Full text data of MON2
MON2
(KIAA1040, SF21)
[Confidence: low (only semi-automatic identification from reviews)]
Protein MON2 homolog (Protein SF21)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein MON2 homolog (Protein SF21)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q7Z3U7
ID MON2_HUMAN Reviewed; 1718 AA.
AC Q7Z3U7; A5D8U7; A7E2Y0; Q86TA2; Q8N3I5; Q8NAI0; Q8NHE2; Q9UPW1;
read moreDT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 22-JAN-2014, entry version 86.
DE RecName: Full=Protein MON2 homolog;
DE AltName: Full=Protein SF21;
GN Name=MON2; Synonyms=KIAA1040, SF21;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), 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.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 2 AND 4), 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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 MRNA] OF 1-1072 (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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
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
RT cytoplasm-to-vacuole transport pathway and is required for Golgi
RT homeostasis.";
RL J. Cell Sci. 118:4751-4764(2005).
RN [8]
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
RT Golgi apparatus.";
RL J. Biol. Chem. 281:2273-2280(2006).
RN [9]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND MASS
RP SPECTROMETRY.
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 [11]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be required for traffic between late Golgi and early
CC endosomes (By similarity).
CC -!- INTERACTION:
CC Q9UJY5:GGA1; NbExp=2; IntAct=EBI-358882, EBI-447141;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q7Z3U7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z3U7-2; Sequence=VSP_027392, VSP_027393;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q7Z3U7-3; Sequence=VSP_027389, VSP_027390, VSP_027391;
CC Name=4;
CC IsoId=Q7Z3U7-4; Sequence=VSP_027388;
CC -!- SIMILARITY: Belongs to the MON2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA82992.3; Type=Erroneous initiation;
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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; BC141817; AAI41818.1; -; mRNA.
DR EMBL; BC142710; AAI42711.1; -; mRNA.
DR EMBL; BC151241; AAI51242.1; -; mRNA.
DR RefSeq; NP_001265398.1; NM_001278469.1.
DR RefSeq; NP_055841.2; NM_015026.2.
DR RefSeq; XP_005268788.1; XM_005268731.1.
DR UniGene; Hs.389378; -.
DR ProteinModelPortal; Q7Z3U7; -.
DR IntAct; Q7Z3U7; 6.
DR MINT; MINT-1149344; -.
DR STRING; 9606.ENSP00000377252; -.
DR PhosphoSite; Q7Z3U7; -.
DR DMDM; 156632594; -.
DR PaxDb; Q7Z3U7; -.
DR PRIDE; Q7Z3U7; -.
DR DNASU; 23041; -.
DR Ensembl; ENST00000280379; ENSP00000280379; ENSG00000061987.
DR Ensembl; ENST00000393630; ENSP00000377250; ENSG00000061987.
DR Ensembl; ENST00000393632; ENSP00000377252; ENSG00000061987.
DR GeneID; 23041; -.
DR KEGG; hsa:23041; -.
DR CTD; 23041; -.
DR GeneCards; GC12P062860; -.
DR H-InvDB; HIX0010775; -.
DR HGNC; HGNC:29177; MON2.
DR HPA; HPA038697; -.
DR neXtProt; NX_Q7Z3U7; -.
DR PharmGKB; PA143485545; -.
DR eggNOG; NOG297097; -.
DR HOVERGEN; HBG108142; -.
DR InParanoid; Q7Z3U7; -.
DR OMA; FPISMRL; -.
DR OrthoDB; EOG7C8GGF; -.
DR ChiTaRS; mon2; human.
DR GeneWiki; MON2; -.
DR GenomeRNAi; 23041; -.
DR NextBio; 44066; -.
DR PRO; PR:Q7Z3U7; -.
DR ArrayExpress; Q7Z3U7; -.
DR Bgee; Q7Z3U7; -.
DR CleanEx; HS_MON2; -.
DR Genevestigator; Q7Z3U7; -.
DR GO; GO:0005802; C:trans-Golgi network; IBA:RefGenome.
DR GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IBA:RefGenome.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:RefGenome.
DR GO; GO:0006895; P:Golgi to endosome transport; ISS:HGNC.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015403; DUF1981_Sec7_assoc.
DR InterPro; IPR026829; Mon2.
DR PANTHER; PTHR10663:SF35; PTHR10663:SF35; 1.
DR Pfam; PF09324; DUF1981; 1.
DR SUPFAM; SSF48371; SSF48371; 5.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Phosphoprotein;
KW Polymorphism; Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1718 Protein MON2 homolog.
FT /FTId=PRO_0000297902.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 205 205 Phosphoserine.
FT VAR_SEQ 1 1126 Missing (in isoform 3).
FT /FTId=VSP_027389.
FT VAR_SEQ 823 823 Missing (in isoform 4).
FT /FTId=VSP_027388.
FT VAR_SEQ 1127 1137 FNTRRYLLQPL -> MIIVFFSLPNI (in isoform
FT 3).
FT /FTId=VSP_027390.
FT VAR_SEQ 1394 1399 Missing (in isoform 3).
FT /FTId=VSP_027391.
FT VAR_SEQ 1665 1676 VDGNTWAQVIAL -> ACISLFGIPPYF (in isoform
FT 2).
FT /FTId=VSP_027392.
FT VAR_SEQ 1677 1718 Missing (in isoform 2).
FT /FTId=VSP_027393.
FT VARIANT 548 548 A -> T (in dbSNP:rs10219555).
FT /FTId=VAR_034689.
FT CONFLICT 163 163 N -> D (in Ref. 5; CAD97657).
FT CONFLICT 197 197 V -> I (in Ref. 5; CAD97657).
FT CONFLICT 238 238 M -> T (in Ref. 5; CAD97657).
FT CONFLICT 268 268 S -> G (in Ref. 5; CAD89933).
FT CONFLICT 650 650 E -> G (in Ref. 5; CAD97657).
FT CONFLICT 734 734 V -> A (in Ref. 5; CAD89933).
FT CONFLICT 1003 1003 E -> K (in Ref. 5; CAD89933).
SQ SEQUENCE 1718 AA; 190487 MW; BE30F73F0CAE4764 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 LEKVCQHPNS RMREWGAEAL
TSLIKAGLTF NHDPPLSQNQ RLQLLLLNPL KEMSNINHPD IRLKQLECVL QILQSQGDSL
GPGWPLVLGV MGAIRNDQGE SLIRTAFQCL QLVVTDFLPT MPCTCLQIVV DVAGSFGLHN
QELNISLTSI GLLWNISDYF FQRGETIEKE LNKEEAAQQK QAEEKGVVLN RPFHPAPPFD
CLWLCLYAKL GELCVDPRPA VRKSAGQTLF STIGAHGTLL QHSTWHTVIW KVLFHLLDRV
RESSTTADKE KIESGGGNIL IHHSRDTAEK QWAETWVLTL AGVARIFNTR RYLLQPLGDF
SRAWDVLLDH IQSAALSKNN EVSLAALKSF QEILQIVSPV RDSDKPETPP VVNVPVPVLI
GPISGMSRPF VRTDSIGEKL GRYSSSEPPI VTDELEDLNL WWAAWNTWYR IGSESTKPPI
TFDKLTFIPS QPFLTALIQI FPALYQHIKT GFNMDDLQKL GVILHSAISV PISSDASPFI
LPSYTEAVLT SLQEAVLTAL DVLQKAICVG PENMQIMYPA IFDQLLAFVE FSCKPPQYGQ
LETKHIANAK YNQIQLFAPA EWVALNYVPF AERSLEVVVD LYQKTACHKA VVNEKVLQNI
IKTLRVPLSL KYSCPSESTW KLAVSSLLRV LSIGLPVARQ HASSGKFDSM WPELANTFED
FLFTKSIPPD NLSIQEFQRN ENIDVEVVQL ISNEILPYAN FIPKEFVGQI MTMLNKGSIH
SQSSSFTEAE IDIRLREEFS KMCFETLLQF SFSNKVTTPQ EGYISRMALS VLLKRSQDVL
HRYIEDERLS GKCPLPRQQV TEIIFVLKAV STLIDSLKKT QPENVDGNTW AQVIALYPTL
VECITCSSSE VCSALKEALV PFKDFMQPPA SRVQNGES
//
ID MON2_HUMAN Reviewed; 1718 AA.
AC Q7Z3U7; A5D8U7; A7E2Y0; Q86TA2; Q8N3I5; Q8NAI0; Q8NHE2; Q9UPW1;
read moreDT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 22-JAN-2014, entry version 86.
DE RecName: Full=Protein MON2 homolog;
DE AltName: Full=Protein SF21;
GN Name=MON2; Synonyms=KIAA1040, SF21;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), 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.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 2 AND 4), 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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 MRNA] OF 1-1072 (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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
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
RT cytoplasm-to-vacuole transport pathway and is required for Golgi
RT homeostasis.";
RL J. Cell Sci. 118:4751-4764(2005).
RN [8]
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
RT Golgi apparatus.";
RL J. Biol. Chem. 281:2273-2280(2006).
RN [9]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND MASS
RP SPECTROMETRY.
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 [11]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be required for traffic between late Golgi and early
CC endosomes (By similarity).
CC -!- INTERACTION:
CC Q9UJY5:GGA1; NbExp=2; IntAct=EBI-358882, EBI-447141;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q7Z3U7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z3U7-2; Sequence=VSP_027392, VSP_027393;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q7Z3U7-3; Sequence=VSP_027389, VSP_027390, VSP_027391;
CC Name=4;
CC IsoId=Q7Z3U7-4; Sequence=VSP_027388;
CC -!- SIMILARITY: Belongs to the MON2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA82992.3; Type=Erroneous initiation;
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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; BC141817; AAI41818.1; -; mRNA.
DR EMBL; BC142710; AAI42711.1; -; mRNA.
DR EMBL; BC151241; AAI51242.1; -; mRNA.
DR RefSeq; NP_001265398.1; NM_001278469.1.
DR RefSeq; NP_055841.2; NM_015026.2.
DR RefSeq; XP_005268788.1; XM_005268731.1.
DR UniGene; Hs.389378; -.
DR ProteinModelPortal; Q7Z3U7; -.
DR IntAct; Q7Z3U7; 6.
DR MINT; MINT-1149344; -.
DR STRING; 9606.ENSP00000377252; -.
DR PhosphoSite; Q7Z3U7; -.
DR DMDM; 156632594; -.
DR PaxDb; Q7Z3U7; -.
DR PRIDE; Q7Z3U7; -.
DR DNASU; 23041; -.
DR Ensembl; ENST00000280379; ENSP00000280379; ENSG00000061987.
DR Ensembl; ENST00000393630; ENSP00000377250; ENSG00000061987.
DR Ensembl; ENST00000393632; ENSP00000377252; ENSG00000061987.
DR GeneID; 23041; -.
DR KEGG; hsa:23041; -.
DR CTD; 23041; -.
DR GeneCards; GC12P062860; -.
DR H-InvDB; HIX0010775; -.
DR HGNC; HGNC:29177; MON2.
DR HPA; HPA038697; -.
DR neXtProt; NX_Q7Z3U7; -.
DR PharmGKB; PA143485545; -.
DR eggNOG; NOG297097; -.
DR HOVERGEN; HBG108142; -.
DR InParanoid; Q7Z3U7; -.
DR OMA; FPISMRL; -.
DR OrthoDB; EOG7C8GGF; -.
DR ChiTaRS; mon2; human.
DR GeneWiki; MON2; -.
DR GenomeRNAi; 23041; -.
DR NextBio; 44066; -.
DR PRO; PR:Q7Z3U7; -.
DR ArrayExpress; Q7Z3U7; -.
DR Bgee; Q7Z3U7; -.
DR CleanEx; HS_MON2; -.
DR Genevestigator; Q7Z3U7; -.
DR GO; GO:0005802; C:trans-Golgi network; IBA:RefGenome.
DR GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IBA:RefGenome.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:RefGenome.
DR GO; GO:0006895; P:Golgi to endosome transport; ISS:HGNC.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015403; DUF1981_Sec7_assoc.
DR InterPro; IPR026829; Mon2.
DR PANTHER; PTHR10663:SF35; PTHR10663:SF35; 1.
DR Pfam; PF09324; DUF1981; 1.
DR SUPFAM; SSF48371; SSF48371; 5.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Phosphoprotein;
KW Polymorphism; Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1718 Protein MON2 homolog.
FT /FTId=PRO_0000297902.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 205 205 Phosphoserine.
FT VAR_SEQ 1 1126 Missing (in isoform 3).
FT /FTId=VSP_027389.
FT VAR_SEQ 823 823 Missing (in isoform 4).
FT /FTId=VSP_027388.
FT VAR_SEQ 1127 1137 FNTRRYLLQPL -> MIIVFFSLPNI (in isoform
FT 3).
FT /FTId=VSP_027390.
FT VAR_SEQ 1394 1399 Missing (in isoform 3).
FT /FTId=VSP_027391.
FT VAR_SEQ 1665 1676 VDGNTWAQVIAL -> ACISLFGIPPYF (in isoform
FT 2).
FT /FTId=VSP_027392.
FT VAR_SEQ 1677 1718 Missing (in isoform 2).
FT /FTId=VSP_027393.
FT VARIANT 548 548 A -> T (in dbSNP:rs10219555).
FT /FTId=VAR_034689.
FT CONFLICT 163 163 N -> D (in Ref. 5; CAD97657).
FT CONFLICT 197 197 V -> I (in Ref. 5; CAD97657).
FT CONFLICT 238 238 M -> T (in Ref. 5; CAD97657).
FT CONFLICT 268 268 S -> G (in Ref. 5; CAD89933).
FT CONFLICT 650 650 E -> G (in Ref. 5; CAD97657).
FT CONFLICT 734 734 V -> A (in Ref. 5; CAD89933).
FT CONFLICT 1003 1003 E -> K (in Ref. 5; CAD89933).
SQ SEQUENCE 1718 AA; 190487 MW; BE30F73F0CAE4764 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 LEKVCQHPNS RMREWGAEAL
TSLIKAGLTF NHDPPLSQNQ RLQLLLLNPL KEMSNINHPD IRLKQLECVL QILQSQGDSL
GPGWPLVLGV MGAIRNDQGE SLIRTAFQCL QLVVTDFLPT MPCTCLQIVV DVAGSFGLHN
QELNISLTSI GLLWNISDYF FQRGETIEKE LNKEEAAQQK QAEEKGVVLN RPFHPAPPFD
CLWLCLYAKL GELCVDPRPA VRKSAGQTLF STIGAHGTLL QHSTWHTVIW KVLFHLLDRV
RESSTTADKE KIESGGGNIL IHHSRDTAEK QWAETWVLTL AGVARIFNTR RYLLQPLGDF
SRAWDVLLDH IQSAALSKNN EVSLAALKSF QEILQIVSPV RDSDKPETPP VVNVPVPVLI
GPISGMSRPF VRTDSIGEKL GRYSSSEPPI VTDELEDLNL WWAAWNTWYR IGSESTKPPI
TFDKLTFIPS QPFLTALIQI FPALYQHIKT GFNMDDLQKL GVILHSAISV PISSDASPFI
LPSYTEAVLT SLQEAVLTAL DVLQKAICVG PENMQIMYPA IFDQLLAFVE FSCKPPQYGQ
LETKHIANAK YNQIQLFAPA EWVALNYVPF AERSLEVVVD LYQKTACHKA VVNEKVLQNI
IKTLRVPLSL KYSCPSESTW KLAVSSLLRV LSIGLPVARQ HASSGKFDSM WPELANTFED
FLFTKSIPPD NLSIQEFQRN ENIDVEVVQL ISNEILPYAN FIPKEFVGQI MTMLNKGSIH
SQSSSFTEAE IDIRLREEFS KMCFETLLQF SFSNKVTTPQ EGYISRMALS VLLKRSQDVL
HRYIEDERLS GKCPLPRQQV TEIIFVLKAV STLIDSLKKT QPENVDGNTW AQVIALYPTL
VECITCSSSE VCSALKEALV PFKDFMQPPA SRVQNGES
//