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Q9NP73

- ALG13_HUMAN

UniProt

Q9NP73 - ALG13_HUMAN

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Protein

Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13

Gene

ALG13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Isoform 1: Possible multifunctional enzyme with both glycosyltransferase and deubiquitinase activities.
Isoform 2: May be involved in protein N-glycosylation, second step of the dolichol-linked oligosaccharide pathway.

Catalytic activityi

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei239 – 2391For deubiquitinase activityBy similarity
Active sitei242 – 2421Nucleophile; for deubiquitinase activityBy similarity
Active sitei345 – 3451For deubiquitinase activityBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. cysteine-type peptidase activity Source: UniProtKB-KW
  3. N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity Source: UniProtKB-EC
  4. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  3. lipid glycosylation Source: InterPro
  4. post-translational protein modification Source: Reactome
  5. protein N-linked glycosylation via asparagine Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Hydrolase, Protease, Thiol protease, Transferase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.
MEROPSiC85.005.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ALG13
Synonyms:CXorf45, GLT28D1
ORF Names:MDS031
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:30881. ALG13.

Subcellular locationi

Isoform 2 : Endoplasmic reticulum Curated
Note: Could be recruited to the cytosolic face of the endoplasmic reticulum membrane through its interaction with ALG14.

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941K → E in CDG1S; there is a decrease enzyme activity at about 17% of wild-type. 1 Publication
VAR_069218

Keywords - Diseasei

Congenital disorder of glycosylation, Disease mutation

Organism-specific databases

MIMi300884. phenotype.
Orphaneti324422. ALG13-CDG.
777. X-linked non-syndromic intellectual disability.
PharmGKBiPA162376235.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11371137Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13PRO_0000254573Add
BLAST

Proteomic databases

MaxQBiQ9NP73.
PaxDbiQ9NP73.
PeptideAtlasiQ9NP73.
PRIDEiQ9NP73.

PTM databases

PhosphoSiteiQ9NP73.

Expressioni

Gene expression databases

BgeeiQ9NP73.
CleanExiHS_ALG13.
ExpressionAtlasiQ9NP73. baseline and differential.
GenevestigatoriQ9NP73.

Organism-specific databases

HPAiHPA002853.

Interactioni

Subunit structurei

Isoform 2 may interact with ALG14.By similarity

Protein-protein interaction databases

BioGridi122956. 9 interactions.
IntActiQ9NP73. 5 interactions.
MINTiMINT-2876406.
STRINGi9606.ENSP00000361047.

Structurei

3D structure databases

ProteinModelPortaliQ9NP73.
SMRiQ9NP73. Positions 2-125, 230-349.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini231 – 352122OTUPROSITE-ProRule annotationAdd
BLAST
Domaini492 – 55261TudorPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 125125Glycosyltransferase activityAdd
BLAST
Regioni126 – 400275Deubiquitinase activityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi887 – 97084Pro-richAdd
BLAST

Domaini

Contains 1 OTU domain with intact active sites. No deubiquitinase activity has been detected when tested (PubMed:23827681).1 Publication

Sequence similaritiesi

Belongs to the glycosyltransferase 28 family.Curated
Contains 1 OTU domain.PROSITE-ProRule annotation
Contains 1 Tudor domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5017.
GeneTreeiENSGT00530000063508.
HOVERGENiHBG081391.
InParanoidiQ9NP73.
KOiK07432.
OMAiVPFPQFD.
OrthoDBiEOG7RFTGJ.
PhylomeDBiQ9NP73.
TreeFamiTF332789.

Family and domain databases

InterProiIPR007235. Glyco_trans_28_C.
IPR003323. OTU.
IPR002999. Tudor.
[Graphical view]
PfamiPF04101. Glyco_tran_28_C. 1 hit.
PF02338. OTU. 1 hit.
[Graphical view]
PROSITEiPS50802. OTU. 1 hit.
PS50304. TUDOR. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NP73-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MKCVFVTVGT TSFDDLIACV SAPDSLQKIE SLGYNRLILQ IGRGTVVPEP
60 70 80 90 100
FSTESFTLDV YRYKDSLKED IQKADLVISH AGAGSCLETL EKGKPLVVVI
110 120 130 140 150
NEKLMNNHQL ELAKQLHKEG HLFYCTCRVL TCPGQAKSIA SAPGKCQDSA
160 170 180 190 200
ALTSTAFSGL DFGLLSGYLH KQALVTATHP TCTLLFPSCH AFFPLPLTPT
210 220 230 240 250
LYKMHKGWKN YCSQKSLNEA SMDEYLGSLG LFRKLTAKDA SCLFRAISEQ
260 270 280 290 300
LFCSQVHHLE IRKACVSYMR ENQQTFESYV EGSFEKYLER LGDPKESAGQ
310 320 330 340 350
LEIRALSLIY NRDFILYRFP GKPPTYVTDN GYEDKILLCY SSSGHYDSVY
360 370 380 390 400
SKQFQSSAAV CQAVLYEILY KDVFVVDEEE LKTAIKLFRS GSKKNRNNAV
410 420 430 440 450
TGSEDAHTDY KSSNQNRMEE WGACYNAENI PEGYNKGTEE TKSPENPSKM
460 470 480 490 500
PFPYKVLKAL DPEIYRNVEF DVWLDSRKEL QKSDYMEYAG RQYYLGDKCQ
510 520 530 540 550
VCLESEGRYY NAHIQEVGNE NNSVTVFIEE LAEKHVVPLA NLKPVTQVMS
560 570 580 590 600
VPAWNAMPSR KGRGYQKMPG GYVPEIVISE MDIKQQKKMF KKIRGKEVYM
610 620 630 640 650
TMAYGKGDPL LPPRLQHSMH YGHDPPMHYS QTAGNVMSNE HFHPQHPSPR
660 670 680 690 700
QGRGYGMPRN SSRFINRHNM PGPKVDFYPG PGKRCCQSYD NFSYRSRSFR
710 720 730 740 750
RSHRQMSCVN KESQYGFTPG NGQMPRGLEE TITFYEVEEG DETAYPTLPN
760 770 780 790 800
HGGPSTMVPA TSGYCVGRRG HSSGKQTLNL EEGNGQSENG RYHEEYLYRA
810 820 830 840 850
EPDYETSGVY STTASTANLS LQDRKSCSMS PQDTVTSYNY PQKMMGNIAA
860 870 880 890 900
VAASCANNVP APVLSNGAAA NQAISTTSVS SQNAIQPLFV SPPTHGRPVI
910 920 930 940 950
ASPSYPCHSA IPHAGASLPP PPPPPPPPPP PPPPPPPPPP PPPPPALDVG
960 970 980 990 1000
ETSNLQPPPP LPPPPYSCDP SGSDLPQDTK VLQYYFNLGL QCYYHSYWHS
1010 1020 1030 1040 1050
MVYVPQMQQQ LHVENYPVYT EPPLVDQTVP QCYSEVRRED GIQAEASAND
1060 1070 1080 1090 1100
TFPNADSSSV PHGAVYYPVM SDPYGQPPLP GFDSCLPVVP DYSCVPPWHP
1110 1120 1130
VGTAYGGSSQ IHGAINPGPI GCIAPSPPAS HYVPQGM
Length:1,137
Mass (Da):126,056
Last modified:June 15, 2010 - v2
Checksum:i4E56437BA2609589
GO
Isoform 2 (identifier: Q9NP73-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:165
Mass (Da):18,225
Checksum:iCEE3C8E7EFFE4E31
GO
Isoform 3 (identifier: Q9NP73-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:1,059
Mass (Da):117,468
Checksum:i2309259465BED07E
GO
Isoform 4 (identifier: Q9NP73-4) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:954
Mass (Da):106,858
Checksum:i5E581DED7B50EB86
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti493 – 4931Y → N in BAH14677. 1 PublicationCurated
Sequence conflicti564 – 5641G → D in BAH13276. 1 PublicationCurated
Sequence conflicti588 – 5881K → R in BAH14677. 1 PublicationCurated
Sequence conflicti624 – 6241D → G in BAH13276. 1 PublicationCurated
Sequence conflicti658 – 6581P → L in BAH13790. 1 PublicationCurated
Sequence conflicti746 – 7483PTL → ATF in BAB15521. 1 PublicationCurated
Sequence conflicti752 – 7521G → E in BAB15521. 1 PublicationCurated
Sequence conflicti866 – 8661N → K in BAH14677. 1 PublicationCurated
Sequence conflicti926 – 9261P → L in BAH14244. 1 PublicationCurated
Sequence conflicti954 – 9541N → S in BAH14244. 1 PublicationCurated
Sequence conflicti1018 – 10181V → A in BAH14244. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941K → E in CDG1S; there is a decrease enzyme activity at about 17% of wild-type. 1 Publication
VAR_069218
Natural varianti107 – 1071N → S.1 Publication
VAR_069412

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 104104Missing in isoform 4. 3 PublicationsVSP_039298Add
BLAST
Alternative sequencei1 – 7878Missing in isoform 3. 1 PublicationVSP_039299Add
BLAST
Alternative sequencei79 – 813SHA → MFT in isoform 3. 1 PublicationVSP_039300
Alternative sequencei128 – 16538RVLTC…DFGLL → STLPGLLQSMDLSTLKCYPP GQPEKFSAFLDKVVGLQK in isoform 2. 3 PublicationsVSP_039301Add
BLAST
Alternative sequencei166 – 1137972Missing in isoform 2. 3 PublicationsVSP_039302Add
BLAST
Alternative sequencei899 – 97779Missing in isoform 4. 3 PublicationsVSP_039303Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14559.1. [Q9NP73-2]
CCDS55477.1. [Q9NP73-1]
CCDS59173.1. [Q9NP73-4]
CCDS76012.1. [Q9NP73-3]
RefSeqiNP_001034299.3. NM_001039210.3.
NP_001093392.1. NM_001099922.2. [Q9NP73-1]
NP_001161857.1. NM_001168385.1.
NP_001244159.1. NM_001257230.1. [Q9NP73-4]
NP_001244160.1. NM_001257231.1. [Q9NP73-3]
NP_001244163.1. NM_001257234.1. [Q9NP73-4]
NP_001244166.1. NM_001257237.1. [Q9NP73-4]
NP_001244170.1. NM_001257241.1.
NP_060936.1. NM_018466.4. [Q9NP73-2]
UniGeneiHs.443061.

Genome annotation databases

EnsembliENST00000251943; ENSP00000251943; ENSG00000101901. [Q9NP73-4]
ENST00000371979; ENSP00000361047; ENSG00000101901. [Q9NP73-2]
ENST00000394780; ENSP00000378260; ENSG00000101901. [Q9NP73-1]
ENST00000610588; ENSP00000479731; ENSG00000101901. [Q9NP73-3]
ENST00000621367; ENSP00000481509; ENSG00000101901. [Q9NP73-4]
GeneIDi79868.
KEGGihsa:79868.
UCSCiuc004epi.2. human. [Q9NP73-2]
uc011msx.2. human. [Q9NP73-4]
uc011msy.2. human. [Q9NP73-1]
uc011msz.2. human. [Q9NP73-3]

Polymorphism databases

DMDMi298286785.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS14559.1. [Q9NP73-2 ]
CCDS55477.1. [Q9NP73-1 ]
CCDS59173.1. [Q9NP73-4 ]
CCDS76012.1. [Q9NP73-3 ]
RefSeqi NP_001034299.3. NM_001039210.3.
NP_001093392.1. NM_001099922.2. [Q9NP73-1 ]
NP_001161857.1. NM_001168385.1.
NP_001244159.1. NM_001257230.1. [Q9NP73-4 ]
NP_001244160.1. NM_001257231.1. [Q9NP73-3 ]
NP_001244163.1. NM_001257234.1. [Q9NP73-4 ]
NP_001244166.1. NM_001257237.1. [Q9NP73-4 ]
NP_001244170.1. NM_001257241.1.
NP_060936.1. NM_018466.4. [Q9NP73-2 ]
UniGenei Hs.443061.

3D structure databases

ProteinModelPortali Q9NP73.
SMRi Q9NP73. Positions 2-125, 230-349.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122956. 9 interactions.
IntActi Q9NP73. 5 interactions.
MINTi MINT-2876406.
STRINGi 9606.ENSP00000361047.

Protein family/group databases

CAZyi GT1. Glycosyltransferase Family 1.
MEROPSi C85.005.

PTM databases

PhosphoSitei Q9NP73.

Polymorphism databases

DMDMi 298286785.

Proteomic databases

MaxQBi Q9NP73.
PaxDbi Q9NP73.
PeptideAtlasi Q9NP73.
PRIDEi Q9NP73.

Protocols and materials databases

DNASUi 79868.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000251943 ; ENSP00000251943 ; ENSG00000101901 . [Q9NP73-4 ]
ENST00000371979 ; ENSP00000361047 ; ENSG00000101901 . [Q9NP73-2 ]
ENST00000394780 ; ENSP00000378260 ; ENSG00000101901 . [Q9NP73-1 ]
ENST00000610588 ; ENSP00000479731 ; ENSG00000101901 . [Q9NP73-3 ]
ENST00000621367 ; ENSP00000481509 ; ENSG00000101901 . [Q9NP73-4 ]
GeneIDi 79868.
KEGGi hsa:79868.
UCSCi uc004epi.2. human. [Q9NP73-2 ]
uc011msx.2. human. [Q9NP73-4 ]
uc011msy.2. human. [Q9NP73-1 ]
uc011msz.2. human. [Q9NP73-3 ]

Organism-specific databases

CTDi 79868.
GeneCardsi GC0XP110909.
GeneReviewsi ALG13.
HGNCi HGNC:30881. ALG13.
HPAi HPA002853.
MIMi 300776. gene.
300884. phenotype.
neXtProti NX_Q9NP73.
Orphaneti 324422. ALG13-CDG.
777. X-linked non-syndromic intellectual disability.
PharmGKBi PA162376235.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5017.
GeneTreei ENSGT00530000063508.
HOVERGENi HBG081391.
InParanoidi Q9NP73.
KOi K07432.
OMAi VPFPQFD.
OrthoDBi EOG7RFTGJ.
PhylomeDBi Q9NP73.
TreeFami TF332789.

Enzyme and pathway databases

Reactomei REACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

GeneWikii ALG13.
GenomeRNAii 79868.
NextBioi 69622.
PROi Q9NP73.
SOURCEi Search...

Gene expression databases

Bgeei Q9NP73.
CleanExi HS_ALG13.
ExpressionAtlasi Q9NP73. baseline and differential.
Genevestigatori Q9NP73.

Family and domain databases

InterProi IPR007235. Glyco_trans_28_C.
IPR003323. OTU.
IPR002999. Tudor.
[Graphical view ]
Pfami PF04101. Glyco_tran_28_C. 1 hit.
PF02338. OTU. 1 hit.
[Graphical view ]
PROSITEi PS50802. OTU. 1 hit.
PS50304. TUDOR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: VARIANT CDG1S GLU-94.
  11. Cited for: VARIANT SER-107.

Entry informationi

Entry nameiALG13_HUMAN
AccessioniPrimary (citable) accession number: Q9NP73
Secondary accession number(s): B1AKD6
, B1AKM1, B2R5L5, B7Z6J0, B7Z804, B7Z847, B7Z9A8, B7ZAJ1, B7ZB57, Q17RC3, Q5JXY9, Q9H5U8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 15, 2010
Last modified: October 29, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3