ID ALG13_HUMAN Reviewed; 1137 AA. AC Q9NP73; B1AKD6; B1AKM1; B2R5L5; B7Z6J0; B7Z804; B7Z847; B7Z9A8; B7ZAJ1; AC B7ZB57; Q17RC3; Q5JXY9; Q9H5U8; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-JUN-2010, sequence version 2. DT 27-MAR-2024, entry version 177. DE RecName: Full=Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13; DE EC=2.4.1.141; DE EC=3.4.19.12; DE AltName: Full=Asparagine-linked glycosylation 13 homolog; DE AltName: Full=Glycosyltransferase 28 domain-containing protein 1; DE AltName: Full=UDP-N-acetylglucosamine transferase subunit ALG13 homolog; GN Name=ALG13; Synonyms=CXorf45, GLT28D1; ORFNames=MDS031; 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 [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Hematopoietic stem cell; RA Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z.; RT "Novel genes expressed in hematopoietic stem/progenitor cells from RT myelodysplastic syndrome patients."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). RC TISSUE=Lung, Placenta, Testis, Trachea, and Uterus; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 592-1137 (ISOFORM 4). RC TISSUE=Colon, and Urinary bladder; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 591-1137 (ISOFORM 4). RC TISSUE=Lung; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP FUNCTION (ISOFORM 2). RX PubMed=16100110; DOI=10.1074/jbc.m507569200; RA Gao X.-D., Tachikawa H., Sato T., Jigami Y., Dean N.; RT "Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum RT to form a novel bipartite UDP-N-acetylglucosamine transferase required for RT the second step of N-linked glycosylation."; RL J. Biol. Chem. 280:36254-36262(2005). RN [8] RP IDENTIFICATION. RX PubMed=23827681; DOI=10.1016/j.cell.2013.05.046; RA Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., RA Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., RA Ovaa H., Komander D.; RT "OTU deubiquitinases reveal mechanisms of linkage specificity and enable RT ubiquitin chain restriction analysis."; RL Cell 154:169-184(2013). RN [9] 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 [10] RP INVOLVEMENT IN DEE36, VARIANT DEE36 GLU-94, AND CHARACTERIZATION OF VARIANT RP DEE36 GLU-94. RX PubMed=22492991; DOI=10.1093/hmg/dds123; RA Timal S., Hoischen A., Lehle L., Adamowicz M., Huijben K., RA Sykut-Cegielska J., Paprocka J., Jamroz E., van Spronsen F.J., Korner C., RA Gilissen C., Rodenburg R.J., Eidhof I., Van den Heuvel L., Thiel C., RA Wevers R.A., Morava E., Veltman J., Lefeber D.J.; RT "Gene identification in the congenital disorders of glycosylation type I by RT whole-exome sequencing."; RL Hum. Mol. Genet. 21:4151-4161(2012). RN [11] RP INVOLVEMENT IN DEE36, AND VARIANT DEE36 SER-107. RX PubMed=23934111; DOI=10.1038/nature12439; RG Epi4K Consortium; RG Epilepsy Phenome/Genome Project; RA Allen A.S., Berkovic S.F., Cossette P., Delanty N., Dlugos D., RA Eichler E.E., Epstein M.P., Glauser T., Goldstein D.B., Han Y., RA Heinzen E.L., Hitomi Y., Howell K.B., Johnson M.R., Kuzniecky R., RA Lowenstein D.H., Lu Y.F., Madou M.R., Marson A.G., Mefford H.C., RA Esmaeeli Nieh S., O'Brien T.J., Ottman R., Petrovski S., Poduri A., RA Ruzzo E.K., Scheffer I.E., Sherr E.H., Yuskaitis C.J., Abou-Khalil B., RA Alldredge B.K., Bautista J.F., Berkovic S.F., Boro A., Cascino G.D., RA Consalvo D., Crumrine P., Devinsky O., Dlugos D., Epstein M.P., Fiol M., RA Fountain N.B., French J., Friedman D., Geller E.B., Glauser T., Glynn S., RA Haut S.R., Hayward J., Helmers S.L., Joshi S., Kanner A., Kirsch H.E., RA Knowlton R.C., Kossoff E.H., Kuperman R., Kuzniecky R., Lowenstein D.H., RA McGuire S.M., Motika P.V., Novotny E.J., Ottman R., Paolicchi J.M., RA Parent J.M., Park K., Poduri A., Scheffer I.E., Shellhaas R.A., Sherr E.H., RA Shih J.J., Singh R., Sirven J., Smith M.C., Sullivan J., Lin Thio L., RA Venkat A., Vining E.P., Von Allmen G.K., Weisenberg J.L., Widdess-Walsh P., RA Winawer M.R.; RT "De novo mutations in epileptic encephalopathies."; RL Nature 501:217-221(2013). RN [12] RP INVOLVEMENT IN DEE36, AND VARIANT DEE36 SER-107. RX PubMed=26138355; DOI=10.1111/cge.12636; RA Dimassi S., Labalme A., Ville D., Calender A., Mignot C., Boutry-Kryza N., RA de Bellescize J., Rivier-Ringenbach C., Bourel-Ponchel E., Cheillan D., RA Simonet T., Maincent K., Rossi M., Till M., Mougou-Zerelli S., Edery P., RA Saad A., Heron D., des Portes V., Sanlaville D., Lesca G.; RT "Whole-exome sequencing improves the diagnosis yield in sporadic infantile RT spasm syndrome."; RL Clin. Genet. 89:198-204(2016). RN [13] RP VARIANT DEE36 SER-107. RX PubMed=23033978; DOI=10.1056/nejmoa1206524; RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., RA Veltman J.A., Vissers L.E.; RT "Diagnostic exome sequencing in persons with severe intellectual RT disability."; RL N. Engl. J. Med. 367:1921-1929(2012). RN [14] RP VARIANT DEE36 SER-107. RX PubMed=27476654; DOI=10.1016/j.ajhg.2016.06.003; RG Epi4K Consortium; RT "De novo mutations in SLC1A2 and CACNA1A are important causes of epileptic RT encephalopathies."; RL Am. J. Hum. Genet. 99:287-298(2016). CC -!- FUNCTION: [Isoform 1]: Possible multifunctional enzyme with both CC glycosyltransferase and deubiquitinase activities. CC -!- FUNCTION: [Isoform 2]: May be involved in protein N-glycosylation, CC second step of the dolichol-linked oligosaccharide pathway. CC -!- CATALYTIC ACTIVITY: CC Reaction=N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N- CC acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl CC diphosphodolichol + UDP; Xref=Rhea:RHEA:23380, Rhea:RHEA-COMP:9519, CC Rhea:RHEA-COMP:9520, ChEBI:CHEBI:15378, ChEBI:CHEBI:57269, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:58427; CC EC=2.4.1.141; CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; CC -!- SUBUNIT: Isoform 2 may interact with ALG14. {ECO:0000250}. CC -!- INTERACTION: CC Q9NP73-4; O95429: BAG4; NbExp=3; IntAct=EBI-10186621, EBI-2949658; CC Q9NP73-4; P49639: HOXA1; NbExp=3; IntAct=EBI-10186621, EBI-740785; CC Q9NP73-4; O60336: MAPKBP1; NbExp=3; IntAct=EBI-10186621, EBI-947402; CC Q9NP73-4; Q01974: ROR2; NbExp=3; IntAct=EBI-10186621, EBI-6422642; CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum {ECO:0000305}. CC Note=Could be recruited to the cytosolic face of the endoplasmic CC reticulum membrane through its interaction with ALG14. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9NP73-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NP73-2; Sequence=VSP_039301, VSP_039302; CC Name=3; CC IsoId=Q9NP73-3; Sequence=VSP_039299, VSP_039300; CC Name=4; CC IsoId=Q9NP73-4; Sequence=VSP_039298, VSP_039303; CC -!- DOMAIN: Contains 1 OTU domain with intact active sites. No CC deubiquitinase activity has been detected when tested CC (PubMed:23827681). {ECO:0000269|PubMed:23827681}. CC -!- DISEASE: Developmental and epileptic encephalopathy 36 (DEE36) CC [MIM:300884]: A form of epileptic encephalopathy, a heterogeneous group CC of severe early-onset epilepsies characterized by refractory seizures, CC neurodevelopmental impairment, and poor prognosis. Development is CC normal prior to seizure onset, after which cognitive and motor delays CC become apparent. Some DEE36 patients may present with an abnormal CC isoelectric focusing of serum transferrin, consistent with a diagnostic CC classification of congenital disorder of glycosylation type I. CC Congenital disorders of glycosylation result in a wide variety of CC clinical features, such as defects in the nervous system development, CC psychomotor retardation, dysmorphic features, hypotonia, coagulation CC disorders, and immunodeficiency. The broad spectrum of features CC reflects the critical role of N-glycoproteins during embryonic CC development, differentiation, and maintenance of cell functions. CC {ECO:0000269|PubMed:22492991, ECO:0000269|PubMed:23033978, CC ECO:0000269|PubMed:23934111, ECO:0000269|PubMed:26138355, CC ECO:0000269|PubMed:27476654}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI17378.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI17380.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB15521.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAD96874.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAH14244.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAH14244.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={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; AF220051; AAF67644.1; -; mRNA. DR EMBL; AK026671; BAB15521.1; ALT_INIT; mRNA. DR EMBL; AK300394; BAH13276.1; -; mRNA. DR EMBL; AK302729; BAH13790.1; -; mRNA. DR EMBL; AK302890; BAH13833.1; -; mRNA. DR EMBL; AK304712; BAH14244.1; ALT_SEQ; mRNA. DR EMBL; AK316306; BAH14677.1; -; mRNA. DR EMBL; AK316522; BAH14893.1; -; mRNA. DR EMBL; AK312229; BAG35162.1; -; mRNA. DR EMBL; AL049563; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL096764; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471120; EAX02635.1; -; Genomic_DNA. DR EMBL; BC005336; AAH05336.1; -; mRNA. DR EMBL; BC117377; AAI17378.1; ALT_INIT; mRNA. DR EMBL; BC117379; AAI17380.1; ALT_INIT; mRNA. DR EMBL; AK223154; BAD96874.1; ALT_INIT; mRNA. DR CCDS; CCDS14559.1; -. [Q9NP73-2] DR CCDS; CCDS55477.1; -. [Q9NP73-1] DR CCDS; CCDS59173.1; -. [Q9NP73-4] DR RefSeq; NP_001034299.3; NM_001039210.4. DR RefSeq; NP_001093392.1; NM_001099922.2. [Q9NP73-1] DR RefSeq; NP_001161857.1; NM_001168385.2. DR RefSeq; NP_001244159.1; NM_001257230.1. [Q9NP73-4] DR RefSeq; NP_001244160.1; NM_001257231.1. [Q9NP73-3] DR RefSeq; NP_001244163.1; NM_001257234.1. [Q9NP73-4] DR RefSeq; NP_001244166.1; NM_001257237.1. [Q9NP73-4] DR RefSeq; NP_001244170.1; NM_001257241.2. DR RefSeq; NP_060936.1; NM_018466.5. [Q9NP73-2] DR AlphaFoldDB; Q9NP73; -. DR SMR; Q9NP73; -. DR BioGRID; 122956; 184. DR IntAct; Q9NP73; 24. DR MINT; Q9NP73; -. DR STRING; 9606.ENSP00000378260; -. DR CAZy; GT1; Glycosyltransferase Family 1. DR MEROPS; C85.005; -. DR GlyGen; Q9NP73; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NP73; -. DR MetOSite; Q9NP73; -. DR PhosphoSitePlus; Q9NP73; -. DR SwissPalm; Q9NP73; -. DR BioMuta; ALG13; -. DR DMDM; 298286785; -. DR EPD; Q9NP73; -. DR jPOST; Q9NP73; -. DR MassIVE; Q9NP73; -. DR MaxQB; Q9NP73; -. DR PaxDb; 9606-ENSP00000378260; -. DR PeptideAtlas; Q9NP73; -. DR ProteomicsDB; 81908; -. [Q9NP73-1] DR ProteomicsDB; 81909; -. [Q9NP73-2] DR ProteomicsDB; 81910; -. [Q9NP73-3] DR ProteomicsDB; 81911; -. [Q9NP73-4] DR Pumba; Q9NP73; -. DR ABCD; Q9NP73; 1 sequenced antibody. DR Antibodypedia; 490; 189 antibodies from 21 providers. DR DNASU; 79868; -. DR Ensembl; ENST00000371979.7; ENSP00000361047.3; ENSG00000101901.13. [Q9NP73-2] DR Ensembl; ENST00000394780.8; ENSP00000378260.3; ENSG00000101901.13. [Q9NP73-1] DR Ensembl; ENST00000436609.5; ENSP00000392990.2; ENSG00000101901.13. [Q9NP73-4] DR GeneID; 79868; -. DR KEGG; hsa:79868; -. DR MANE-Select; ENST00000394780.8; ENSP00000378260.3; NM_001099922.3; NP_001093392.1. DR UCSC; uc004epi.3; human. [Q9NP73-1] DR AGR; HGNC:30881; -. DR CTD; 79868; -. DR DisGeNET; 79868; -. DR GeneCards; ALG13; -. DR GeneReviews; ALG13; -. DR HGNC; HGNC:30881; ALG13. DR HPA; ENSG00000101901; Low tissue specificity. DR MalaCards; ALG13; -. DR MIM; 300776; gene. DR MIM; 300884; phenotype. DR neXtProt; NX_Q9NP73; -. DR OpenTargets; ENSG00000101901; -. DR Orphanet; 324422; ALG13-CDG. DR Orphanet; 777; X-linked non-syndromic intellectual disability. DR PharmGKB; PA162376235; -. DR VEuPathDB; HostDB:ENSG00000101901; -. DR eggNOG; KOG2605; Eukaryota. DR eggNOG; KOG3349; Eukaryota. DR GeneTree; ENSGT00940000159922; -. DR HOGENOM; CLU_009906_0_0_1; -. DR InParanoid; Q9NP73; -. DR OMA; QYKFRPN; -. DR OrthoDB; 5406292at2759; -. DR PhylomeDB; Q9NP73; -. DR TreeFam; TF332789; -. DR PathwayCommons; Q9NP73; -. DR Reactome; R-HSA-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein. DR Reactome; R-HSA-5633231; Defective ALG14 causes ALG14-CMS. DR SignaLink; Q9NP73; -. DR BioGRID-ORCS; 79868; 248 hits in 806 CRISPR screens. DR ChiTaRS; ALG13; human. DR GeneWiki; ALG13; -. DR GenomeRNAi; 79868; -. DR Pharos; Q9NP73; Tbio. DR PRO; PR:Q9NP73; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9NP73; Protein. DR Bgee; ENSG00000101901; Expressed in calcaneal tendon and 197 other cell types or tissues. DR ExpressionAtlas; Q9NP73; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC. DR GO; GO:0004577; F:N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd22795; OTU_ALG13; 1. DR CDD; cd20447; Tudor_TDRD13; 1. DR Gene3D; 3.90.70.80; -; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1. DR InterPro; IPR039042; Alg13-like. DR InterPro; IPR007235; Glyco_trans_28_C. DR InterPro; IPR047387; OTU_ALG13. DR InterPro; IPR003323; OTU_dom. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR002999; Tudor. DR PANTHER; PTHR12867:SF7; BIFUNCTIONAL UDP-N-ACETYLGLUCOSAMINE TRANSFERASE AND DEUBIQUITINASE ALG13-RELATED; 1. DR PANTHER; PTHR12867; GLYCOSYL TRANSFERASE-RELATED; 1. DR Pfam; PF04101; Glyco_tran_28_C; 1. DR Pfam; PF02338; OTU; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR PROSITE; PS50802; OTU; 1. DR PROSITE; PS50304; TUDOR; 1. DR Genevisible; Q9NP73; HS. PE 1: Evidence at protein level; KW Alternative splicing; Congenital disorder of glycosylation; KW Disease variant; Endoplasmic reticulum; Epilepsy; Glycosyltransferase; KW Hydrolase; Multifunctional enzyme; Protease; Reference proteome; KW Thiol protease; Transferase; Ubl conjugation pathway. FT CHAIN 1..1137 FT /note="Putative bifunctional UDP-N-acetylglucosamine FT transferase and deubiquitinase ALG13" FT /id="PRO_0000254573" FT DOMAIN 231..352 FT /note="OTU" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139" FT DOMAIN 492..552 FT /note="Tudor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211" FT REGION 1..125 FT /note="Glycosyltransferase activity" FT REGION 126..400 FT /note="Deubiquitinase activity" FT REGION 641..673 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 911..974 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 915..948 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 955..970 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 239 FT /note="For deubiquitinase activity" FT /evidence="ECO:0000250" FT ACT_SITE 242 FT /note="Nucleophile; for deubiquitinase activity" FT /evidence="ECO:0000250" FT ACT_SITE 345 FT /note="For deubiquitinase activity" FT /evidence="ECO:0000250" FT VAR_SEQ 1..104 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6" FT /id="VSP_039298" FT VAR_SEQ 1..78 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039299" FT VAR_SEQ 79..81 FT /note="SHA -> MFT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039300" FT VAR_SEQ 128..165 FT /note="RVLTCPGQAKSIASAPGKCQDSAALTSTAFSGLDFGLL -> STLPGLLQSM FT DLSTLKCYPPGQPEKFSAFLDKVVGLQK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1" FT /id="VSP_039301" FT VAR_SEQ 166..1137 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1" FT /id="VSP_039302" FT VAR_SEQ 899..977 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6" FT /id="VSP_039303" FT VARIANT 94 FT /note="K -> E (in DEE36; disease features include abnormal FT isoelectric focusing of serum transferrin consistent with a FT glycosylation defect; enzyme activity at about 17% of FT wild-type; dbSNP:rs867599353)" FT /evidence="ECO:0000269|PubMed:22492991" FT /id="VAR_069218" FT VARIANT 107 FT /note="N -> S (in DEE36; de novo mutation detected in FT unrelated patients; dbSNP:rs398122394)" FT /evidence="ECO:0000269|PubMed:23033978, FT ECO:0000269|PubMed:23934111, ECO:0000269|PubMed:26138355, FT ECO:0000269|PubMed:27476654" FT /id="VAR_069412" FT CONFLICT 493 FT /note="Y -> N (in Ref. 1; BAH14677)" FT /evidence="ECO:0000305" FT CONFLICT 564 FT /note="G -> D (in Ref. 1; BAH13276)" FT /evidence="ECO:0000305" FT CONFLICT 588 FT /note="K -> R (in Ref. 1; BAH14677)" FT /evidence="ECO:0000305" FT CONFLICT 624 FT /note="D -> G (in Ref. 1; BAH13276)" FT /evidence="ECO:0000305" FT CONFLICT 658 FT /note="P -> L (in Ref. 1; BAH13790)" FT /evidence="ECO:0000305" FT CONFLICT 746..748 FT /note="PTL -> ATF (in Ref. 1; BAB15521)" FT /evidence="ECO:0000305" FT CONFLICT 752 FT /note="G -> E (in Ref. 1; BAB15521)" FT /evidence="ECO:0000305" FT CONFLICT 866 FT /note="N -> K (in Ref. 1; BAH14677)" FT /evidence="ECO:0000305" FT CONFLICT 926 FT /note="P -> L (in Ref. 1; BAH14244)" FT /evidence="ECO:0000305" FT CONFLICT 954 FT /note="N -> S (in Ref. 1; BAH14244)" FT /evidence="ECO:0000305" FT CONFLICT 1018 FT /note="V -> A (in Ref. 1; BAH14244)" FT /evidence="ECO:0000305" SQ SEQUENCE 1137 AA; 126056 MW; 4E56437BA2609589 CRC64; MKCVFVTVGT TSFDDLIACV SAPDSLQKIE SLGYNRLILQ IGRGTVVPEP FSTESFTLDV YRYKDSLKED IQKADLVISH AGAGSCLETL EKGKPLVVVI NEKLMNNHQL ELAKQLHKEG HLFYCTCRVL TCPGQAKSIA SAPGKCQDSA ALTSTAFSGL DFGLLSGYLH KQALVTATHP TCTLLFPSCH AFFPLPLTPT LYKMHKGWKN YCSQKSLNEA SMDEYLGSLG LFRKLTAKDA SCLFRAISEQ LFCSQVHHLE IRKACVSYMR ENQQTFESYV EGSFEKYLER LGDPKESAGQ LEIRALSLIY NRDFILYRFP GKPPTYVTDN GYEDKILLCY SSSGHYDSVY SKQFQSSAAV CQAVLYEILY KDVFVVDEEE LKTAIKLFRS GSKKNRNNAV TGSEDAHTDY KSSNQNRMEE WGACYNAENI PEGYNKGTEE TKSPENPSKM PFPYKVLKAL DPEIYRNVEF DVWLDSRKEL QKSDYMEYAG RQYYLGDKCQ VCLESEGRYY NAHIQEVGNE NNSVTVFIEE LAEKHVVPLA NLKPVTQVMS VPAWNAMPSR KGRGYQKMPG GYVPEIVISE MDIKQQKKMF KKIRGKEVYM TMAYGKGDPL LPPRLQHSMH YGHDPPMHYS QTAGNVMSNE HFHPQHPSPR QGRGYGMPRN SSRFINRHNM PGPKVDFYPG PGKRCCQSYD NFSYRSRSFR RSHRQMSCVN KESQYGFTPG NGQMPRGLEE TITFYEVEEG DETAYPTLPN HGGPSTMVPA TSGYCVGRRG HSSGKQTLNL EEGNGQSENG RYHEEYLYRA EPDYETSGVY STTASTANLS LQDRKSCSMS PQDTVTSYNY PQKMMGNIAA VAASCANNVP APVLSNGAAA NQAISTTSVS SQNAIQPLFV SPPTHGRPVI ASPSYPCHSA IPHAGASLPP PPPPPPPPPP PPPPPPPPPP PPPPPALDVG ETSNLQPPPP LPPPPYSCDP SGSDLPQDTK VLQYYFNLGL QCYYHSYWHS MVYVPQMQQQ LHVENYPVYT EPPLVDQTVP QCYSEVRRED GIQAEASAND TFPNADSSSV PHGAVYYPVM SDPYGQPPLP GFDSCLPVVP DYSCVPPWHP VGTAYGGSSQ IHGAINPGPI GCIAPSPPAS HYVPQGM //