TPPC9_MOUSE
ID TPPC9_MOUSE Reviewed; 1148 AA.
AC Q3U0M1; Q3UU81; Q69Z79; Q6NS50; Q8CD01; Q8CFV8; Q9D8R6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Trafficking protein particle complex subunit 9;
DE AltName: Full=NIK- and IKBKB-binding protein;
GN Name=Trappc9; Synonyms=Kiaa1882, Nibp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH IKBKB
RP AND MAP3K14, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15951441; DOI=10.1074/jbc.m501670200;
RA Hu W.-H., Pendergast J.S., Mo X.-M., Brambilla R., Bracchi-Ricard V.,
RA Li F., Walters W.M., Blits B., He L., Schaal S.M., Bethea J.R.;
RT "NIBP, a novel NIK and IKK(beta)-binding protein that enhances NF-(kappa)B
RT activation.";
RL J. Biol. Chem. 280:29233-29241(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, Pancreas, Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 593-1148 (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-953, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Functions as an activator of NF-kappa-B through increased
CC phosphorylation of the IKK complex. May function in neuronal cells
CC differentiation. May play a role in vesicular transport from
CC endoplasmic reticulum to Golgi. {ECO:0000269|PubMed:15951441}.
CC -!- SUBUNIT: Component of the multisubunit TRAPP (transport protein
CC particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3,
CC TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and
CC TRAPPC12 (By similarity). Directly interacts with IKBKB and MAP3K14.
CC {ECO:0000250, ECO:0000269|PubMed:15951441}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}.
CC Endoplasmic reticulum {ECO:0000250}. Cytoplasm
CC {ECO:0000305|PubMed:15951441}. Note=Processes and cell bodies of
CC neurons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q3U0M1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U0M1-2; Sequence=VSP_034353;
CC Name=3;
CC IsoId=Q3U0M1-3; Sequence=VSP_034351, VSP_034352;
CC Name=4;
CC IsoId=Q3U0M1-4; Sequence=VSP_034353, VSP_034356;
CC Name=5;
CC IsoId=Q3U0M1-5; Sequence=VSP_034353, VSP_034354, VSP_034355;
CC -!- TISSUE SPECIFICITY: Expressed in neurons of the pyramidal layer of the
CC cortex, in spinal cord motor neurons and white matter neurons (at
CC protein level). {ECO:0000269|PubMed:15951441}.
CC -!- SIMILARITY: Belongs to the NIBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB25242.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY630620; AAV31909.1; -; mRNA.
DR EMBL; AK007766; BAB25242.1; ALT_INIT; mRNA.
DR EMBL; AK031788; BAC27550.1; -; mRNA.
DR EMBL; AK138682; BAE23746.1; -; mRNA.
DR EMBL; AK156739; BAE33831.1; -; mRNA.
DR EMBL; BC034590; AAH34590.1; -; mRNA.
DR EMBL; BC070463; AAH70463.1; -; mRNA.
DR EMBL; AK173287; BAD32565.1; -; mRNA.
DR CCDS; CCDS37095.1; -. [Q3U0M1-2]
DR CCDS; CCDS37096.1; -. [Q3U0M1-3]
DR CCDS; CCDS88775.1; -. [Q3U0M1-5]
DR RefSeq; NP_001158113.1; NM_001164641.1.
DR RefSeq; NP_001158114.1; NM_001164642.1.
DR RefSeq; NP_001158115.1; NM_001164643.1. [Q3U0M1-5]
DR RefSeq; NP_083916.1; NM_029640.2. [Q3U0M1-3]
DR RefSeq; NP_850993.2; NM_180662.2. [Q3U0M1-2]
DR RefSeq; XP_006521590.1; XM_006521527.3. [Q3U0M1-1]
DR AlphaFoldDB; Q3U0M1; -.
DR BioGRID; 218162; 6.
DR ComplexPortal; CPX-4764; TRAPP II complex.
DR IntAct; Q3U0M1; 3.
DR MINT; Q3U0M1; -.
DR STRING; 10090.ENSMUSP00000087202; -.
DR iPTMnet; Q3U0M1; -.
DR PhosphoSitePlus; Q3U0M1; -.
DR SwissPalm; Q3U0M1; -.
DR EPD; Q3U0M1; -.
DR MaxQB; Q3U0M1; -.
DR PaxDb; Q3U0M1; -.
DR PeptideAtlas; Q3U0M1; -.
DR PRIDE; Q3U0M1; -.
DR ProteomicsDB; 259064; -. [Q3U0M1-1]
DR ProteomicsDB; 259065; -. [Q3U0M1-2]
DR ProteomicsDB; 259066; -. [Q3U0M1-3]
DR ProteomicsDB; 259067; -. [Q3U0M1-4]
DR ProteomicsDB; 259068; -. [Q3U0M1-5]
DR Antibodypedia; 14382; 130 antibodies from 20 providers.
DR Ensembl; ENSMUST00000023276; ENSMUSP00000023276; ENSMUSG00000047921. [Q3U0M1-3]
DR Ensembl; ENSMUST00000089770; ENSMUSP00000087202; ENSMUSG00000047921. [Q3U0M1-2]
DR Ensembl; ENSMUST00000228960; ENSMUSP00000155105; ENSMUSG00000047921. [Q3U0M1-5]
DR GeneID; 76510; -.
DR KEGG; mmu:76510; -.
DR UCSC; uc007wbl.2; mouse. [Q3U0M1-3]
DR UCSC; uc007wbm.1; mouse. [Q3U0M1-2]
DR UCSC; uc007wbp.1; mouse. [Q3U0M1-4]
DR UCSC; uc011ztt.1; mouse. [Q3U0M1-5]
DR CTD; 83696; -.
DR MGI; MGI:1923760; Trappc9.
DR VEuPathDB; HostDB:ENSMUSG00000047921; -.
DR eggNOG; KOG1953; Eukaryota.
DR GeneTree; ENSGT00390000006486; -.
DR InParanoid; Q3U0M1; -.
DR OMA; HDHPVEH; -.
DR OrthoDB; 71855at2759; -.
DR PhylomeDB; Q3U0M1; -.
DR TreeFam; TF314341; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 76510; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Trappc9; mouse.
DR PRO; PR:Q3U0M1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q3U0M1; protein.
DR Bgee; ENSMUSG00000047921; Expressed in retinal neural layer and 216 other tissues.
DR ExpressionAtlas; Q3U0M1; baseline and differential.
DR Genevisible; Q3U0M1; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0030008; C:TRAPP complex; ISO:MGI.
DR GO; GO:1990071; C:TRAPPII protein complex; IC:ComplexPortal.
DR GO; GO:0021987; P:cerebral cortex development; ISO:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IC:ComplexPortal.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:MGI.
DR GO; GO:0006901; P:vesicle coating; IC:ComplexPortal.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR InterPro; IPR013935; TRAPP_II_complex_Trs120.
DR PANTHER; PTHR21512; PTHR21512; 1.
DR Pfam; PF08626; TRAPPC9-Trs120; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Differentiation; Endoplasmic reticulum;
KW Golgi apparatus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1148
FT /note="Trafficking protein particle complex subunit 9"
FT /id="PRO_0000341587"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q05"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..188
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15951441"
FT /id="VSP_034351"
FT VAR_SEQ 189..194
FT /note="GLDTDS -> MLLGLK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15951441"
FT /id="VSP_034352"
FT VAR_SEQ 286..294
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034353"
FT VAR_SEQ 499..503
FT /note="EKKDV -> ETLAT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034354"
FT VAR_SEQ 504..1148
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034355"
FT VAR_SEQ 706..1148
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034356"
FT CONFLICT 773
FT /note="E -> D (in Ref. 3; AAH70463)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1148 AA; 128232 MW; FB3C68229B691327 CRC64;
MSVPDYMQCA EDHQTLLVVV QAVGIVSEEN FFRIYKRICS VSQLSVRDTQ RALFIRYRHH
YPPENNEWGD FQTHRKVVGL ITITDCFSPK DWPQTFEKFH VQKEIYGSTL YDSRLFVFGL
QGDVAEQPRP DVAFYPNYDD CDSVEKRIED FIESLFIVLE SKRLDRATDK SGDKIPLLCV
PFEKKDFVGL DTDSRHYKKR CQGRMRKHVG DLCLQAGMLQ DALVHYHMSV ELLRSVNDFL
WLGAALEGLC SASVIYHYPG GTGGKTGARR LQGSSLPSEA ANRHRPGAQE VLIDPGALTT
NGINPDTSTE IGRAKNCLSP EDIIDKYKEA ISYYSKYKNA GVIELEACVK AVRVLAIQKR
GMEASEFLQN AVYINLRQLS EEEKIQRYSI LSELYELIGF HRKSAFFKRV AAMQCVAPSI
AEPGWRACYK LLLETLPGYS LSLDPKDFSK GTHRGWAAVQ MRLLHELVYA SRRMGNPALS
VRHLSFLLQT MLDFLSDQEK KDVTQSLENY TAKCPGTMEP ITLPDGLTLP PVPFTKLPIV
RCVKLLSLPT SLRPHKVKSL LGQSMSTKSP FIYSPIIAHN RGEERNKKID FQWVQGDVCE
VQLMVYNPMP FELRVENMGL LTSGVEFESL PAALSLPAES GLYPVTLVGV PQTTGMITVN
GYHTTVFGVF SDCLLDNLPG LKTGGSTVEV IPALPRLQIS TSLPRSARSL QPSAGDEIAT
NVSVQLYNGE TQQLAVTLEN IGLEPLEQLE VTSKLLTTKE KLYGDFLSWK LEETLAQFPL
QPGKVATFTI NIKAKLDFSC QENLLQDLSD DGISVSGFPL SSPFRQVVRP RVESRPTNPS
EGSKTGDLGH VKTLEAVLNF KYSGGPGHVE GYYRNLSLGL HVEVEPSVFF TRVSTLPATS
TRQCHLLLDV FNSTEHELTV CARNNSELVL HASECQRMAI QVDKFNFESV PESPGEKGHF
ANLKQLEEER QEARGLEISS KLDIRWRIPS LKRSGEASVE GLLNQLILEH LQLAPLQWDV
LVDGQPCDCE VAAACQVGDP VRLEVRLTNR SPRSVGPFAL TVVPFQDHQN GVHNYDLHDV
ISFVGSSTFY LDTVQPSGQS TCLGALLFLY TGDFFLNIRF HEDCKSKELP PSWVCLPSVH
VRALGAQA
