GO45_HUMAN
ID GO45_HUMAN Reviewed; 400 AA.
AC Q9H2G9; O15298; Q5T531; Q5T533; Q9GZX4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Golgin-45;
DE AltName: Full=Basic leucine zipper nuclear factor 1;
DE AltName: Full=JEM-1 {ECO:0000303|PubMed:11056056, ECO:0000303|PubMed:9129147};
DE AltName: Full=p45 basic leucine-zipper nuclear factor;
GN Name=BLZF1; Synonyms=JEM1;
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), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=9129147; DOI=10.1038/sj.onc.1200995;
RA Duprez E., Tong J.-H., Derre J., Chen S.-J., Berger R., Chen Z.,
RA Lanotte M.;
RT "JEM-1, a novel gene encoding a leucine-zipper nuclear factor upregulated
RT during retinoid-induced maturation of NB4 promyelocytic leukaemia.";
RL Oncogene 14:1563-1570(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11056056; DOI=10.1006/geno.2000.6347;
RA Tong J.-H., Fant X., Benoit G., Chen S.-J., Chen Z., Lanotte M.;
RT "Genomic organization of the JEM-1 (BLZF1) gene on human chromosome 1q24:
RT molecular cloning and analysis of its promoter region.";
RL Genomics 69:380-390(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH GORASP2 AND THE GTP
RP FORM OF RAB2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Testis;
RX PubMed=11739401; DOI=10.1083/jcb.200108079;
RA Short B., Preisinger C., Koerner R., Kopajtich R., Byron O., Barr F.A.;
RT "A GRASP55-rab2 effector complex linking Golgi structure to membrane
RT traffic.";
RL J. Cell Biol. 155:877-883(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-348 AND SER-353, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, 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 [9]
RP ADP-RIBOSYLATION, UBIQUITINATION, AND DOMAIN TANKYRASE-BINDING MOTIF.
RX PubMed=21478859; DOI=10.1038/ncb2222;
RA Zhang Y., Liu S., Mickanin C., Feng Y., Charlat O., Michaud G.A.,
RA Schirle M., Shi X., Hild M., Bauer A., Myer V.E., Finan P.M., Porter J.A.,
RA Huang S.M., Cong F.;
RT "RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin
RT degradation and Wnt signalling.";
RL Nat. Cell Biol. 13:623-629(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Required for normal Golgi structure and for protein transport
CC from the endoplasmic reticulum (ER) through the Golgi apparatus to the
CC cell surface. {ECO:0000269|PubMed:11739401}.
CC -!- SUBUNIT: Interacts with GORASP2. Interacts with the GTP-bound form of
CC RAB2, but not with other Golgi Rab proteins (PubMed:11739401).
CC Identified in a complex with RAB2 and GORASP2 (PubMed:11739401).
CC {ECO:0000269|PubMed:11739401}.
CC -!- INTERACTION:
CC Q9H2G9; Q99996-2: AKAP9; NbExp=3; IntAct=EBI-2548012, EBI-9641546;
CC Q9H2G9; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-2548012, EBI-10187270;
CC Q9H2G9; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-2548012, EBI-11954519;
CC Q9H2G9; P29972: AQP1; NbExp=3; IntAct=EBI-2548012, EBI-745213;
CC Q9H2G9; O95817: BAG3; NbExp=3; IntAct=EBI-2548012, EBI-747185;
CC Q9H2G9; O95429: BAG4; NbExp=3; IntAct=EBI-2548012, EBI-2949658;
CC Q9H2G9; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-2548012, EBI-11524452;
CC Q9H2G9; P41182: BCL6; NbExp=4; IntAct=EBI-2548012, EBI-765407;
CC Q9H2G9; Q9BXY8: BEX2; NbExp=6; IntAct=EBI-2548012, EBI-745073;
CC Q9H2G9; Q9H257: CARD9; NbExp=3; IntAct=EBI-2548012, EBI-751319;
CC Q9H2G9; Q96HB5: CCDC120; NbExp=5; IntAct=EBI-2548012, EBI-744556;
CC Q9H2G9; P51946: CCNH; NbExp=3; IntAct=EBI-2548012, EBI-741406;
CC Q9H2G9; Q86Y33-5: CDC20B; NbExp=5; IntAct=EBI-2548012, EBI-11983537;
CC Q9H2G9; Q16543: CDC37; NbExp=3; IntAct=EBI-2548012, EBI-295634;
CC Q9H2G9; Q07002: CDK18; NbExp=3; IntAct=EBI-2548012, EBI-746238;
CC Q9H2G9; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-2548012, EBI-749051;
CC Q9H2G9; Q9NX63: CHCHD3; NbExp=6; IntAct=EBI-2548012, EBI-743375;
CC Q9H2G9; Q9BW66: CINP; NbExp=7; IntAct=EBI-2548012, EBI-739784;
CC Q9H2G9; P51800-3: CLCNKA; NbExp=3; IntAct=EBI-2548012, EBI-11980535;
CC Q9H2G9; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-2548012, EBI-11962928;
CC Q9H2G9; Q9H0I2: ENKD1; NbExp=5; IntAct=EBI-2548012, EBI-744099;
CC Q9H2G9; O15197-2: EPHB6; NbExp=3; IntAct=EBI-2548012, EBI-10182490;
CC Q9H2G9; P19447: ERCC3; NbExp=3; IntAct=EBI-2548012, EBI-1183307;
CC Q9H2G9; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-2548012, EBI-742102;
CC Q9H2G9; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-2548012, EBI-11986315;
CC Q9H2G9; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-2548012, EBI-6658203;
CC Q9H2G9; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-2548012, EBI-10244131;
CC Q9H2G9; P22607: FGFR3; NbExp=3; IntAct=EBI-2548012, EBI-348399;
CC Q9H2G9; Q14192: FHL2; NbExp=10; IntAct=EBI-2548012, EBI-701903;
CC Q9H2G9; Q96NE9: FRMD6; NbExp=3; IntAct=EBI-2548012, EBI-741729;
CC Q9H2G9; O43559: FRS3; NbExp=3; IntAct=EBI-2548012, EBI-725515;
CC Q9H2G9; P55040: GEM; NbExp=6; IntAct=EBI-2548012, EBI-744104;
CC Q9H2G9; Q14957: GRIN2C; NbExp=3; IntAct=EBI-2548012, EBI-8285963;
CC Q9H2G9; P06396: GSN; NbExp=3; IntAct=EBI-2548012, EBI-351506;
CC Q9H2G9; P56524-2: HDAC4; NbExp=3; IntAct=EBI-2548012, EBI-11953488;
CC Q9H2G9; P49639: HOXA1; NbExp=6; IntAct=EBI-2548012, EBI-740785;
CC Q9H2G9; P31273: HOXC8; NbExp=3; IntAct=EBI-2548012, EBI-1752118;
CC Q9H2G9; P01112: HRAS; NbExp=4; IntAct=EBI-2548012, EBI-350145;
CC Q9H2G9; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-2548012, EBI-11955401;
CC Q9H2G9; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-2548012, EBI-747204;
CC Q9H2G9; Q14005-2: IL16; NbExp=3; IntAct=EBI-2548012, EBI-17178971;
CC Q9H2G9; Q9C086: INO80B; NbExp=3; IntAct=EBI-2548012, EBI-715611;
CC Q9H2G9; Q8NA54: IQUB; NbExp=6; IntAct=EBI-2548012, EBI-10220600;
CC Q9H2G9; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-2548012, EBI-2556193;
CC Q9H2G9; Q92993: KAT5; NbExp=3; IntAct=EBI-2548012, EBI-399080;
CC Q9H2G9; Q7L273: KCTD9; NbExp=3; IntAct=EBI-2548012, EBI-4397613;
CC Q9H2G9; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-2548012, EBI-8472129;
CC Q9H2G9; Q2WGJ6: KLHL38; NbExp=8; IntAct=EBI-2548012, EBI-6426443;
CC Q9H2G9; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-2548012, EBI-10274069;
CC Q9H2G9; P25800: LMO1; NbExp=7; IntAct=EBI-2548012, EBI-8639312;
CC Q9H2G9; P25791: LMO2; NbExp=3; IntAct=EBI-2548012, EBI-739696;
CC Q9H2G9; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2548012, EBI-11742507;
CC Q9H2G9; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2548012, EBI-739832;
CC Q9H2G9; P55081: MFAP1; NbExp=3; IntAct=EBI-2548012, EBI-1048159;
CC Q9H2G9; Q9UJV3-2: MID2; NbExp=5; IntAct=EBI-2548012, EBI-10172526;
CC Q9H2G9; Q8IVT2: MISP; NbExp=5; IntAct=EBI-2548012, EBI-2555085;
CC Q9H2G9; Q13064: MKRN3; NbExp=3; IntAct=EBI-2548012, EBI-2340269;
CC Q9H2G9; Q6PF18: MORN3; NbExp=3; IntAct=EBI-2548012, EBI-9675802;
CC Q9H2G9; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-2548012, EBI-928842;
CC Q9H2G9; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2548012, EBI-741158;
CC Q9H2G9; Q9UMX2: OAZ3; NbExp=4; IntAct=EBI-2548012, EBI-10281601;
CC Q9H2G9; Q9Y5F1: PCDHB12; NbExp=3; IntAct=EBI-2548012, EBI-12012016;
CC Q9H2G9; Q92569: PIK3R3; NbExp=5; IntAct=EBI-2548012, EBI-79893;
CC Q9H2G9; Q16512: PKN1; NbExp=3; IntAct=EBI-2548012, EBI-602382;
CC Q9H2G9; O15160: POLR1C; NbExp=3; IntAct=EBI-2548012, EBI-1055079;
CC Q9H2G9; O43741: PRKAB2; NbExp=9; IntAct=EBI-2548012, EBI-1053424;
CC Q9H2G9; Q99633: PRPF18; NbExp=5; IntAct=EBI-2548012, EBI-2798416;
CC Q9H2G9; P25786: PSMA1; NbExp=3; IntAct=EBI-2548012, EBI-359352;
CC Q9H2G9; P61019: RAB2A; NbExp=9; IntAct=EBI-2548012, EBI-752037;
CC Q9H2G9; Q8WUD1: RAB2B; NbExp=10; IntAct=EBI-2548012, EBI-5542466;
CC Q9H2G9; Q14964: RAB39A; NbExp=8; IntAct=EBI-2548012, EBI-3048577;
CC Q9H2G9; P40937: RFC5; NbExp=3; IntAct=EBI-2548012, EBI-712376;
CC Q9H2G9; Q9H4E5: RHOJ; NbExp=3; IntAct=EBI-2548012, EBI-6285694;
CC Q9H2G9; Q9BWG6: SCNM1; NbExp=6; IntAct=EBI-2548012, EBI-748391;
CC Q9H2G9; P84022: SMAD3; NbExp=9; IntAct=EBI-2548012, EBI-347161;
CC Q9H2G9; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2548012, EBI-5235340;
CC Q9H2G9; Q16385: SSX2B; NbExp=3; IntAct=EBI-2548012, EBI-2210673;
CC Q9H2G9; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-2548012, EBI-745392;
CC Q9H2G9; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-2548012, EBI-8787464;
CC Q9H2G9; Q9P0N9: TBC1D7; NbExp=8; IntAct=EBI-2548012, EBI-3258000;
CC Q9H2G9; O15273: TCAP; NbExp=3; IntAct=EBI-2548012, EBI-954089;
CC Q9H2G9; Q9Y242: TCF19; NbExp=7; IntAct=EBI-2548012, EBI-7413767;
CC Q9H2G9; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-2548012, EBI-750487;
CC Q9H2G9; O95271: TNKS; NbExp=2; IntAct=EBI-2548012, EBI-1105254;
CC Q9H2G9; Q63HR2: TNS2; NbExp=3; IntAct=EBI-2548012, EBI-949753;
CC Q9H2G9; Q9UL33: TRAPPC2L; NbExp=3; IntAct=EBI-2548012, EBI-747601;
CC Q9H2G9; Q9UL33-2: TRAPPC2L; NbExp=3; IntAct=EBI-2548012, EBI-11119202;
CC Q9H2G9; Q8IWR1: TRIM59; NbExp=3; IntAct=EBI-2548012, EBI-10262539;
CC Q9H2G9; Q8IV54: TSC22D4; NbExp=3; IntAct=EBI-2548012, EBI-10261521;
CC Q9H2G9; Q5T7W7: TSTD2; NbExp=5; IntAct=EBI-2548012, EBI-8994397;
CC Q9H2G9; Q5W5X9-3: TTC23; NbExp=5; IntAct=EBI-2548012, EBI-9090990;
CC Q9H2G9; Q86UY0: TXNDC5; NbExp=3; IntAct=EBI-2548012, EBI-2825190;
CC Q9H2G9; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-2548012, EBI-741480;
CC Q9H2G9; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-2548012, EBI-739895;
CC Q9H2G9; Q548N1: VPS28; NbExp=3; IntAct=EBI-2548012, EBI-10243107;
CC Q9H2G9; Q9UK41: VPS28; NbExp=3; IntAct=EBI-2548012, EBI-727424;
CC Q9H2G9; Q05516: ZBTB16; NbExp=3; IntAct=EBI-2548012, EBI-711925;
CC Q9H2G9; O43167: ZBTB24; NbExp=9; IntAct=EBI-2548012, EBI-744471;
CC Q9H2G9; A0A0S2Z6H0: ZGPAT; NbExp=3; IntAct=EBI-2548012, EBI-16428984;
CC Q9H2G9; Q8N5A5: ZGPAT; NbExp=3; IntAct=EBI-2548012, EBI-3439227;
CC Q9H2G9; Q8N5A5-2: ZGPAT; NbExp=6; IntAct=EBI-2548012, EBI-10183064;
CC Q9H2G9; Q15915: ZIC1; NbExp=3; IntAct=EBI-2548012, EBI-11963196;
CC Q9H2G9; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-2548012, EBI-11962760;
CC Q9H2G9; Q15973: ZNF124; NbExp=3; IntAct=EBI-2548012, EBI-2555767;
CC Q9H2G9; Q86VK4: ZNF410; NbExp=4; IntAct=EBI-2548012, EBI-720304;
CC Q9H2G9; Q86VK4-3: ZNF410; NbExp=7; IntAct=EBI-2548012, EBI-11741890;
CC Q9H2G9; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-2548012, EBI-740727;
CC Q9H2G9; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-2548012, EBI-16429014;
CC Q9H2G9; P36508: ZNF76; NbExp=3; IntAct=EBI-2548012, EBI-7254550;
CC Q9H2G9; A0A384ME25; NbExp=3; IntAct=EBI-2548012, EBI-10211777;
CC Q9H2G9; Q9Y649; NbExp=3; IntAct=EBI-2548012, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11739401}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:11056056, ECO:0000269|PubMed:9129147}.
CC Note=Detected in the nucleus upon heterologous expression. Not detected
CC in the cytoplasm. {ECO:0000269|PubMed:11056056,
CC ECO:0000269|PubMed:9129147}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:11056056}. Note=Not detected in the nucleus.
CC {ECO:0000269|PubMed:11056056}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H2G9-1; Sequence=Displayed;
CC Name=2; Synonyms=JEM1s;
CC IsoId=Q9H2G9-2; Sequence=VSP_011186, VSP_011187;
CC -!- TISSUE SPECIFICITY: Detected in adrenal gland (PubMed:9129147).
CC {ECO:0000269|PubMed:11056056, ECO:0000269|PubMed:11739401,
CC ECO:0000269|PubMed:9129147}.
CC -!- INDUCTION: Up-regulated by retinoids. {ECO:0000269|PubMed:11056056,
CC ECO:0000269|PubMed:9129147}.
CC -!- DOMAIN: The tankyrase-binding motif (also named TBD) is required for
CC interaction with tankyrase TNKS and TNKS2.
CC {ECO:0000269|PubMed:21478859}.
CC -!- PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated
CC protein is recognized by RNF146, followed by ubiquitination.
CC {ECO:0000269|PubMed:21478859}.
CC -!- PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its
CC degradation. {ECO:0000269|PubMed:21478859}.
CC -!- CAUTION: Was originally identified as a potential transcription factor,
CC because of the presence of a potential basic motif and leucine-zipper
CC domain, and because isoform 1 is detected in the nucleus upon
CC heterologous expression. However, homology at several typical position
CC for basic or hydrophobic residues is missing. Besides, another
CC publication showed it is important for normal Golgi apparatus structure
CC and function. {ECO:0000305|PubMed:11056056,
CC ECO:0000305|PubMed:11739401, ECO:0000305|PubMed:9129147}.
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DR EMBL; U79751; AAB63110.1; -; mRNA.
DR EMBL; AF288161; AAG37835.1; -; mRNA.
DR EMBL; AF273875; AAG37821.1; -; Genomic_DNA.
DR EMBL; AF288162; AAG37821.1; JOINED; Genomic_DNA.
DR EMBL; AF272386; AAG37822.1; -; Genomic_DNA.
DR EMBL; AF272387; AAG37822.1; JOINED; Genomic_DNA.
DR EMBL; AF272388; AAG37822.1; JOINED; Genomic_DNA.
DR EMBL; AF273875; AAG37822.1; JOINED; Genomic_DNA.
DR EMBL; AF288162; AAG37822.1; JOINED; Genomic_DNA.
DR EMBL; AL356852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90837.1; -; Genomic_DNA.
DR EMBL; BC020716; AAH20716.1; -; mRNA.
DR CCDS; CCDS1278.1; -. [Q9H2G9-1]
DR CCDS; CCDS81397.1; -. [Q9H2G9-2]
DR RefSeq; NP_001307901.1; NM_001320972.1. [Q9H2G9-2]
DR RefSeq; NP_001307902.1; NM_001320973.1. [Q9H2G9-1]
DR RefSeq; NP_003657.1; NM_003666.3. [Q9H2G9-1]
DR RefSeq; XP_011508394.1; XM_011510092.2.
DR AlphaFoldDB; Q9H2G9; -.
DR SMR; Q9H2G9; -.
DR BioGRID; 114118; 132.
DR ComplexPortal; CPX-6092; GRASP55-GM45 Golgi stacking complex.
DR IntAct; Q9H2G9; 136.
DR MINT; Q9H2G9; -.
DR STRING; 9606.ENSP00000356782; -.
DR iPTMnet; Q9H2G9; -.
DR PhosphoSitePlus; Q9H2G9; -.
DR BioMuta; BLZF1; -.
DR DMDM; 116242501; -.
DR EPD; Q9H2G9; -.
DR jPOST; Q9H2G9; -.
DR MassIVE; Q9H2G9; -.
DR MaxQB; Q9H2G9; -.
DR PaxDb; Q9H2G9; -.
DR PeptideAtlas; Q9H2G9; -.
DR PRIDE; Q9H2G9; -.
DR ProteomicsDB; 80547; -. [Q9H2G9-1]
DR ProteomicsDB; 80548; -. [Q9H2G9-2]
DR Antibodypedia; 20542; 311 antibodies from 29 providers.
DR DNASU; 8548; -.
DR Ensembl; ENST00000329281.6; ENSP00000327541.2; ENSG00000117475.14. [Q9H2G9-1]
DR Ensembl; ENST00000367807.7; ENSP00000356781.3; ENSG00000117475.14. [Q9H2G9-2]
DR Ensembl; ENST00000367808.8; ENSP00000356782.3; ENSG00000117475.14. [Q9H2G9-1]
DR GeneID; 8548; -.
DR KEGG; hsa:8548; -.
DR MANE-Select; ENST00000367808.8; ENSP00000356782.3; NM_001320973.2; NP_001307902.1.
DR UCSC; uc001gfw.4; human. [Q9H2G9-1]
DR CTD; 8548; -.
DR DisGeNET; 8548; -.
DR GeneCards; BLZF1; -.
DR HGNC; HGNC:1065; BLZF1.
DR HPA; ENSG00000117475; Low tissue specificity.
DR MIM; 608692; gene.
DR neXtProt; NX_Q9H2G9; -.
DR OpenTargets; ENSG00000117475; -.
DR PharmGKB; PA25375; -.
DR VEuPathDB; HostDB:ENSG00000117475; -.
DR eggNOG; KOG4074; Eukaryota.
DR GeneTree; ENSGT00390000009400; -.
DR HOGENOM; CLU_131589_0_0_1; -.
DR InParanoid; Q9H2G9; -.
DR OMA; HVVPTKN; -.
DR PhylomeDB; Q9H2G9; -.
DR TreeFam; TF317238; -.
DR PathwayCommons; Q9H2G9; -.
DR Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR SignaLink; Q9H2G9; -.
DR SIGNOR; Q9H2G9; -.
DR BioGRID-ORCS; 8548; 6 hits in 1083 CRISPR screens.
DR ChiTaRS; BLZF1; human.
DR GeneWiki; BLZF1; -.
DR GenomeRNAi; 8548; -.
DR Pharos; Q9H2G9; Tbio.
DR PRO; PR:Q9H2G9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H2G9; protein.
DR Bgee; ENSG00000117475; Expressed in calcaneal tendon and 189 other tissues.
DR ExpressionAtlas; Q9H2G9; baseline and differential.
DR Genevisible; Q9H2G9; HS.
DR GO; GO:0005801; C:cis-Golgi network; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IDA:MGI.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:MGI.
DR InterPro; IPR027095; Golgin-45.
DR InterPro; IPR013183; Hsk3-like.
DR PANTHER; PTHR13066; PTHR13066; 1.
DR Pfam; PF08227; DASH_Hsk3; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Alternative splicing; Coiled coil; Cytoplasm;
KW ER-Golgi transport; Golgi apparatus; Membrane; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..400
FT /note="Golgin-45"
FT /id="PRO_0000087539"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..400
FT /note="Essential for interaction with GORASP2"
FT /evidence="ECO:0000269|PubMed:11739401"
FT COILED 120..213
FT /evidence="ECO:0000255"
FT MOTIF 18..22
FT /note="Tankyrase-binding motif"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 158..174
FT /note="NRELKKLLVASVGDDLQ -> RRALIDKMSTTLYVWTF (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:11056056"
FT /id="VSP_011186"
FT VAR_SEQ 175..400
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11056056"
FT /id="VSP_011187"
FT VARIANT 40
FT /note="Q -> R (in dbSNP:rs1028180)"
FT /id="VAR_028142"
FT VARIANT 196
FT /note="R -> Q (in dbSNP:rs1064274)"
FT /id="VAR_028143"
FT CONFLICT 368
FT /note="A -> V (in Ref. 2; AAG37822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 44910 MW; F3F9DA9B13DF45B5 CRC64;
MTTKNLETKV TVTSSPIRGA GDGMETEEPP KSVEVTSGVQ SRKHHSLQSP WKKAVPSESP
GVLQLGKMLT EKAMEVKAVR ILVPKAAITH DIPNKNTKVK SLGHHKGEFL GQSEGVIEPN
KELSEVKNVL EKLKNSERRL LQDKEGLSNQ LRVQTEVNRE LKKLLVASVG DDLQYHFERL
AREKNQLILE NEALGRNTAQ LSEQLERMSI QCDVWRSKFL ASRVMADELT NSRAALQRQN
RDAHGAIQDL LSEREQFRQE MIATQKLLEE LLVSLQWGRE QTYSPSVQPH STAELALTNH
KLAKAVNSHL LGNVGINNQK KIPSTVEFCS TPAEKMAETV LRILDPVTCK ESSPDNPFFE
SSPTTLLATK KNIGRFHPYT RYENITFNCC NHCRGELIAL
