ID TPC2A_HUMAN Reviewed; 140 AA.
AC P0DI81; A6NEG0; O14582; Q9HD16;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Trafficking protein particle complex subunit 2;
DE AltName: Full=Sedlin;
GN Name=TRAPPC2; Synonyms=SEDL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INVOLVEMENT IN
RP SEDT.
RX PubMed=10431248; DOI=10.1038/11976;
RA Gedeon A.K., Colley A., Jamieson R., Thompson E.M., Rogers J., Sillence D.,
RA Tiller G.E., Mulley J.C., Gecz J.;
RT "Identification of the gene (SEDL) causing X-linked spondyloepiphyseal
RT dysplasia tarda.";
RL Nat. Genet. 22:400-404(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-130 (ISOFORM 3).
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary, and Prostate;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP GENOMIC ORGANIZATION, ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION.
RX PubMed=11031107; DOI=10.1006/geno.2000.6326;
RA Gecz J., Hillman M.A., Gedeon A.K., Cox T.C., Baker E., Mulley J.C.;
RT "Gene structure and expression study of the SEDL gene for
RT spondyloepiphyseal dysplasia tarda.";
RL Genomics 69:242-251(2000).
RN [6]
RP IDENTIFICATION IN TRAPP COMPLEX.
RX PubMed=11805826; DOI=10.1038/415141a;
RA Gavin A.-C., Boesche M., Krause R., Grandi P., Marzioch M., Bauer A.,
RA Schultz J., Rick J.M., Michon A.-M., Cruciat C.-M., Remor M., Hoefert C.,
RA Schelder M., Brajenovic M., Ruffner H., Merino A., Klein K., Hudak M.,
RA Dickson D., Rudi T., Gnau V., Bauch A., Bastuck S., Huhse B., Leutwein C.,
RA Heurtier M.-A., Copley R.R., Edelmann A., Querfurth E., Rybin V.,
RA Drewes G., Raida M., Bouwmeester T., Bork P., Seraphin B., Kuster B.,
RA Neubauer G., Superti-Furga G.;
RT "Functional organization of the yeast proteome by systematic analysis of
RT protein complexes.";
RL Nature 415:141-147(2002).
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., Buerckstuemmer T.,
RA 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 early
RT stage in ER-to-Golgi trafficking.";
RL Mol. Biol. Cell 22:2083-2093(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=25918224; DOI=10.1083/jcb.201501090;
RA Milev M.P., Hasaj B., Saint-Dic D., Snounou S., Zhao Q., Sacher M.;
RT "TRAMM/TrappC12 plays a role in chromosome congression, kinetochore
RT stability, and CENP-E recruitment.";
RL J. Cell Biol. 209:221-234(2015).
RN [11]
RP CHARACTERIZATION OF VARIANT SEDL TYR-47.
RX PubMed=14597397; DOI=10.1016/s0378-1119(03)00819-9;
RA Gecz J., Shaw M.A., Bellon J.R., de Barros Lopes M.;
RT "Human wild-type SEDL protein functionally complements yeast Trs20p but
RT some naturally occurring SEDL mutants do not.";
RL Gene 320:137-144(2003).
RN [12]
RP IDENTIFICATION IN TRAPP COMPLEX, AND INTERACTION WITH TRAPPC2L.
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 [13]
RP SELF-ASSOCIATION, INTERACTION WITH ENO1; PITX1 AND SF1, SUBCELLULAR
RP LOCATION, AND CHARACTERIZATION OF VARIANTS SEDL TYR-47; LEU-73; SER-83 AND
RP ASP-130.
RX PubMed=20498720; DOI=10.1371/journal.pone.0010646;
RA Jeyabalan J., Nesbit M.A., Galvanovskis J., Callaghan R., Rorsman P.,
RA Thakker R.V.;
RT "SEDLIN forms homodimers: characterisation of SEDLIN mutations and their
RT interactions with transcription factors MBP1, PITX1 and SF1.";
RL PLoS ONE 5:E10646-E10646(2010).
RN [14]
RP VARIANTS SEDT TYR-47; LEU-73 AND ASP-130.
RX PubMed=11349230; DOI=10.1086/320592;
RA Gedeon A.K., Tiller G.E., Le Merrer M., Heuertz S., Tranebjaerg L.,
RA Chitayat D., Robertson S., Glass I.A., Savarirayan R., Cole W.G.,
RA Rimoin D.L., Kousseff B.G., Ohashi H., Zabel B., Munnich A., Gecz J.,
RA Mulley J.C.;
RT "The molecular basis of X-linked spondyloepiphyseal dysplasia tarda.";
RL Am. J. Hum. Genet. 68:1386-1397(2001).
RN [15]
RP VARIANT SEDT SER-83.
RX PubMed=11424925; DOI=10.1136/jmg.38.6.409;
RA Grunebaum E., Arpaia E., MacKenzie J.J., Fitzpatrick J., Ray P.N.,
RA Roifman C.M.;
RT "A missense mutation in the SEDL gene results in delayed onset of X linked
RT spondyloepiphyseal dysplasia in a large pedigree.";
RL J. Med. Genet. 38:409-411(2001).
CC -!- FUNCTION: Prevents transcriptional repression and induction of cell
CC death by ENO1 (By similarity). May play a role in vesicular transport
CC from endoplasmic reticulum to Golgi. {ECO:0000250}.
CC -!- SUBUNIT: Can homodimerize. Component of the multisubunit TRAPP
CC (transport protein particle) complex, which includes TRAPPC2, TRAPPC2L,
CC TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10,
CC TRAPPC11 and TRAPPC12. Interacts with ENO1, PITX1 and SF1.
CC {ECO:0000269|PubMed:11805826, ECO:0000269|PubMed:19416478,
CC ECO:0000269|PubMed:20498720, ECO:0000269|PubMed:21525244}.
CC -!- INTERACTION:
CC P0DI81; Q9UBC2: EPS15L1; NbExp=3; IntAct=EBI-5663373, EBI-2556746;
CC P0DI81; Q719H9: KCTD1; NbExp=3; IntAct=EBI-5663373, EBI-9027502;
CC P0DI81; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-5663373, EBI-5235829;
CC P0DI81-3; Q9UBC2-3: EPS15L1; NbExp=3; IntAct=EBI-11961968, EBI-11958621;
CC P0DI81-3; Q0VD86: INCA1; NbExp=3; IntAct=EBI-11961968, EBI-6509505;
CC P0DI81-3; Q8TAC2: JOSD2; NbExp=3; IntAct=EBI-11961968, EBI-12205593;
CC P0DI81-3; Q719H9: KCTD1; NbExp=3; IntAct=EBI-11961968, EBI-9027502;
CC P0DI81-3; P62310: LSM3; NbExp=3; IntAct=EBI-11961968, EBI-348239;
CC P0DI81-3; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-11961968, EBI-12516603;
CC P0DI81-3; Q9BSH3: NICN1; NbExp=3; IntAct=EBI-11961968, EBI-13324229;
CC P0DI81-3; O00746: NME4; NbExp=3; IntAct=EBI-11961968, EBI-744871;
CC P0DI81-3; Q3KQZ1-4: SLC25A35; NbExp=3; IntAct=EBI-11961968, EBI-13054652;
CC P0DI81-3; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-11961968, EBI-12004298;
CC P0DI81-3; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-11961968, EBI-11139477;
CC P0DI81-3; O43617: TRAPPC3; NbExp=8; IntAct=EBI-11961968, EBI-743566;
CC P0DI81-3; Q8IUR0: TRAPPC5; NbExp=5; IntAct=EBI-11961968, EBI-3246160;
CC P0DI81-3; Q9BRT2: UQCC2; NbExp=3; IntAct=EBI-11961968, EBI-1054584;
CC P0DI81-3; O96006: ZBED1; NbExp=3; IntAct=EBI-11961968, EBI-740037;
CC P0DI81-3; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-11961968, EBI-11962468;
CC P0DI81-3; Q8N720: ZNF655; NbExp=3; IntAct=EBI-11961968, EBI-625509;
CC P0DI81-3; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-11961968, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:11031107}. Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000269|PubMed:11031107}. Nucleus
CC {ECO:0000269|PubMed:20498720, ECO:0000269|PubMed:25918224}. Cytoplasm
CC {ECO:0000269|PubMed:20498720}. Note=Localized in perinuclear granular
CC structures. {ECO:0000269|PubMed:11031107}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Major;
CC IsoId=P0DI81-1, O14582-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P0DI81-2, O14582-2;
CC Sequence=VSP_041681, VSP_006040, VSP_041682;
CC Name=3;
CC IsoId=P0DI81-3; Sequence=VSP_041681;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC pancreas, placenta, skeletal muscle, fetal cartilage, fibroblasts,
CC placenta and lymphocytes. {ECO:0000269|PubMed:10431248}.
CC -!- DISEASE: Spondyloepiphyseal dysplasia tarda (SEDT) [MIM:313400]: X-
CC linked recessive disorder of endochondral bone formation.
CC {ECO:0000269|PubMed:10431248, ECO:0000269|PubMed:11349230,
CC ECO:0000269|PubMed:11424925}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: A paralogous gene encoding an identical protein appears
CC to have arisen by retrotransposition of a cDNA from this locus and to
CC have acquired a promoter and non-coding 5' UTR from the ZNF547 gene.
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. Sedlin
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF157065; AAD49845.1; -; Genomic_DNA.
DR EMBL; AF157062; AAD49845.1; JOINED; Genomic_DNA.
DR EMBL; AF157063; AAD49845.1; JOINED; Genomic_DNA.
DR EMBL; AF157064; AAD49845.1; JOINED; Genomic_DNA.
DR EMBL; AC003037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK310542; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DA542477; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DB101396; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC016915; AAH16915.1; -; mRNA.
DR EMBL; BC052618; AAH52618.1; -; mRNA.
DR CCDS; CCDS48082.1; -.
DR CCDS; CCDS48083.2; -. [P0DI81-3]
DR RefSeq; NP_001011658.1; NM_001011658.3. [P0DI81-1]
DR RefSeq; NP_001122307.2; NM_001128835.2. [P0DI81-3]
DR RefSeq; NP_055378.1; NM_014563.5. [P0DI81-1]
DR RefSeq; XP_011543867.1; XM_011545565.1.
DR RefSeq; XP_011543868.1; XM_011545566.2. [P0DI81-1]
DR AlphaFoldDB; P0DI81; -.
DR SMR; P0DI81; -.
DR BioGRID; 112299; 139.
DR ComplexPortal; CPX-4749; TRAPP II complex, TRAPPC2 variant.
DR ComplexPortal; CPX-4750; TRAPP III complex, TRAPPC2 variant.
DR CORUM; P0DI81; -.
DR IntAct; P0DI81; 30.
DR STRING; 9606.ENSP00000392495; -.
DR iPTMnet; P0DI81; -.
DR PhosphoSitePlus; P0DI81; -.
DR BioMuta; TRAPPC2; -.
DR DMDM; 347662477; -.
DR EPD; P0DI81; -.
DR jPOST; P0DI81; -.
DR MassIVE; P0DI81; -.
DR MaxQB; P0DI81; -.
DR PaxDb; 9606-ENSP00000392495; -.
DR PeptideAtlas; P0DI81; -.
DR Pumba; P0DI81; -.
DR TopDownProteomics; P0DI81-1; -. [P0DI81-1]
DR Antibodypedia; 23846; 197 antibodies from 27 providers.
DR DNASU; 6399; -.
DR Ensembl; ENST00000359680.9; ENSP00000352708.5; ENSG00000196459.15. [P0DI81-1]
DR Ensembl; ENST00000380579.6; ENSP00000369953.1; ENSG00000196459.15. [P0DI81-1]
DR Ensembl; ENST00000458511.7; ENSP00000392495.3; ENSG00000196459.15. [P0DI81-1]
DR Ensembl; ENST00000518847.2; ENSP00000428900.2; ENSG00000196459.15. [P0DI81-1]
DR Ensembl; ENST00000683569.1; ENSP00000508155.1; ENSG00000196459.15. [P0DI81-1]
DR Ensembl; ENST00000683983.1; ENSP00000507474.1; ENSG00000196459.15. [P0DI81-3]
DR GeneID; 6399; -.
DR KEGG; hsa:6399; -.
DR MANE-Select; ENST00000380579.6; ENSP00000369953.1; NM_001011658.4; NP_001011658.1.
DR UCSC; uc064yav.1; human.
DR AGR; HGNC:10710; -.
DR AGR; HGNC:23068; -.
DR CTD; 6399; -.
DR DisGeNET; 6399; -.
DR GeneCards; TRAPPC2; -.
DR GeneReviews; TRAPPC2; -.
DR HGNC; HGNC:23068; TRAPPC2.
DR HPA; ENSG00000196459; Low tissue specificity.
DR MalaCards; TRAPPC2; -.
DR MIM; 300202; gene.
DR MIM; 313400; phenotype.
DR neXtProt; NX_P0DI81; -.
DR OpenTargets; ENSG00000196459; -.
DR OpenTargets; ENSG00000256060; -.
DR Orphanet; 93284; Spondyloepiphyseal dysplasia tarda.
DR VEuPathDB; HostDB:ENSG00000196459; -.
DR eggNOG; KOG3487; Eukaryota.
DR GeneTree; ENSGT00510000047168; -.
DR HOGENOM; CLU_085828_0_2_1; -.
DR InParanoid; P0DI81; -.
DR OMA; FFQELHE; -.
DR OrthoDB; 5045079at2759; -.
DR PhylomeDB; P0DI81; -.
DR TreeFam; TF314814; -.
DR PathwayCommons; P0DI81; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; P0DI81; -.
DR BioGRID-ORCS; 6399; 314 hits in 684 CRISPR screens.
DR ChiTaRS; TRAPPC2; human.
DR GeneWiki; TRAPPC2; -.
DR GenomeRNAi; 6399; -.
DR Pharos; P0DI81; Tbio.
DR PRO; PR:P0DI81; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P0DI81; Protein.
DR Bgee; ENSG00000196459; Expressed in cortical plate and 204 other cell types or tissues.
DR ExpressionAtlas; P0DI81; baseline and differential.
DR Genevisible; P0DI81; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0030008; C:TRAPP complex; IDA:UniProtKB.
DR GO; GO:1990071; C:TRAPPII protein complex; NAS:ComplexPortal.
DR GO; GO:1990072; C:TRAPPIII protein complex; NAS:ComplexPortal.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0048208; P:COPII vesicle coating; NAS:ComplexPortal.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
DR GO; GO:0006901; P:vesicle coating; NAS:ComplexPortal.
DR GO; GO:0099022; P:vesicle tethering; NAS:ComplexPortal.
DR CDD; cd14825; TRAPPC2_sedlin; 1.
DR Gene3D; 3.30.450.70; -; 1.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR006722; Sedlin.
DR PANTHER; PTHR12403; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 2; 1.
DR PANTHER; PTHR12403:SF1; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 2-RELATED; 1.
DR Pfam; PF04628; Sedlin_N; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant; ER-Golgi transport;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription; Transport.
FT CHAIN 1..140
FT /note="Trafficking protein particle complex subunit 2"
FT /id="PRO_0000211566"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1
FT /note="M -> MSSWKQDRSGLRSTELNVLEYQPLCAVRSHILKTM (in isoform
FT 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041681"
FT VAR_SEQ 80
FT /note="H -> HILTFLVKVTN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_006040"
FT VAR_SEQ 81..140
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041682"
FT VARIANT 47
FT /note="D -> Y (in SEDT; loss-of-function mutation)"
FT /evidence="ECO:0000269|PubMed:11349230,
FT ECO:0000269|PubMed:14597397, ECO:0000269|PubMed:20498720"
FT /id="VAR_012358"
FT VARIANT 73
FT /note="S -> L (in SEDT; loss of interaction with ENO1,
FT PITX1 and SF1; dbSNP:rs769218264)"
FT /evidence="ECO:0000269|PubMed:11349230,
FT ECO:0000269|PubMed:20498720"
FT /id="VAR_012359"
FT VARIANT 83
FT /note="F -> S (in SEDT; mild form; loss of interaction with
FT ENO1, PITX1 and SF1; dbSNP:rs104894948)"
FT /evidence="ECO:0000269|PubMed:11424925,
FT ECO:0000269|PubMed:20498720"
FT /id="VAR_012361"
FT VARIANT 130
FT /note="V -> D (in SEDT; loss of interaction with ENO1,
FT PITX1 and SF1)"
FT /evidence="ECO:0000269|PubMed:11349230,
FT ECO:0000269|PubMed:20498720"
FT /id="VAR_012360"
SQ SEQUENCE 140 AA; 16445 MW; B099943C6F88952C CRC64;
MSGSFYFVIV GHHDNPVFEM EFLPAGKAES KDDHRHLNQF IAHAALDLVD ENMWLSNNMY
LKTVDKFNEW FVSAFVTAGH MRFIMLHDIR QEDGIKNFFT DVYDLYIKFS MNPFYEPNSP
IRSSAFDRKV QFLGKKHLLS
//
