MON2_HUMAN
ID MON2_HUMAN Reviewed; 1717 AA.
AC Q7Z3U7; A5D8U7; A7E2Y0; B9EGP5; F8VWA6; F8W1Z6; Q86TA2; Q8N3I5; Q8NAI0;
AC Q8NHE2; Q9UPW1;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein MON2 homolog;
DE AltName: Full=Protein SF21;
GN Name=MON2 {ECO:0000303|PubMed:30213940, ECO:0000312|HGNC:HGNC:29177};
GN Synonyms=KIAA1040, SF21;
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 VARIANT THR-548.
RC TISSUE=Hippocampus;
RA Inagaki S.;
RT "Human homologue to C. elegans F11A10.4 hypothetical protein.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Prostate;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP THR-548.
RC TISSUE=Amygdala, and Spinal cord;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1071 (ISOFORMS 1/2).
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 [8]
RP IDENTIFICATION.
RX PubMed=16219684; DOI=10.1242/jcs.02599;
RA Efe J.A., Plattner F., Hulo N., Kressler D., Emr S.D., Deloche O.;
RT "Yeast Mon2p is a highly conserved protein that functions in the cytoplasm-
RT to-vacuole transport pathway and is required for Golgi homeostasis.";
RL J. Cell Sci. 118:4751-4764(2005).
RN [9]
RP IDENTIFICATION.
RX PubMed=16301316; DOI=10.1074/jbc.m510176200;
RA Gillingham A.K., Whyte J.R.C., Panic B., Munro S.;
RT "Mon2, a relative of large Arf exchange factors, recruits Dop1 to the Golgi
RT apparatus.";
RL J. Biol. Chem. 281:2273-2280(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, 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 [12]
RP IDENTIFICATION BY 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 [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP 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).
RN [16]
RP FUNCTION, INTERACTION WITH SNX3; ATP9A AND DOP1B, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=30213940; DOI=10.1038/s41467-018-06114-3;
RA McGough I.J., de Groot R.E.A., Jellett A.P., Betist M.C., Varandas K.C.,
RA Danson C.M., Heesom K.J., Korswagen H.C., Cullen P.J.;
RT "SNX3-retromer requires an evolutionary conserved MON2:DOPEY2:ATP9A complex
RT to mediate Wntless sorting and Wnt secretion.";
RL Nat. Commun. 9:3737-3737(2018).
CC -!- FUNCTION: Plays a role in regulating membrane trafficking of cargo
CC proteins. Together with ATP9A and DOP1B, regulates SNX3 retromer-
CC mediated endosomal sorting of WLS away from lysosomal degradation.
CC {ECO:0000269|PubMed:30213940}.
CC -!- SUBUNIT: Homooligomer (PubMed:30213940). Heterotrimer with ATP9A and
CC DOP1B; this interaction is retromer-independent (PubMed:30213940).
CC Interacts with SNX3 (PubMed:30213940). {ECO:0000269|PubMed:30213940}.
CC -!- INTERACTION:
CC Q7Z3U7; Q9UJY5: GGA1; NbExp=2; IntAct=EBI-358882, EBI-447141;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:30213940}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q7Z3U7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z3U7-2; Sequence=VSP_027392, VSP_027393;
CC Name=3;
CC IsoId=Q7Z3U7-3; Sequence=VSP_027389, VSP_027390, VSP_027391;
CC Name=5;
CC IsoId=Q7Z3U7-5; Sequence=VSP_027391;
CC Name=6;
CC IsoId=Q7Z3U7-6; Sequence=VSP_055628, VSP_027391;
CC -!- SIMILARITY: Belongs to the MON2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA82992.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB017814; BAC11707.1; -; mRNA.
DR EMBL; AB028963; BAA82992.3; ALT_INIT; mRNA.
DR EMBL; AK092646; BAC03935.1; -; mRNA.
DR EMBL; AL834320; CAD38989.1; -; mRNA.
DR EMBL; BX537415; CAD97657.1; -; mRNA.
DR EMBL; AL833066; CAD89933.1; -; mRNA.
DR EMBL; AC026115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136621; AAI36622.1; -; mRNA.
DR EMBL; BC141817; AAI41818.1; -; mRNA.
DR EMBL; BC142710; AAI42711.1; -; mRNA.
DR EMBL; BC151241; AAI51242.1; -; mRNA.
DR CCDS; CCDS31849.1; -. [Q7Z3U7-1]
DR CCDS; CCDS61175.1; -. [Q7Z3U7-6]
DR CCDS; CCDS61177.1; -. [Q7Z3U7-2]
DR CCDS; CCDS61178.1; -. [Q7Z3U7-5]
DR RefSeq; NP_001265398.1; NM_001278469.1. [Q7Z3U7-2]
DR RefSeq; NP_001265399.1; NM_001278470.1. [Q7Z3U7-5]
DR RefSeq; NP_055841.2; NM_015026.2. [Q7Z3U7-1]
DR RefSeq; XP_016874530.1; XM_017019041.1.
DR AlphaFoldDB; Q7Z3U7; -.
DR SMR; Q7Z3U7; -.
DR BioGRID; 116680; 163.
DR IntAct; Q7Z3U7; 29.
DR MINT; Q7Z3U7; -.
DR STRING; 9606.ENSP00000377250; -.
DR ChEMBL; CHEMBL4105804; -.
DR GlyGen; Q7Z3U7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z3U7; -.
DR PhosphoSitePlus; Q7Z3U7; -.
DR BioMuta; MON2; -.
DR DMDM; 156632594; -.
DR EPD; Q7Z3U7; -.
DR jPOST; Q7Z3U7; -.
DR MassIVE; Q7Z3U7; -.
DR MaxQB; Q7Z3U7; -.
DR PaxDb; Q7Z3U7; -.
DR PeptideAtlas; Q7Z3U7; -.
DR PRIDE; Q7Z3U7; -.
DR ProteomicsDB; 28957; -.
DR ProteomicsDB; 29715; -.
DR ProteomicsDB; 69085; -. [Q7Z3U7-1]
DR ProteomicsDB; 69086; -. [Q7Z3U7-2]
DR ProteomicsDB; 69087; -. [Q7Z3U7-3]
DR ProteomicsDB; 7528; -.
DR Antibodypedia; 51455; 31 antibodies from 12 providers.
DR DNASU; 23041; -.
DR Ensembl; ENST00000393629.6; ENSP00000377249.2; ENSG00000061987.16. [Q7Z3U7-5]
DR Ensembl; ENST00000393630.8; ENSP00000377250.4; ENSG00000061987.16. [Q7Z3U7-1]
DR Ensembl; ENST00000546600.5; ENSP00000447407.1; ENSG00000061987.16. [Q7Z3U7-2]
DR Ensembl; ENST00000552738.5; ENSP00000449215.1; ENSG00000061987.16. [Q7Z3U7-6]
DR GeneID; 23041; -.
DR KEGG; hsa:23041; -.
DR MANE-Select; ENST00000393630.8; ENSP00000377250.4; NM_015026.3; NP_055841.2.
DR UCSC; uc001sre.4; human. [Q7Z3U7-1]
DR CTD; 23041; -.
DR DisGeNET; 23041; -.
DR GeneCards; MON2; -.
DR HGNC; HGNC:29177; MON2.
DR HPA; ENSG00000061987; Low tissue specificity.
DR neXtProt; NX_Q7Z3U7; -.
DR OpenTargets; ENSG00000061987; -.
DR PharmGKB; PA143485545; -.
DR VEuPathDB; HostDB:ENSG00000061987; -.
DR eggNOG; KOG0929; Eukaryota.
DR eggNOG; KOG1848; Eukaryota.
DR GeneTree; ENSGT00390000013286; -.
DR HOGENOM; CLU_001169_2_0_1; -.
DR InParanoid; Q7Z3U7; -.
DR OrthoDB; 411011at2759; -.
DR TreeFam; TF314287; -.
DR PathwayCommons; Q7Z3U7; -.
DR SignaLink; Q7Z3U7; -.
DR BioGRID-ORCS; 23041; 69 hits in 1070 CRISPR screens.
DR ChiTaRS; MON2; human.
DR GeneWiki; MON2; -.
DR GenomeRNAi; 23041; -.
DR Pharos; Q7Z3U7; Tbio.
DR PRO; PR:Q7Z3U7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q7Z3U7; protein.
DR Bgee; ENSG00000061987; Expressed in body of pancreas and 203 other tissues.
DR ExpressionAtlas; Q7Z3U7; baseline and differential.
DR Genevisible; Q7Z3U7; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0006895; P:Golgi to endosome transport; ISS:HGNC-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032629; DCB_dom.
DR InterPro; IPR026829; Mon2-like.
DR InterPro; IPR032817; Mon2_C.
DR InterPro; IPR015403; Sec7_C.
DR InterPro; IPR032691; Sec7_N.
DR PANTHER; PTHR10663:SF333; PTHR10663:SF333; 1.
DR Pfam; PF16213; DCB; 1.
DR Pfam; PF09324; DUF1981; 1.
DR Pfam; PF16206; Mon2_C; 1.
DR Pfam; PF12783; Sec7_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1717
FT /note="Protein MON2 homolog"
FT /id="PRO_0000297902"
FT REGION 511..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TL7"
FT VAR_SEQ 1..1125
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027389"
FT VAR_SEQ 611..634
FT /note="GSLPPHYALTVLNTTTAATLSNKS -> A (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_055628"
FT VAR_SEQ 1126..1136
FT /note="FNTRRYLLQPL -> MIIVFFSLPNI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027390"
FT VAR_SEQ 1393..1398
FT /note="Missing (in isoform 3, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_027391"
FT VAR_SEQ 1664..1675
FT /note="VDGNTWAQVIAL -> ACISLFGIPPYF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_027392"
FT VAR_SEQ 1676..1717
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_027393"
FT VARIANT 548
FT /note="A -> T (in dbSNP:rs10219555)"
FT /evidence="ECO:0000269|PubMed:17974005, ECO:0000269|Ref.1"
FT /id="VAR_034689"
FT CONFLICT 163
FT /note="N -> D (in Ref. 5; CAD97657)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="V -> I (in Ref. 5; CAD97657)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="M -> T (in Ref. 5; CAD97657)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="S -> G (in Ref. 5; CAD89933)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="E -> G (in Ref. 5; CAD97657)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="V -> A (in Ref. 5; CAD89933)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="E -> EK (in Ref. 2; BAA82992 and 7; AAI41818/
FT AAI42711/AAI51242)"
FT /evidence="ECO:0000305"
FT CONFLICT 1002
FT /note="E -> K (in Ref. 5; CAD89933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1717 AA; 190359 MW; A95DCDF2A69BC0D2 CRC64;
MSGTSSPEAV KKLLENMQSD LRALSLECKK KFPPVKEAAE SGIIKVKTIA ARNTEILAAL
KENSSEVVQP FLMGCGTKEP KITQLCLAAI QRLMSHEVVS ETAAGNIINM LWQLMENSLE
ELKLLQTVLV LLTTNTVVHD EALSKAIVLC FRLHFTKDNI TNNTAAATVR QVVTVVFERM
VAEDERHRDI IEQPVLVQGN SNRRSVSTLK PCAKDAYMLF QDLCQLVNAD APYWLVGMTE
MTRTFGLELL ESVLNDFPQV FLQHQEFSFL LKERVCPLVI KLFSPNIKFR QGSSTSSSPA
PVEKPYFPIC MRLLRVVSVL IKQFYSLLVT ECEIFLSLLV KFLDADKPQW LRAVAVESIH
RFCVQPQLLR SFCQSYDMKQ HSTKVFRDIV NALGSFIQSL FLVPPTGNPA TSNQAGNNNL
GGSVSAPANS GMVGIGGGVT LLPAFEYRGT WIPILTITVQ GSAKATYLEM LDKVEPPTIP
EGYAMSVAFH CLLDLVRGIT SMIEGELGEL ETECQTTTEE GSSPTQSTEQ QDLQSTSDQM
DKEIVSRAVW EEMVNACWCG LLAALSLLLD ASTDEAATEN ILKAELTMAA LCGRLGLVTS
RDAFITAICK GSLPPHYALT VLNTTTAATL SNKSYSVQGQ SVMMISPSSE SHQQVVAVGQ
PLAVQPQGTV MLTSKNIQCM RTLLNLAHCH GAVLGTSWQL VLATLQHLVW ILGLKPSSGG
ALKPGRAVEG PSTVLTTAVM TDLPVISNIL SRLFESSQYL DDVSLHHLIN ALCSLSLEAM
DMAYGNNKEP SLFAVAKLLE TGLVNMHRIE ILWRPLTGHL LEVCQHPNSR MREWGAEALT
SLIKAGLTFN HDPPLSQNQR LQLLLLNPLK EMSNINHPDI RLKQLECVLQ ILQSQGDSLG
PGWPLVLGVM GAIRNDQGES LIRTAFQCLQ LVVTDFLPTM PCTCLQIVVD VAGSFGLHNQ
ELNISLTSIG LLWNISDYFF QRGETIEKEL NKEEAAQQKQ AEEKGVVLNR PFHPAPPFDC
LWLCLYAKLG ELCVDPRPAV RKSAGQTLFS TIGAHGTLLQ HSTWHTVIWK VLFHLLDRVR
ESSTTADKEK IESGGGNILI HHSRDTAEKQ WAETWVLTLA GVARIFNTRR YLLQPLGDFS
RAWDVLLDHI QSAALSKNNE VSLAALKSFQ EILQIVSPVR DSDKPETPPV VNVPVPVLIG
PISGMSRPFV RTDSIGEKLG RYSSSEPPIV TDELEDLNLW WAAWNTWYRI GSESTKPPIT
FDKLTFIPSQ PFLTALIQIF PALYQHIKTG FNMDDLQKLG VILHSAISVP ISSDASPFIL
PSYTEAVLTS LQEAVLTALD VLQKAICVGP ENMQIMYPAI FDQLLAFVEF SCKPPQYGQL
ETKHIANAKY NQIQLFAPAE WVALNYVPFA ERSLEVVVDL YQKTACHKAV VNEKVLQNII
KTLRVPLSLK YSCPSESTWK LAVSSLLRVL SIGLPVARQH ASSGKFDSMW PELANTFEDF
LFTKSIPPDN LSIQEFQRNE NIDVEVVQLI SNEILPYANF IPKEFVGQIM TMLNKGSIHS
QSSSFTEAEI DIRLREEFSK MCFETLLQFS FSNKVTTPQE GYISRMALSV LLKRSQDVLH
RYIEDERLSG KCPLPRQQVT EIIFVLKAVS TLIDSLKKTQ PENVDGNTWA QVIALYPTLV
ECITCSSSEV CSALKEALVP FKDFMQPPAS RVQNGES
