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Q9BVK6

- TMED9_HUMAN

UniProt

Q9BVK6 - TMED9_HUMAN

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Protein

Transmembrane emp24 domain-containing protein 9

Gene
TMED9, GP25L2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Molecular functioni

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

GO - Biological processi

  1. COPI coating of Golgi vesicle Source: UniProtKB
  2. Golgi organization Source: UniProtKB
  3. positive regulation of organelle organization Source: UniProtKB
  4. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Transmembrane emp24 domain-containing protein 9
Alternative name(s):
GMP25
Glycoprotein 25L2
p24 family protein alpha-2
Short name:
p24alpha2
p25
Gene namesi
Name:TMED9
Synonyms:GP25L2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:24878. TMED9.

Subcellular locationi

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.3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini38 – 202165Lumenal Reviewed predictionAdd
BLAST
Transmembranei203 – 22220Helical; Reviewed predictionAdd
BLAST
Topological domaini223 – 23513Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  3. endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB-SubCell
  4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  5. extracellular vesicular exosome Source: UniProt
  6. Golgi apparatus Source: UniProtKB
  7. Golgi membrane Source: GOC
  8. integral component of membrane Source: UniProtKB-KW
  9. trans-Golgi network transport vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi232 – 2332KK → SS: Localization to plasma membrane and endocytosis. 1 Publication

Organism-specific databases

PharmGKBiPA134881976.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3737 By similarityAdd
BLAST
Chaini38 – 235198Transmembrane emp24 domain-containing protein 9PRO_0000010396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi125 – 1251N-linked (GlcNAc...)2 Publications
Modified residuei160 – 1601N6-acetyllysine By similarity

Post-translational modificationi

N-linked glycosylated containing high mannose.2 Publications

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiQ9BVK6.
PaxDbiQ9BVK6.
PRIDEiQ9BVK6.

PTM databases

PhosphoSiteiQ9BVK6.

Expressioni

Gene expression databases

BgeeiQ9BVK6.
CleanExiHS_TMED9.
GenevestigatoriQ9BVK6.

Organism-specific databases

HPAiHPA014650.

Interactioni

Subunit structurei

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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPN2P17706-15EBI-1056827,EBI-4409481

Protein-protein interaction databases

BioGridi120115. 36 interactions.
IntActiQ9BVK6. 20 interactions.
MINTiMINT-5001958.
STRINGi9606.ENSP00000330945.

Structurei

3D structure databases

ProteinModelPortaliQ9BVK6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 14599GOLDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni121 – 16040Required for interaction with STX17Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili154 – 18431 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi228 – 2358COPI vesicle coat-binding Reviewed prediction
Motifi228 – 2292COPII vesicle coat-binding Reviewed prediction

Sequence similaritiesi

Belongs to the EMP24/GP25L family.
Contains 1 GOLD domain.

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG323830.
HOGENOMiHOG000160228.
HOVERGENiHBG105357.
InParanoidiQ9BVK6.
OMAiVLWWSIV.
OrthoDBiEOG74BJT2.
PhylomeDBiQ9BVK6.
TreeFamiTF314123.

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.

Q9BVK6-1 [UniParc]FASTAAdd to Basket

« Hide

MAVELGVLLV RPRPGTGLGR VMRTLLLVLW LATRGSALYF HIGETEKKCF    50
IEEIPDETMV IGNYRTQLYD KQREEYQPAT PGLGMFVEVK DPEDKVILAR 100
QYGSEGRFTF TSHTPGEHQI CLHSNSTKFS LFAGGMLRVH LDIQVGEHAN 150
DYAEIAAKDK LSELQLRVRQ LVEQVEQIQK EQNYQRWREE RFRQTSESTN 200
QRVLWWSILQ TLILVAIGVW QMRHLKSFFE AKKLV 235
Length:235
Mass (Da):27,277
Last modified:June 16, 2009 - v2
Checksum:i9B6D2D517D9E77D8
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161T → S.
Corresponds to variant rs57960711 [ dbSNP | Ensembl ].
VAR_061178

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831L → F in CAA62380. 1 Publication
Sequence conflicti86 – 861F → C in CAA62380. 1 Publication
Sequence conflicti101 – 1011Q → E in CAA62380. 1 Publication
Sequence conflicti102 – 1021Y → C in AAL35268. 1 Publication
Sequence conflicti156 – 1561A → P in CAA62380. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4428.1.
RefSeqiNP_059980.2. NM_017510.4.
UniGeneiHs.279929.

Genome annotation databases

EnsembliENST00000332598; ENSP00000330945; ENSG00000184840.
GeneIDi54732.
KEGGihsa:54732.
UCSCiuc003mhx.3. human.

Polymorphism databases

DMDMi239938724.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS4428.1.
RefSeqi NP_059980.2. NM_017510.4.
UniGenei Hs.279929.

3D structure databases

ProteinModelPortali Q9BVK6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120115. 36 interactions.
IntActi Q9BVK6. 20 interactions.
MINTi MINT-5001958.
STRINGi 9606.ENSP00000330945.

PTM databases

PhosphoSitei Q9BVK6.

Polymorphism databases

DMDMi 239938724.

Proteomic databases

MaxQBi Q9BVK6.
PaxDbi Q9BVK6.
PRIDEi Q9BVK6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000332598 ; ENSP00000330945 ; ENSG00000184840 .
GeneIDi 54732.
KEGGi hsa:54732.
UCSCi uc003mhx.3. human.

Organism-specific databases

CTDi 54732.
GeneCardsi GC05P177019.
H-InvDB HIX0005470.
HGNCi HGNC:24878. TMED9.
HPAi HPA014650.
neXtProti NX_Q9BVK6.
PharmGKBi PA134881976.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG323830.
HOGENOMi HOG000160228.
HOVERGENi HBG105357.
InParanoidi Q9BVK6.
OMAi VLWWSIV.
OrthoDBi EOG74BJT2.
PhylomeDBi Q9BVK6.
TreeFami TF314123.

Miscellaneous databases

ChiTaRSi TMED9. human.
GenomeRNAii 54732.
NextBioi 57312.
PROi Q9BVK6.

Gene expression databases

Bgeei Q9BVK6.
CleanExi HS_TMED9.
Genevestigatori Q9BVK6.

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. "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.
    , 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. 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.

Entry informationi

Entry nameiTMED9_HUMAN
AccessioniPrimary (citable) accession number: Q9BVK6
Secondary accession number(s): Q14437, Q8WZ61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: June 16, 2009
Last modified: September 3, 2014
This is version 110 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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