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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, CXorf45, GLT28D1, MDS031
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.1 Publication
Isoform 2: May be involved in protein N-glycosylation, second step of the dolichol-linked oligosaccharide pathway.1 Publication

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 activity By similarity
Active sitei242 – 2421Nucleophile; for deubiquitinase activity By similarity
Active sitei345 – 3451For deubiquitinase activity By similarity

GO - Molecular functioni

  1. N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity Source: UniProtKB-EC
  2. carbohydrate binding Source: InterPro
  3. cysteine-type peptidase activity Source: UniProtKB-KW
  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 Inferred
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 ALG13
PRO_0000254573Add
BLAST

Proteomic databases

MaxQBiQ9NP73.
PaxDbiQ9NP73.
PeptideAtlasiQ9NP73.
PRIDEiQ9NP73.

PTM databases

PhosphoSiteiQ9NP73.

Expressioni

Gene expression databases

ArrayExpressiQ9NP73.
BgeeiQ9NP73.
CleanExiHS_ALG13.
GenevestigatoriQ9NP73.

Organism-specific databases

HPAiHPA002853.

Interactioni

Subunit structurei

Isoform 2 may interact with ALG14 By similarity.

Protein-protein interaction databases

BioGridi122956. 6 interactions.
IntActiQ9NP73. 5 interactions.
MINTiMINT-2876406.
STRINGi9606.ENSP00000361047.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini231 – 352122OTU
Add
BLAST
Domaini492 – 55261Tudor
Add
BLAST

Region

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

Compositional bias

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

Domaini

Sequence similaritiesi

Contains 1 OTU domain.
Contains 1 Tudor domain.

Phylogenomic databases

eggNOGiCOG5017.
HOVERGENiHBG081391.
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

MKCVFVTVGT TSFDDLIACV SAPDSLQKIE SLGYNRLILQ IGRGTVVPEP     50
FSTESFTLDV YRYKDSLKED IQKADLVISH AGAGSCLETL EKGKPLVVVI 100
NEKLMNNHQL ELAKQLHKEG HLFYCTCRVL TCPGQAKSIA SAPGKCQDSA 150
ALTSTAFSGL DFGLLSGYLH KQALVTATHP TCTLLFPSCH AFFPLPLTPT 200
LYKMHKGWKN YCSQKSLNEA SMDEYLGSLG LFRKLTAKDA SCLFRAISEQ 250
LFCSQVHHLE IRKACVSYMR ENQQTFESYV EGSFEKYLER LGDPKESAGQ 300
LEIRALSLIY NRDFILYRFP GKPPTYVTDN GYEDKILLCY SSSGHYDSVY 350
SKQFQSSAAV CQAVLYEILY KDVFVVDEEE LKTAIKLFRS GSKKNRNNAV 400
TGSEDAHTDY KSSNQNRMEE WGACYNAENI PEGYNKGTEE TKSPENPSKM 450
PFPYKVLKAL DPEIYRNVEF DVWLDSRKEL QKSDYMEYAG RQYYLGDKCQ 500
VCLESEGRYY NAHIQEVGNE NNSVTVFIEE LAEKHVVPLA NLKPVTQVMS 550
VPAWNAMPSR KGRGYQKMPG GYVPEIVISE MDIKQQKKMF KKIRGKEVYM 600
TMAYGKGDPL LPPRLQHSMH YGHDPPMHYS QTAGNVMSNE HFHPQHPSPR 650
QGRGYGMPRN SSRFINRHNM PGPKVDFYPG PGKRCCQSYD NFSYRSRSFR 700
RSHRQMSCVN KESQYGFTPG NGQMPRGLEE TITFYEVEEG DETAYPTLPN 750
HGGPSTMVPA TSGYCVGRRG HSSGKQTLNL EEGNGQSENG RYHEEYLYRA 800
EPDYETSGVY STTASTANLS LQDRKSCSMS PQDTVTSYNY PQKMMGNIAA 850
VAASCANNVP APVLSNGAAA NQAISTTSVS SQNAIQPLFV SPPTHGRPVI 900
ASPSYPCHSA IPHAGASLPP PPPPPPPPPP PPPPPPPPPP PPPPPALDVG 950
ETSNLQPPPP LPPPPYSCDP SGSDLPQDTK VLQYYFNLGL QCYYHSYWHS 1000
MVYVPQMQQQ LHVENYPVYT EPPLVDQTVP QCYSEVRRED GIQAEASAND 1050
TFPNADSSSV PHGAVYYPVM SDPYGQPPLP GFDSCLPVVP DYSCVPPWHP 1100
VGTAYGGSSQ IHGAINPGPI GCIAPSPPAS HYVPQGM 1137
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.

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.
VSP_039298Add
BLAST
Alternative sequencei1 – 7878Missing in isoform 3.
VSP_039299Add
BLAST
Alternative sequencei79 – 813SHA → MFT in isoform 3.
VSP_039300
Alternative sequencei128 – 16538RVLTC…DFGLL → STLPGLLQSMDLSTLKCYPP GQPEKFSAFLDKVVGLQK in isoform 2.
VSP_039301Add
BLAST
Alternative sequencei166 – 1137972Missing in isoform 2.
VSP_039302Add
BLAST
Alternative sequencei899 – 97779Missing in isoform 4.
VSP_039303Add
BLAST

Sequence conflict

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

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]
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]
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 ]
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. 6 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 ]
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.
HOVERGENi HBG081391.
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

ArrayExpressi Q9NP73.
Bgeei Q9NP73.
CleanExi HS_ALG13.
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: September 3, 2014
This is version 112 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

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