P20933 (ASPG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase
EC=3.5.1.26

Alternative name(s):
Aspartylglucosaminidase
Glycosylasparaginase
N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase

Cleaved into the following 2 chains:

1. Glycosylasparaginase alpha chain
2. Glycosylasparaginase beta chain

Gene names

Name:

AGA

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	346 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.
Catalytic activity	N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate. Ref.3 Ref.5
Subunit structure	Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers. Ref.14
Subcellular location	Lysosome.
Post-translational modification	Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.
Involvement in disease	Aspartylglucosaminuria (AGU) [MIM:208400]: An inborn lysosomal storage disease causing excess accumulation of glycoasparagine in the body tissues and its increased excretion in urine. Clinical features include mild to severe mental retardation manifesting from the age of two, coarse facial features and mild connective tissue abnormalities. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.5 Ref.6 Ref.16 Ref.17 Ref.18
Sequence similarities	Belongs to the Ntn-hydrolase family.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal
Molecular function	Hydrolase Protease
PTM	Autocatalytic cleavage Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein deglycosylation Inferred from direct assay Ref.12. Source: UniProtKB protein maturation Inferred from electronic annotation. Source: Compara proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.16. Source: UniProtKB lysosome Inferred from direct assay Ref.16. Source: UniProtKB
Molecular_function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Inferred from direct assay Ref.12. Source: UniProtKB peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.6

Chain

24 – 205

182

Glycosylasparaginase alpha chain

PRO_0000002333

Chain

206 – 346

141

Glycosylasparaginase beta chain

PRO_0000002334

Regions

Region

234 – 237

4

Substrate binding

Region

257 – 260

4

Substrate binding

Sites

Active site

206

1

Nucleophile Ref.14

Amino acid modifications

Modified residue

24

1

Blocked amino end (Ser)

Glycosylation

38

1

N-linked (GlcNAc...) Ref.1 Ref.12 Ref.14

Glycosylation

308

1

N-linked (GlcNAc...) Ref.14

Disulfide bond

64 ↔ 69

Ref.14

Disulfide bond

163 ↔ 179

Ref.14

Disulfide bond

286 ↔ 306

Ref.14

Disulfide bond

317 ↔ 345

Ref.14

Natural variations

Natural variant

12

1

V → L in AGU; uncertain pathological significance. Ref.18

VAR_015427

Natural variant

60

1

G → D in AGU.

VAR_005069

Natural variant

72

1

S → P in AGU; specifically prevents the proteolytic activation cleavage of AGA in the endoplasmic reticulum. Ref.16

VAR_005070

Natural variant

100

1

G → E in AGU. Ref.17

VAR_015428

Natural variant

101

1

A → V in AGU.

VAR_005071

Natural variant

135

1

F → S in AGU. Ref.17

VAR_015429

Natural variant

149

1

T → S. Ref.1 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.10 Ref.11
Corresponds to variant rs2228119 [ dbSNP | Ensembl ].

VAR_033533

Natural variant

161

1

R → Q in AGU. Ref.3 Ref.5 Ref.6

VAR_005072

Natural variant

163

1

C → S in AGU; most frequent mutation; abolishes autocatalytic cleavage and enzyme activity. Ref.3 Ref.5 Ref.6

VAR_005073

Natural variant

252

1

G → E in AGU. Ref.18

VAR_015430

Natural variant

252

1

G → R in AGU. Ref.18

VAR_015431

Natural variant

257

1

T → I in AGU. Ref.18

VAR_015432

Natural variant

302

1

G → R in AGU.

VAR_005074

Natural variant

306

1

C → R in AGU.

VAR_005075

Natural variant

322

1

T → I.
Corresponds to variant rs56849061 [ dbSNP | Ensembl ].

VAR_061026

Experimental info

Sequence conflict

21

1

V → A in AAB60655. Ref.4

Sequence conflict

21

1

V → A in CAA43958. Ref.4

Sequence conflict

25

1

S → C AA sequence Ref.6

Secondary structure

1

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346

Helix Strand Turn

Details...

Beta strand

28 – 35

8

Helix

37 – 48

12

Helix

53 – 67

15

Helix

69 – 71

3

Beta strand

72 – 77

6

Beta strand

87 – 93

7

Turn

94 – 96

3

Beta strand

99 – 105

7

Helix

111 – 121

11

Beta strand

125 – 128

4

Helix

129 – 138

10

Helix

149 – 160

12

Turn

175 – 177

3

Beta strand

207 – 212

6

Beta strand

218 – 224

7

Turn

241 – 243

3

Beta strand

244 – 248

5

Turn

249 – 251

3

Beta strand

252 – 258

7

Helix

260 – 263

4

Helix

264 – 266

3

Helix

268 – 277

10

Helix

282 – 296

15

Beta strand

302 – 308

7

Beta strand

313 – 318

6

Beta strand

325 – 331

7

Beta strand

339 – 344

6

Sequences

	Sequence		Length	Mass (Da)
	P20933 [UniParc]. Last modified February 9, 2010. Version 2. Checksum: 766F1690B5B62FFA	FASTA	346	37,208
	10 20 30 40 50 60 MARKSNLPVL LVPFLLCQAL VRCSSPLPLV VNTWPFKNAT EAAWRALASG GSALDAVESG 70 80 90 100 110 120 CAMCEREQCD GSVGFGGSPD ELGETTLDAM IMDGTTMDVG AVGDLRRIKN AIGVARKVLE 130 140 150 160 170 180 HTTHTLLVGE SATTFAQSMG FINEDLSTTA SQALHSDWLA RNCQPNYWRN VIPDPSKYCG 190 200 210 220 230 240 PYKPPGILKQ DIPIHKETED DRGHDTIGMV VIHKTGHIAA GTSTNGIKFK IHGRVGDSPI 250 260 270 280 290 300 PGAGAYADDT AGAAAATGNG DILMRFLPSY QAVEYMRRGE DPTIACQKVI SRIQKHFPEF 310 320 330 340 FGAVICANVT GSYGAACNKL STFTQFSFMV YNSEKNQPTE EKVDCI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase." Fisher K.J., Tollersrud O.-K., Aronson N.N. Jr. FEBS Lett. 269:440-444(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-149.
[2]	Erratum Fisher K.J., Tollersrud O.-K., Aronson N.N. Jr. FEBS Lett. 276:232-232(1990) [PubMed] [Europe PMC] [Abstract]
[3]	"Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease." Ikonen E., Baumann M., Groen K., Syvaenen A.-C., Enomaa N., Halila R., Aula P., Peltonen L. EMBO J. 10:51-58(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 206-235, ACTIVATION BY CLEAVAGE, CATALYTIC ACTIVITY, VARIANTS SER-149; AGU GLN-161 AND SER-163, CHARACTERIZATION OF VARIANT AGU SER-163. Tissue: Fetal liver.
[4]	"Genomic structure of human lysosomal glycosylasparaginase." Park H., Fisher K.J., Aronson N.N. Jr. FEBS Lett. 288:168-172(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-149.
[5]	"Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163-->Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits." Fisher K.J., Aronson N.N. Jr. J. Biol. Chem. 266:12105-12113(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], AUTOCATALYTIC CLEAVAGE, CATALYTIC ACTIVITY, VARIANTS SER-149; AGU GLN-161 AND SER-163.
[6]	"Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase." Mononen I., Heisterkamp N., Kaartinen V., Williams J.C., Yates J.R. III, Griffin P.R., Hood L.E., Groffen J. Proc. Natl. Acad. Sci. U.S.A. 88:2941-2945(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-45; 47-60; 67-84; 98-120; 123-190; 206-314 AND 320-343, VARIANTS AGU GLN-161 AND SER-163.
[7]	"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], VARIANT SER-149. Tissue: Urinary bladder.
[8]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-149.
[9]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	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], VARIANT SER-149.
[11]	"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], VARIANT SER-149. Tissue: Ovary.
[12]	"Purification and structure of human liver aspartylglucosaminidase." Rip J.W., Coulter-Mackie M.B., Rupar C.A., Gordon B.A. Biochem. J. 288:1005-1010(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-44 AND 206-231, GLYCOSYLATION AT ASN-38. Tissue: Liver.
[13]	"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].
[14]	"Three-dimensional structure of human lysosomal aspartylglucosaminidase." Oinonen C., Tikkanen R., Rouvinen J., Peltonen L. Nat. Struct. Biol. 2:1102-1108(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-185 IN COMPLEX WITH ASPARTIC ACID, SUBUNIT, ACTIVE SITE, GLYCOSYLATION AT ASN-38 AND ASN-308, DISULFIDE BONDS.
[15]	"Mutations causing aspartylglucosaminuria (AGU): a lysosomal accumulation disease." Ikonen E., Peltonen L. Hum. Mutat. 1:361-365(1992) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON AGU VARIANTS.
[16]	"Ser72-->Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation." Peltola M., Tikkanen R., Peltonen L., Jalanko A. Hum. Mol. Genet. 5:737-743(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AGU PRO-72.
[17]	"Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation." Laitinen A., Hietala M., Haworth J.C., Schroeder M.L., Seargeant L.E., Greenberg C.R., Aula P. Clin. Genet. 51:174-178(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AGU GLU-100 AND SER-135.
[18]	"Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations." Saarela J., Laine M., Oinonen C., Schantz C., Jalanko A., Rouvinen J., Peltonen L. Hum. Mol. Genet. 10:983-995(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AGU LEU-12; ARG-252; GLU-252 AND ILE-257.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X55762 mRNA. Translation: CAA39288.1.
X55330 mRNA. Translation: CAA39029.1.
U21281 , U21273, U21274, U21275, U21277, U21278, U21279, U21280 Genomic DNA. Translation: AAB60655.1.
X61959 Genomic DNA. Translation: CAA43958.1.
M64073 mRNA. Translation: AAA35903.1.
M64075 mRNA. Translation: AAA35904.1. Sequence problems.
M64076 mRNA. Translation: AAA35905.1. Sequence problems.
M60808 mRNA. Translation: AAA35901.1.
M60809 mRNA. Translation: AAA35902.1.
AK312982 mRNA. Translation: BAG35819.1.
CR541715 mRNA. Translation: CAG46516.1.
AC078881 Genomic DNA. Translation: AAY40915.1.
AC027627 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04714.1.
CH471056 Genomic DNA. Translation: EAX04715.1.
BC012392 mRNA. Translation: AAH12392.1.

IPI

IPI00026259.

PIR

MUHUGD. S11343.

RefSeq

NP_000018.2. NM_000027.3.
NP_001165459.1. NM_001171988.1.

UniGene

Hs.207776.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1APY	X-ray	2.00	A/C	24-185	[»]
			B/D	206-346	[»]
1APZ	X-ray	2.30	A/C	24-185	[»]
			B/D	206-346	[»]

ProteinModelPortal

P20933.

SMR

P20933. Positions 25-185, 206-346.

ModBase

Search...

Protein-protein interaction databases

IntAct

P20933. 2 interactions.

STRING

9606.ENSP00000264595.

Protein family/group databases

MEROPS

T02.001.

PTM databases

PhosphoSite

P20933.

Polymorphism databases

DMDM

288558804.

Proteomic databases

PaxDb

P20933.

PRIDE

P20933.

Protocols and materials databases

DNASU

175.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264595; ENSP00000264595; ENSG00000038002.

GeneID

175.

KEGG

hsa:175.

UCSC

uc003iuu.2. human.

Organism-specific databases

CTD

175.

GeneCards

GC04M178351.

H-InvDB

HIX0004652.

HGNC

HGNC:318. AGA.

HPA

HPA031415.
HPA031417.

MIM

208400. phenotype.
613228. gene.

neXtProt

NX_P20933.

Orphanet

93. Aspartylglucosaminuria.

PharmGKB

PA24615.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1446.

HOVERGEN

HBG004289.

InParanoid

P20933.

KO

K01444.

OMA

EQCDGSV.

OrthoDB

EOG4K6G4H.

PhylomeDB

P20933.

Enzyme and pathway databases

BRENDA

3.5.1.26. 2681.

SABIO-RK

P20933.

Gene expression databases

ArrayExpress

P20933.

Bgee

P20933.

CleanEx

HS_AGA.

Genevestigator

P20933.

GermOnline

ENSG00000038002. Homo sapiens.

Family and domain databases

InterPro

IPR000246. Peptidase_T2.
[Graphical view]

PANTHER

PTHR10188. PTHR10188. 1 hit.

Pfam

PF01112. Asparaginase_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P20933.

ChiTaRS

AGA. human.

EvolutionaryTrace

P20933.

GenomeRNAi

175.

NextBio

702.

PMAP-CutDB

P20933.

SOURCE

Search...

Entry information

Entry name

ASPG_HUMAN

Accession

Primary (citable) accession number: P20933
Secondary accession number(s): B2R7H2 , D3DP47, Q4W5Q2, Q6FHN6, Q9UCK6, Q9UCK7, Q9UCK8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 9, 2010
Last modified:	May 1, 2013
This is version 140 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.