-Golgi intermediate compartment membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

gamma-secretase complex

Inferred from direct assay Ref.22. Source: UniProtKB

integral component of membrane

Inferred from sequence or structural similarity. Source: HGNC

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

secretory granule membrane

Inferred from sequence or structural similarity. Source: UniProtKB

trans-Golgi network transport vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

transport vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

zymogen granule membrane

Inferred from sequence or structural similarity. Source: HGNC

   Molecular_functionsyntaxin binding

Inferred from physical interaction Ref.29. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.11
Chain32 – 219188Transmembrane emp24 domain-containing protein 10
PRO_0000010399

Regions

Topological domain32 – 185154Lumenal Potential
Transmembrane186 – 20621Helical; Potential
Topological domain207 – 21913Cytoplasmic Potential
Domain41 – 193153GOLD
Region1 – 142142Required for interaction with STX17
Region147 – 17832Required for TMED10 and TMED2 cis-Golgi network localization
Region204 – 21916Interaction with COPG1
Region207 – 21913Interaction with ARF1
Motif211 – 2199COPI vesicle coat-binding
Motif211 – 2122COPII vesicle coat-binding

Amino acid modifications

Modified residue1711Omega-N-methylated arginine By similarity
Modified residue1761Omega-N-methylated arginine By similarity
Glycosylation1791N-linked (GlcNAc...) Potential

Natural variations

Natural variant641S → Y.
Corresponds to variant rs4929 [ dbSNP | Ensembl ].
VAR_012051
Natural variant1521R → G.
Corresponds to variant rs17103066 [ dbSNP | Ensembl ].
VAR_049111

Experimental info

Mutagenesis211 – 2122FF → AA: Disrupts interaction with COPG1 and association with coatomer; when associated with 215-A-A-216. Ref.12 Ref.15 Ref.16
Mutagenesis211 – 2122FF → AA: No decrease in binding to COPG1. Disrupts interaction with SEC23A. Ref.12 Ref.15 Ref.16
Mutagenesis215 – 2162KK → AA: Disrupts interaction with COPG1 and association with coatomer; when associated with 211-A-A-212. Ref.12 Ref.15 Ref.16
Mutagenesis215 – 2162KK → AA: Significant reduction in binding to COPG1. Ref.12 Ref.15 Ref.16
Sequence conflict751K → R in CAD89913. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P49755 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 0A0486BE65C4DBBB

FASTA21924,976
        10         20         30         40         50         60 
MSGLSGPPAR RGPFPLALLL LFLLGPRLVL AISFHLPINS RKCLREEIHK DLLVTGAYEI 

        70         80         90        100        110        120 
SDQSGGAGGL RSHLKITDSA GHILYSKEDA TKGKFAFTTE DYDMFEVCFE SKGTGRIPDQ 

       130        140        150        160        170        180 
LVILDMKHGV EAKNYEEIAK VEKLKPLEVE LRRLEDLSES IVNDFAYMKK REEEMRDTNE 

       190        200        210 
STNTRVLYFS IFSMFCLIGL ATWQVFYLRR FFKAKKLIE 

« Hide

References

« Hide 'large scale' references
[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]"Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease."
Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., Ikeda M., Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F., Bruni A.C., Montesi M.P., Sorbi S., Rainero I., Pinessi L. expand/collapse author list , Nee L., Chumakov I., Pollen D., Brookes A., Sanseau P., Polinsky R.J., Wasco W., da Silva H.A.R., Haines J.L., Pericak-Vance M.A., Tanzi R.E., Roses A.D., Fraser P.E., Rommens J.M., St George-Hyslop P.H.
Nature 375:754-760(1995) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
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]"TMP21 is a presenilin complex component that modulates gamma-secretase but not epsilon-secretase activity."
Chen F., Hasegawa H., Schmitt-Ulms G., Kawarai T., Bohm C., Katayama T., Gu Y., Sanjo N., Glista M., Rogaeva E., Wakutani Y., Pardossi-Piquard R., Ruan X., Tandon A., Checler F., Marambaud P., Hansen K., Westaway D., St George-Hyslop P., Fraser P.
Nature 440:1208-1212(2006) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRG01159.
RefSeqNP_006818.3. NM_006827.5.
UniGeneHs.74137.

3D structure databases

ProteinModelPortalP49755.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116169. 27 interactions.
IntActP49755. 23 interactions.
MINTMINT-3017717.
STRING9606.ENSP00000303145.

PTM databases

PhosphoSiteP49755.

Polymorphism databases

DMDM3915893.

Proteomic databases

PaxDbP49755.
PeptideAtlasP49755.
PRIDEP49755.

Protocols and materials databases

DNASU10972.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303575; ENSP00000303145; ENSG00000170348.
GeneID10972.
KEGGhsa:10972.
UCSCuc001xrm.1. human.

Organism-specific databases

CTD10972.
GeneCardsGC14M075598.
HGNCHGNC:16998. TMED10.
HPACAB034442.
CAB037251.
HPA047139.
HPA050539.
MIM605406. gene.
neXtProtNX_P49755.
PharmGKBPA128394579.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG323830.
HOVERGENHBG107275.
InParanoidP49755.
OMAVCFESKS.
OrthoDBEOG7PZRZM.
PhylomeDBP49755.
TreeFamTF313729.

Gene expression databases

ArrayExpressP49755.
BgeeP49755.
CleanExHS_TMED10.
GenevestigatorP49755.

Family and domain databases

InterProIPR009038. GOLD.
[Graphical view]
PfamPF01105. EMP24_GP25L. 1 hit.
[Graphical view]
PROSITEPS50866. GOLD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTMED10. human.
GeneWikiTMED10.
GenomeRNAi10972.
NextBio41690.
PROP49755.
SOURCESearch...

Entry information

Entry nameTMEDA_HUMAN
AccessionPrimary (citable) accession number: P49755
Secondary accession number(s): B2R605 expand/collapse secondary AC list , Q15602, Q16536, Q86TC2, Q86TS5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 15, 1998
Last modified: April 16, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM