Full text data of TRAPPC6B
TRAPPC6B
[Confidence: low (only semi-automatic identification from reviews)]
Trafficking protein particle complex subunit 6B
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Trafficking protein particle complex subunit 6B
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q86SZ2
ID TPC6B_HUMAN Reviewed; 158 AA.
AC Q86SZ2; B3KPS2; Q5JPD6; Q86U35; Q86X35;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Trafficking protein particle complex subunit 6B;
GN Name=TRAPPC6B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix carcinoma, and Fetal liver;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=16025134; DOI=10.1038/sj.embor.7400463;
RA Kuemmel D., Mueller J.J., Roske Y., Misselwitz R., Buessow K.,
RA Heinemann U.;
RT "The structure of the TRAPP subunit TPC6 suggests a model for a TRAPP
RT subcomplex.";
RL EMBO Rep. 6:787-793(2005).
CC -!- FUNCTION: May play a role in vesicular transport from endoplasmic
CC reticulum to Golgi (By similarity).
CC -!- SUBUNIT: Part of the multisubunit TRAPP (transport protein
CC particle) complex. Homodimer. Heterodimer with TRAPPC3.
CC -!- INTERACTION:
CC O43617:TRAPPC3; NbExp=2; IntAct=EBI-6160531, EBI-743566;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network (By
CC similarity). Endoplasmic reticulum (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86SZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86SZ2-2; Sequence=VSP_009659;
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. BET3
CC subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD62341.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; BX161510; CAD61947.1; -; mRNA.
DR EMBL; BX248013; CAD62341.1; ALT_INIT; mRNA.
DR EMBL; AL833179; CAI46185.1; -; mRNA.
DR EMBL; AK056690; BAG51784.1; -; mRNA.
DR EMBL; CH471078; EAW65823.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65824.1; -; Genomic_DNA.
DR EMBL; BC047328; AAH47328.1; -; mRNA.
DR RefSeq; NP_001073005.1; NM_001079537.1.
DR RefSeq; NP_803235.1; NM_177452.3.
DR UniGene; Hs.13303; -.
DR PDB; 2BJN; X-ray; 1.70 A; A/B=1-158.
DR PDB; 2CFH; X-ray; 2.30 A; C/D=1-158.
DR PDB; 3KXC; X-ray; 2.00 A; C=1-158.
DR PDBsum; 2BJN; -.
DR PDBsum; 2CFH; -.
DR PDBsum; 3KXC; -.
DR ProteinModelPortal; Q86SZ2; -.
DR SMR; Q86SZ2; 2-157.
DR IntAct; Q86SZ2; 4.
DR MINT; MINT-3035051; -.
DR STRING; 9606.ENSP00000330289; -.
DR PhosphoSite; Q86SZ2; -.
DR DMDM; 45477299; -.
DR PaxDb; Q86SZ2; -.
DR PRIDE; Q86SZ2; -.
DR DNASU; 122553; -.
DR Ensembl; ENST00000330149; ENSP00000330289; ENSG00000182400.
DR Ensembl; ENST00000347691; ENSP00000335171; ENSG00000182400.
DR GeneID; 122553; -.
DR KEGG; hsa:122553; -.
DR UCSC; uc001wut.1; human.
DR CTD; 122553; -.
DR GeneCards; GC14M039617; -.
DR HGNC; HGNC:23066; TRAPPC6B.
DR HPA; HPA047928; -.
DR MIM; 610397; gene.
DR neXtProt; NX_Q86SZ2; -.
DR PharmGKB; PA134973191; -.
DR eggNOG; NOG255558; -.
DR HOGENOM; HOG000200502; -.
DR HOVERGEN; HBG056159; -.
DR InParanoid; Q86SZ2; -.
DR OMA; KFVAFTC; -.
DR OrthoDB; EOG75TMDD; -.
DR PhylomeDB; Q86SZ2; -.
DR EvolutionaryTrace; Q86SZ2; -.
DR GenomeRNAi; 122553; -.
DR NextBio; 80914; -.
DR PRO; PR:Q86SZ2; -.
DR ArrayExpress; Q86SZ2; -.
DR Bgee; Q86SZ2; -.
DR CleanEx; HS_TRAPPC6B; -.
DR Genevestigator; Q86SZ2; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR007194; TRAPP_component.
DR Pfam; PF04051; TRAPP; 1.
DR SUPFAM; SSF111126; SSF111126; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Reference proteome; Transport.
FT CHAIN 1 158 Trafficking protein particle complex
FT subunit 6B.
FT /FTId=PRO_0000211587.
FT VAR_SEQ 90 117 Missing (in isoform 2).
FT /FTId=VSP_009659.
FT HELIX 1 20
FT TURN 24 30
FT HELIX 31 48
FT HELIX 62 69
FT HELIX 71 77
FT STRAND 82 88
FT STRAND 91 98
FT HELIX 100 102
FT HELIX 116 118
FT HELIX 120 132
FT STRAND 136 145
FT STRAND 149 156
SQ SEQUENCE 158 AA; 17983 MW; 5A8B0474548C304B CRC64;
MADEALFLLL HNEMVSGVYK SAEQGEVENG RCITKLENMG FRVGQGLIER FTKDTARFKD
ELDIMKFICK DFWTTVFKKQ IDNLRTNHQG IYVLQDNKFR LLTQMSAGKQ YLEHASKYLA
FTCGLIRGGL SNLGIKSIVT AEVSSMPACK FQVMIQKL
//
ID TPC6B_HUMAN Reviewed; 158 AA.
AC Q86SZ2; B3KPS2; Q5JPD6; Q86U35; Q86X35;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Trafficking protein particle complex subunit 6B;
GN Name=TRAPPC6B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix carcinoma, and Fetal liver;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=16025134; DOI=10.1038/sj.embor.7400463;
RA Kuemmel D., Mueller J.J., Roske Y., Misselwitz R., Buessow K.,
RA Heinemann U.;
RT "The structure of the TRAPP subunit TPC6 suggests a model for a TRAPP
RT subcomplex.";
RL EMBO Rep. 6:787-793(2005).
CC -!- FUNCTION: May play a role in vesicular transport from endoplasmic
CC reticulum to Golgi (By similarity).
CC -!- SUBUNIT: Part of the multisubunit TRAPP (transport protein
CC particle) complex. Homodimer. Heterodimer with TRAPPC3.
CC -!- INTERACTION:
CC O43617:TRAPPC3; NbExp=2; IntAct=EBI-6160531, EBI-743566;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network (By
CC similarity). Endoplasmic reticulum (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86SZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86SZ2-2; Sequence=VSP_009659;
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. BET3
CC subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD62341.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; BX161510; CAD61947.1; -; mRNA.
DR EMBL; BX248013; CAD62341.1; ALT_INIT; mRNA.
DR EMBL; AL833179; CAI46185.1; -; mRNA.
DR EMBL; AK056690; BAG51784.1; -; mRNA.
DR EMBL; CH471078; EAW65823.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65824.1; -; Genomic_DNA.
DR EMBL; BC047328; AAH47328.1; -; mRNA.
DR RefSeq; NP_001073005.1; NM_001079537.1.
DR RefSeq; NP_803235.1; NM_177452.3.
DR UniGene; Hs.13303; -.
DR PDB; 2BJN; X-ray; 1.70 A; A/B=1-158.
DR PDB; 2CFH; X-ray; 2.30 A; C/D=1-158.
DR PDB; 3KXC; X-ray; 2.00 A; C=1-158.
DR PDBsum; 2BJN; -.
DR PDBsum; 2CFH; -.
DR PDBsum; 3KXC; -.
DR ProteinModelPortal; Q86SZ2; -.
DR SMR; Q86SZ2; 2-157.
DR IntAct; Q86SZ2; 4.
DR MINT; MINT-3035051; -.
DR STRING; 9606.ENSP00000330289; -.
DR PhosphoSite; Q86SZ2; -.
DR DMDM; 45477299; -.
DR PaxDb; Q86SZ2; -.
DR PRIDE; Q86SZ2; -.
DR DNASU; 122553; -.
DR Ensembl; ENST00000330149; ENSP00000330289; ENSG00000182400.
DR Ensembl; ENST00000347691; ENSP00000335171; ENSG00000182400.
DR GeneID; 122553; -.
DR KEGG; hsa:122553; -.
DR UCSC; uc001wut.1; human.
DR CTD; 122553; -.
DR GeneCards; GC14M039617; -.
DR HGNC; HGNC:23066; TRAPPC6B.
DR HPA; HPA047928; -.
DR MIM; 610397; gene.
DR neXtProt; NX_Q86SZ2; -.
DR PharmGKB; PA134973191; -.
DR eggNOG; NOG255558; -.
DR HOGENOM; HOG000200502; -.
DR HOVERGEN; HBG056159; -.
DR InParanoid; Q86SZ2; -.
DR OMA; KFVAFTC; -.
DR OrthoDB; EOG75TMDD; -.
DR PhylomeDB; Q86SZ2; -.
DR EvolutionaryTrace; Q86SZ2; -.
DR GenomeRNAi; 122553; -.
DR NextBio; 80914; -.
DR PRO; PR:Q86SZ2; -.
DR ArrayExpress; Q86SZ2; -.
DR Bgee; Q86SZ2; -.
DR CleanEx; HS_TRAPPC6B; -.
DR Genevestigator; Q86SZ2; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR007194; TRAPP_component.
DR Pfam; PF04051; TRAPP; 1.
DR SUPFAM; SSF111126; SSF111126; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Reference proteome; Transport.
FT CHAIN 1 158 Trafficking protein particle complex
FT subunit 6B.
FT /FTId=PRO_0000211587.
FT VAR_SEQ 90 117 Missing (in isoform 2).
FT /FTId=VSP_009659.
FT HELIX 1 20
FT TURN 24 30
FT HELIX 31 48
FT HELIX 62 69
FT HELIX 71 77
FT STRAND 82 88
FT STRAND 91 98
FT HELIX 100 102
FT HELIX 116 118
FT HELIX 120 132
FT STRAND 136 145
FT STRAND 149 156
SQ SEQUENCE 158 AA; 17983 MW; 5A8B0474548C304B CRC64;
MADEALFLLL HNEMVSGVYK SAEQGEVENG RCITKLENMG FRVGQGLIER FTKDTARFKD
ELDIMKFICK DFWTTVFKKQ IDNLRTNHQG IYVLQDNKFR LLTQMSAGKQ YLEHASKYLA
FTCGLIRGGL SNLGIKSIVT AEVSSMPACK FQVMIQKL
//
MIM
610397
*RECORD*
*FIELD* NO
610397
*FIELD* TI
*610397 TRAFFICKING PROTEIN PARTICLE COMPLEX, SUBUNIT 6B; TRAPPC6B
;;TRAPP COMPLEX, SUBUNIT 6B;;
read moreTPC6
*FIELD* TX
DESCRIPTION
TRAPPC6B is a component of TRAPP complexes, which are tethering
complexes involved in vesicle transport (Kummel et al., 2005).
CLONING
Gwynn et al. (2006) identified mouse Trappc6b. Trappc6b contains 2
motifs conserved in TRAPPC6A (610396) and several yeast TRAPP subunits,
including Trs33, the putative homolog of TRAPPC6A and TRAPPC6B.
BIOCHEMICAL FEATURES
Kummel et al. (2005) determined the 1.7-angstrom crystal structure of
human TPC6. TPC6 adopted an alpha-beta-plait topology and formed dimers.
In spite of their low sequence similarity, the structure of TPC6
resembled that of BET3 (TRAPPC3; 610955), particularly at the
dimerization interface.
GENE FUNCTION
By immunoprecipitation and protein pull-down experiments, Kummel et al.
(2005) found that TPC6 could heterodimerize with BET3.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the
TRAPPC6B gene to chromosome 14 (TMAP WI-15625). Gwynn et al. (2006)
stated that the mouse Trappc6b gene maps to chromosome 12.
*FIELD* RF
1. Gwynn, B.; Smith, R. S.; Rowe, L. B.; Taylor, B. A.; Peters, L.
L.: A mouse TRAPP-related protein is involved in pigmentation. Genomics 88:
196-203, 2006.
2. Kummel, D.; Muller, J. J.; Roske, Y.; Misselwitz, R.; Bussow, K.;
Heinemann, U.: The structure of the TRAPP subunit TPC6 suggests a
model for a TRAPP subcomplex. EMBO Rep. 6: 787-793, 2005.
*FIELD* CD
Patricia A. Hartz: 9/11/2006
*FIELD* ED
mgross: 04/20/2007
mgross: 9/11/2006
*RECORD*
*FIELD* NO
610397
*FIELD* TI
*610397 TRAFFICKING PROTEIN PARTICLE COMPLEX, SUBUNIT 6B; TRAPPC6B
;;TRAPP COMPLEX, SUBUNIT 6B;;
read moreTPC6
*FIELD* TX
DESCRIPTION
TRAPPC6B is a component of TRAPP complexes, which are tethering
complexes involved in vesicle transport (Kummel et al., 2005).
CLONING
Gwynn et al. (2006) identified mouse Trappc6b. Trappc6b contains 2
motifs conserved in TRAPPC6A (610396) and several yeast TRAPP subunits,
including Trs33, the putative homolog of TRAPPC6A and TRAPPC6B.
BIOCHEMICAL FEATURES
Kummel et al. (2005) determined the 1.7-angstrom crystal structure of
human TPC6. TPC6 adopted an alpha-beta-plait topology and formed dimers.
In spite of their low sequence similarity, the structure of TPC6
resembled that of BET3 (TRAPPC3; 610955), particularly at the
dimerization interface.
GENE FUNCTION
By immunoprecipitation and protein pull-down experiments, Kummel et al.
(2005) found that TPC6 could heterodimerize with BET3.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the
TRAPPC6B gene to chromosome 14 (TMAP WI-15625). Gwynn et al. (2006)
stated that the mouse Trappc6b gene maps to chromosome 12.
*FIELD* RF
1. Gwynn, B.; Smith, R. S.; Rowe, L. B.; Taylor, B. A.; Peters, L.
L.: A mouse TRAPP-related protein is involved in pigmentation. Genomics 88:
196-203, 2006.
2. Kummel, D.; Muller, J. J.; Roske, Y.; Misselwitz, R.; Bussow, K.;
Heinemann, U.: The structure of the TRAPP subunit TPC6 suggests a
model for a TRAPP subcomplex. EMBO Rep. 6: 787-793, 2005.
*FIELD* CD
Patricia A. Hartz: 9/11/2006
*FIELD* ED
mgross: 04/20/2007
mgross: 9/11/2006