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O43617 (TPPC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trafficking protein particle complex subunit 3
Alternative name(s):
BET3 homolog
Gene names
Name:TRAPPC3
Synonyms:BET3
ORF Names:CDABP0066
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in vesicular transport from endoplasmic reticulum to Golgi.

Subunit structure

Homodimer. Component of the multisubunit TRAPP (transport protein particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and TRAPPC12. Heterodimer with TRAPPC6A. The heterodimer TRAPPC3-TRAPPC6A interacts with TRAPPC2L. Ref.8 Ref.9 Ref.11 Ref.12

Subcellular location

Golgi apparatuscis-Golgi network By similarity. Endoplasmic reticulum By similarity.

Sequence similarities

Belongs to the TRAPP small subunits family. BET3 subfamily.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43617-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O43617-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 180180Trafficking protein particle complex subunit 3
PRO_0000211572

Amino acid modifications

Lipidation681S-palmitoyl cysteine Ref.12

Natural variations

Alternative sequence1 – 4646Missing in isoform 2.
VSP_047015

Experimental info

Mutagenesis681C → S: Loss of palmitoylation. Ref.12

Secondary structure

........................ 180
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: B5E2D92BE8A39599

FASTA18020,274
        10         20         30         40         50         60 
MSRQANRGTE SKKMSSELFT LTYGALVTQL CKDYENDEDV NKQLDKMGFN IGVRLIEDFL 

        70         80         90        100        110        120 
ARSNVGRCHD FRETADVIAK VAFKMYLGIT PSITNWSPAG DEFSLILENN PLVDFVELPD 

       130        140        150        160        170        180 
NHSSLIYSNL LCGVLRGALE MVQMAVEAKF VQDTLKGDGV TEIRMRFIRR IEDNLPAGEE 

« Hide

Isoform 2 [UniParc].

Checksum: 927EE13435BDE8B9
Show »

FASTA13415,005

References

« Hide 'large scale' references
[1]"TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion."
Sacher M., Jiang Y., Barrowman J., Scarpa A., Burston J., Zhang L., Schieltz D., Yates J.R. III, Abeliovich H., Ferro-Novick S.
EMBO J. 17:2494-2503(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]Eva L., Subramaniam V.N., Hong W.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Pediatric leukemia cDNA sequencing project."
Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Leukemia.
[4]"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] (ISOFORM 1).
Tissue: Skeletal muscle.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM 1).
Tissue: Colon.
[8]"Functional organization of the yeast proteome by systematic analysis of protein complexes."
Gavin A.-C., Boesche M., Krause R., Grandi P., Marzioch M., Bauer A., Schultz J., Rick J.M., Michon A.-M., Cruciat C.-M., Remor M., Hoefert C., Schelder M., Brajenovic M., Ruffner H., Merino A., Klein K., Hudak M. expand/collapse author list , Dickson D., Rudi T., Gnau V., Bauch A., Bastuck S., Huhse B., Leutwein C., Heurtier M.-A., Copley R.R., Edelmann A., Querfurth E., Rybin V., Drewes G., Raida M., Bouwmeester T., Bork P., Seraphin B., Kuster B., Neubauer G., Superti-Furga G.
Nature 415:141-147(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN TRAPP COMPLEX.
[9]"TRAPPC2L is a novel, highly conserved TRAPP-interacting protein."
Scrivens P.J., Shahrzad N., Moores A., Morin A., Brunet S., Sacher M.
Traffic 10:724-736(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN TRAPP COMPLEX, INTERACTION WITH TRAPPC2L.
[10]"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].
[11]"C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early stage in ER-to-Golgi trafficking."
Scrivens P.J., Noueihed B., Shahrzad N., Hul S., Brunet S., Sacher M.
Mol. Biol. Cell 22:2083-2093(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN TRAPP COMPLEX.
[12]"Structure of palmitoylated BET3: insights into TRAPP complex assembly and membrane localization."
Turnbull A.P., Kummel D., Prinz B., Holz C., Schultchen J., Lang C., Niesen F.H., Hofmann K.P., Delbruck H., Behlke J., Muller E.C., Jarosch E., Sommer T., Heinemann U.
EMBO J. 24:875-884(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-180, SUBUNIT, MUTAGENESIS OF CYS-68, PALMITOYLATION AT CYS-68.
[13]"Biochemical and crystallographic studies reveal a specific interaction between TRAPP subunits Trs33p and Bet3p."
Kim M.-S., Yi M.-J., Lee K.-H., Wagner J., Munger C., Kim Y.-G., Whiteway M., Cygler M., Oh B.-H., Sacher M.
Traffic 6:1183-1195(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 15-175 IN COMPLEX WITH TRAPPC6A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ224335 mRNA. Translation: CAA11902.1.
AF041432 mRNA. Translation: AAB96936.1.
AY007139 mRNA. Translation: AAG02000.1.
AK315610 mRNA. Translation: BAG37979.1.
AC114484 Genomic DNA. No translation available.
CH471059 Genomic DNA. Translation: EAX07385.1.
CH471059 Genomic DNA. Translation: EAX07386.1.
CH471059 Genomic DNA. Translation: EAX07387.1.
BC007662 mRNA. Translation: AAH07662.1.
CCDSCCDS404.1. [O43617-1]
CCDS59194.1. [O43617-2]
RefSeqNP_001257823.1. NM_001270894.1.
NP_001257824.1. NM_001270895.1. [O43617-2]
NP_001257825.1. NM_001270896.1. [O43617-2]
NP_001257826.1. NM_001270897.1.
NP_055223.1. NM_014408.4. [O43617-1]
UniGeneHs.523131.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SZ7X-ray1.55A2-180[»]
2C0JX-ray2.20A15-175[»]
2CFHX-ray2.30A/B1-180[»]
3KXCX-ray2.00A1-180[»]
ProteinModelPortalO43617.
SMRO43617. Positions 13-171.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117997. 17 interactions.
DIPDIP-47627N.
IntActO43617. 12 interactions.
MINTMINT-5002244.
STRING9606.ENSP00000362261.

PTM databases

PhosphoSiteO43617.

Proteomic databases

MaxQBO43617.
PaxDbO43617.
PRIDEO43617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373162; ENSP00000362256; ENSG00000054116. [O43617-2]
ENST00000373163; ENSP00000362257; ENSG00000054116. [O43617-2]
ENST00000373166; ENSP00000362261; ENSG00000054116. [O43617-1]
GeneID27095.
KEGGhsa:27095.
UCSCuc001bzx.4. human. [O43617-1]

Organism-specific databases

CTD27095.
GeneCardsGC01M036602.
HGNCHGNC:19942. TRAPPC3.
HPAHPA028408.
MIM610955. gene.
neXtProtNX_O43617.
PharmGKBPA134972272.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG286899.
HOGENOMHOG000186184.
HOVERGENHBG055045.
InParanoidO43617.
OMALWYSNIL.
OrthoDBEOG73JKWX.
PhylomeDBO43617.
TreeFamTF300091.

Gene expression databases

ArrayExpressO43617.
BgeeO43617.
CleanExHS_TRAPPC3.
GenevestigatorO43617.

Family and domain databases

InterProIPR024096. NO_sig/Golgi_transp_ligand-bd.
IPR007194. TRAPP_component.
IPR016721. TRAPP_I_complex_Bet3.
[Graphical view]
PANTHERPTHR13048. PTHR13048. 1 hit.
PfamPF04051. TRAPP. 1 hit.
[Graphical view]
PIRSFPIRSF018293. TRAPP_I_complex_Bet3. 1 hit.
SUPFAMSSF111126. SSF111126. 1 hit.
ProtoNetSearch...

Other

ChiTaRSTRAPPC3. human.
EvolutionaryTraceO43617.
GeneWikiTRAPPC3.
GenomeRNAi27095.
NextBio35462482.
PROO43617.
SOURCESearch...

Entry information

Entry nameTPPC3_HUMAN
AccessionPrimary (citable) accession number: O43617
Secondary accession number(s): A6NDN0, B2RDN2, D3DPS2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 122 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM