ID MGT4B_HUMAN Reviewed; 548 AA. AC Q9UQ53; A8MPR0; Q86TF1; Q96GH4; Q9NSK6; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 02-SEP-2026, entry version 172. DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B {ECO:0000305}; DE EC=2.4.1.145 {ECO:0000269|PubMed:17006639}; DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVb; DE Short=GlcNAc-T IVb; DE Short=GnT-IVb; DE Short=N-acetylglucosaminyltransferase IVb; DE AltName: Full=UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVb; GN Name=MGAT4B {ECO:0000312|HGNC:HGNC:7048}; ORFNames=UNQ906/PRO1927; 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), TISSUE SPECIFICITY, CATALYTIC RP ACTIVITY, FUNCTION, AND PATHWAY. RC TISSUE=Lung; RX PubMed=10372966; DOI=10.1023/a:1006951519522; RA Yoshida A., Minowa M.T., Takamatsu S., Hara T., Ikenaga H., Takeuchi M.; RT "A novel second isoenzyme of the human UDP-N-acetylglucosamine:alpha1,3-D- RT mannoside beta1,4-N-acetylglucosaminyltransferase family: cDNA cloning, RT expression, and chromosomal assignment."; RL Glycoconj. J. 15:1115-1123(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). 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=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-491. RC TISSUE=PNS, and Uterus; 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 [LARGE SCALE MRNA] OF 176-548 (ISOFORM 2). RC TISSUE=Melanoma; 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 [8] RP OVEREXPRESSION IN PANCREATIC CANCER. RX PubMed=16434023; DOI=10.1016/j.bbrc.2005.12.208; RA Ide Y., Miyoshi E., Nakagawa T., Gu J., Tanemura M., Nishida T., Ito T., RA Yamamoto H., Kozutsumi Y., Taniguchi N.; RT "Aberrant expression of N-acetylglucosaminyltransferase-IVa and IVb (GnT- RT IVa and b) in pancreatic cancer."; RL Biochem. Biophys. Res. Commun. 341:478-482(2006). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, RP AND PATHWAY. RX PubMed=17006639; DOI=10.1007/s10719-006-6216-3; RA Oguri S., Yoshida A., Minowa M.T., Takeuchi M.; RT "Kinetic properties and substrate specificities of two recombinant human N- RT acetylglucosaminyltransferase-IV isozymes."; RL Glycoconj. J. 23:473-480(2006). RN [10] RP INTERACTION WITH SLC35A3. RX PubMed=34981577; DOI=10.1096/fj.202101520r; RA Song W., Isaji T., Nakano M., Liang C., Fukuda T., Gu J.; RT "O-GlcNAcylation regulates beta1,4-GlcNAc-branched N-glycan biosynthesis RT via the OGT/SLC35A3/GnT-IV axis."; RL FASEB J. 36:e22149-e22149(2022). CC -!- FUNCTION: Glycosyltransferase that catalyzes the transfer of GlcNAc CC from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core CC structure of N-linked glycans through a beta1-4 linkage and CC participates in the production of tri- and tetra-antennary N-linked CC sugar chains (PubMed:10372966, PubMed:17006639). Prefers complex-type CC N-glycans over hybrid-types (PubMed:17006639). Has lower affinities for CC donors or acceptors than MGAT4A, suggesting that, under physiological CC conditions, it is not the main contributor in N-glycan biosynthesis CC (PubMed:17006639). {ECO:0000269|PubMed:10372966, CC ECO:0000269|PubMed:17006639}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man- CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L- CC asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = an CC N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)- CC [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D- CC GlcNAc}-L-asparaginyl-[protein] + UDP + H(+); Xref=Rhea:RHEA:69615, CC Rhea:RHEA-COMP:14369, Rhea:RHEA-COMP:17732, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60615, CC ChEBI:CHEBI:187873; Evidence={ECO:0000269|PubMed:17006639}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69616; CC Evidence={ECO:0000305|PubMed:17006639}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc- CC (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)- CC beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D- CC glucosamine = N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]- CC alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D- CC Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl- CC [protein] + UDP + H(+); Xref=Rhea:RHEA:16057, Rhea:RHEA-COMP:13526, CC Rhea:RHEA-COMP:14374, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:60651, ChEBI:CHEBI:139507; CC EC=2.4.1.145; Evidence={ECO:0000269|PubMed:10372966, CC ECO:0000269|PubMed:17006639}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16058; CC Evidence={ECO:0000269|PubMed:10372966, ECO:0000305|PubMed:17006639}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D- CC GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man- CC (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + CC UDP-N-acetyl-alpha-D-glucosamine = an N(4)-{beta-D-GlcNAc-(1->2)- CC [beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)- CC [beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D- CC GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP + H(+); CC Xref=Rhea:RHEA:69619, Rhea:RHEA-COMP:17733, Rhea:RHEA-COMP:17734, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:187874, ChEBI:CHEBI:187875; CC Evidence={ECO:0000269|PubMed:17006639}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69620; CC Evidence={ECO:0000305|PubMed:17006639}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D- CC GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc- CC (1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc}-L-asparaginyl-[protein] + CC UDP-N-acetyl-alpha-D-glucosamine = N(4)-{beta-D-GlcNAc-(1->2)-[beta- CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D- CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc- CC (1->6)]-beta-D-GlcNAc}-asparaginyl-[protein] + UDP + H(+); CC Xref=Rhea:RHEA:69623, Rhea:RHEA-COMP:13532, Rhea:RHEA-COMP:18198, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:137207, ChEBI:CHEBI:187877; CC Evidence={ECO:0000269|PubMed:17006639}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69624; CC Evidence={ECO:0000305|PubMed:17006639}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-Gal- CC (1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)- CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N- CC acetyl-alpha-D-glucosamine = an N(4)-{beta-D-GlcNAc-(1->2)-[beta-D- CC GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-Gal-(1->4)-beta-D-GlcNAc- CC (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)- CC beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP + H(+); CC Xref=Rhea:RHEA:69627, Rhea:RHEA-COMP:17737, Rhea:RHEA-COMP:17738, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:187878, ChEBI:CHEBI:187879; CC Evidence={ECO:0000269|PubMed:17006639}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69628; CC Evidence={ECO:0000305|PubMed:17006639}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man- CC (1->3)-{alpha-D-Man-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)- CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N- CC acetyl-alpha-D-glucosamine = N(4)-{beta-D-GlcNAc-(1->2)-[beta-D- CC GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-{alpha-D-Man- CC (1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)- CC beta-D-GlcNAc}-asparaginyl-[protein] + UDP + H(+); CC Xref=Rhea:RHEA:69631, Rhea:RHEA-COMP:17739, Rhea:RHEA-COMP:17740, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:187880, ChEBI:CHEBI:187881; CC Evidence={ECO:0000269|PubMed:17006639}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69632; CC Evidence={ECO:0000305|PubMed:17006639}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-beta-D-Man- CC (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + CC UDP-N-acetyl-alpha-D-glucosamine = N(4)-{beta-D-GlcNAc-(1->2)-[beta- CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc- CC (1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP + H(+); CC Xref=Rhea:RHEA:69635, Rhea:RHEA-COMP:17741, Rhea:RHEA-COMP:17742, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:187882, ChEBI:CHEBI:187883; CC Evidence={ECO:0000269|PubMed:17006639}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69636; CC Evidence={ECO:0000305|PubMed:17006639}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250|UniProtKB:O77836}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.242 mM for UDP-GlcNAc {ECO:0000269|PubMed:17006639}; CC KM=10.5 mM for CC N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-Asn CC residue {ECO:0000269|PubMed:17006639}; CC KM=5.72 mM for CC N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-Asn CC residue {ECO:0000269|PubMed:17006639}; CC KM=3.35 mM for CC N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-Asn CC residue {ECO:0000269|PubMed:17006639}; CC KM=0.341 mM for UDP-GlcNAc (soluble form) CC {ECO:0000269|PubMed:17006639}; CC KM=6.94 mM for CC N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc} CC (soluble form) {ECO:0000269|PubMed:17006639}; CC Vmax=0.792 pmol/min/mg enzyme (for CC N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-Asn CC residue) {ECO:0000269|PubMed:17006639}; CC Vmax=0.887 pmol/min/mg enzyme (for CC N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-Asn CC residue) {ECO:0000269|PubMed:17006639}; CC Vmax=1.64 pmol/min/mg enzyme (for CC N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-Asn CC residue) {ECO:0000269|PubMed:17006639}; CC Vmax=46.6 nmol/min/mg enzyme (for CC N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-L-Asn CC residue} with soluble form) {ECO:0000269|PubMed:17006639}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:17006639}. CC -!- SUBUNIT: Interacts with SLC35A3. {ECO:0000269|PubMed:34981577}. CC -!- INTERACTION: CC Q9UQ53; Q92624: APPBP2; NbExp=3; IntAct=EBI-725713, EBI-743771; CC Q9UQ53; Q96CV9: OPTN; NbExp=3; IntAct=EBI-725713, EBI-748974; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000250|UniProtKB:Q9D4R2}; Single-pass type II membrane protein CC {ECO:0000250|UniProtKB:Q9D4R2}. Note=A processed soluble form also CC exists. {ECO:0000269|PubMed:17006639}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9UQ53-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UQ53-2; Sequence=VSP_025716; CC Name=3; CC IsoId=Q9UQ53-3; Sequence=VSP_043231; CC -!- TISSUE SPECIFICITY: Widely expressed. Strongly overexpressed in CC pancreatic cancer. {ECO:0000269|PubMed:10372966}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17006639}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 54 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB000624; BAA83464.1; -; mRNA. DR EMBL; AY358984; AAQ89343.1; -; mRNA. DR EMBL; AK023137; BAG51162.1; -; mRNA. DR EMBL; AC008393; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471165; EAW53791.1; -; Genomic_DNA. DR EMBL; BC009464; AAH09464.2; -; mRNA. DR EMBL; BC051835; AAH51835.1; -; mRNA. DR EMBL; AL162067; CAB82404.2; -; mRNA. DR CCDS; CCDS4448.1; -. [Q9UQ53-1] DR CCDS; CCDS4449.1; -. [Q9UQ53-3] DR PIR; T47170; T47170. DR RefSeq; NP_055090.1; NM_014275.5. [Q9UQ53-1] DR RefSeq; NP_463459.1; NM_054013.3. [Q9UQ53-3] DR AlphaFoldDB; Q9UQ53; -. DR SMR; Q9UQ53; -. DR BioGRID; 116438; 39. DR CORUM; Q9UQ53; -. DR FunCoup; Q9UQ53; 1425. DR IntAct; Q9UQ53; 28. DR NDEx; IQUERY-CP-MGAT4B; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000338487; -. DR CAZy; CBM94; Carbohydrate-Binding Module Family 94. DR CAZy; GT54; Glycosyltransferase Family 54. DR GlyCosmos; Q9UQ53; 2 sites, No reported glycans. DR GlyGen; Q9UQ53; 6 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (3 sites). DR iPTMnet; Q9UQ53; -. DR PhosphoSitePlus; Q9UQ53; -. DR BioMuta; MGAT4B; -. DR DMDM; 74735195; -. DR jPOST; Q9UQ53; -. DR MassIVE; Q9UQ53; -. DR PaxDb; 9606-ENSP00000338487; -. DR PeptideAtlas; Q9UQ53; -. DR ProteomicsDB; 85509; -. [Q9UQ53-1] DR ProteomicsDB; 85510; -. [Q9UQ53-2] DR ProteomicsDB; 85511; -. [Q9UQ53-3] DR Pumba; Q9UQ53; -. DR Antibodypedia; 29519; 74 antibodies from 18 providers. DR DNASU; 11282; -. DR Ensembl; ENST00000292591.12; ENSP00000292591.7; ENSG00000161013.18. [Q9UQ53-1] DR Ensembl; ENST00000337755.9; ENSP00000338487.5; ENSG00000161013.18. [Q9UQ53-3] DR Ensembl; ENST00000638266.2; ENSP00000492708.1; ENSG00000284501.2. [Q9UQ53-1] DR Ensembl; ENST00000639538.1; ENSP00000491766.1; ENSG00000284501.2. [Q9UQ53-3] DR GeneID; 11282; -. DR KEGG; hsa:11282; -. DR MANE-Select; ENST00000292591.12; ENSP00000292591.7; NM_014275.5; NP_055090.1. DR UCSC; uc003mkr.4; human. [Q9UQ53-1] DR AGR; HGNC:7048; -. DR ClinPGx; PA30783; -. DR CTD; 11282; -. DR DisGeNET; 11282; -. DR GeneCards; MGAT4B; -. DR HGNC; HGNC:7048; MGAT4B. DR HPA; ENSG00000161013; Tissue enhanced (liver). DR MIM; 604561; gene. DR OpenTargets; ENSG00000161013; -. DR VEuPathDB; HostDB:ENSG00000161013; -. DR eggNOG; ENOG502QPQJ; Eukaryota. DR GeneTree; ENSGT00940000156526; -. DR HOGENOM; CLU_027046_3_0_1; -. DR InParanoid; Q9UQ53; -. DR OMA; FLMFHND; -. DR OrthoDB; 2016523at2759; -. DR PAN-GO; Q9UQ53; 5 GO annotations based on evolutionary models. DR PhylomeDB; Q9UQ53; -. DR BioCyc; MetaCyc:HS08564-MONOMER; -. DR BRENDA; 2.4.1.145; 2681. DR PathwayCommons; Q9UQ53; -. DR Reactome; R-HSA-9694548; Maturation of spike protein. DR Reactome; R-HSA-975577; N-Glycan antennae elongation. DR SignaLink; Q9UQ53; -. DR UniPathway; UPA00378; -. DR Agora; ENSG00000161013; -. DR BioGRID-ORCS; 11282; 18 hits in 1157 CRISPR screens. DR ChiTaRS; MGAT4B; human. DR GeneWiki; MGAT4B; -. DR GenomeRNAi; 11282; -. DR Pharos; Q9UQ53; Tbio. DR PRO; PR:Q9UQ53; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q9UQ53; protein. DR Bgee; ENSG00000161013; Expressed in mucosa of transverse colon and 97 other cell types or tissues. DR ExpressionAtlas; Q9UQ53; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB. DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central. DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central. DR GO; GO:0008454; F:alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity; IDA:UniProtKB. DR GO; GO:0009101; P:glycoprotein biosynthetic process; IDA:UniProtKB. DR GO; GO:0006491; P:N-glycan processing; TAS:ProtInc. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0019082; P:viral protein processing; TAS:Reactome. DR InterPro; IPR006759; Glyco_transf_54. DR InterPro; IPR057279; MGAT4. DR InterPro; IPR056576; MGAT4_A/B/C_C. DR PANTHER; PTHR12062:SF1; ALPHA-1,3-MANNOSYL-GLYCOPROTEIN 4-BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE B; 1. DR PANTHER; PTHR12062; N-ACETYLGLUCOSAMINYLTRANSFERASE VI; 1. DR Pfam; PF04666; MGAT4_cons; 1. DR Pfam; PF23524; MGAT4A_C; 1. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Glycoprotein; Glycosyltransferase; KW Golgi apparatus; Membrane; Metal-binding; Proteomics identification; KW Reference proteome; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..548 FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N- FT acetylglucosaminyltransferase B" FT /id="PRO_0000288593" FT TOPO_DOM 1..7 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 8..28 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 29..548 FT /note="Lumenal" FT /evidence="ECO:0000255" FT COILED 36..83 FT /evidence="ECO:0000255" FT CARBOHYD 87 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 103 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..32 FT /note="MRLRNGTFLTLLLFCLCAFLSLSWYAALSGQK -> MSRVAGTRTDVNELLQ FT RWTPRCVRWHTGGARRVALDRPLVTACLPPA (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043231" FT VAR_SEQ 348 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_025716" FT VARIANT 257 FT /note="Q -> H (in dbSNP:rs190631)" FT /id="VAR_053913" FT VARIANT 491 FT /note="L -> F (in dbSNP:rs17854722)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_032446" SQ SEQUENCE 548 AA; 63198 MW; 1EFF2E681D683C4D CRC64; MRLRNGTFLT LLLFCLCAFL SLSWYAALSG QKGDVVDVYQ REFLALRDRL HAAEQESLKR SKELNLVLDE IKRAVSERQA LRDGDGNRTW GRLTEDPRLK PWNGSHRHVL HLPTVFHHLP HLLAKESSLQ PAVRVGQGRT GVSVVMGIPS VRREVHSYLT DTLHSLISEL SPQEKEDSVI VVLIAETDSQ YTSAVTENIK ALFPTEIHSG LLEVISPSPH FYPDFSRLRE SFGDPKERVR WRTKQNLDYC FLMMYAQSKG IYYVQLEDDI VAKPNYLSTM KNFALQQPSE DWMILEFSQL GFIGKMFKSL DLSLIVEFIL MFYRDKPIDW LLDHILWVKV CNPEKDAKHC DRQKANLRIR FKPSLFQHVG THSSLAGKIQ KLKDKDFGKQ ALRKEHVNPP AEVSTSLKTY QHFTLEKAYL REDFFWAFTP AAGDFIRFRF FQPLRLERFF FRSGNIEHPE DKLFNTSVEV LPFDNPQSDK EALQEGRTAT LRYPRSPDGY LQIGSFYKGV AEGEVDPAFG PLEALRLSIQ TDSPVWVILS EIFLKKAD //