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MON1B_HUMAN
ID   MON1B_HUMAN             Reviewed;         547 AA.
AC   Q7L1V2; B4DDZ0; O94949;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Vacuolar fusion protein MON1 homolog B;
DE   AltName: Full=HSV-1 stimulation-related gene 1 protein;
DE   AltName: Full=HSV-I stimulating-related protein;
GN   Name=MON1B; Synonyms=HSRG1, KIAA0872, SAND2;
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 [MRNA] (ISOFORM 1), AND INDUCTION BY HSV-1.
RC   TISSUE=Lung;
RX   PubMed=12828340;
RA   Dong S.Z., Dong C.H., Liu L.D., Li Q.H.;
RT   "Identification of a novel human MON1/SAND family protein in human
RT   fibroblasts induced by herpes simplex virus 1 binding.";
RL   Acta Virol. 47:27-32(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:355-364(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Urinary bladder;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   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   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [7]
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   [8]
RP   INTERACTION WITH CCNT2.
RX   PubMed=21509660; DOI=10.1007/s11427-011-4160-3;
RA   Wu W., Yu X., Li W., Guo L., Liu L., Wang L., Li Q.;
RT   "HSV-1 stimulation-related protein HSRG1 inhibits viral gene
RT   transcriptional elongation by interacting with Cyclin T2.";
RL   Sci. China Life Sci. 54:359-365(2011).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-61, 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   IDENTIFICATION IN A COMPLEX RMC1; CCZ1; MON1A AND MON1B.
RX   PubMed=29038162; DOI=10.1128/mcb.00392-17;
RA   Pontano Vaites L., Paulo J.A., Huttlin E.L., Harper J.W.;
RT   "Systematic analysis of human cells lacking ATG8 proteins uncovers roles
RT   for GABARAPs and the CCZ1/MON1 regulator C18orf8/RMC1 in macro and
RT   selective autophagic flux.";
RL   Mol. Cell. Biol. 0:0-0(2017).
CC   -!- SUBUNIT: Interacts with CCNT2; down-regulates CCNT2-mediated activation
CC       of viral promoters during herpes simplex virus 1/HHV-1 infection
CC       (PubMed:21509660). Found in a complex with RMC1, CCZ1 MON1A and MON1B
CC       (PubMed:29038162). {ECO:0000269|PubMed:21509660,
CC       ECO:0000269|PubMed:29038162}.
CC   -!- INTERACTION:
CC       Q7L1V2; Q9P253: VPS18; NbExp=2; IntAct=EBI-2655311, EBI-1053363;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7L1V2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7L1V2-2; Sequence=VSP_054664, VSP_054665;
CC   -!- INDUCTION: Induced in fibroblast KMB17 cells by HSV-1.
CC       {ECO:0000269|PubMed:12828340}.
CC   -!- SIMILARITY: Belongs to the MON1/SAND family. {ECO:0000305}.
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DR   EMBL; AF442486; AAL35292.1; -; mRNA.
DR   EMBL; AB020679; BAA74895.2; -; mRNA.
DR   EMBL; AK293392; BAG56901.1; -; mRNA.
DR   EMBL; AC009139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC024277; AAH24277.1; -; mRNA.
DR   CCDS; CCDS10925.1; -. [Q7L1V2-1]
DR   CCDS; CCDS67082.1; -. [Q7L1V2-2]
DR   RefSeq; NP_001273568.1; NM_001286639.1.
DR   RefSeq; NP_001273569.1; NM_001286640.1. [Q7L1V2-2]
DR   RefSeq; NP_055755.1; NM_014940.3. [Q7L1V2-1]
DR   AlphaFoldDB; Q7L1V2; -.
DR   SMR; Q7L1V2; -.
DR   BioGRID; 116546; 17.
DR   IntAct; Q7L1V2; 10.
DR   STRING; 9606.ENSP00000248248; -.
DR   iPTMnet; Q7L1V2; -.
DR   PhosphoSitePlus; Q7L1V2; -.
DR   BioMuta; MON1B; -.
DR   DMDM; 74738536; -.
DR   EPD; Q7L1V2; -.
DR   jPOST; Q7L1V2; -.
DR   MassIVE; Q7L1V2; -.
DR   MaxQB; Q7L1V2; -.
DR   PaxDb; Q7L1V2; -.
DR   PeptideAtlas; Q7L1V2; -.
DR   PRIDE; Q7L1V2; -.
DR   ProteomicsDB; 3908; -.
DR   ProteomicsDB; 68751; -. [Q7L1V2-1]
DR   TopDownProteomics; Q7L1V2-1; -. [Q7L1V2-1]
DR   Antibodypedia; 30376; 97 antibodies from 19 providers.
DR   DNASU; 22879; -.
DR   Ensembl; ENST00000248248.8; ENSP00000248248.3; ENSG00000103111.15. [Q7L1V2-1]
DR   Ensembl; ENST00000545553.1; ENSP00000444881.1; ENSG00000103111.15. [Q7L1V2-2]
DR   GeneID; 22879; -.
DR   KEGG; hsa:22879; -.
DR   MANE-Select; ENST00000248248.8; ENSP00000248248.3; NM_014940.4; NP_055755.1.
DR   UCSC; uc002fez.5; human. [Q7L1V2-1]
DR   CTD; 22879; -.
DR   DisGeNET; 22879; -.
DR   GeneCards; MON1B; -.
DR   HGNC; HGNC:25020; MON1B.
DR   HPA; ENSG00000103111; Low tissue specificity.
DR   MIM; 608954; gene.
DR   neXtProt; NX_Q7L1V2; -.
DR   OpenTargets; ENSG00000103111; -.
DR   PharmGKB; PA142671341; -.
DR   VEuPathDB; HostDB:ENSG00000103111; -.
DR   eggNOG; KOG0997; Eukaryota.
DR   GeneTree; ENSGT00390000006665; -.
DR   HOGENOM; CLU_014574_4_1_1; -.
DR   InParanoid; Q7L1V2; -.
DR   OMA; TKTCAIT; -.
DR   PhylomeDB; Q7L1V2; -.
DR   PathwayCommons; Q7L1V2; -.
DR   Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   SignaLink; Q7L1V2; -.
DR   BioGRID-ORCS; 22879; 15 hits in 1069 CRISPR screens.
DR   ChiTaRS; MON1B; human.
DR   GenomeRNAi; 22879; -.
DR   Pharos; Q7L1V2; Tbio.
DR   PRO; PR:Q7L1V2; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q7L1V2; protein.
DR   Bgee; ENSG00000103111; Expressed in palpebral conjunctiva and 186 other tissues.
DR   ExpressionAtlas; Q7L1V2; baseline and differential.
DR   Genevisible; Q7L1V2; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0035658; C:Mon1-Ccz1 complex; IDA:UniProtKB.
DR   GO; GO:0019085; P:early viral transcription; IDA:UniProtKB.
DR   GO; GO:0019086; P:late viral transcription; IDA:UniProtKB.
DR   GO; GO:0006623; P:protein targeting to vacuole; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR043972; FUZ/MON1/HPS1_longin_1.
DR   InterPro; IPR043971; FUZ/MON1/HPS1_longin_2.
DR   InterPro; IPR043970; FUZ/MON1/HPS1_longin_3.
DR   InterPro; IPR004353; Mon1.
DR   PANTHER; PTHR13027; PTHR13027; 1.
DR   Pfam; PF19036; Fuz_longin_1; 1.
DR   Pfam; PF19037; Fuz_longin_2; 1.
DR   Pfam; PF19038; Fuz_longin_3; 1.
DR   PRINTS; PR01546; YEAST73DUF.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Phosphoprotein; Reference proteome.
FT   CHAIN           1..547
FT                   /note="Vacuolar fusion protein MON1 homolog B"
FT                   /id="PRO_0000285765"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         61
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..12
FT                   /note="MEVGGDTAAPAP -> MVSGQLRFGVKT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054664"
FT   VAR_SEQ         13..158
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054665"
SQ   SEQUENCE   547 AA;  59217 MW;  06ED0B7C42AA2D17 CRC64;
     MEVGGDTAAP APGGAEDLED TQFPSEEARE GGGVHAVPPD PEDEGLEETG SKDKDQPPSP
     SPPPQSEALS STSRLWSPAA PENSPTCSPE SSSGGQGGDP SDEEWRSQRK HVFVLSEAGK
     PIYSRYGSVE ALSATMGVMT ALVSFVQSAG DAIRAIYAED HKLVFLQQGP LLLVAMSRTS
     QSAAQLRGEL LAVHAQIVST LTRASVARIF AHKQNYDLRR LLAGSERTLD RLLDSMEQDP
     GALLLGAVRC VPLARPLRDA LGALLRRCTA PGLALSVLAV GGRLITAAQE RNVLAECRLD
     PADLQLLLDW VGAPAFAAGE AWAPVCLPRF NPDGFFYAYV ARLDAMPVCL LLLGTQREAF
     HAMAACRRLV EDGMHALGAM RALGEAASFS NASSASAPAY SVQAVGAPGL RHFLYKPLDI
     PDHHRQLPQF TSPELEAPYS REEERQRLSD LYHRLHARLH STSRPLRLIY HVAEKETLLA
     WVTSKFELYT CLSPLVTKAG AILVVTKLLR WVKKEEDRLF IRYPPKYSTP PATSTDQAAH
     NGLFTGL
 
 
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