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TM192_HUMAN
ID   TM192_HUMAN             Reviewed;         271 AA.
AC   Q8IY95; Q7Z3A1; Q8N928;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Transmembrane protein 192;
GN   Name=TMEM192;
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 2).
RC   TISSUE=Brain;
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 MRNA] (ISOFORM 1).
RC   TISSUE=Endometrial tumor;
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 GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skin;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-17, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Placenta;
RX   PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA   Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA   Elsaesser H.-P., Mann M., Hasilik A.;
RT   "Integral and associated lysosomal membrane proteins.";
RL   Traffic 8:1676-1686(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213, 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   [8]
RP   SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RX   PubMed=20370317; DOI=10.1515/bc.2010.062;
RA   Schroder B., Wrocklage C., Hasilik A., Saftig P.;
RT   "Molecular characterisation of 'transmembrane protein 192' (TMEM192), a
RT   novel protein of the lysosomal membrane.";
RL   Biol. Chem. 391:695-704(2010).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND SER-230, 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, 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).
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:20370317}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17897319,
CC       ECO:0000269|PubMed:20370317}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:17897319}. Late endosome
CC       {ECO:0000269|PubMed:20370317}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IY95-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IY95-2; Sequence=VSP_029502;
CC   -!- TISSUE SPECIFICITY: Strongly expressed in kidney, liver, lung and
CC       pancreas. {ECO:0000269|PubMed:20370317}.
CC   -!- PTM: Not N-glycosylated.
CC   -!- SIMILARITY: Belongs to the TMEM192 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD97974.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK095801; BAC04628.1; -; mRNA.
DR   EMBL; BX538029; CAD97974.1; ALT_INIT; mRNA.
DR   EMBL; CH471056; EAX04826.1; -; Genomic_DNA.
DR   EMBL; BC036301; AAH36301.1; -; mRNA.
DR   CCDS; CCDS43279.1; -. [Q8IY95-1]
DR   RefSeq; NP_001093859.1; NM_001100389.1. [Q8IY95-1]
DR   AlphaFoldDB; Q8IY95; -.
DR   SMR; Q8IY95; -.
DR   BioGRID; 128407; 187.
DR   IntAct; Q8IY95; 23.
DR   MINT; Q8IY95; -.
DR   STRING; 9606.ENSP00000305069; -.
DR   TCDB; 9.B.134.1.1; the lysosomal autophagy and apoptosis-related protein, tmem192 (tmem192) family.
DR   iPTMnet; Q8IY95; -.
DR   PhosphoSitePlus; Q8IY95; -.
DR   SwissPalm; Q8IY95; -.
DR   BioMuta; TMEM192; -.
DR   DMDM; 74728307; -.
DR   EPD; Q8IY95; -.
DR   jPOST; Q8IY95; -.
DR   MassIVE; Q8IY95; -.
DR   MaxQB; Q8IY95; -.
DR   PaxDb; Q8IY95; -.
DR   PeptideAtlas; Q8IY95; -.
DR   PRIDE; Q8IY95; -.
DR   ProteomicsDB; 71129; -. [Q8IY95-1]
DR   ProteomicsDB; 71130; -. [Q8IY95-2]
DR   Antibodypedia; 7685; 89 antibodies from 23 providers.
DR   DNASU; 201931; -.
DR   Ensembl; ENST00000306480.11; ENSP00000305069.4; ENSG00000170088.14. [Q8IY95-1]
DR   Ensembl; ENST00000506087.5; ENSP00000425335.1; ENSG00000170088.14. [Q8IY95-2]
DR   GeneID; 201931; -.
DR   KEGG; hsa:201931; -.
DR   MANE-Select; ENST00000306480.11; ENSP00000305069.4; NM_001100389.2; NP_001093859.1.
DR   UCSC; uc003iqz.5; human. [Q8IY95-1]
DR   CTD; 201931; -.
DR   DisGeNET; 201931; -.
DR   GeneCards; TMEM192; -.
DR   HGNC; HGNC:26775; TMEM192.
DR   HPA; ENSG00000170088; Low tissue specificity.
DR   neXtProt; NX_Q8IY95; -.
DR   OpenTargets; ENSG00000170088; -.
DR   PharmGKB; PA162406273; -.
DR   VEuPathDB; HostDB:ENSG00000170088; -.
DR   eggNOG; ENOG502RYVA; Eukaryota.
DR   GeneTree; ENSGT00390000013749; -.
DR   HOGENOM; CLU_086771_0_0_1; -.
DR   InParanoid; Q8IY95; -.
DR   OMA; RCEAYFI; -.
DR   OrthoDB; 1249559at2759; -.
DR   PhylomeDB; Q8IY95; -.
DR   TreeFam; TF323773; -.
DR   PathwayCommons; Q8IY95; -.
DR   SignaLink; Q8IY95; -.
DR   BioGRID-ORCS; 201931; 6 hits in 1077 CRISPR screens.
DR   ChiTaRS; TMEM192; human.
DR   GenomeRNAi; 201931; -.
DR   Pharos; Q8IY95; Tbio.
DR   PRO; PR:Q8IY95; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q8IY95; protein.
DR   Bgee; ENSG00000170088; Expressed in caput epididymis and 182 other tissues.
DR   ExpressionAtlas; Q8IY95; baseline and differential.
DR   Genevisible; Q8IY95; HS.
DR   GO; GO:0005768; C:endosome; IDA:HPA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   InterPro; IPR029399; TMEM192.
DR   PANTHER; PTHR31592; PTHR31592; 1.
DR   Pfam; PF14802; TMEM192; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endosome; Lysosome; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..271
FT                   /note="Transmembrane protein 192"
FT                   /id="PRO_0000311267"
FT   TOPO_DOM        1..46
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..93
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..171
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        193..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         15
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   MOD_RES         213
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         229
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         230
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         269
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         1..9
FT                   /note="MAAGGRMED -> MNKAT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_029502"
FT   CONFLICT        94
FT                   /note="T -> A (in Ref. 2; CAD97974)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="E -> K (in Ref. 2; CAD97974)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190
FT                   /note="Y -> C (in Ref. 1; BAC04628)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   271 AA;  30922 MW;  F156D08011315D04 CRC64;
     MAAGGRMEDG SLDITQSIED DPLLDAQLLP HHSLQAHFRP RFHPLPTVII VNLLWFIHLV
     FVVLAFLTGV LCSYPNPNED KCPGNYTNPL KVQTVIILGK VILWILHLLL ECYIQYHHSK
     IRNRGYNLIY RSTRHLKRLA LMIQSSGNTV LLLILCMQHS FPEPGRLYLD LILAILALEL
     ICSLICLLIY TVKIRRFNKA KPEPDILEEE KIYAYPSNIT SETGFRTISS LEEIVEKQGD
     TIEYLKRHNA LLSKRLLALT SSDLGCQPSR T
 
 
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