P49755 (TMEDA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TMED10
Synonyms:	TMP21

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	219 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 togther 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.29
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. Ref.14 Ref.16 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24 Ref.25 Ref.29
Subcellular location	Golgi apparatus › cis-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 vesicle › secretory vesicle membrane; Single-pass type I membrane protein By similarity. Cell membrane By similarity. Golgi apparatus › trans-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 process	ER-Golgi transport Protein transport Transport
Cellular component	Cell membrane Cytoplasmic vesicle Endoplasmic reticulum Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
PTM	Glycoprotein Methylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	COPI coating of Golgi vesicle Traceable author statement Ref.15. Source: UniProtKB COPII vesicle coating Traceable author statement Ref.27. Source: UniProtKB Golgi organization Inferred from electronic annotation. Source: Compara 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: Compara protein oligomerization Inferred from electronic annotation. Source: Compara regulated secretory pathway Inferred from sequence or structural similarity. Source: HGNC response to acid Inferred from electronic annotation. Source: Compara response to alkaloid Inferred from electronic annotation. Source: Compara retrograde vesicle-mediated transport, Golgi to ER Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	COPI-coated vesicle Inferred from sequence or structural similarity. Source: UniProtKB 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 to membrane Inferred from sequence or structural similarity. Source: HGNC melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCSTN	Q92542	5	EBI-998422,EBI-998440
PSEN1	P49768	3	EBI-998422,EBI-297277
PSENEN	Q9NZ42	3	EBI-998422,EBI-998468
PTPN2	P17706-1	5	EBI-998422,EBI-4409481
TMED2	Q15363	7	EBI-998422,EBI-998485

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Ref.11
	Chain	32 – 219	188	Transmembrane emp24 domain-containing protein 10		PRO_0000010399
Regions
	Topological domain	32 – 185	154	Lumenal Potential
	Transmembrane	186 – 206	21	Helical; Potential
	Topological domain	207 – 219	13	Cytoplasmic Potential
	Domain	41 – 193	153	GOLD
	Region	147 – 178	32	Required for TMED10 and TMED2 cis-Golgi network localization
	Region	204 – 219	16	Interaction with COPG1
	Region	207 – 219	13	Interaction with ARF1
	Motif	211 – 219	9	COPI vesicle coat-binding
	Motif	211 – 212	2	COPII vesicle coat-binding
Amino acid modifications
	Modified residue	171	1	Omega-N-methylated arginine By similarity
	Modified residue	176	1	Omega-N-methylated arginine By similarity
	Glycosylation	179	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	64	1	S → Y. Corresponds to variant rs4929 [ dbSNP | Ensembl ].		VAR_012051
	Natural variant	152	1	R → G. Corresponds to variant rs17103066 [ dbSNP | Ensembl ].		VAR_049111
Experimental info
	Mutagenesis	211 – 212	2	FF → AA: Disrupts interaction with COPG1 and association with coatomer; when associated with 215-A-A-216. Ref.12 Ref.15 Ref.16
	Mutagenesis	211 – 212	2	FF → AA: No decrease in binding to COPG1. Disrupts interaction with SEC23A. Ref.12 Ref.15 Ref.16
	Mutagenesis	215 – 216	2	KK → AA: Disrupts interaction with COPG1 and association with coatomer; when associated with 211-A-A-212. Ref.12 Ref.15 Ref.16
	Mutagenesis	215 – 216	2	KK → AA: Significant reduction in binding to COPG1. Ref.12 Ref.15 Ref.16
	Sequence conflict	75	1	K → R in CAD89913. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P49755 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: 0A0486BE65C4DBBB	FASTA	219	24,976
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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], MASS SPECTROMETRY. 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]	"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.
IPI	IPI00028055.
PIR	G01159.
RefSeq	NP_006818.3. NM_006827.5.
UniGene	Hs.74137.
3D structure databases
ProteinModelPortal	P49755.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49755. 21 interactions.
STRING	9606.ENSP00000303145.
PTM databases
PhosphoSite	P49755.
Polymorphism databases
DMDM	3915893.
Proteomic databases
PaxDb	P49755.
PeptideAtlas	P49755.
PRIDE	P49755.
Protocols and materials databases
DNASU	10972.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000303575; ENSP00000303145; ENSG00000170348.
GeneID	10972.
KEGG	hsa:10972.
UCSC	uc001xrm.1. human.
Organism-specific databases
CTD	10972.
GeneCards	GC14M075598.
HGNC	HGNC:16998. TMED10.
HPA	CAB037251.
MIM	605406. gene.
neXtProt	NX_P49755.
PharmGKB	PA128394579.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG323830.
HOVERGEN	HBG107275.
InParanoid	P49755.
OMA	YSKEDAS.
OrthoDB	EOG4HX520.
PhylomeDB	P49755.
Gene expression databases
ArrayExpress	P49755.
Bgee	P49755.
CleanEx	HS_TMED10.
Genevestigator	P49755.
GermOnline	ENSG00000170348. Homo sapiens.
Family and domain databases
InterPro	IPR009038. GOLD. [Graphical view]
Pfam	PF01105. EMP24_GP25L. 1 hit. [Graphical view]
PROSITE	PS50866. GOLD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TMED10. human.
GenomeRNAi	10972.
NextBio	41690.
SOURCE	Search...

Entry information

Entry name

TMEDA_HUMAN

Accession

Primary (citable) accession number: P49755
Secondary accession number(s): B2R605 , Q15602, Q16536, Q86TC2, Q86TS5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 15, 1998
Last modified:	May 1, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.