ID   TPPC2_HUMAN             Reviewed;         140 AA.
AC   O14582; A6NEG0; Q9HD16;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 3.
DT   03-NOV-2009, entry version 102.
DE   RecName: Full=Trafficking protein particle complex subunit 2;
DE   AltName: Full=Sedlin;
DE   AltName: Full=MBP-1-interacting protein 2A;
DE            Short=MIP-2A;
GN   Name=TRAPPC2; Synonyms=SEDL;
GN   and
GN   Name=TRAPPC2P1; Synonyms=SEDLP;
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 [GENOMIC DNA].
RX   MEDLINE=99364423; PubMed=10431248; DOI=10.1038/11976;
RA   Gedeon A.K., Colley A., Jamieson R., Thompson E.M., Rogers J.,
RA   Sillence D., 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 [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP   MBP1.
RX   MEDLINE=20576881; PubMed=11134351; DOI=10.1128/MCB.21.2.655-662.2001;
RA   Ghosh A.K., Majumder M., Steele R., White R.A., Ray R.B.;
RT   "A novel 16-kilodalton cellular protein physically interacts with and
RT   antagonizes the functional activity of c-myc promoter-binding protein
RT   1.";
RL   Mol. Cell. Biol. 21:655-662(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Hu G.;
RT   "Human cDNA complete cds homolog to yeast protein P38334.";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [5]
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.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   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.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   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.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   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.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   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.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, Lung, 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   GENOMIC ORGANIZATION, ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION.
RX   MEDLINE=20487551; 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   [8]
RP   IDENTIFICATION IN TRAPP COMPLEX.
RX   MEDLINE=21664186; 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.,
RA   Hoefert C., Schelder M., Brajenovic M., Ruffner H., Merino A.,
RA   Klein K., Hudak M., Dickson D., Rudi T., Gnau V., Bauch A.,
RA   Bastuck S., Huhse B., Leutwein C., Heurtier M.-A., Copley R.R.,
RA   Edelmann A., Querfurth E., Rybin V., Drewes G., Raida M.,
RA   Bouwmeester T., Bork P., Seraphin B., Kuster B., Neubauer G.,
RA   Superti-Furga G.;
RT   "Functional organization of the yeast proteome by systematic analysis
RT   of protein complexes.";
RL   Nature 415:141-147(2002).
RN   [9]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [10]
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   [11]
RP   VARIANTS SEDT TYR-47; LEU-73 AND ASP-130.
RX   MEDLINE=21313110; 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   [12]
RP   VARIANT SEDT SER-83.
RX   MEDLINE=21317613; 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
RT   linked spondyloepiphyseal dysplasia in a large pedigree.";
RL   J. Med. Genet. 38:409-411(2001).
CC   -!- FUNCTION: Prevents MBP1-mediated transcriptional repression and
CC       antagonizes MBP1-mediated cell death. May play a role in vesicular
CC       transport from endoplasmic reticulum to Golgi.
CC   -!- SUBUNIT: Part of the multisubunit TRAPP (transport protein
CC       particle) complex. Interacts with MBP1 and TRAPPC2L.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Endoplasmic
CC       reticulum. Golgi apparatus. Note=Localized in perinuclear granular
CC       structures.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1; Synonyms=Major;
CC         IsoId=O14582-1; Sequence=Displayed;
CC       Name=2; Synonyms=Minor;
CC         IsoId=O14582-2; Sequence=VSP_006040;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DISEASE: Defects in TRAPPC2 are the cause of spondyloepiphyseal
CC       dysplasia tarda (SEDT) [MIM:313400]. SEDT is an X-linked recessive
CC       disorder of endochondral bone formation.
CC   -!- SIMILARITY: Belongs to the TRAPP small subunits family. Sedlin
CC       subfamily.
CC   -!- CAUTION: There are 2 copies of the gene for this protein: one on
CC       chromosome X and the other on chromosome 19; the one on 19 is said
CC       to be a processed pseudogene that shares a non-coding exon with
CC       ZNF547.
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/TRAPPC2";
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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; AF291676; AAG02469.1; -; mRNA.
DR   EMBL; AF058918; AAC14421.1; -; mRNA.
DR   EMBL; AC003037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC003002; AAB80684.1; -; Genomic_DNA.
DR   EMBL; BC008889; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC016915; AAH16915.1; -; mRNA.
DR   EMBL; BC032809; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC052618; AAH52618.1; -; mRNA.
DR   IPI; IPI00005119; -.
DR   IPI; IPI00217250; -.
DR   RefSeq; NP_001011658.1; -.
DR   RefSeq; NP_055378.1; -.
DR   UniGene; Hs.446620; -.
DR   UniGene; Hs.592238; -.
DR   UniGene; Hs.622292; -.
DR   SMR; O14582; 1-140.
DR   IntAct; O14582; 1.
DR   STRING; O14582; -.
DR   PRIDE; O14582; -.
DR   Ensembl; ENST00000358231; ENSP00000350966; ENSG00000196459; Homo sapiens.
DR   Ensembl; ENST00000359680; ENSP00000352708; ENSG00000196459; Homo sapiens.
DR   Ensembl; ENST00000380578; ENSP00000369952; ENSG00000196459; Homo sapiens.
DR   Ensembl; ENST00000380579; ENSP00000369953; ENSG00000196459; Homo sapiens.
DR   Ensembl; ENST00000426522; ENSP00000393394; ENSG00000196459; Homo sapiens.
DR   Ensembl; ENST00000453655; ENSP00000394629; ENSG00000196459; Homo sapiens.
DR   Ensembl; ENST00000458511; ENSP00000392495; ENSG00000196459; Homo sapiens.
DR   GeneID; 6399; -.
DR   KEGG; hsa:6399; -.
DR   CTD; 6399; -.
DR   GeneCards; GC0XM013640; -.
DR   H-InvDB; HIX0015497; -.
DR   H-InvDB; HIX0016661; -.
DR   HGNC; HGNC:23068; TRAPPC2.
DR   HGNC; HGNC:10710; TRAPPC2P1.
DR   HPA; CAB004665; -.
DR   MIM; 300202; gene.
DR   MIM; 313400; phenotype.
DR   Orphanet; 253; Spondyloepiphyseal dysplasia.
DR   Orphanet; 93284; Spondyloepiphyseal dysplasia tarda.
DR   PharmGKB; PA35631; -.
DR   HOVERGEN; O14582; -.
DR   OMA; GIKNFFN; -.
DR   NextBio; 24860; -.
DR   ArrayExpress; O14582; -.
DR   Bgee; O14582; -.
DR   CleanEx; HS_TRAPPC2; -.
DR   Genevestigator; O14582; -.
DR   GermOnline; ENSG00000152433; Homo sapiens.
DR   GermOnline; ENSG00000196459; Homo sapiens.
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:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; NAS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR   GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR006722; Sedlin.
DR   PANTHER; PTHR12403; Sedlin; 1.
DR   Pfam; PF04628; Sedlin_N; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Cytoplasm; Disease mutation;
KW   Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW   Transcription; Transport.
FT   CHAIN         1    140       Trafficking protein particle complex
FT                                subunit 2.
FT                                /FTId=PRO_0000211566.
FT   VAR_SEQ      80     80       H -> HILTFLVK (in isoform 2).
FT                                /FTId=VSP_006040.
FT   VARIANT      47     47       D -> Y (in SEDT).
FT                                /FTId=VAR_012358.
FT   VARIANT      73     73       S -> L (in SEDT).
FT                                /FTId=VAR_012359.
FT   VARIANT      83     83       F -> S (in SEDT; mild form).
FT                                /FTId=VAR_012361.
FT   VARIANT     130    130       V -> D (in SEDT).
FT                                /FTId=VAR_012360.
FT   CONFLICT    105    105       L -> P (in Ref. 2; AAG02469).
SQ   SEQUENCE   140 AA;  16445 MW;  B099943C6F88952C CRC64;
     MSGSFYFVIV GHHDNPVFEM EFLPAGKAES KDDHRHLNQF IAHAALDLVD ENMWLSNNMY
     LKTVDKFNEW FVSAFVTAGH MRFIMLHDIR QEDGIKNFFT DVYDLYIKFS MNPFYEPNSP
     IRSSAFDRKV QFLGKKHLLS
//