Reviewed, UniProtKB/Swiss-Prot P30566 (PUR8_HUMAN)

Names and origin

Protein names

Recommended name:
    Adenylosuccinate lyase
      Short name=ASL
    EC=4.3.2.2
Alternative name(s):
    Adenylosuccinase
      Short name=ASase

Gene names

Name:	ADSL
Synonyms:	AMPS

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	484 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)

Catalytic activity	N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2. Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
Tissue specificity	Ubiquitously expressed. Both isoforms are produced by all tissues.
Involvement in disease	Defects in ADSL are the cause of adenylosuccinase deficiency (ADSL deficiency) [MIM:103050]. ADSL deficiency is an autosomal recessive disorder characterized by the accumulation in the body fluids of succinylaminoimidazole-carboxamide riboside (SAICA-riboside) and succinyladenosine (S-Ado). Most children display marked psychomotor delay, often accompanied by epilepsy or autistic features, or both, although some patients may be less profoundly retarded. Occasionally, growth retardation and muscular wasting are also present.
Sequence similarities	Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.

Ontologies

Keywords
Biological process	Purine biosynthesis
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Epilepsy
Molecular function	Lyase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from Experiment. Source: Reactome AMP biosynthetic process Inferred from direct assay. Source: UniProtKB protein tetramerization Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Inferred from electronic annotation. Source: EC N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P30566-1)

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: P30566-2)

Also known as: Delta-ADSL;

The sequence of this isoform differs from the canonical sequence as follows:
     398-456: Missing.

Note: No enzymatic activity. 10-fold less abundant than isoform 1.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 484

483

Adenylosuccinate lyase

PRO_0000137892

Sites

Active site

86

1

Proton donor By similarity

Active site

159

1

Proton acceptor By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7

Modified residue

9

1

Phosphoserine Ref.9

Modified residue

147

1

N6-acetyllysine Ref.12

Modified residue

295

1

N6-acetyllysine Ref.12

Natural variations

Alternative sequence

398 – 456

59

Missing in isoform 2.

VSP_000318

Natural variant

2

1

A → V in ADSL deficiency; severe. Ref.16

VAR_016930

Natural variant

3

1

A → V in ADSL deficiency; severe. Ref.2

VAR_017078

Natural variant

26

1

M → L in ADSL deficiency; severe. Ref.16

VAR_016931

Natural variant

31

1

S → N: dbSNP rs5757921.

VAR_037883

Natural variant

72

1

I → V in ADSL deficiency; severe. Ref.15

VAR_007972

Natural variant

100

1

P → A in ADSL deficiency; moderate. Ref.14

VAR_017079

Natural variant

114

1

Y → H in ADSL deficiency; severe. Total loss of activity. Ref.2

VAR_017080

Natural variant

141

1

R → W in ADSL deficiency; severe. Ref.16 Ref.15

VAR_007973

Natural variant

147

1

K → M: dbSNP rs11089991.

VAR_037884

Natural variant

190

1

R → Q in ADSL deficiency; moderate. dbSNP rs28941471.

VAR_007974

Natural variant

194

1

R → C in ADSL deficiency; severe. Ref.2

VAR_017081

Natural variant

246

1

K → E in ADSL deficiency; moderate. Ref.15

VAR_007975

Natural variant

268

1

D → N in ADSL deficiency; severe. Total loss of activity. Ref.2

VAR_017082

Natural variant

303

1

R → C in ADSL deficiency; mild. Ref.16 Ref.15

VAR_007976

Natural variant

311

1

L → V in ADSL deficiency; severe. Ref.17

VAR_017083

Natural variant

318

1

P → L in ADSL deficiency; severe.

VAR_017084

Natural variant

364

1

V → M in ADSL deficiency; severe. Ref.17

VAR_017085

Natural variant

374

1

R → W in ADSL deficiency; severe.

VAR_017086

Natural variant

395

1

S → R in ADSL deficiency; severe. Ref.16 Ref.15

VAR_007977

Natural variant

396

1

R → C in ADSL deficiency; severe.

VAR_017087

Natural variant

396

1

R → H in ADSL deficiency; severe. Ref.17

VAR_017088

Natural variant

422

1

D → Y in ADSL deficiency; moderate. Ref.14

VAR_017089

Natural variant

423

1

L → V in ADSL deficiency; moderate.

VAR_017090

Natural variant

426

1

R → H in ADSL deficiency; severe. Most frequent mutation. Ref.16 Ref.2 Ref.15 Ref.13 Ref.18

VAR_007978

Natural variant

430

1

D → N in ADSL deficiency; mild. Ref.2

VAR_017091

Natural variant

438

1

S → P in ADSL deficiency; severe. Ref.7

VAR_000680

Natural variant

447

1

S → P in ADSL deficiency; severe.

VAR_017092

Natural variant

450

1

T → S in ADSL deficiency; moderate. Ref.16

VAR_016932

Natural variant

452

1

R → P in ADSL deficiency; severe. Ref.17

VAR_017093

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

484

Helix Strand Turn

Details...

Helix

16 – 19

4

Helix

24 – 29

6

Helix

32 – 53

22

Helix

59 – 66

8

Helix

74 – 84

11

Helix

87 – 98

12

Turn

100 – 102

3

Helix

103 – 105

3

Turn

106 – 109

4

Helix

113 – 148

36

Turn

149 – 151

3

Beta strand

153 – 158

6

Beta strand

161 – 167

7

Helix

168 – 192

25

Helix

206 – 211

6

Turn

212 – 214

3

Helix

216 – 229

14

Beta strand

240 – 242

3

Helix

246 – 274

29

Beta strand

277 – 279

3

Helix

299 – 313

15

Helix

316 – 323

8

Helix

331 – 333

3

Helix

334 – 360

27

Helix

366 – 380

15

Helix

382 – 389

8

Helix

396 – 416

21

Helix

423 – 429

7

Helix

431 – 433

3

Helix

434 – 437

4

Helix

440 – 443

4

Helix

446 – 449

4

Helix

453 – 463

11

Helix

465 – 469

5

Helix

470 – 472

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 7AA3A0A2C681FD94	FASTA	484	54,889
	10 20 30 40 50 60 MAAGGDHGSP DSYRSPLASR YASPEMCFVF SDRYKFRTWR QLWLWLAEAE QTLGLPITDE 70 80 90 100 110 120 QIQEMKSNLE NIDFKMAAEE EKRLRHDVMA HVHTFGHCCP KAAGIIHLGA TSCYVGDNTD 130 140 150 160 170 180 LIILRNALDL LLPKLARVIS RLADFAKERA SLPTLGFTHF QPAQLTTVGK RCCLWIQDLC 190 200 210 220 230 240 MDLQNLKRVR DDLRFRGVKG TTGTQASFLQ LFEGDDHKVE QLDKMVTEKA GFKRAFIITG 250 260 270 280 290 300 QTYTRKVDIE VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR 310 320 330 340 350 360 SERCCSLARH LMTLVMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT ILNTLQNISE 370 380 390 400 410 420 GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQDCH EKIRVLSQQA ASVVKQEGGD 430 440 450 460 470 480 NDLIERIQVD AYFSPIHSQL DHLLDPSSFT GRASQQVQRF LEEEVYPLLK PYESVMKVKA ELCL
	Isoform 2 (Delta-ADSL). Checksum: 66356963E46FDA3D	FASTA	425	48,328
	10 20 30 40 50 60 MAAGGDHGSP DSYRSPLASR YASPEMCFVF SDRYKFRTWR QLWLWLAEAE QTLGLPITDE 70 80 90 100 110 120 QIQEMKSNLE NIDFKMAAEE EKRLRHDVMA HVHTFGHCCP KAAGIIHLGA TSCYVGDNTD 130 140 150 160 170 180 LIILRNALDL LLPKLARVIS RLADFAKERA SLPTLGFTHF QPAQLTTVGK RCCLWIQDLC 190 200 210 220 230 240 MDLQNLKRVR DDLRFRGVKG TTGTQASFLQ LFEGDDHKVE QLDKMVTEKA GFKRAFIITG 250 260 270 280 290 300 QTYTRKVDIE VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR 310 320 330 340 350 360 SERCCSLARH LMTLVMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT ILNTLQNISE 370 380 390 400 410 420 GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQVQR FLEEEVYPLL KPYESVMKVK AELCL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mapping of the human adenylosuccinate lyase (ADSL) gene to chromosome 22q13.1-->q13.2." Fon E.A., Demczuk S., Delattre O., Thomas G., Rouleau G.A. Cytogenet. Cell Genet. 64:201-203(1993) [PubMed: 8404037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Human adenylosuccinate lyase (ADSL), cloning and characterization of full-length cDNA and its isoform, gene structure and molecular basis for ADSL deficiency in six patients." Kmoch S., Hartmannova H., Stiburkova B., Krijt J., Zikanova M., Sebesta I. Hum. Mol. Genet. 9:1501-1513(2000) [PubMed: 10888601] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS ADSL DEFICIENCY VAL-3; HIS-114; GLN-190; CYS-194; ASN-268; HIS-426 AND ASN-430. Tissue: Skeletal muscle.
[3]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Eye.
[7]	"A mutation in adenylosuccinate lyase associated with mental retardation and autistic features." Stone R.L., Aimi J., Barshop B.A., Jaeken J., van den Berghe G., Zalkin H., Dixon J.E. Nat. Genet. 1:59-63(1992) [PubMed: 1302001] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-484 (ISOFORM 1), VARIANT ADSL DEFICIENCY PRO-438.
[8]	Bienvenut W.V., Ramsay A., Leung H.Y. Submitted (JUN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-20 AND 235-245, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] ATSER-9, MASS SPECTROMETRY.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147 AND LYS-295, MASS SPECTROMETRY.
[13]	"Adenylosuccinase deficiency presenting with epilepsy in early infancy." Maaswinkel-Mooij P.D., Laan L.A.E.M., Onkenhout W., Brouwer O.F., Jaeken J., Poorthuis B.J.H.M. J. Inherit. Metab. Dis. 20:606-607(1997) [PubMed: 9266401] [Abstract] Cited for: VARIANT ADSL DEFICIENCY HIS-426.
[14]	"Identification of new mutations in the adenylosuccinate lyase gene associated with impaired enzyme activity in lymphocytes and red blood cells." Verginelli D., Luckow B., Crifo C., Salerno C., Gross M. Biochim. Biophys. Acta 1406:81-84(1998) [PubMed: 9545543] [Abstract] Cited for: VARIANTS ADSL DEFICIENCY ALA-100 AND TYR-422.
[15]	"Mutation analysis in adenylosuccinate lyase deficiency: eight novel mutations in the re-evaluated full ADSL coding sequence." Marie S., Cuppens H., Heuterspreute M., Jaspers M., Tola E.Z., Gu X.X., Legius E., Vincent M.-F., Jaeken J., Cassiman J.-J., van den Berghe G. Hum. Mutat. 13:197-202(1999) [PubMed: 10090474] [Abstract] Cited for: VARIANTS ADSL DEFICIENCY VAL-72; TRP-141; GLN-190; GLU-246; CYS-303; ARG-395 AND HIS-426.
[16]	"Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency." Race V., Marie S., Vincent M.-F., Van den Berghe G. Hum. Mol. Genet. 9:2159-2165(2000) [PubMed: 10958654] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS ADSL DEFICIENCY VAL-2; LEU-26; TRP-141; CYS-303; ARG-395; HIS-426 AND SER-450.
[17]	"Screening for adenylosuccinate lyase deficiency: clinical, biochemical and molecular findings in four patients." Castro M., Perez-Cerda C., Merinero B., Garcia M.J., Bernar J., Gil Nagel A., Torres J., Bermudez M., Garavito P., Marie S., Vincent F., Van den Berghe G., Ugarte M. Neuropediatrics 33:186-189(2002) [PubMed: 12368987] [Abstract] Cited for: VARIANTS ADSL DEFICIENCY VAL-311; MET-364; HIS-396 AND PRO-452.
[18]	"Intrafamilial variability in the phenotypic expression of adenylosuccinate lyase deficiency: a report on three patients." Edery P., Chabrier S., Ceballos-Picot I., Marie S., Vincent M.-F., Tardieu M. Am. J. Med. Genet. A 120:185-190(2003) [PubMed: 12833398] [Abstract] Cited for: VARIANT ADSL DEFICIENCY HIS-426.
+	Additional computationally mapped references.

Web resources

ADSLdb

Adenylosuccinate lyase mutations database

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

X65867 mRNA. Translation: CAA46696.1.
X65867 mRNA. Translation: CAA46697.1. Different initiation.
AF067853 mRNA. Translation: AAC21560.1.
AF067854 mRNA. Translation: AAC21561.1.
CR456368 mRNA. Translation: CAG30254.1.
AL022238 Genomic DNA. Translation: CAI18983.1.
AL022238 Genomic DNA. Translation: CAQ08930.1.
CH471095 Genomic DNA. Translation: EAW60375.1.
BC000253 mRNA. Translation: AAH00253.1.
S60710 mRNA. Translation: AAC60603.1. Different initiation.

IPI

IPI00220887.
IPI00942092.

RefSeq

NP_000017.1.
NP_001116850.1.

UniGene

Hs.75527

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J91	X-ray	1.80	A/B/C/D	1-481	[»]
2VD6	X-ray	2.00	A/B/C/D	1-481	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P30566.

PTM databases

PhosphoSite

P30566.

Proteomic databases

PeptideAtlas

P30566.

PRIDE

P30566.

Genome annotation databases

Ensembl

ENST00000216194; ENSP00000216194; ENSG00000239900; Homo sapiens. [Genome view]

GeneID

158.

KEGG

hsa:158.

UCSC

uc003ayp.2. human.
uc003ays.2. human.

Organism-specific databases

CTD

158.

GeneCards

GC22P039067.

H-InvDB

HIX0016502.

HGNC

HGNC:291. ADSL.

HPA

CAB019285.
HPA000525.

MIM

103050. phenotype.
608222. gene.

Orphanet

46. Adenylosuccinate lyase deficiency.

PharmGKB

PA24600.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P30566.

HOVERGEN

P30566.

Enzyme and pathway databases

BRENDA

4.3.2.2. 247.

Reactome

REACT_1698. Metablism of nucleotides.

Gene expression databases

ArrayExpress

P30566.

Bgee

P30566.

CleanEx

HS_ADSL.

Genevestigator

P30566.

GermOnline

ENSG00000100357. Homo sapiens.

Family and domain databases

InterPro

IPR019468. Adenylosuccinate_lyase_C.
IPR003031. D_crystallin.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]

Pfam

PF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]

PRINTS

PR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.

TIGRFAMs

TIGR00928. purB. 1 hit.

PROSITE

PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

629.

SOURCE

Search...

Entry information

Entry name

PUR8_HUMAN

Accession

Primary (citable) accession number: P30566
Secondary accession number(s): B0QY76, O75495, Q5TI34

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	May 30, 2000
Last modified:	November 24, 2009
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.