TM87B_HUMAN
ID TM87B_HUMAN Reviewed; 555 AA.
AC Q96K49; A8K2M9; Q1RLN2; Q53R54;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Transmembrane protein 87B {ECO:0000305};
DE Flags: Precursor;
GN Name=TMEM87B {ECO:0000312|HGNC:HGNC:25913};
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=Teratocarcinoma, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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-469, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-496 AND SER-534, AND
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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-534, AND IDENTIFICATION BY
RP 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 [9]
RP FUNCTION.
RX PubMed=26157166; DOI=10.1091/mbc.e14-11-1568;
RA Hirata T., Fujita M., Nakamura S., Gotoh K., Motooka D., Murakami Y.,
RA Maeda Y., Kinoshita T.;
RT "Post-Golgi anterograde transport requires GARP-dependent endosome-to-TGN
RT retrograde transport.";
RL Mol. Biol. Cell 26:3071-3084(2015).
RN [10]
RP VARIANT ASP-456.
RX PubMed=27148590; DOI=10.1101/mcs.a000844;
RA Yu H.C., Coughlin C.R., Geiger E.A., Salvador B.J., Elias E.R.,
RA Cavanaugh J.L., Chatfield K.C., Miyamoto S.D., Shaikh T.H.;
RT "Discovery of a potentially deleterious variant in TMEM87B in a patient
RT with a hemizygous 2q13 microdeletion suggests a recessive condition
RT characterized by congenital heart disease and restrictive cardiomyopathy.";
RL Cold Spring Harb. Mol. Case Stud. 2:A000844-A000844(2016).
CC -!- FUNCTION: May be involved in retrograde transport from endosomes to the
CC trans-Golgi network (TGN). {ECO:0000269|PubMed:26157166}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:26157166}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96K49-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96K49-2; Sequence=VSP_026219;
CC -!- DISEASE: Note=TMEM87B mutations may be involved in restrictive
CC cardiomyopathy (RCM), a rare non-ischemic myocardial disease. RCM is
CC characterized by restrictive ventricular-filling physiology in the
CC presence of normal or reduced diastolic and/or systolic volumes (of 1
CC or both ventricles), biatrial enlargement, and normal ventricular wall
CC thickness. {ECO:0000269|PubMed:27148590}.
CC -!- SIMILARITY: Belongs to the LU7TM family. TMEM87 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK027587; BAB55214.1; -; mRNA.
DR EMBL; AK290294; BAF82983.1; -; mRNA.
DR EMBL; AC092645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093675; AAY24214.1; -; Genomic_DNA.
DR EMBL; BC115373; AAI15374.1; -; mRNA.
DR CCDS; CCDS33275.1; -. [Q96K49-1]
DR RefSeq; NP_116213.1; NM_032824.2. [Q96K49-1]
DR RefSeq; XP_005263884.1; XM_005263827.2. [Q96K49-2]
DR AlphaFoldDB; Q96K49; -.
DR BioGRID; 124347; 23.
DR IntAct; Q96K49; 4.
DR MINT; Q96K49; -.
DR STRING; 9606.ENSP00000283206; -.
DR GlyConnect; 1855; 1 N-Linked glycan (1 site).
DR GlyGen; Q96K49; 6 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q96K49; -.
DR PhosphoSitePlus; Q96K49; -.
DR SwissPalm; Q96K49; -.
DR BioMuta; TMEM87B; -.
DR DMDM; 74732185; -.
DR EPD; Q96K49; -.
DR jPOST; Q96K49; -.
DR MassIVE; Q96K49; -.
DR MaxQB; Q96K49; -.
DR PaxDb; Q96K49; -.
DR PeptideAtlas; Q96K49; -.
DR PRIDE; Q96K49; -.
DR ProteomicsDB; 77041; -. [Q96K49-1]
DR ProteomicsDB; 77042; -. [Q96K49-2]
DR Antibodypedia; 33259; 69 antibodies from 16 providers.
DR DNASU; 84910; -.
DR Ensembl; ENST00000283206.9; ENSP00000283206.4; ENSG00000153214.11. [Q96K49-1]
DR GeneID; 84910; -.
DR KEGG; hsa:84910; -.
DR MANE-Select; ENST00000283206.9; ENSP00000283206.4; NM_032824.3; NP_116213.1.
DR UCSC; uc002thm.2; human. [Q96K49-1]
DR CTD; 84910; -.
DR DisGeNET; 84910; -.
DR GeneCards; TMEM87B; -.
DR HGNC; HGNC:25913; TMEM87B.
DR HPA; ENSG00000153214; Low tissue specificity.
DR MIM; 617203; gene.
DR neXtProt; NX_Q96K49; -.
DR OpenTargets; ENSG00000153214; -.
DR PharmGKB; PA142670740; -.
DR VEuPathDB; HostDB:ENSG00000153214; -.
DR eggNOG; KOG2568; Eukaryota.
DR GeneTree; ENSGT00940000156844; -.
DR HOGENOM; CLU_027525_1_1_1; -.
DR InParanoid; Q96K49; -.
DR OMA; PCIFDDR; -.
DR OrthoDB; 1448608at2759; -.
DR PhylomeDB; Q96K49; -.
DR TreeFam; TF314452; -.
DR PathwayCommons; Q96K49; -.
DR SignaLink; Q96K49; -.
DR BioGRID-ORCS; 84910; 12 hits in 1080 CRISPR screens.
DR ChiTaRS; TMEM87B; human.
DR GenomeRNAi; 84910; -.
DR Pharos; Q96K49; Tdark.
DR PRO; PR:Q96K49; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96K49; protein.
DR Bgee; ENSG00000153214; Expressed in mucosa of sigmoid colon and 169 other tissues.
DR ExpressionAtlas; Q96K49; baseline and differential.
DR Genevisible; Q96K49; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IGI:UniProtKB.
DR InterPro; IPR009637; GPR107/GPR108-like.
DR PANTHER; PTHR21229; PTHR21229; 1.
DR Pfam; PF06814; Lung_7-TM_R; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..555
FT /note="Transmembrane protein 87B"
FT /id="PRO_0000291753"
FT TOPO_DOM 43..214
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 215..235
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 248..268
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..299
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 300..320
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 323..343
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..350
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 351..371
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 397..417
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..429
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 430..450
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 167
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026219"
FT VARIANT 456
FT /note="N -> D (found in restrictive cardiomyopathy; unknown
FT pathological significance; dbSNP:rs369634007)"
FT /evidence="ECO:0000269|PubMed:27148590"
FT /id="VAR_078997"
SQ SEQUENCE 555 AA; 63536 MW; 7D9B61E5AADF0AA3 CRC64;
MVAACRSVAG LLPRRRRCFP ARAPLLRVAL CLLCWTPAAV RAVPELGLWL ETVNDKSGPL
IFRKTMFNST DIKLSVKSFH CSGPVKFTIV WHLKYHTCHN EHSNLEELFQ KHKLSVDEDF
CHYLKNDNCW TTKNENLDCN SDSQVFPSLN NKELINIRNV SNQERSMDVV ARTQKDGFHI
FIVSIKTENT DASWNLNVSL SMIGPHGYIS ASDWPLMIFY MVMCIVYILY GILWLTWSAC
YWKDILRIQF WIAAVIFLGM LEKAVFYSEY QNISNTGLST QGLLIFAELI SAIKRTLARL
LVIIVSLGYG IVKPRLGTVM HRVIGLGLLY LIFAAVEGVM RVIGGSNHLA VVLDDIILAV
IDSIFVWFIF ISLAQTMKTL RLRKNTVKFS LYRHFKNTLI FAVLASIVFM GWTTKTFRIA
KCQSDWMERW VDDAFWSFLF SLILIVIMFL WRPSANNQRY AFMPLIDDSD DEIEEFMVTS
ENLTEGIKLR ASKSVSNGTA KPATSENFDE DLKWVEENIP SSFTDVALPV LVDSDEEIMT
RSEMAEKMFS SEKIM
