TPC2B_HUMAN
ID TPC2B_HUMAN Reviewed; 140 AA.
AC P0DI82; A6NEG0; O14582; Q9HD16;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Trafficking protein particle complex subunit 2B;
DE AltName: Full=MBP-1-interacting protein 2A;
DE Short=MIP-2A;
GN Name=TRAPPC2B; Synonyms=SEDLP1, TRAPPC2.19, TRAPPC2P1;
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 [MRNA], FUNCTION, INTERACTION WITH ENO1, AND
RP SUBCELLULAR LOCATION.
RX 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 1.";
RL Mol. Cell. Biol. 21:655-662(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hu G.;
RT "Human cDNA complete cds homolog to yeast protein P38334.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
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., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung carcinoma;
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 TISSUE SPECIFICITY.
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 [6]
RP GENOMIC ORGANIZATION.
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 [7]
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 [8]
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 [9]
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 [10]
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).
CC -!- FUNCTION: Prevents transcriptional repression and induction of cell
CC death by ENO1. May play a role in vesicular transport from endoplasmic
CC reticulum to Golgi. {ECO:0000269|PubMed:11134351}.
CC -!- SUBUNIT: Interacts with PITX1, SF1, and TRAPPC3 (By similarity). Can
CC homodimerize (By similarity). Part of the multisubunit TRAPP (transport
CC protein particle) complex. Interacts with ENO1 and TRAPPC2L.
CC {ECO:0000250, ECO:0000269|PubMed:11134351, ECO:0000269|PubMed:11805826,
CC ECO:0000269|PubMed:19416478}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0DI81}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:11134351}.
CC Endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm
CC {ECO:0000250|UniProtKB:P0DI81}. Note=Localized in perinuclear granular
CC structures. {ECO:0000250|UniProtKB:P0DI81}.
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 -!- MISCELLANEOUS: The gene encoding this protein appears to have arisen by
CC retrotransposition of a cDNA from the X-linked locus TRAPPC2. The site
CC of integration of this retrotransposed cDNA appears to lie within an
CC intron of the ZNF547 gene, which provides a promoter and non-coding 5'
CC exon. TRAPPC2 and this protein are indistinguishable at protein level,
CC and both proteins have been identified and functionally characterized.
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. Sedlin
CC subfamily. {ECO:0000305}.
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DR EMBL; AF291676; AAG02469.1; -; mRNA.
DR EMBL; AF058918; AAC14421.1; -; mRNA.
DR EMBL; AC003002; AAB80684.1; -; Genomic_DNA.
DR EMBL; BC008889; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC032809; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS86812.1; -.
DR RefSeq; NP_001011658.1; NM_001011658.3.
DR RefSeq; NP_055378.1; NM_014563.5.
DR RefSeq; XP_011543867.1; XM_011545565.1.
DR RefSeq; XP_011543868.1; XM_011545566.2.
DR AlphaFoldDB; P0DI82; -.
DR SMR; P0DI82; -.
DR BioGRID; 112299; 118.
DR ComplexPortal; CPX-6902; TRAPP II complex, TRAPPC2B variant.
DR ComplexPortal; CPX-6903; TRAPP III complex, TRAPPC2B variant.
DR IntAct; P0DI82; 2.
DR iPTMnet; P0DI82; -.
DR PhosphoSitePlus; P0DI82; -.
DR BioMuta; HGNC:10710; -.
DR DMDM; 347662478; -.
DR EPD; P0DI82; -.
DR jPOST; P0DI82; -.
DR MassIVE; P0DI82; -.
DR PRIDE; P0DI82; -.
DR Antibodypedia; 52678; 3 antibodies from 1 providers.
DR DNASU; 6399; -.
DR Ensembl; ENST00000543226.2; ENSP00000442778.1; ENSG00000256060.3.
DR Ensembl; ENST00000596755.1; ENSP00000469888.1; ENSG00000256060.3.
DR GeneID; 6399; -.
DR KEGG; hsa:6399; -.
DR MANE-Select; ENST00000380579.6; ENSP00000369953.1; NM_001011658.4; NP_001011658.1.
DR MANE-Select; ENST00000543226.2; ENSP00000442778.1; NM_001355204.2; NP_001342133.1.
DR CTD; 6399; -.
DR DisGeNET; 6399; -.
DR GeneCards; TRAPPC2B; -.
DR HGNC; HGNC:10710; TRAPPC2B.
DR HPA; ENSG00000256060; Low tissue specificity.
DR neXtProt; NX_P0DI82; -.
DR OpenTargets; ENSG00000196459; -.
DR OpenTargets; ENSG00000256060; -.
DR VEuPathDB; HostDB:ENSG00000256060; -.
DR GeneTree; ENSGT00510000047168; -.
DR HOGENOM; CLU_085828_0_2_1; -.
DR InParanoid; P0DI82; -.
DR OMA; VDKFNQW; -.
DR PhylomeDB; P0DI82; -.
DR TreeFam; TF314814; -.
DR PathwayCommons; P0DI82; -.
DR SignaLink; P0DI82; -.
DR BioGRID-ORCS; 6399; 312 hits in 629 CRISPR screens.
DR GenomeRNAi; 6399; -.
DR Pharos; P0DI82; Tdark.
DR PRO; PR:P0DI82; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P0DI82; protein.
DR Bgee; ENSG00000256060; Expressed in gastrocnemius and 107 other tissues.
DR ExpressionAtlas; P0DI82; baseline and differential.
DR Genevisible; P0DI82; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005640; C:nuclear outer membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030008; C:TRAPP complex; IBA:GO_Central.
DR GO; GO:1990071; C:TRAPPII protein complex; IC:ComplexPortal.
DR GO; GO:1990072; C:TRAPPIII protein complex; IC:ComplexPortal.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:UniProtKB.
DR GO; GO:0048208; P:COPII vesicle coating; IC:ComplexPortal.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0006901; P:vesicle coating; IC:ComplexPortal.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR InterPro; IPR011012; Longin-like_dom_sf.
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 Cytoplasm; ER-Golgi transport; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transport.
FT CHAIN 1..140
FT /note="Trafficking protein particle complex subunit 2B"
FT /id="PRO_0000412454"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 105
FT /note="L -> P (in Ref. 1; AAG02469)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 140 AA; 16445 MW; B099943C6F88952C CRC64;
MSGSFYFVIV GHHDNPVFEM EFLPAGKAES KDDHRHLNQF IAHAALDLVD ENMWLSNNMY
LKTVDKFNEW FVSAFVTAGH MRFIMLHDIR QEDGIKNFFT DVYDLYIKFS MNPFYEPNSP
IRSSAFDRKV QFLGKKHLLS
