TPC10_HUMAN
ID TPC10_HUMAN Reviewed; 1259 AA.
AC P48553; Q3MIR2; Q86SI7; Q9UMD4; Q9Y4L3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Trafficking protein particle complex subunit 10;
DE AltName: Full=Epilepsy holoprosencephaly candidate 1 protein;
DE Short=EHOC-1;
DE AltName: Full=Protein GT334;
DE AltName: Full=Trafficking protein particle complex subunit TMEM1;
DE AltName: Full=Transport protein particle subunit TMEM1;
DE Short=TRAPP subunit TMEM1;
GN Name=TRAPPC10; Synonyms=EHOC1, TMEM1;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=7633421; DOI=10.1093/hmg/4.4.709;
RA Yamakawa K., Mitchell S., Hubert R., Chen X.-N., Colbern S., Huo Y.-K.,
RA Gadomski C., Kim U.-J., Korenberg J.R.;
RT "Isolation and characterization of a candidate gene for progressive
RT myoclonus epilepsy on 21q22.3.";
RL Hum. Mol. Genet. 4:709-716(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9196060; DOI=10.1006/bbrc.1997.6758;
RA Nagamine K., Kudoh J., Kawasaki K., Minoshima S., Asakawa S., Ito F.,
RA Shimizu N.;
RT "Genomic organization and complete nucleotide sequence of the TMEM1 gene on
RT human chromosome 21q22.3.";
RL Biochem. Biophys. Res. Commun. 235:185-190(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANTS GLU-257;
RP MET-633 AND MET-726.
RX PubMed=9370297; DOI=10.1016/s0378-1119(97)00333-8;
RA Lafreniere R.G., Kibar Z., Rochefort D.L., Han F.-Y., Fon E.A., Dube M.-P.,
RA Kang X., Baird S., Korneluk R.G., Rommens J.M., Rouleau G.A.;
RT "Genomic structure of the human GT334 (EHOC-1) gene mapping to 21q22.3.";
RL Gene 198:313-321(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lymph;
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 [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].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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-708, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP VARIANT LEU-929.
RX PubMed=30167849; DOI=10.1007/s00439-018-1928-6;
RA Santos-Cortez R.L.P., Khan V., Khan F.S., Mughal Z.U., Chakchouk I.,
RA Lee K., Rasheed M., Hamza R., Acharya A., Ullah E., Saqib M.A.N., Abbe I.,
RA Ali G., Hassan M.J., Khan S., Azeem Z., Ullah I., Bamshad M.J.,
RA Nickerson D.A., Schrauwen I., Ahmad W., Ansar M., Leal S.M.;
RT "Novel candidate genes and variants underlying autosomal recessive
RT neurodevelopmental disorders with intellectual disability.";
RL Hum. Genet. 137:735-752(2018).
RN [12]
RP IDENTIFICATION IN THE TRAPP II COMPLEX, AND INTERACTION WITH TRAPPC14.
RX PubMed=31467083; DOI=10.1074/jbc.ra119.008615;
RA Cuenca A., Insinna C., Zhao H., John P., Weiss M.A., Lu Q., Walia V.,
RA Specht S., Manivannan S., Stauffer J., Peden A.A., Westlake C.J.;
RT "The C7orf43/TRAPPC14 component links the TRAPPII complex to Rabin8 for
RT preciliary vesicle tethering at the mother centriole during ciliogenesis.";
RL J. Biol. Chem. 294:15418-15434(2019).
CC -!- FUNCTION: Specific subunit of the TRAPP (transport protein particle) II
CC complex, a highly conserved vesicle tethering complex that functions in
CC late Golgi trafficking as a membrane tether.
CC {ECO:0000269|PubMed:11805826, ECO:0000269|PubMed:31467083}.
CC -!- SUBUNIT: Specific component of the multisubunit TRAPP II complex, which
CC includes at least TRAPPC1, TRAPPC2, TRAPPC3, TRAPPC4, TRAPPC5,
CC TRAPPC6A/B, TRAPPC9, TRAPPC10 and TRAPPC14. TRAPPC9, TRAPPC10 and
CC TRAPPC14 are specific subunits of the TRAPP II complex
CC (PubMed:31467083, PubMed:21525244, PubMed:11805826). Interacts with
CC TRAPPC14 (PubMed:31467083). {ECO:0000269|PubMed:11805826,
CC ECO:0000269|PubMed:21525244, ECO:0000269|PubMed:31467083}.
CC -!- INTERACTION:
CC P48553; Q96QF0: RAB3IP; NbExp=7; IntAct=EBI-6160572, EBI-747844;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48553-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48553-2; Sequence=VSP_056589, VSP_056590;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC -!- DISEASE: Note=Defects in this gene may cause an autosomal recessive
CC disorder characterized by severe intellectual disability, poor speech
CC and aggressive behavior. {ECO:0000269|PubMed:30167849}.
CC -!- SIMILARITY: Belongs to the TRAPPC10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50134.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U19252; AAC50134.1; ALT_FRAME; mRNA.
DR EMBL; AB001523; BAA21099.1; -; Genomic_DNA.
DR EMBL; U61500; AAC51826.1; -; mRNA.
DR EMBL; U61520; AAB58468.1; -; Genomic_DNA.
DR EMBL; U61501; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61502; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61503; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61504; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61505; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61506; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61507; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61508; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61509; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61510; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61511; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61512; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61513; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61514; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61515; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61516; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61517; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61518; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; U61519; AAB58468.1; JOINED; Genomic_DNA.
DR EMBL; AB001517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046241; AAH46241.1; -; mRNA.
DR EMBL; BC052247; AAH52247.1; -; mRNA.
DR EMBL; BC094823; AAH94823.1; -; mRNA.
DR EMBL; BC101728; AAI01729.1; -; mRNA.
DR CCDS; CCDS13704.1; -. [P48553-1]
DR PIR; JC5523; JC5523.
DR RefSeq; NP_003265.3; NM_003274.4. [P48553-1]
DR RefSeq; XP_016855323.1; XM_016999834.1.
DR AlphaFoldDB; P48553; -.
DR BioGRID; 112964; 99.
DR ComplexPortal; CPX-4749; TRAPP II complex, TRAPPC2 variant.
DR ComplexPortal; CPX-6902; TRAPP II complex, TRAPPC2B variant.
DR CORUM; P48553; -.
DR DIP; DIP-48281N; -.
DR IntAct; P48553; 30.
DR MINT; P48553; -.
DR STRING; 9606.ENSP00000291574; -.
DR iPTMnet; P48553; -.
DR PhosphoSitePlus; P48553; -.
DR BioMuta; TRAPPC10; -.
DR DMDM; 12644285; -.
DR EPD; P48553; -.
DR jPOST; P48553; -.
DR MassIVE; P48553; -.
DR MaxQB; P48553; -.
DR PaxDb; P48553; -.
DR PeptideAtlas; P48553; -.
DR PRIDE; P48553; -.
DR ProteomicsDB; 55909; -. [P48553-1]
DR ProteomicsDB; 69592; -.
DR Antibodypedia; 24094; 138 antibodies from 21 providers.
DR DNASU; 7109; -.
DR Ensembl; ENST00000291574.9; ENSP00000291574.4; ENSG00000160218.13. [P48553-1]
DR Ensembl; ENST00000380221.7; ENSP00000369570.3; ENSG00000160218.13. [P48553-2]
DR GeneID; 7109; -.
DR KEGG; hsa:7109; -.
DR MANE-Select; ENST00000291574.9; ENSP00000291574.4; NM_003274.5; NP_003265.3.
DR UCSC; uc002zdz.4; human. [P48553-1]
DR CTD; 7109; -.
DR DisGeNET; 7109; -.
DR GeneCards; TRAPPC10; -.
DR HGNC; HGNC:11868; TRAPPC10.
DR HPA; ENSG00000160218; Low tissue specificity.
DR MIM; 602103; gene.
DR neXtProt; NX_P48553; -.
DR OpenTargets; ENSG00000160218; -.
DR PharmGKB; PA162406870; -.
DR VEuPathDB; HostDB:ENSG00000160218; -.
DR eggNOG; KOG1931; Eukaryota.
DR GeneTree; ENSGT00390000003873; -.
DR HOGENOM; CLU_006893_0_0_1; -.
DR InParanoid; P48553; -.
DR OMA; TKVHENP; -.
DR OrthoDB; 537782at2759; -.
DR PhylomeDB; P48553; -.
DR TreeFam; TF320954; -.
DR PathwayCommons; P48553; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; P48553; -.
DR BioGRID-ORCS; 7109; 18 hits in 1074 CRISPR screens.
DR ChiTaRS; TRAPPC10; human.
DR GeneWiki; TMEM1; -.
DR GenomeRNAi; 7109; -.
DR Pharos; P48553; Tbio.
DR PRO; PR:P48553; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P48553; protein.
DR Bgee; ENSG00000160218; Expressed in bone marrow cell and 123 other tissues.
DR ExpressionAtlas; P48553; baseline and differential.
DR Genevisible; P48553; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030008; C:TRAPP complex; IDA:UniProtKB.
DR GO; GO:1990071; C:TRAPPII protein complex; IBA:GO_Central.
DR GO; GO:0034498; P:early endosome to Golgi transport; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IC:ComplexPortal.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006901; P:vesicle coating; IC:ComplexPortal.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR InterPro; IPR022233; TRAPP_II_complex_TRAPPC10_C.
DR InterPro; IPR045126; TRAPPC10/Trs130.
DR PANTHER; PTHR13251; PTHR13251; 1.
DR Pfam; PF12584; TRAPPC10; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ER-Golgi transport; Golgi apparatus; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..1259
FT /note="Trafficking protein particle complex subunit 10"
FT /id="PRO_0000193509"
FT REGION 1189..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 264..276
FT /note="DGANWLTFFCQPV -> GIKCPFHNSVACW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056589"
FT VAR_SEQ 277..1259
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056590"
FT VARIANT 257
FT /note="V -> E"
FT /evidence="ECO:0000269|PubMed:9370297"
FT /id="VAR_009514"
FT VARIANT 633
FT /note="I -> M (in dbSNP:rs915877)"
FT /evidence="ECO:0000269|PubMed:9370297"
FT /id="VAR_009515"
FT VARIANT 726
FT /note="V -> M (in dbSNP:rs2071152)"
FT /evidence="ECO:0000269|PubMed:9370297"
FT /id="VAR_009516"
FT VARIANT 929
FT /note="P -> L (found in 2 patients with intellectual
FT disability; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:30167849"
FT /id="VAR_084045"
FT CONFLICT 114
FT /note="V -> A (in Ref. 3; AAB58468)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="V -> A (in Ref. 3; AAB58468)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="Y -> D (in Ref. 1; AAC50134)"
FT /evidence="ECO:0000305"
FT CONFLICT 910
FT /note="K -> Q (in Ref. 3; AAC51826/AAB58468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1259 AA; 142189 MW; E8AB6847C9C6FE0C CRC64;
MDASEEPLPP VIYTMENKPI VTCAGDQNLF TSVYPTLSQQ LPREPMEWRR SYGRAPKMIH
LESNFVQFKE ELLPKEGNKA LLTFPFLHIY WTECCDTEVY KATVKDDLTK WQNVLKAHSS
VDWLIVIVEN DAKKKNKTNI LPRTSIVDKI RNDFCNKQSD RCVVLSDPLK DSSRTQESWN
AFLTKLRTLL LMSFTKNLGK FEDDMRTLRE KRTEPGWSFC EYFMVQEELA FVFEMLQQFE
DALVQYDELD ALFSQYVVNF GAGDGANWLT FFCQPVKSWN GLILRKPIDM EKRESIQRRE
ATLLDLRSYL FSRQCTLLLF LQRPWEVAQR ALELLHNCVQ ELKLLEVSVP PGALDCWVFL
SCLEVLQRIE GCCDRAQIDS NIAHTVGLWS YATEKLKSLG YLCGLVSEKG PNSEDLNRTV
DLLAGLGAER PETANTAQSP YKKLKEALSS VEAFEKHYLD LSHATIEMYT SIGRIRSAKF
VGKDLAEFYM RKKAPQKAEI YLQGALKNYL AEGWALPITH TRKQLAECQK HLGQIENYLQ
TSSLLASDHH LTEEERKHFC QEILDFASQP SDSPGHKIVL PMHSFAQLRD LHFDPSNAVV
HVGGVLCVEI TMYSQMPVPV HVEQIVVNVH FSIEKNSYRK TAEWLTKHKT SNGIINFPPE
TAPFPVSQNS LPALELYEMF ERSPSDNSLN TTGIICRNVH MLLRRQESSS SLEMPSGVAL
EEGAHVLRCS HVTLEPGANQ ITFRTQAKEP GTYTLRQLCA SVGSVWFVLP HIYPIVQYDV
YSQEPQLHVE PLADSLLAGI PQRVKFTVTT GHYTIKNGDS LQLSNAEAML ILCQAESRAV
VYSNTREQSS EAALRIQSSD KVTSISLPVA PAYHVIEFEL EVLSLPSAPA LGGESDMLGM
AEPHRKHKDK QRTGRCMVTT DHKVSIDCPW SIYSTVIALT FSVPFRTTHS LLSSGTRKYV
QVCVQNLSEL DFQLSDSYLV DTGDSTDLQL VPLNTQSQQP IYSKQSVFFV WELKWTEEPP
PSLHCRFSVG FSPASEEQLS ISLKPYTYEF KVENFFTLYN VKAEIFPPSG MEYCRTGSLC
SLEVLITRLS DLLEVDKDEA LTESDEHFST KLMYEVVDNS SNWAVCGKSC GVISMPVAAR
ATHRVHMEVM PLFAGYLPLP DVRLFKYLPH HSAHSSQLDA DSWIENDSLS VDKHGDDQPD
SSSLKSRGSV HSACSSEHKG LPMPRLQALP AGQVFNSSSG TQVLVIPSQD DHVLEVSVT
