Full text data of TRAPPC2L
TRAPPC2L
[Confidence: low (only semi-automatic identification from reviews)]
Trafficking protein particle complex subunit 2-like protein
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Trafficking protein particle complex subunit 2-like protein
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UL33
ID TPC2L_HUMAN Reviewed; 140 AA.
AC Q9UL33; B2R4M9; Q6ZTA7; Q9NZZ4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 87.
DE RecName: Full=Trafficking protein particle complex subunit 2-like protein;
GN Name=TRAPPC2L; ORFNames=HSPC126;
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 [MRNA] (ISOFORM 1).
RA Zhu X., Qu Z.;
RT "Human cDNA complete cds with product weakly homologous to yeast
RT P38334 hypothetical 19.7 KD protein.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum, and Pericardium;
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].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Eye;
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 FUNCTION, IDENTIFICATION IN TRAPP COMPLEX, INTERACTION WITH TRAPPC2;
RP TRAPPC3; TRAPPC4 AND TRAPPC6A, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19416478; DOI=10.1111/j.1600-0854.2009.00906.x;
RA Scrivens P.J., Shahrzad N., Moores A., Morin A., Brunet S., Sacher M.;
RT "TRAPPC2L is a novel, highly conserved TRAPP-interacting protein.";
RL Traffic 10:724-736(2009).
RN [7]
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 [8]
RP IDENTIFICATION IN TRAPP COMPLEX.
RX PubMed=21525244; DOI=10.1091/mbc.E10-11-0873;
RA Scrivens P.J., Noueihed B., Shahrzad N., Hul S., Brunet S., Sacher M.;
RT "C4orf41 and TTC-15 are mammalian TRAPP components with a role at an
RT early stage in ER-to-Golgi trafficking.";
RL Mol. Biol. Cell 22:2083-2093(2011).
CC -!- FUNCTION: May play a role in vesicular transport from endoplasmic
CC reticulum to Golgi.
CC -!- SUBUNIT: Component of the multisubunit TRAPP (transport protein
CC particle) complex, which includes at least TRAPPC2, TRAPPC2L,
CC TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10,
CC TRAPPC11 and TRAPPC12. Interacts with the heterodimer TRAPPC3-
CC TRAPPC6A. Interacts with TRAPPC6A.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Endoplasmic
CC reticulum. Golgi apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UL33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UL33-2; Sequence=VSP_026641;
CC -!- TISSUE SPECIFICITY: Expressed in testis, liver, bladder, lung,
CC spleen and brain, several cell lines and primary chondrocytes cell
CC line.
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. Sedlin
CC subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC86686.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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; AF089106; AAF00568.1; -; mRNA.
DR EMBL; AF161524; AAF29139.1; -; mRNA.
DR EMBL; AK126779; BAC86686.1; ALT_SEQ; mRNA.
DR EMBL; AK311885; BAG34826.1; -; mRNA.
DR EMBL; AC092384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011369; AAH11369.1; -; mRNA.
DR EMBL; BC018024; AAH18024.1; -; mRNA.
DR EMBL; BC105809; AAI05810.1; -; mRNA.
DR RefSeq; NP_057293.1; NM_016209.3.
DR UniGene; Hs.461722; -.
DR ProteinModelPortal; Q9UL33; -.
DR SMR; Q9UL33; 29-132.
DR IntAct; Q9UL33; 7.
DR MINT; MINT-4541589; -.
DR STRING; 9606.ENSP00000301021; -.
DR PhosphoSite; Q9UL33; -.
DR DMDM; 74721024; -.
DR PaxDb; Q9UL33; -.
DR PRIDE; Q9UL33; -.
DR Ensembl; ENST00000301021; ENSP00000301021; ENSG00000167515.
DR GeneID; 51693; -.
DR KEGG; hsa:51693; -.
DR UCSC; uc002fmc.3; human.
DR CTD; 51693; -.
DR GeneCards; GC16P088923; -.
DR H-InvDB; HIX0019527; -.
DR HGNC; HGNC:30887; TRAPPC2L.
DR HPA; HPA041714; -.
DR MIM; 610970; gene.
DR neXtProt; NX_Q9UL33; -.
DR PharmGKB; PA145147879; -.
DR eggNOG; NOG238004; -.
DR HOGENOM; HOG000230646; -.
DR HOVERGEN; HBG056603; -.
DR InParanoid; Q9UL33; -.
DR PhylomeDB; Q9UL33; -.
DR GenomeRNAi; 51693; -.
DR NextBio; 55706; -.
DR PRO; PR:Q9UL33; -.
DR ArrayExpress; Q9UL33; -.
DR Bgee; Q9UL33; -.
DR CleanEx; HS_TRAPPC2L; -.
DR Genevestigator; Q9UL33; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:InterPro.
DR InterPro; IPR011012; Longin-like_dom.
DR InterPro; IPR006722; Sedlin.
DR PANTHER; PTHR12403; PTHR12403; 1.
DR Pfam; PF04628; Sedlin_N; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Reference proteome; Transport.
FT CHAIN 1 140 Trafficking protein particle complex
FT subunit 2-like protein.
FT /FTId=PRO_0000294451.
FT VAR_SEQ 125 125 Missing (in isoform 2).
FT /FTId=VSP_026641.
SQ SEQUENCE 140 AA; 16146 MW; 4549BCA7CE9566DC CRC64;
MAVCIAVIAK ENYPLYIRST PTENELKFHY MVHTSLDVVD EKISAMGKAL VDQRELYLGL
LYPTEDYKVY GYVTNSKVKF VMVVDSSNTA LRDNEIRSMF RKLHNSYTDV MCNPFYNPGD
RIQSSRAFDN MVTSMMIQVC
//
ID TPC2L_HUMAN Reviewed; 140 AA.
AC Q9UL33; B2R4M9; Q6ZTA7; Q9NZZ4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 87.
DE RecName: Full=Trafficking protein particle complex subunit 2-like protein;
GN Name=TRAPPC2L; ORFNames=HSPC126;
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 [MRNA] (ISOFORM 1).
RA Zhu X., Qu Z.;
RT "Human cDNA complete cds with product weakly homologous to yeast
RT P38334 hypothetical 19.7 KD protein.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum, and Pericardium;
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].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Eye;
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 FUNCTION, IDENTIFICATION IN TRAPP COMPLEX, INTERACTION WITH TRAPPC2;
RP TRAPPC3; TRAPPC4 AND TRAPPC6A, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19416478; DOI=10.1111/j.1600-0854.2009.00906.x;
RA Scrivens P.J., Shahrzad N., Moores A., Morin A., Brunet S., Sacher M.;
RT "TRAPPC2L is a novel, highly conserved TRAPP-interacting protein.";
RL Traffic 10:724-736(2009).
RN [7]
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 [8]
RP IDENTIFICATION IN TRAPP COMPLEX.
RX PubMed=21525244; DOI=10.1091/mbc.E10-11-0873;
RA Scrivens P.J., Noueihed B., Shahrzad N., Hul S., Brunet S., Sacher M.;
RT "C4orf41 and TTC-15 are mammalian TRAPP components with a role at an
RT early stage in ER-to-Golgi trafficking.";
RL Mol. Biol. Cell 22:2083-2093(2011).
CC -!- FUNCTION: May play a role in vesicular transport from endoplasmic
CC reticulum to Golgi.
CC -!- SUBUNIT: Component of the multisubunit TRAPP (transport protein
CC particle) complex, which includes at least TRAPPC2, TRAPPC2L,
CC TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10,
CC TRAPPC11 and TRAPPC12. Interacts with the heterodimer TRAPPC3-
CC TRAPPC6A. Interacts with TRAPPC6A.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Endoplasmic
CC reticulum. Golgi apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UL33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UL33-2; Sequence=VSP_026641;
CC -!- TISSUE SPECIFICITY: Expressed in testis, liver, bladder, lung,
CC spleen and brain, several cell lines and primary chondrocytes cell
CC line.
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. Sedlin
CC subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC86686.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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; AF089106; AAF00568.1; -; mRNA.
DR EMBL; AF161524; AAF29139.1; -; mRNA.
DR EMBL; AK126779; BAC86686.1; ALT_SEQ; mRNA.
DR EMBL; AK311885; BAG34826.1; -; mRNA.
DR EMBL; AC092384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011369; AAH11369.1; -; mRNA.
DR EMBL; BC018024; AAH18024.1; -; mRNA.
DR EMBL; BC105809; AAI05810.1; -; mRNA.
DR RefSeq; NP_057293.1; NM_016209.3.
DR UniGene; Hs.461722; -.
DR ProteinModelPortal; Q9UL33; -.
DR SMR; Q9UL33; 29-132.
DR IntAct; Q9UL33; 7.
DR MINT; MINT-4541589; -.
DR STRING; 9606.ENSP00000301021; -.
DR PhosphoSite; Q9UL33; -.
DR DMDM; 74721024; -.
DR PaxDb; Q9UL33; -.
DR PRIDE; Q9UL33; -.
DR Ensembl; ENST00000301021; ENSP00000301021; ENSG00000167515.
DR GeneID; 51693; -.
DR KEGG; hsa:51693; -.
DR UCSC; uc002fmc.3; human.
DR CTD; 51693; -.
DR GeneCards; GC16P088923; -.
DR H-InvDB; HIX0019527; -.
DR HGNC; HGNC:30887; TRAPPC2L.
DR HPA; HPA041714; -.
DR MIM; 610970; gene.
DR neXtProt; NX_Q9UL33; -.
DR PharmGKB; PA145147879; -.
DR eggNOG; NOG238004; -.
DR HOGENOM; HOG000230646; -.
DR HOVERGEN; HBG056603; -.
DR InParanoid; Q9UL33; -.
DR PhylomeDB; Q9UL33; -.
DR GenomeRNAi; 51693; -.
DR NextBio; 55706; -.
DR PRO; PR:Q9UL33; -.
DR ArrayExpress; Q9UL33; -.
DR Bgee; Q9UL33; -.
DR CleanEx; HS_TRAPPC2L; -.
DR Genevestigator; Q9UL33; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:InterPro.
DR InterPro; IPR011012; Longin-like_dom.
DR InterPro; IPR006722; Sedlin.
DR PANTHER; PTHR12403; PTHR12403; 1.
DR Pfam; PF04628; Sedlin_N; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Reference proteome; Transport.
FT CHAIN 1 140 Trafficking protein particle complex
FT subunit 2-like protein.
FT /FTId=PRO_0000294451.
FT VAR_SEQ 125 125 Missing (in isoform 2).
FT /FTId=VSP_026641.
SQ SEQUENCE 140 AA; 16146 MW; 4549BCA7CE9566DC CRC64;
MAVCIAVIAK ENYPLYIRST PTENELKFHY MVHTSLDVVD EKISAMGKAL VDQRELYLGL
LYPTEDYKVY GYVTNSKVKF VMVVDSSNTA LRDNEIRSMF RKLHNSYTDV MCNPFYNPGD
RIQSSRAFDN MVTSMMIQVC
//
MIM
610970
*RECORD*
*FIELD* NO
610970
*FIELD* TI
*610970 TRAFFICKING PROTEIN PARTICLE COMPLEX 2-LIKE; TRAPPC2L
*FIELD* TX
DESCRIPTION
read more
TRAPPC2L is a component of the TRAPP multisubunit tethering complex
involved in intracellular vesicle trafficking (Scrivens et al., 2011).
CLONING
By sequencing clones obtained from a CD34 (142230)-positive
hematopoietic stem/progenitor cell cDNA library, Zhang et al. (2000)
cloned TRAPPC2L. The deduced protein contains 139 amino acids. TRAPPC2L
was expressed in all 5 human hematopoietic cell lines examined.
GENE STRUCTURE
Zhang et al. (2000) determined that the TRAPPC2L gene contains at least
4 exons.
MAPPING
Zhang et al. (2000) stated that the TRAPPC2L gene maps to chromosome
16q22.1-q22.2.
GENE FUNCTION
Scrivens et al. (2011) used tandem affinity purification-tagged TRAPPC2
(300202) and TRAPPC2L to identify purified TRAPP complexes from HEK293
cells. Knockdown of individual components of the TRAPP complexes caused
Golgi fragmentation and arrested anterograde trafficking, suggesting
that the TRAPP complex functions in an early trafficking step between
the endoplasmic reticulum and Golgi. Gel filtration analysis suggested
that TRAPP complexes can join to form larger oligomers.
*FIELD* RF
1. Scrivens, P. J.; Noueihed, B.; Shahrzad, N.; Hul, S.; Brunet, S.;
Sacher, M.: C4orf41 and TTC-15 are mammalian TRAPP components with
a role at an early stage in ER-to-Golgi trafficking. Molec. Biol.
Cell 22: 2083-2093, 2011.
2. Zhang, Q.-H.; Ye, M.; Wu., X.-Y.; Ren, S.-X.; Zhao, M.; Zhao, C.-J.;
Fu, G.; Shen, Y.; Fan, H.-Y.; Lu, G.; Zhong, M.; Xu, X.-R.; and 9
others: Cloning and functional analysis of cDNAs with open reading
frames for 300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells. Genome Res. 10: 1546-1560, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 7/22/2011
*FIELD* CD
Patricia A. Hartz: 4/24/2007
*FIELD* ED
wwang: 08/05/2011
terry: 7/22/2011
joanna: 5/21/2007
wwang: 4/24/2007
*RECORD*
*FIELD* NO
610970
*FIELD* TI
*610970 TRAFFICKING PROTEIN PARTICLE COMPLEX 2-LIKE; TRAPPC2L
*FIELD* TX
DESCRIPTION
read more
TRAPPC2L is a component of the TRAPP multisubunit tethering complex
involved in intracellular vesicle trafficking (Scrivens et al., 2011).
CLONING
By sequencing clones obtained from a CD34 (142230)-positive
hematopoietic stem/progenitor cell cDNA library, Zhang et al. (2000)
cloned TRAPPC2L. The deduced protein contains 139 amino acids. TRAPPC2L
was expressed in all 5 human hematopoietic cell lines examined.
GENE STRUCTURE
Zhang et al. (2000) determined that the TRAPPC2L gene contains at least
4 exons.
MAPPING
Zhang et al. (2000) stated that the TRAPPC2L gene maps to chromosome
16q22.1-q22.2.
GENE FUNCTION
Scrivens et al. (2011) used tandem affinity purification-tagged TRAPPC2
(300202) and TRAPPC2L to identify purified TRAPP complexes from HEK293
cells. Knockdown of individual components of the TRAPP complexes caused
Golgi fragmentation and arrested anterograde trafficking, suggesting
that the TRAPP complex functions in an early trafficking step between
the endoplasmic reticulum and Golgi. Gel filtration analysis suggested
that TRAPP complexes can join to form larger oligomers.
*FIELD* RF
1. Scrivens, P. J.; Noueihed, B.; Shahrzad, N.; Hul, S.; Brunet, S.;
Sacher, M.: C4orf41 and TTC-15 are mammalian TRAPP components with
a role at an early stage in ER-to-Golgi trafficking. Molec. Biol.
Cell 22: 2083-2093, 2011.
2. Zhang, Q.-H.; Ye, M.; Wu., X.-Y.; Ren, S.-X.; Zhao, M.; Zhao, C.-J.;
Fu, G.; Shen, Y.; Fan, H.-Y.; Lu, G.; Zhong, M.; Xu, X.-R.; and 9
others: Cloning and functional analysis of cDNAs with open reading
frames for 300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells. Genome Res. 10: 1546-1560, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 7/22/2011
*FIELD* CD
Patricia A. Hartz: 4/24/2007
*FIELD* ED
wwang: 08/05/2011
terry: 7/22/2011
joanna: 5/21/2007
wwang: 4/24/2007