MI4GD_HUMAN
ID MI4GD_HUMAN Reviewed; 222 AA.
AC A9UHW6; B4DUM7; Q8N4Q5; Q9HBL5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=MIF4G domain-containing protein;
DE AltName: Full=SLBP-interacting protein 1;
DE Short=hSLIP1;
GN Name=MIF4GD; Synonyms=SLIP1;
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), FUNCTION, INTERACTION WITH EIF4G1;
RP EIF4G2 AND SLBP, AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=18025107; DOI=10.1128/mcb.01500-07;
RA Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.;
RT "SLIP1, a factor required for activation of histone mRNA translation by the
RT stem-loop binding protein.";
RL Mol. Cell. Biol. 28:1182-1194(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Cervix carcinoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Skeletal muscle;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(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 2).
RC TISSUE=Blood;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-164 (ISOFORM 1).
RC TISSUE=Adrenal gland;
RA Xiao H., Song H., Gao G., Ren S., Chen Z., Han Z.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
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).
CC -!- FUNCTION: Functions in replication-dependent translation of histone
CC mRNAs which differ from other eukaryotic mRNAs in that they do not end
CC with a poly-A tail but a stem-loop. May participate in circularizing
CC those mRNAs specifically enhancing their translation.
CC {ECO:0000269|PubMed:18025107}.
CC -!- SUBUNIT: Interacts with EIF4G1, EIF4G2 and SLBP; probably tethered by
CC SLBP to the 3'-end of mRNAs ending with the histone stem-loop, it also
CC interacts with EIF4G1 which is bound to their 5'-end.
CC {ECO:0000269|PubMed:18025107}.
CC -!- INTERACTION:
CC A9UHW6; Q9NUU7: DDX19A; NbExp=7; IntAct=EBI-373498, EBI-740301;
CC A9UHW6; Q9UMR2: DDX19B; NbExp=11; IntAct=EBI-373498, EBI-719232;
CC A9UHW6; O75821: EIF3G; NbExp=2; IntAct=EBI-373498, EBI-366632;
CC A9UHW6; Q8IV48: ERI1; NbExp=2; IntAct=EBI-373498, EBI-5459222;
CC A9UHW6; P56524: HDAC4; NbExp=4; IntAct=EBI-373498, EBI-308629;
CC A9UHW6; O14964: HGS; NbExp=5; IntAct=EBI-373498, EBI-740220;
CC A9UHW6; A9UHW6: MIF4GD; NbExp=6; IntAct=EBI-373498, EBI-373498;
CC A9UHW6; P01106: MYC; NbExp=2; IntAct=EBI-373498, EBI-447544;
CC A9UHW6; Q5VU43: PDE4DIP; NbExp=3; IntAct=EBI-373498, EBI-1105124;
CC A9UHW6; Q14493: SLBP; NbExp=10; IntAct=EBI-373498, EBI-2696402;
CC A9UHW6; PRO_0000037314 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-373498, EBI-25487672;
CC A9UHW6-2; P29972: AQP1; NbExp=3; IntAct=EBI-9118295, EBI-745213;
CC A9UHW6-2; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-9118295, EBI-1166928;
CC A9UHW6-2; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-9118295, EBI-749051;
CC A9UHW6-2; Q9Y6H1: CHCHD2; NbExp=3; IntAct=EBI-9118295, EBI-2321769;
CC A9UHW6-2; P53673: CRYBA4; NbExp=3; IntAct=EBI-9118295, EBI-7519711;
CC A9UHW6-2; O43310-2: CTIF; NbExp=3; IntAct=EBI-9118295, EBI-12180013;
CC A9UHW6-2; Q9NUU7: DDX19A; NbExp=3; IntAct=EBI-9118295, EBI-740301;
CC A9UHW6-2; Q9UMR2: DDX19B; NbExp=6; IntAct=EBI-9118295, EBI-719232;
CC A9UHW6-2; O75821: EIF3G; NbExp=3; IntAct=EBI-9118295, EBI-366632;
CC A9UHW6-2; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-9118295, EBI-744099;
CC A9UHW6-2; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-9118295, EBI-1752811;
CC A9UHW6-2; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-9118295, EBI-16429135;
CC A9UHW6-2; O14964: HGS; NbExp=6; IntAct=EBI-9118295, EBI-740220;
CC A9UHW6-2; Q13064: MKRN3; NbExp=3; IntAct=EBI-9118295, EBI-2340269;
CC A9UHW6-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-9118295, EBI-741158;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18025107}. Nucleus
CC {ECO:0000269|PubMed:18025107}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A9UHW6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A9UHW6-2; Sequence=VSP_033877;
CC Name=3;
CC IsoId=A9UHW6-3; Sequence=VSP_047408;
CC -!- MISCELLANEOUS: Depletion of MIF4GD results in cell death and reduced
CC histone mRNA translation.
CC -!- SIMILARITY: Belongs to the MIF4GD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09724.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; EU287989; ABX83907.1; -; mRNA.
DR EMBL; AL555095; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK300711; BAG62389.1; -; mRNA.
DR EMBL; AC022211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89263.1; -; Genomic_DNA.
DR EMBL; BC033759; AAH33759.1; -; mRNA.
DR EMBL; AF225422; AAG09724.1; ALT_FRAME; mRNA.
DR CCDS; CCDS11719.1; -. [A9UHW6-2]
DR CCDS; CCDS56044.1; -. [A9UHW6-1]
DR CCDS; CCDS58598.1; -. [A9UHW6-3]
DR RefSeq; NP_001229427.1; NM_001242498.1. [A9UHW6-3]
DR RefSeq; NP_001229429.1; NM_001242500.1. [A9UHW6-2]
DR RefSeq; NP_001229430.1; NM_001242501.1. [A9UHW6-1]
DR RefSeq; NP_065730.2; NM_020679.3. [A9UHW6-2]
DR RefSeq; XP_005257587.1; XM_005257530.1.
DR RefSeq; XP_005257589.1; XM_005257532.4.
DR RefSeq; XP_005257590.1; XM_005257533.1.
DR RefSeq; XP_016880382.1; XM_017024893.1.
DR RefSeq; XP_016880383.1; XM_017024894.1.
DR AlphaFoldDB; A9UHW6; -.
DR SMR; A9UHW6; -.
DR BioGRID; 121511; 51.
DR ComplexPortal; CPX-1313; SLBP-SLIP1 complex.
DR IntAct; A9UHW6; 32.
DR MINT; A9UHW6; -.
DR iPTMnet; A9UHW6; -.
DR PhosphoSitePlus; A9UHW6; -.
DR BioMuta; MIF4GD; -.
DR EPD; A9UHW6; -.
DR jPOST; A9UHW6; -.
DR MassIVE; A9UHW6; -.
DR MaxQB; A9UHW6; -.
DR PeptideAtlas; A9UHW6; -.
DR PRIDE; A9UHW6; -.
DR ProteomicsDB; 2507; -. [A9UHW6-1]
DR ProteomicsDB; 2508; -. [A9UHW6-2]
DR Antibodypedia; 32154; 148 antibodies from 18 providers.
DR DNASU; 57409; -.
DR Ensembl; ENST00000245551.9; ENSP00000245551.5; ENSG00000125457.15. [A9UHW6-2]
DR Ensembl; ENST00000325102.13; ENSP00000321625.8; ENSG00000125457.15. [A9UHW6-1]
DR Ensembl; ENST00000577542.5; ENSP00000463334.1; ENSG00000125457.15. [A9UHW6-3]
DR Ensembl; ENST00000579194.6; ENSP00000462655.2; ENSG00000125457.15. [A9UHW6-3]
DR Ensembl; ENST00000579297.5; ENSP00000462459.1; ENSG00000125457.15. [A9UHW6-3]
DR Ensembl; ENST00000618645.5; ENSP00000484245.1; ENSG00000125457.15. [A9UHW6-1]
DR GeneID; 57409; -.
DR KEGG; hsa:57409; -.
DR MANE-Select; ENST00000325102.13; ENSP00000321625.8; NM_001370592.1; NP_001357521.1.
DR UCSC; uc002jnp.5; human. [A9UHW6-1]
DR CTD; 57409; -.
DR DisGeNET; 57409; -.
DR GeneCards; MIF4GD; -.
DR HGNC; HGNC:24030; MIF4GD.
DR HPA; ENSG00000125457; Low tissue specificity.
DR MIM; 612072; gene.
DR neXtProt; NX_A9UHW6; -.
DR OpenTargets; ENSG00000125457; -.
DR PharmGKB; PA142671457; -.
DR VEuPathDB; HostDB:ENSG00000125457; -.
DR GeneTree; ENSGT00940000153432; -.
DR InParanoid; A9UHW6; -.
DR OrthoDB; 1168859at2759; -.
DR PhylomeDB; A9UHW6; -.
DR PathwayCommons; A9UHW6; -.
DR SignaLink; A9UHW6; -.
DR BioGRID-ORCS; 57409; 17 hits in 1083 CRISPR screens.
DR GenomeRNAi; 57409; -.
DR Pharos; A9UHW6; Tbio.
DR PRO; PR:A9UHW6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; A9UHW6; protein.
DR Bgee; ENSG00000125457; Expressed in upper arm skin and 186 other tissues.
DR ExpressionAtlas; A9UHW6; baseline and differential.
DR Genevisible; A9UHW6; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0062073; C:histone mRNA stem-loop binding complex; IPI:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008494; F:translation activator activity; IBA:GO_Central.
DR GO; GO:0002191; P:cap-dependent translational initiation; IDA:ComplexPortal.
DR GO; GO:0006446; P:regulation of translational initiation; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Reference proteome;
KW Translation regulation.
FT CHAIN 1..222
FT /note="MIF4G domain-containing protein"
FT /id="PRO_0000337089"
FT DOMAIN 3..205
FT /note="MIF4G"
FT VAR_SEQ 27
FT /note="K -> KVACFETEDGEYSVCQRSYSNCSRLMPSRCNTQYR (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033877"
FT VAR_SEQ 27
FT /note="K -> KAPSLECTVACFETEDGEYSVCQRSYSNCSRLMPSRCNTQYR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_047408"
SQ SEQUENCE 222 AA; 25423 MW; 07E5B651D638AC9D CRC64;
MGEPSREEYK IQSFDAETQQ LLKTALKDPG AVDLEKVANV IVDHSLQDCV FSKEAGRMCY
AIIQAESKQA GQSVFRRGLL NRLQQEYQAR EQLRARSLQG WVCYVTFICN IFDYLRVNNM
PMMALVNPVY DCLFRLAQPD SLSKEEEVDC LVLQLHRVGE QLEKMNGQRM DELFVLIRDG
FLLPTGLSSL AQLLLLEIIE FRAAGWKTTP AAHKYYYSEV SD
