TEX2_HUMAN
ID TEX2_HUMAN Reviewed; 1127 AA.
AC Q8IWB9; Q6AHZ5; Q8N3L0; Q9C0C5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Testis-expressed protein 2;
DE AltName: Full=Transmembrane protein 96;
GN Name=TEX2; Synonyms=KIAA1738, TMEM96;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196; SER-266; SER-270 AND
RP SER-295, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196; SER-266 AND SER-732, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-295; SER-732;
RP SER-738 AND SER-744, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=22250200; DOI=10.1242/jcs.085118;
RA Toulmay A., Prinz W.A.;
RT "A conserved membrane-binding domain targets proteins to organelle contact
RT sites.";
RL J. Cell Sci. 125:49-58(2012).
RN [10]
RP FUNCTION.
RX PubMed=28011845; DOI=10.1083/jcb.201606059;
RA Liu L.K., Choudhary V., Toulmay A., Prinz W.A.;
RT "An inducible ER-Golgi tether facilitates ceramide transport to alleviate
RT lipotoxicity.";
RL J. Cell Biol. 216:131-147(2017).
CC -!- FUNCTION: During endoplasmic reticulum (ER) stress or when cellular
CC ceramide levels increase, may induce contacts between the ER and
CC medial-Golgi complex to facilitate non-vesicular transport of ceramides
CC from the ER to the Golgi complex where they are converted to complex
CC sphingolipids, preventing toxic ceramide accumulation.
CC {ECO:0000269|PubMed:28011845}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q06833}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q06833}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Enriched at the nucleus-
CC vacuole junction (PubMed:22250200). During endoplasmic reticulum (ER)
CC stress, localizes to ER-Golgi contacts (By similarity).
CC {ECO:0000250|UniProtKB:Q06833, ECO:0000269|PubMed:22250200}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IWB9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IWB9-2; Sequence=VSP_019569;
CC -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that can bind
CC various types of glycerophospholipids in its interior and mediate their
CC transfer between two adjacent bilayers. {ECO:0000255|PROSITE-
CC ProRule:PRU01194}.
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DR EMBL; AB051525; BAB21829.2; -; mRNA.
DR EMBL; AL834251; CAD38927.1; -; mRNA.
DR EMBL; CR627433; CAH10519.1; -; mRNA.
DR EMBL; BC040521; AAH40521.1; -; mRNA.
DR CCDS; CCDS11658.1; -. [Q8IWB9-2]
DR CCDS; CCDS74131.1; -. [Q8IWB9-1]
DR RefSeq; NP_001275661.1; NM_001288732.1. [Q8IWB9-1]
DR RefSeq; NP_001275662.1; NM_001288733.1. [Q8IWB9-1]
DR RefSeq; NP_060939.3; NM_018469.4. [Q8IWB9-2]
DR RefSeq; XP_011523300.1; XM_011524998.1. [Q8IWB9-2]
DR RefSeq; XP_011523301.1; XM_011524999.1. [Q8IWB9-2]
DR AlphaFoldDB; Q8IWB9; -.
DR BioGRID; 120954; 77.
DR DIP; DIP-47321N; -.
DR IntAct; Q8IWB9; 13.
DR MINT; Q8IWB9; -.
DR STRING; 9606.ENSP00000258991; -.
DR GlyGen; Q8IWB9; 3 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8IWB9; -.
DR PhosphoSitePlus; Q8IWB9; -.
DR BioMuta; TEX2; -.
DR DMDM; 109895136; -.
DR EPD; Q8IWB9; -.
DR jPOST; Q8IWB9; -.
DR MassIVE; Q8IWB9; -.
DR MaxQB; Q8IWB9; -.
DR PaxDb; Q8IWB9; -.
DR PeptideAtlas; Q8IWB9; -.
DR PRIDE; Q8IWB9; -.
DR ProteomicsDB; 70839; -. [Q8IWB9-1]
DR ProteomicsDB; 70840; -. [Q8IWB9-2]
DR Antibodypedia; 19114; 96 antibodies from 22 providers.
DR DNASU; 55852; -.
DR Ensembl; ENST00000258991.7; ENSP00000258991.3; ENSG00000136478.9. [Q8IWB9-2]
DR Ensembl; ENST00000583097.5; ENSP00000462665.1; ENSG00000136478.9. [Q8IWB9-1]
DR Ensembl; ENST00000584379.6; ENSP00000463001.1; ENSG00000136478.9. [Q8IWB9-1]
DR GeneID; 55852; -.
DR KEGG; hsa:55852; -.
DR MANE-Select; ENST00000584379.6; ENSP00000463001.1; NM_001288732.2; NP_001275661.1.
DR UCSC; uc002jec.5; human. [Q8IWB9-1]
DR CTD; 55852; -.
DR DisGeNET; 55852; -.
DR GeneCards; TEX2; -.
DR HGNC; HGNC:30884; TEX2.
DR HPA; ENSG00000136478; Low tissue specificity.
DR neXtProt; NX_Q8IWB9; -.
DR OpenTargets; ENSG00000136478; -.
DR PharmGKB; PA142670820; -.
DR VEuPathDB; HostDB:ENSG00000136478; -.
DR eggNOG; KOG2238; Eukaryota.
DR GeneTree; ENSGT00390000000463; -.
DR HOGENOM; CLU_008315_0_0_1; -.
DR InParanoid; Q8IWB9; -.
DR OMA; IIPLPGY; -.
DR OrthoDB; 332149at2759; -.
DR PhylomeDB; Q8IWB9; -.
DR TreeFam; TF314900; -.
DR PathwayCommons; Q8IWB9; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR SignaLink; Q8IWB9; -.
DR BioGRID-ORCS; 55852; 36 hits in 1077 CRISPR screens.
DR ChiTaRS; TEX2; human.
DR GenomeRNAi; 55852; -.
DR Pharos; Q8IWB9; Tbio.
DR PRO; PR:Q8IWB9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8IWB9; protein.
DR Bgee; ENSG00000136478; Expressed in medial globus pallidus and 202 other tissues.
DR ExpressionAtlas; Q8IWB9; baseline and differential.
DR Genevisible; Q8IWB9; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0006665; P:sphingolipid metabolic process; NAS:UniProtKB.
DR InterPro; IPR031468; SMP_LBD.
DR PROSITE; PS51847; SMP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Lipid transport;
KW Lipid-binding; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1127
FT /note="Testis-expressed protein 2"
FT /id="PRO_0000244479"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 816..1101
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 262
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPJ0"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPJ0"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPJ0"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPJ0"
FT MOD_RES 798
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPJ0"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPJ0"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 724
FT /note="K -> KPAPVFLA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019569"
FT VARIANT 158
FT /note="T -> I (in dbSNP:rs28605685)"
FT /id="VAR_061712"
FT CONFLICT 53
FT /note="R -> K (in Ref. 3; AAH40521)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="N -> S (in Ref. 2; CAD38927)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="P -> S (in Ref. 2; CAH10519)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="E -> K (in Ref. 3; AAH40521)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="I -> V (in Ref. 2; CAD38927)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="P -> L (in Ref. 2; CAD38927)"
FT /evidence="ECO:0000305"
FT CONFLICT 725..729
FT /note="PGLLP -> LRAFA (in Ref. 2; CAH10519)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="F -> S (in Ref. 2; CAD38927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1127 AA; 125303 MW; 100D99905117CD57 CRC64;
MTSLYGRHAE KTTDMPKPSA PKVHVQRSVS RDTIAIHFSA SGEEEEEEEE EFREYFEEGL
DDQSIVTGLE AKEDLYLEPQ VGHDPAGPAA SPVLADGLSV SQAPAILPVS KNTVKLLESP
VPAAQVLSTV PLAVSPGSSS SGPLASSPSV SSLSEQKTSS SSPLSSPSKS PILSSSASTS
TLSSAKPFMS LVKSLSTEVE PKESPHPARH RHLMKTLVKS LSTDTSRQES DTVSYKPPDS
KLNLHLFKQF TQPRNTGGDS KTAPSSPLTS PSDTRSFFKV PEMEAKIEDT KRRLSEVIYE
PFQLLSKIIG EESGSHRPKA LSSSASELSN LSSLNGHLES NNNYSIKEEE CDSEGDGYGS
DSNIPRSDHP KSTGEPTREI ELKSSQGSSL KDLGLKTSSL VLEKCSLSAL VSKEDEEFCE
LYTEDFDLET EGESKVDKLS DIPLKPEVLA EDGVVLDSED EVDSAVQHPE LPVKTLGFFI
MCVYVYLILP LPHYVSGLFL GIGLGFMTAV CVIWFFTPPS AHKYHKLHKN LRHWNTRSLD
IKEPEILKGW MNEIYNYDPE TYHATLTHSV FVRLEGGTLR LSKPNKNISR RASYNEPKPE
VTYISQKIYD LSDSKIYLVP KTLARKRIWN KKYPICIELG QQDDFMSKAQ TDKETSEEKP
PAEGSEDPKK PPRPQEGTRS SQRDQILYLF GRTGREKEEW FRRFILASKL KSEIKKSSGV
SGGKPGLLPA HSRHNSPSGH LTHSRSSSKG SVEEIMSQPK QKELAGSVRQ KMLLDYSVYM
GRCVPQESRS PQRSPLQSAE SSPTAGKKLP EVPPSEEEEQ EAWVNALLGR IFWDFLGEKY
WSDLVSKKIQ MKLSKIKLPY FMNELTLTEL DMGVAVPKIL QAFKPYVDHQ GLWIDLEMSY
NGSFLMTLET KMNLTKLGKE PLVEALKVGE IGKEGCRPRA FCLADSDEES SSAGSSEEDD
APEPSGGDKQ LLPGAEGYVG GHRTSKIMRF VDKITKSKYF QKATETEFIK KKIEEVSNTP
LLLTVEVQEC RGTLAVNIPP PPTDRVWYGF RKPPHVELKA RPKLGEREVT LVHVTDWIEK
KLEQEFQKVF VMPNMDDVYI TIMHSAMDPR STSCLLKDPP VEAADQP
