ALG13_HUMAN
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 03-AUG-2022, entry version 168.
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};
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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 CCDS; CCDS76012.1; -. [Q9NP73-3]
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; 176.
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; Q9NP73; -.
DR PeptideAtlas; Q9NP73; -.
DR PRIDE; Q9NP73; -.
DR ProteomicsDB; 81908; -. [Q9NP73-1]
DR ProteomicsDB; 81909; -. [Q9NP73-2]
DR ProteomicsDB; 81910; -. [Q9NP73-3]
DR ProteomicsDB; 81911; -. [Q9NP73-4]
DR ABCD; Q9NP73; 1 sequenced antibody.
DR Antibodypedia; 490; 170 antibodies from 20 providers.
DR DNASU; 79868; -.
DR Ensembl; ENST00000251943.8; ENSP00000251943.4; ENSG00000101901.12. [Q9NP73-4]
DR Ensembl; ENST00000371979.7; ENSP00000361047.3; ENSG00000101901.12. [Q9NP73-2]
DR Ensembl; ENST00000394780.8; ENSP00000378260.3; ENSG00000101901.12. [Q9NP73-1]
DR Ensembl; ENST00000436609.5; ENSP00000392990.2; ENSG00000101901.12. [Q9NP73-4]
DR Ensembl; ENST00000610588.4; ENSP00000479731.1; ENSG00000101901.12. [Q9NP73-3]
DR Ensembl; ENST00000621367.4; ENSP00000481509.1; ENSG00000101901.12. [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 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; NYLYYCK; -.
DR OrthoDB; 222767at2759; -.
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; 218 hits in 723 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 195 other tissues.
DR ExpressionAtlas; Q9NP73; baseline and differential.
DR Genevisible; Q9NP73; HS.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04508; TUDOR; 1.
DR InterPro; IPR007235; Glyco_trans_28_C.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF04101; Glyco_tran_28_C; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS50304; TUDOR; 1.
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 wild-
FT 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
