TM131_HUMAN
ID TM131_HUMAN Reviewed; 1883 AA.
AC Q92545;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Transmembrane protein 131;
DE AltName: Full=Protein RW1;
GN Name=TMEM131; Synonyms=KIAA0257, RW1;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-1883.
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1863, AND IDENTIFICATION BY
RP 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-300.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1375, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1342 AND SER-1863, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1322; SER-1375 AND SER-1871,
RP AND 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).
CC -!- FUNCTION: May play a role in the immune response to viral infection.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TMEM131 family. {ECO:0000305}.
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DR EMBL; AC079337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D87446; BAA13387.1; -; mRNA.
DR CCDS; CCDS46368.1; -.
DR RefSeq; NP_056163.1; NM_015348.1.
DR AlphaFoldDB; Q92545; -.
DR BioGRID; 117052; 179.
DR IntAct; Q92545; 24.
DR STRING; 9606.ENSP00000186436; -.
DR GlyConnect; 1850; 4 N-Linked glycans (3 sites).
DR GlyGen; Q92545; 8 sites, 3 N-linked glycans (3 sites).
DR iPTMnet; Q92545; -.
DR PhosphoSitePlus; Q92545; -.
DR BioMuta; TMEM131; -.
DR DMDM; 327478552; -.
DR EPD; Q92545; -.
DR jPOST; Q92545; -.
DR MassIVE; Q92545; -.
DR MaxQB; Q92545; -.
DR PaxDb; Q92545; -.
DR PeptideAtlas; Q92545; -.
DR PRIDE; Q92545; -.
DR ProteomicsDB; 75306; -.
DR Antibodypedia; 9002; 23 antibodies from 9 providers.
DR DNASU; 23505; -.
DR Ensembl; ENST00000186436.10; ENSP00000186436.5; ENSG00000075568.17.
DR GeneID; 23505; -.
DR KEGG; hsa:23505; -.
DR MANE-Select; ENST00000186436.10; ENSP00000186436.5; NM_015348.2; NP_056163.1.
DR UCSC; uc002syh.5; human.
DR CTD; 23505; -.
DR DisGeNET; 23505; -.
DR GeneCards; TMEM131; -.
DR HGNC; HGNC:30366; TMEM131.
DR HPA; ENSG00000075568; Low tissue specificity.
DR MIM; 615659; gene.
DR neXtProt; NX_Q92545; -.
DR OpenTargets; ENSG00000075568; -.
DR PharmGKB; PA143485651; -.
DR VEuPathDB; HostDB:ENSG00000075568; -.
DR eggNOG; KOG3620; Eukaryota.
DR GeneTree; ENSGT00530000063614; -.
DR HOGENOM; CLU_002491_1_1_1; -.
DR InParanoid; Q92545; -.
DR OMA; EGPQNLW; -.
DR OrthoDB; 45814at2759; -.
DR PhylomeDB; Q92545; -.
DR TreeFam; TF321435; -.
DR PathwayCommons; Q92545; -.
DR SignaLink; Q92545; -.
DR BioGRID-ORCS; 23505; 21 hits in 1079 CRISPR screens.
DR ChiTaRS; TMEM131; human.
DR GeneWiki; TMEM131; -.
DR GenomeRNAi; 23505; -.
DR Pharos; Q92545; Tdark.
DR PRO; PR:Q92545; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q92545; protein.
DR Bgee; ENSG00000075568; Expressed in bronchial epithelial cell and 213 other tissues.
DR ExpressionAtlas; Q92545; baseline and differential.
DR Genevisible; Q92545; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR039877; TMEM131-like.
DR InterPro; IPR045695; TMEM131-like_conserved.
DR InterPro; IPR022113; TMEM131-like_N.
DR PANTHER; PTHR22050; PTHR22050; 1.
DR Pfam; PF19532; TMEM131_like; 2.
DR Pfam; PF12371; TMEM131_like_N; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1883
FT /note="Transmembrane protein 131"
FT /id="PRO_0000097538"
FT TRANSMEM 1091..1111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1118..1138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1198..1580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1593..1656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1670..1712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1766..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1832..1858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1674..1712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 803
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 1322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
SQ SEQUENCE 1883 AA; 205138 MW; BBC61F6C939A336E CRC64;
MGKRAGGGAT GATTAAVSTS AGAGLEPAAA RSGGPRSAAA GLLGALHLVM TLVVAAARAE
KEAFVQSESI IEVLRFDDGG LLQTETTLGL SSYQQKSISL YRGNCRPIRF EPPMLDFHEQ
PVGMPKMEKV YLHNPSSEET ITLVSISATT SHFHASFFQN RKILPGGNTS FDVVFLARVV
GNVENTLFIN TSNHGVFTYQ VFGVGVPNPY RLRPFLGARV PVNSSFSPII NIHNPHSEPL
QVVEMYSSGG DLHLELPTGQ QGGTRKLWEI PPYETKGVMR ASFSSREADN HTAFIRIKTN
ASDSTEFIIL PVEVEVTTAP GIYSSTEMLD FGTLRTQDLP KVLNLHLLNS GTKDVPITSV
RPTPQNDAIT VHFKPITLKA SESKYTKVAS ISFDASKAKK PSQFSGKITV KAKEKSYSKL
EIPYQAEVLD GYLGFDHAAT LFHIRDSPAD PVERPIYLTN TFSFAILIHD VLLPEEAKTM
FKVHNFSKPV LILPNESGYI FTLLFMPSTS SMHIDNNILL ITNASKFHLP VRVYTGFLDY
FVLPPKIEER FIDFGVLSAT EASNILFAII NSNPIELAIK SWHIIGDGLS IELVAVERGN
RTTIISSLPE FEKSSLSDQS SVTLASGYFA VFRVKLTAKK LEGIHDGAIQ ITTDYEILTI
PVKAVIAVGS LTCFPKHVVL PPSFPGKIVH QSLNIMNSFS QKVKIQQIRS LSEDVRFYYK
RLRGNKEDLE PGKKSKIANI YFDPGLQCGD HCYVGLPFLS KSEPKVQPGV AMQEDMWDAD
WDLHQSLFKG WTGIKENSGH RLSAIFEVNT DLQKNIISKI TAELSWPSIL SSPRHLKFPL
TNTNCSSEEE ITLENPADVP VYVQFIPLAL YSNPSVFVDK LVSRFNLSKV AKIDLRTLEF
QVFRNSAHPL QSSTGFMEGL SRHLILNLIL KPGEKKSVKV KFTPVHNRTV SSLIIVRNNL
TVMDAVMVQG QGTTENLRVA GKLPGPGSSL RFKITEALLK DCTDSLKLRE PNFTLKRTFK
VENTGQLQIH IETIEISGYS CEGYGFKVVN CQEFTLSANA SRDIIILFTP DFTASRVIRE
LKFITTSGSE FVFILNASLP YHMLATCAEA LPRPNWELAL YIIISGIMSA LFLLVIGTAY
LEAQGIWEPF RRRLSFEASN PPFDVGRPFD LRRIVGISSE GNLNTLSCDP GHSRGFCGAG
GSSSRPSAGS HKQCGPSVHP HSSHSNRNSA DVENVRAKNS SSTSSRTSAQ AASSQSANKT
SPLVLDSNTV TQGHTAGRKS KGAKQSQHGS QHHAHSPLEQ HPQPPLPPPV PQPQEPQPER
LSPAPLAHPS HPERASSARH SSEDSDITSL IEAMDKDFDH HDSPALEVFT EQPPSPLPKS
KGKGKPLQRK VKPPKKQEEK EKKGKGKPQE DELKDSLADD DSSSTTTETS NPDTEPLLKE
DTEKQKGKQA MPEKHESEMS QVKQKSKKLL NIKKEIPTDV KPSSLELPYT PPLESKQRRN
LPSKIPLPTA MTSGSKSRNA QKTKGTSKLV DNRPPALAKF LPNSQELGNT SSSEGEKDSP
PPEWDSVPVH KPGSSTDSLY KLSLQTLNAD IFLKQRQTSP TPASPSPPAA PCPFVARGSY
SSIVNSSSSS DPKIKQPNGS KHKLTKAASL PGKNGNPTFA AVTAGYDKSP GGNGFAKVSS
NKTGFSSSLG ISHAPVDSDG SDSSGLWSPV SNPSSPDFTP LNSFSAFGNS FNLTGEVFSK
LGLSRSCNQA SQRSWNEFNS GPSYLWESPA TDPSPSWPAS SGSPTHTATS VLGNTSGLWS
TTPFSSSIWS SNLSSALPFT TPANTLASIG LMGTENSPAP HAPSTSSPAD DLGQTYNPWR
IWSPTIGRRS SDPWSNSHFP HEN
