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Q9NP73 (ALG13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13

EC=2.4.1.141
EC=3.4.19.12
Alternative name(s):
Asparagine-linked glycosylation 13 homolog
Glycosyltransferase 28 domain-containing protein 1
UDP-N-acetylglucosamine transferase subunit ALG13 homolog
Gene names
Name:ALG13
Synonyms:CXorf45, GLT28D1
ORF Names:MDS031
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1137 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 1:Possible multifunctional enzyme with both glycosyltransferase and deubiquitinase activities. Ref.7

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.

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

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.

Domain

Contains 1 OTU domain with intact active sites. No deubiquitinase activity has been detected when tested (Ref.8).

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.10

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11371137Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13
PRO_0000254573

Regions

Domain231 – 352122OTU
Domain492 – 55261Tudor
Region1 – 125125Glycosyltransferase activity
Region126 – 400275Deubiquitinase activity
Compositional bias887 – 97084Pro-rich

Sites

Active site2391For deubiquitinase activity By similarity
Active site2421Nucleophile; for deubiquitinase activity By similarity
Active site3451For deubiquitinase activity By similarity

Natural variations

Alternative sequence1 – 104104Missing in isoform 4.
VSP_039298
Alternative sequence1 – 7878Missing in isoform 3.
VSP_039299
Alternative sequence79 – 813SHA → MFT in isoform 3.
VSP_039300
Alternative sequence128 – 16538RVLTC…DFGLL → STLPGLLQSMDLSTLKCYPP GQPEKFSAFLDKVVGLQK in isoform 2.
VSP_039301
Alternative sequence166 – 1137972Missing in isoform 2.
VSP_039302
Alternative sequence899 – 97779Missing in isoform 4.
VSP_039303
Natural variant941K → E in CDG1S; there is a decrease enzyme activity at about 17% of wild-type. Ref.10
VAR_069218
Natural variant1071N → S. Ref.11
VAR_069412

Experimental info

Sequence conflict4931Y → N in BAH14677. Ref.1
Sequence conflict5641G → D in BAH13276. Ref.1
Sequence conflict5881K → R in BAH14677. Ref.1
Sequence conflict6241D → G in BAH13276. Ref.1
Sequence conflict6581P → L in BAH13790. Ref.1
Sequence conflict746 – 7483PTL → ATF in BAB15521. Ref.1
Sequence conflict7521G → E in BAB15521. Ref.1
Sequence conflict8661N → K in BAH14677. Ref.1
Sequence conflict9261P → L in BAH14244. Ref.1
Sequence conflict9541N → S in BAH14244. Ref.1
Sequence conflict10181V → A in BAH14244. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 15, 2010. Version 2.
Checksum: 4E56437BA2609589

FASTA1,137126,056
        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 

« Hide

Isoform 2 [UniParc].

Checksum: CEE3C8E7EFFE4E31
Show »

FASTA16518,225
Isoform 3 [UniParc].

Checksum: 2309259465BED07E
Show »

FASTA1,059117,468
Isoform 4 [UniParc].

Checksum: 5E581DED7B50EB86
Show »

FASTA954106,858

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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 (ISOFORM 2).
[8]"OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[9]"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].
[10]"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.
[11]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-107.

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.
RefSeqNP_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.
UniGeneHs.443061.

3D structure databases

ProteinModelPortalQ9NP73.
SMRQ9NP73. Positions 2-125, 230-349, 491-548.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122956. 6 interactions.
IntActQ9NP73. 5 interactions.
MINTMINT-2876406.
STRING9606.ENSP00000361047.

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.
MEROPSC85.005.

PTM databases

PhosphoSiteQ9NP73.

Polymorphism databases

DMDM298286785.

Proteomic databases

PaxDbQ9NP73.
PeptideAtlasQ9NP73.
PRIDEQ9NP73.

Protocols and materials databases

DNASU79868.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000251943; ENSP00000251943; ENSG00000101901. [Q9NP73-4]
ENST00000371979; ENSP00000361047; ENSG00000101901. [Q9NP73-2]
ENST00000394780; ENSP00000378260; ENSG00000101901. [Q9NP73-1]
GeneID79868.
KEGGhsa:79868.
UCSCuc004epi.2. human. [Q9NP73-2]
uc011msx.2. human. [Q9NP73-4]
uc011msy.2. human. [Q9NP73-1]
uc011msz.2. human. [Q9NP73-3]

Organism-specific databases

CTD79868.
GeneCardsGC0XP110909.
HGNCHGNC:30881. ALG13.
HPAHPA002853.
MIM300776. gene.
300884. phenotype.
neXtProtNX_Q9NP73.
Orphanet324422. ALG13-CDG.
PharmGKBPA162376235.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5017.
HOVERGENHBG081391.
KOK07432.
OMALLHNHQE.
OrthoDBEOG7RFTGJ.
PhylomeDBQ9NP73.
TreeFamTF332789.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9NP73.
BgeeQ9NP73.
CleanExHS_ALG13.
GenevestigatorQ9NP73.

Family and domain databases

InterProIPR007235. Glyco_trans_28_C.
IPR003323. OTU.
IPR002999. Tudor.
[Graphical view]
PfamPF04101. Glyco_tran_28_C. 1 hit.
PF02338. OTU. 1 hit.
[Graphical view]
PROSITEPS50802. OTU. 1 hit.
PS50304. TUDOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiALG13.
GenomeRNAi79868.
NextBio69622.
PROQ9NP73.
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Entry information

Entry nameALG13_HUMAN
AccessionPrimary (citable) accession number: Q9NP73
Secondary accession number(s): B1AKD6 expand/collapse secondary AC list , 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: April 16, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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