Q9NP73 (ALG13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-N-acetylglucosamine transferase subunit ALG13 homolog
EC=2.4.1.141

Alternative name(s):
Asparagine-linked glycosylation 13 homolog
Glycosyltransferase 28 domain-containing protein 1

Gene names

Name:	ALG13
Synonyms:	CXorf45
ORF Names:	GLT28D1, MDS031

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1137 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Isoform 2 may be involved in protein N-glycosylation, second step of the dolichol-linked oligosaccharide pathway. Ref.7
Catalytic activity	UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-diphosphodolichol = UDP + N,N'-diacetylchitobiosyl-diphosphodolichol.
Subunit structure	Isoform 2 may interact with ALG14 By similarity.
Subcellular location	Isoform 2: Endoplasmic reticulum Probable. Note: Could be recruited to the cytosolic face of the endoplasmic reticulum membrane through its interaction with ALG14.
Involvement in disease	Congenital disorder of glycosylation 1S (CDG1S) [MIM:300884]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9
Sequence similarities	Belongs to the glycosyltransferase 28 family. Contains 1 OTU domain. Contains 1 Tudor domain.
Sequence caution	The sequence AAI17378.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAI17380.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB15521.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAD96874.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAH14244.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAH14244.1 differs from that shown. Reason: Erroneous termination at position 424. Translated as Cys. The sequence CAI43016.2 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAM28219.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Alternative splicing
Disease	Congenital disorder of glycosylation Disease mutation
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dolichol-linked oligosaccharide biosynthetic process Traceable author statement. Source: Reactome lipid glycosylation Inferred from electronic annotation. Source: InterPro post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome
Molecular_function	N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC carbohydrate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NP73-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9NP73-2)

The sequence of this isoform differs from the canonical sequence as follows:
     128-165: RVLTCPGQAK...AFSGLDFGLL → STLPGLLQSM...FLDKVVGLQK
     166-1137: Missing.

Isoform 3 (identifier: Q9NP73-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.
     79-81: SHA → MFT

Note: No experimental confirmation available.

Isoform 4 (identifier: Q9NP73-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-104: Missing.
     899-977: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1137	1137	UDP-N-acetylglucosamine transferase subunit ALG13 homolog		PRO_0000254573
Regions
	Domain	231 – 352	122	OTU
	Domain	492 – 552	61	Tudor
	Compositional bias	887 – 970	84	Pro-rich
Natural variations
	Alternative sequence	1 – 104	104	Missing in isoform 4.		VSP_039298
	Alternative sequence	1 – 78	78	Missing in isoform 3.		VSP_039299
	Alternative sequence	79 – 81	3	SHA → MFT in isoform 3.		VSP_039300
	Alternative sequence	128 – 165	38	RVLTC…DFGLL → STLPGLLQSMDLSTLKCYPP GQPEKFSAFLDKVVGLQK in isoform 2.		VSP_039301
	Alternative sequence	166 – 1137	972	Missing in isoform 2.		VSP_039302
	Alternative sequence	899 – 977	79	Missing in isoform 4.		VSP_039303
	Natural variant	94	1	K → E in CDG1S; there is a decrease enzyme activity at about 17% of wild-type. Ref.9		VAR_069218
Experimental info
	Sequence conflict	493	1	Y → N in BAH14677. Ref.1
	Sequence conflict	564	1	G → D in BAH13276. Ref.1
	Sequence conflict	588	1	K → R in BAH14677. Ref.1
	Sequence conflict	624	1	D → G in BAH13276. Ref.1
	Sequence conflict	658	1	P → L in BAH13790. Ref.1
	Sequence conflict	746 – 748	3	PTL → ATF in BAB15521. Ref.1
	Sequence conflict	752	1	G → E in BAB15521. Ref.1
	Sequence conflict	866	1	N → K in BAH14677. Ref.1
	Sequence conflict	926	1	P → L in BAH14244. Ref.1
	Sequence conflict	954	1	N → S in BAH14244. Ref.1
	Sequence conflict	1018	1	V → A in BAH14244. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 15, 2010. Version 2. Checksum: 4E56437BA2609589	FASTA	1,137	126,056
	10 20 30 40 50 60 MKCVFVTVGT TSFDDLIACV SAPDSLQKIE SLGYNRLILQ IGRGTVVPEP FSTESFTLDV 70 80 90 100 110 120 YRYKDSLKED IQKADLVISH AGAGSCLETL EKGKPLVVVI NEKLMNNHQL ELAKQLHKEG 130 140 150 160 170 180 HLFYCTCRVL TCPGQAKSIA SAPGKCQDSA ALTSTAFSGL DFGLLSGYLH KQALVTATHP 190 200 210 220 230 240 TCTLLFPSCH AFFPLPLTPT LYKMHKGWKN YCSQKSLNEA SMDEYLGSLG LFRKLTAKDA 250 260 270 280 290 300 SCLFRAISEQ LFCSQVHHLE IRKACVSYMR ENQQTFESYV EGSFEKYLER LGDPKESAGQ 310 320 330 340 350 360 LEIRALSLIY NRDFILYRFP GKPPTYVTDN GYEDKILLCY SSSGHYDSVY SKQFQSSAAV 370 380 390 400 410 420 CQAVLYEILY KDVFVVDEEE LKTAIKLFRS GSKKNRNNAV TGSEDAHTDY KSSNQNRMEE 430 440 450 460 470 480 WGACYNAENI PEGYNKGTEE TKSPENPSKM PFPYKVLKAL DPEIYRNVEF DVWLDSRKEL 490 500 510 520 530 540 QKSDYMEYAG RQYYLGDKCQ VCLESEGRYY NAHIQEVGNE NNSVTVFIEE LAEKHVVPLA 550 560 570 580 590 600 NLKPVTQVMS VPAWNAMPSR KGRGYQKMPG GYVPEIVISE MDIKQQKKMF KKIRGKEVYM 610 620 630 640 650 660 TMAYGKGDPL LPPRLQHSMH YGHDPPMHYS QTAGNVMSNE HFHPQHPSPR QGRGYGMPRN 670 680 690 700 710 720 SSRFINRHNM PGPKVDFYPG PGKRCCQSYD NFSYRSRSFR RSHRQMSCVN KESQYGFTPG 730 740 750 760 770 780 NGQMPRGLEE TITFYEVEEG DETAYPTLPN HGGPSTMVPA TSGYCVGRRG HSSGKQTLNL 790 800 810 820 830 840 EEGNGQSENG RYHEEYLYRA EPDYETSGVY STTASTANLS LQDRKSCSMS PQDTVTSYNY 850 860 870 880 890 900 PQKMMGNIAA VAASCANNVP APVLSNGAAA NQAISTTSVS SQNAIQPLFV SPPTHGRPVI 910 920 930 940 950 960 ASPSYPCHSA IPHAGASLPP PPPPPPPPPP PPPPPPPPPP PPPPPALDVG ETSNLQPPPP 970 980 990 1000 1010 1020 LPPPPYSCDP SGSDLPQDTK VLQYYFNLGL QCYYHSYWHS MVYVPQMQQQ LHVENYPVYT 1030 1040 1050 1060 1070 1080 EPPLVDQTVP QCYSEVRRED GIQAEASAND TFPNADSSSV PHGAVYYPVM SDPYGQPPLP 1090 1100 1110 1120 1130 GFDSCLPVVP DYSCVPPWHP VGTAYGGSSQ IHGAINPGPI GCIAPSPPAS HYVPQGM
	Isoform 2 [UniParc]. Checksum: CEE3C8E7EFFE4E31	FASTA	165	18,225
	10 20 30 40 50 60 MKCVFVTVGT TSFDDLIACV SAPDSLQKIE SLGYNRLILQ IGRGTVVPEP FSTESFTLDV 70 80 90 100 110 120 YRYKDSLKED IQKADLVISH AGAGSCLETL EKGKPLVVVI NEKLMNNHQL ELAKQLHKEG 130 140 150 160 HLFYCTCSTL PGLLQSMDLS TLKCYPPGQP EKFSAFLDKV VGLQK
	Isoform 3 [UniParc]. Checksum: 2309259465BED07E	FASTA	1,059	117,468
	10 20 30 40 50 60 MFTGAGSCLE TLEKGKPLVV VINEKLMNNH QLELAKQLHK EGHLFYCTCR VLTCPGQAKS 70 80 90 100 110 120 IASAPGKCQD SAALTSTAFS GLDFGLLSGY LHKQALVTAT HPTCTLLFPS CHAFFPLPLT 130 140 150 160 170 180 PTLYKMHKGW KNYCSQKSLN EASMDEYLGS LGLFRKLTAK DASCLFRAIS EQLFCSQVHH 190 200 210 220 230 240 LEIRKACVSY MRENQQTFES YVEGSFEKYL ERLGDPKESA GQLEIRALSL IYNRDFILYR 250 260 270 280 290 300 FPGKPPTYVT DNGYEDKILL CYSSSGHYDS VYSKQFQSSA AVCQAVLYEI LYKDVFVVDE 310 320 330 340 350 360 EELKTAIKLF RSGSKKNRNN AVTGSEDAHT DYKSSNQNRM EEWGACYNAE NIPEGYNKGT 370 380 390 400 410 420 EETKSPENPS KMPFPYKVLK ALDPEIYRNV EFDVWLDSRK ELQKSDYMEY AGRQYYLGDK 430 440 450 460 470 480 CQVCLESEGR YYNAHIQEVG NENNSVTVFI EELAEKHVVP LANLKPVTQV MSVPAWNAMP 490 500 510 520 530 540 SRKGRGYQKM PGGYVPEIVI SEMDIKQQKK MFKKIRGKEV YMTMAYGKGD PLLPPRLQHS 550 560 570 580 590 600 MHYGHDPPMH YSQTAGNVMS NEHFHPQHPS PRQGRGYGMP RNSSRFINRH NMPGPKVDFY 610 620 630 640 650 660 PGPGKRCCQS YDNFSYRSRS FRRSHRQMSC VNKESQYGFT PGNGQMPRGL EETITFYEVE 670 680 690 700 710 720 EGDETAYPTL PNHGGPSTMV PATSGYCVGR RGHSSGKQTL NLEEGNGQSE NGRYHEEYLY 730 740 750 760 770 780 RAEPDYETSG VYSTTASTAN LSLQDRKSCS MSPQDTVTSY NYPQKMMGNI AAVAASCANN 790 800 810 820 830 840 VPAPVLSNGA AANQAISTTS VSSQNAIQPL FVSPPTHGRP VIASPSYPCH SAIPHAGASL 850 860 870 880 890 900 PPPPPPPPPP PPPPPPPPPP PPPPPPPALD VGETSNLQPP PPLPPPPYSC DPSGSDLPQD 910 920 930 940 950 960 TKVLQYYFNL GLQCYYHSYW HSMVYVPQMQ QQLHVENYPV YTEPPLVDQT VPQCYSEVRR 970 980 990 1000 1010 1020 EDGIQAEASA NDTFPNADSS SVPHGAVYYP VMSDPYGQPP LPGFDSCLPV VPDYSCVPPW 1030 1040 1050 HPVGTAYGGS SQIHGAINPG PIGCIAPSPP ASHYVPQGM
	Isoform 4 [UniParc]. Checksum: 5E581DED7B50EB86	FASTA	954	106,858
	10 20 30 40 50 60 MNNHQLELAK QLHKEGHLFY CTCRVLTCPG QAKSIASAPG KCQDSAALTS TAFSGLDFGL 70 80 90 100 110 120 LSGYLHKQAL VTATHPTCTL LFPSCHAFFP LPLTPTLYKM HKGWKNYCSQ KSLNEASMDE 130 140 150 160 170 180 YLGSLGLFRK LTAKDASCLF RAISEQLFCS QVHHLEIRKA CVSYMRENQQ TFESYVEGSF 190 200 210 220 230 240 EKYLERLGDP KESAGQLEIR ALSLIYNRDF ILYRFPGKPP TYVTDNGYED KILLCYSSSG 250 260 270 280 290 300 HYDSVYSKQF QSSAAVCQAV LYEILYKDVF VVDEEELKTA IKLFRSGSKK NRNNAVTGSE 310 320 330 340 350 360 DAHTDYKSSN QNRMEEWGAC YNAENIPEGY NKGTEETKSP ENPSKMPFPY KVLKALDPEI 370 380 390 400 410 420 YRNVEFDVWL DSRKELQKSD YMEYAGRQYY LGDKCQVCLE SEGRYYNAHI QEVGNENNSV 430 440 450 460 470 480 TVFIEELAEK HVVPLANLKP VTQVMSVPAW NAMPSRKGRG YQKMPGGYVP EIVISEMDIK 490 500 510 520 530 540 QQKKMFKKIR GKEVYMTMAY GKGDPLLPPR LQHSMHYGHD PPMHYSQTAG NVMSNEHFHP 550 560 570 580 590 600 QHPSPRQGRG YGMPRNSSRF INRHNMPGPK VDFYPGPGKR CCQSYDNFSY RSRSFRRSHR 610 620 630 640 650 660 QMSCVNKESQ YGFTPGNGQM PRGLEETITF YEVEEGDETA YPTLPNHGGP STMVPATSGY 670 680 690 700 710 720 CVGRRGHSSG KQTLNLEEGN GQSENGRYHE EYLYRAEPDY ETSGVYSTTA STANLSLQDR 730 740 750 760 770 780 KSCSMSPQDT VTSYNYPQKM MGNIAAVAAS CANNVPAPVL SNGAAANQAI STTSVSSQNA 790 800 810 820 830 840 IQPLFVSPPT HGRPDTKVLQ YYFNLGLQCY YHSYWHSMVY VPQMQQQLHV ENYPVYTEPP 850 860 870 880 890 900 LVDQTVPQCY SEVRREDGIQ AEASANDTFP NADSSSVPHG AVYYPVMSDP YGQPPLPGFD 910 920 930 940 950 SCLPVVPDYS CVPPWHPVGT AYGGSSQIHG AINPGPIGCI APSPPASHYV PQGM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients." Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Hematopoietic stem cell.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). Tissue: Lung, Placenta, Testis, Trachea and Uterus.
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 592-1137 (ISOFORM 4). Tissue: Colon and Urinary bladder.
[6]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 591-1137 (ISOFORM 4). Tissue: Lung.
[7]	"Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation." Gao X.-D., Tachikawa H., Sato T., Jigami Y., Dean N. J. Biol. Chem. 280:36254-36262(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"Gene identification in the congenital disorders of glycosylation type I by whole-exome sequencing." Timal S., Hoischen A., Lehle L., Adamowicz M., Huijben K., Sykut-Cegielska J., Paprocka J., Jamroz E., van Spronsen F.J., Korner C., Gilissen C., Rodenburg R.J., Eidhof I., Van den Heuvel L., Thiel C., Wevers R.A., Morava E., Veltman J., Lefeber D.J. Hum. Mol. Genet. 21:4151-4161(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CDG1S GLU-94.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF220051 mRNA. Translation: AAF67644.1. AK026671 mRNA. Translation: BAB15521.1. Different initiation. AK300394 mRNA. Translation: BAH13276.1. AK302729 mRNA. Translation: BAH13790.1. AK302890 mRNA. Translation: BAH13833.1. AK304712 mRNA. Translation: BAH14244.1. Sequence problems. AK316306 mRNA. Translation: BAH14677.1. AK316522 mRNA. Translation: BAH14893.1. AK312229 mRNA. Translation: BAG35162.1. AL096764 Genomic DNA. Translation: CAB89277.1. AL049563 Genomic DNA. Translation: CAI43016.2. Sequence problems. AL096764, AL049563 Genomic DNA. Translation: CAM28218.1. AL096764, AL049563 Genomic DNA. Translation: CAM28219.1. Sequence problems. AL049563, AL096764 Genomic DNA. Translation: CAM28289.1. CH471120 Genomic DNA. Translation: EAX02635.1. BC005336 mRNA. Translation: AAH05336.1. BC117377 mRNA. Translation: AAI17378.1. Different initiation. BC117379 mRNA. Translation: AAI17380.1. Different initiation. AK223154 mRNA. Translation: BAD96874.1. Different initiation.
IPI	IPI00020512. IPI00795917. IPI00963893. IPI00967654.
RefSeq	NP_001034299.3. NM_001039210.3. NP_001093392.1. NM_001099922.2. NP_001161857.1. NM_001168385.1. NP_001244159.1. NM_001257230.1. NP_001244160.1. NM_001257231.1. NP_001244163.1. NM_001257234.1. NP_001244166.1. NM_001257237.1. NP_001244170.1. NM_001257241.1. NP_060936.1. NM_018466.4.
UniGene	Hs.443061.
3D structure databases
ProteinModelPortal	Q9NP73.
SMR	Q9NP73. Positions 2-125, 230-349.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NP73. 3 interactions.
MINT	MINT-3071434.
STRING	9606.ENSP00000361047.
Protein family/group databases
CAZy	GT1. Glycosyltransferase Family 1.
MEROPS	C85.005.
PTM databases
PhosphoSite	Q9NP73.
Polymorphism databases
DMDM	298286785.
Proteomic databases
PaxDb	Q9NP73.
PeptideAtlas	Q9NP73.
PRIDE	Q9NP73.
Protocols and materials databases
DNASU	79868.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000251943; ENSP00000251943; ENSG00000101901. ENST00000371979; ENSP00000361047; ENSG00000101901. ENST00000394780; ENSP00000378260; ENSG00000101901. ENST00000436609; ENSP00000392990; ENSG00000101901.
GeneID	79868.
KEGG	hsa:79868.
UCSC	uc004epi.2. human. uc011msx.2. human. uc011msy.2. human. uc011msz.2. human.
Organism-specific databases
CTD	79868.
GeneCards	GC0XP110909.
HGNC	HGNC:30881. ALG13.
HPA	HPA002853.
MIM	300776. gene. 300884. phenotype.
neXtProt	NX_Q9NP73.
PharmGKB	PA162376235.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5017.
HOVERGEN	HBG081391.
KO	K07432.
OMA	SHLLYCT.
OrthoDB	EOG44J2H7.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	Q9NP73.
Bgee	Q9NP73.
CleanEx	HS_ALG13.
Genevestigator	Q9NP73.
GermOnline	ENSG00000072319. Homo sapiens.
Family and domain databases
InterPro	IPR007235. Glyco_trans_28_C. IPR003323. OTU. IPR002999. Tudor. [Graphical view]
Pfam	PF04101. Glyco_tran_28_C. 1 hit. PF02338. OTU. 1 hit. [Graphical view]
PROSITE	PS50802. OTU. 1 hit. PS50304. TUDOR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	79868.
NextBio	69622.
SOURCE	Search...

Entry information

Entry name

ALG13_HUMAN

Accession

Primary (citable) accession number: Q9NP73
Secondary accession number(s): B1AKD6 , B1AKM1, B2R5L5, B7Z6J0, B7Z804, B7Z847, B7Z9A8, B7ZAJ1, B7ZB57, Q17RC3, Q5JXY9, Q9H5U8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	June 15, 2010
Last modified:	May 1, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.