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Q9BVK6 (TMED9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 9
Alternative name(s):
GMP25
Glycoprotein 25L2
p24 family protein alpha-2
Short name=p24alpha2
p25
Gene names
Name:TMED9
Synonyms:GP25L2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length235 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Appears to be involved in vesicular protein trafficking, mainly in the early secretory pathway. In COPI vesicle-mediated retrograde transport involved in the coatomer recruitment to membranes of the early secretory pathway. Increases coatomer-dependent activity of ARFGAP2. Thought to play a crucial role in the specific retention of p24 complexes in cis-Golgi membranes; specifically contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. May be involved in organization of intracellular membranes, such as of the ER-Golgi intermediate compartment and the Golgi apparatus. Involved in ER localization of PTPN2 isoform PTPB Ref.7 Ref.9 Ref.12 Ref.14 Ref.15

Subunit structure

Monomer and homodimer in endoplasmic reticulum. Predominantly monomeric and to lesser extent homodimeric in endoplasmic reticulum-Golgi intermediate compartment and cis-Golgi network. Probably oligomerizes with other members of the EMP24/GP25L family such as TMED2, TMED7 and TMED10. Interacts with TMED5. Interacts (via C-terminus) with COPG1; the interaction involves dimeric TMED9. Interacts with PTPN2 and SPAST. Interacts with STX17; the interaction is direct. Ref.6 Ref.8 Ref.11 Ref.12 Ref.13 Ref.17 Ref.19

Subcellular location

Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatuscis-Golgi network membrane; Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein By similarity. Note: Cycles between compartments of the early secretatory pathway. Ref.7 Ref.8 Ref.9

Post-translational modification

N-linked glycosylated containing high mannose. Ref.6 Ref.10

Sequence similarities

Belongs to the EMP24/GP25L family.

Contains 1 GOLD domain.

Sequence caution

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

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

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentEndoplasmic reticulum
Golgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Signal
Transmembrane
Transmembrane helix
   PTMAcetylation
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCOPI coating of Golgi vesicle

Inferred from mutant phenotype Ref.14. Source: UniProtKB

Golgi organization

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of organelle organization

Inferred from mutant phenotype Ref.14. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.8. Source: UniProtKB

Golgi membrane

Inferred from mutant phenotype Ref.14. Source: GOC

endoplasmic reticulum

Inferred from direct assay Ref.8. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum-Golgi intermediate compartment

Inferred from direct assay Ref.8. Source: UniProtKB

endoplasmic reticulum-Golgi intermediate compartment membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

trans-Golgi network transport vesicle

Traceable author statement PubMed 9527489. Source: UniProtKB

   Molecular_functionsyntaxin binding

Inferred from physical interaction Ref.19. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PTPN2P17706-15EBI-1056827,EBI-4409481

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3737 By similarity
Chain38 – 235198Transmembrane emp24 domain-containing protein 9
PRO_0000010396

Regions

Topological domain38 – 202165Lumenal Potential
Transmembrane203 – 22220Helical; Potential
Topological domain223 – 23513Cytoplasmic Potential
Domain47 – 14599GOLD
Region121 – 16040Required for interaction with STX17
Coiled coil154 – 18431 Potential
Motif228 – 2358COPI vesicle coat-binding Potential
Motif228 – 2292COPII vesicle coat-binding Potential

Amino acid modifications

Modified residue1601N6-acetyllysine By similarity
Glycosylation1251N-linked (GlcNAc...) Ref.10 Ref.16

Natural variations

Natural variant161T → S.
Corresponds to variant rs57960711 [ dbSNP | Ensembl ].
VAR_061178

Experimental info

Mutagenesis232 – 2332KK → SS: Localization to plasma membrane and endocytosis. Ref.9
Sequence conflict831L → F in CAA62380. Ref.2
Sequence conflict861F → C in CAA62380. Ref.2
Sequence conflict1011Q → E in CAA62380. Ref.2
Sequence conflict1021Y → C in AAL35268. Ref.3
Sequence conflict1561A → P in CAA62380. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9BVK6 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 9B6D2D517D9E77D8

FASTA23527,277
        10         20         30         40         50         60 
MAVELGVLLV RPRPGTGLGR VMRTLLLVLW LATRGSALYF HIGETEKKCF IEEIPDETMV 

        70         80         90        100        110        120 
IGNYRTQLYD KQREEYQPAT PGLGMFVEVK DPEDKVILAR QYGSEGRFTF TSHTPGEHQI 

       130        140        150        160        170        180 
CLHSNSTKFS LFAGGMLRVH LDIQVGEHAN DYAEIAAKDK LSELQLRVRQ LVEQVEQIQK 

       190        200        210        220        230 
EQNYQRWREE RFRQTSESTN QRVLWWSILQ TLILVAIGVW QMRHLKSFFE AKKLV 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[3]Dominguez M., Fazel A., Parlati F., Bell A.W., Thomas D.Y., Bergeron J.J.M.
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-235.
Tissue: Liver.
[4]"A novel human cDNA that shares sequence homology with Homo sapiens mRNAs LOC96645 and gp25L2."
Wang C., Li Y.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-235.
[5]Bienvenut W.V.
Submitted (MAR-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 129-138 AND 170-180, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[6]"Localization and recycling of gp27 (hp24gamma3): complex formation with other p24 family members."
Fullekrug J., Suganuma T., Tang B.L., Hong W., Storrie B., Nilsson T.
Mol. Biol. Cell 10:1939-1955(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, SUBUNIT.
[7]"Coupled transport of p24 family members."
Emery G., Rojo M., Gruenberg J.
J. Cell Sci. 113:2507-2516(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Oligomeric state and stoichiometry of p24 proteins in the early secretory pathway."
Jenne N., Frey K., Brugger B., Wieland F.T.
J. Biol. Chem. 277:46504-46511(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUBUNIT.
[9]"The trans-membrane protein p25 forms highly specialized domains that regulate membrane composition and dynamics."
Emery G., Parton R.G., Rojo M., Gruenberg J.
J. Cell Sci. 116:4821-4832(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 232-LYS-LYS-233.
[10]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-125.
[11]"The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B."
Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E., Sanderson C.M.
Hum. Mol. Genet. 14:19-38(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPAST.
[12]"Evidence for a role of transmembrane protein p25 in localization of protein tyrosine phosphatase TC48 to the ER."
Gupta V., Swarup G.
J. Cell Sci. 119:1703-1714(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PTPN2.
[13]"Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins."
Bethune J., Kol M., Hoffmann J., Reckmann I., Brugger B., Wieland F.
Mol. Cell. Biol. 26:8011-8021(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COPG1.
[14]"The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53, and p25 are required to maintain the architecture of ERGIC and Golgi."
Mitrovic S., Ben-Tekaya H., Koegler E., Gruenberg J., Hauri H.-P.
Mol. Biol. Cell 19:1976-1990(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Arf GAP2 is positively regulated by coatomer and cargo."
Luo R., Ha V.L., Hayashi R., Randazzo P.A.
Cell. Signal. 21:1169-1179(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125.
Tissue: Liver.
[17]"p28, a novel ERGIC/cis Golgi protein, required for Golgi ribbon formation."
Koegler E., Bonnon C., Waldmeier L., Mitrovic S., Halbeisen R., Hauri H.P.
Traffic 11:70-89(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMED5.
[18]"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].
[19]"Syntaxin 17 cycles between the ER and ERGIC and is required to maintain the architecture of ERGIC and Golgi."
Muppirala M., Gupta V., Swarup G.
Biol. Cell 103:333-350(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STX17.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC139795 Genomic DNA. No translation available.
BC001123 mRNA. Translation: AAH01123.2.
X90872 mRNA. Translation: CAA62380.1. Different initiation.
AF441399 mRNA. Translation: AAL35268.1. Different initiation.
RefSeqNP_059980.2. NM_017510.4.
UniGeneHs.279929.

3D structure databases

ProteinModelPortalQ9BVK6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120115. 35 interactions.
IntActQ9BVK6. 20 interactions.
MINTMINT-5001958.
STRING9606.ENSP00000330945.

PTM databases

PhosphoSiteQ9BVK6.

Polymorphism databases

DMDM239938724.

Proteomic databases

PaxDbQ9BVK6.
PRIDEQ9BVK6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332598; ENSP00000330945; ENSG00000184840.
GeneID54732.
KEGGhsa:54732.
UCSCuc003mhx.3. human.

Organism-specific databases

CTD54732.
GeneCardsGC05P177019.
H-InvDBHIX0005470.
HGNCHGNC:24878. TMED9.
HPAHPA014650.
neXtProtNX_Q9BVK6.
PharmGKBPA134881976.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG323830.
HOGENOMHOG000160228.
HOVERGENHBG105357.
InParanoidQ9BVK6.
OMAVLWWSIV.
OrthoDBEOG74BJT2.
PhylomeDBQ9BVK6.
TreeFamTF314123.

Gene expression databases

BgeeQ9BVK6.
CleanExHS_TMED9.
GenevestigatorQ9BVK6.

Family and domain databases

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

Other

ChiTaRSTMED9. human.
GenomeRNAi54732.
NextBio57312.
PROQ9BVK6.

Entry information

Entry nameTMED9_HUMAN
AccessionPrimary (citable) accession number: Q9BVK6
Secondary accession number(s): Q14437, Q8WZ61
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: June 16, 2009
Last modified: April 16, 2014
This is version 106 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

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 5

Human chromosome 5: entries, gene names and cross-references to MIM