Q8N142 (PURA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylosuccinate synthetase isozyme 1
Short name=AMPSase 1
Short name=AdSS 1
EC=6.3.4.4

Alternative name(s):
Adenylosuccinate synthetase, basic isozyme
Adenylosuccinate synthetase, muscle isozyme
Short name=M-type adenylosuccinate synthetase
IMP--aspartate ligase 1

Gene names

Name:	ADSSL1
Synonyms:	ADSS1

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	457 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP By similarity. HAMAP-Rule MF_03126
Catalytic activity	GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP-Rule MF_03126
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP-Rule MF_03126
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Ref.1.
Tissue specificity	Predominantly expressed in skeletal muscle and heart, as well as in several hematopoietic cell lines and solid tumors. Ref.1
Sequence similarities	Belongs to the adenylosuccinate synthetase family.
Sequence caution	The sequence AAH32039.1 differs from that shown. Reason: Frameshift at position 1. The sequence CAD62614.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Purine biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' AMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway AMP biosynthetic process Inferred from direct assay Ref.1. Source: UniProtKB immune system process Non-traceable author statement Ref.1. Source: UniProtKB purine nucleobase metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	GTP binding Non-traceable author statement Ref.1. Source: UniProtKB adenylosuccinate synthase activity Inferred from direct assay Ref.1. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphate ion binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q8N142-1)

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: Q8N142-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-64: MSGTRASNDR...TDADIISRCQ → MVGRSCGVAT...AGSLTPGGER

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 457	457	Adenylosuccinate synthetase isozyme 1 HAMAP-Rule MF_03126		PRO_0000095132
Regions
	Nucleotide binding	42 – 48	7	GTP By similarity
	Nucleotide binding	70 – 72	3	GTP By similarity
	Nucleotide binding	363 – 365	3	GTP By similarity
	Nucleotide binding	445 – 448	4	GTP By similarity
	Region	43 – 46	4	IMP binding By similarity
	Region	68 – 71	4	IMP binding By similarity
	Region	331 – 337	7	Substrate binding By similarity
Sites
	Active site	43	1	Proton acceptor By similarity
	Active site	71	1	Proton donor By similarity
	Metal binding	43	1	Magnesium By similarity
	Metal binding	70	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	43	1	Substrate By similarity
	Binding site	163	1	IMP By similarity
	Binding site	177	1	IMP; shared with dimeric partner By similarity
	Binding site	256	1	IMP By similarity
	Binding site	271	1	IMP By similarity
	Binding site	335	1	IMP By similarity
	Binding site	337	1	GTP By similarity
Natural variations
	Alternative sequence	1 – 64	64	MSGTR…ISRCQ → MVGRSCGVATQRQGGGQRPT NLALTLSSSPAHSTALPWLP PRSLQLLSGHSVPAQPTPHL PSACGGPTRVTLGEERAWRS HGSNAGGHTCLPRRTAGAGS LTPGGER in isoform 2.		VSP_008421

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 387341D49721B2EF	FASTA	457	50,208
	10 20 30 40 50 60 MSGTRASNDR PPGAGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV DLLATDADII 70 80 90 100 110 120 SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN GVVIHLPGLF EEAEKNEKKG 130 140 150 160 170 180 LKDWEKRLII SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTKKGIGPT YSSKAARTGL 190 200 210 220 230 240 RICDLLSDFD EFSSRFKNLA HQHQSMFPTL EIDIEGQLKR LKGFAERIRP MVRDGVYFMY 250 260 270 280 290 300 EALHGPPKKI LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA 310 320 330 340 350 360 YTTRVGIGAF PTEQINEIGG LLQTRGHEWG VTTGRKRRCG WLDLMILRYA HMVNGFTALA 370 380 390 400 410 420 LTKLDILDVL GEVKVGVSYK LNGKRIPYFP ANQEMLQKVE VEYETLPGWK ADTTGARRWE 430 440 450 DLPPQAQNYI RFVENHVGVA VKWVGVGKSR ESMIQLF
	Isoform 2 [UniParc]. Checksum: 9C561192088BDAAF	FASTA	500	54,562
	10 20 30 40 50 60 MVGRSCGVAT QRQGGGQRPT NLALTLSSSP AHSTALPWLP PRSLQLLSGH SVPAQPTPHL 70 80 90 100 110 120 PSACGGPTRV TLGEERAWRS HGSNAGGHTC LPRRTAGAGS LTPGGERGGN NAGHTVVVDG 130 140 150 160 170 180 KEYDFHLLPS GIINTKAVSF IGNGVVIHLP GLFEEAEKNE KKGLKDWEKR LIISDRAHLV 190 200 210 220 230 240 FDFHQAVDGL QEVQRQAQEG KNIGTTKKGI GPTYSSKAAR TGLRICDLLS DFDEFSSRFK 250 260 270 280 290 300 NLAHQHQSMF PTLEIDIEGQ LKRLKGFAER IRPMVRDGVY FMYEALHGPP KKILVEGANA 310 320 330 340 350 360 ALLDIDFGTY PFVTSSNCTV GGVCTGLGIP PQNIGDVYGV VKAYTTRVGI GAFPTEQINE 370 380 390 400 410 420 IGGLLQTRGH EWGVTTGRKR RCGWLDLMIL RYAHMVNGFT ALALTKLDIL DVLGEVKVGV 430 440 450 460 470 480 SYKLNGKRIP YFPANQEMLQ KVEVEYETLP GWKADTTGAR RWEDLPPQAQ NYIRFVENHV 490 500 GVAVKWVGVG KSRESMIQLF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells." Sun H., Li N., Wang X., Chen T., Shi L., Zhang L., Wang J., Wan T., Cao X. Mol. Cell. Biochem. 269:85-94(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Bone marrow stroma.
[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] (ISOFORM 1). Tissue: Heart.
[3]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta.
[4]	"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] (ISOFORMS 1 AND 2). Tissue: Testis.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY037159 mRNA. Translation: AAK67646.1.
AK095921 mRNA. Translation: BAC04649.1.
BX248286 mRNA. Translation: CAD62614.1. Different initiation.
BC032039 mRNA. Translation: AAH32039.1. Frameshift.
BC047904 mRNA. Translation: AAH47904.1.

IPI

IPI00167065.
IPI00170914.

RefSeq

NP_689541.1. NM_152328.3.
NP_954634.1. NM_199165.1.

UniGene

Hs.592327.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GJO	model	-	A	27-457	[»]

ProteinModelPortal

Q8N142.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8N142. 2 interactions.

MINT

MINT-3319213.

STRING

9606.ENSP00000333019.

PTM databases

PhosphoSite

Q8N142.

Polymorphism databases

DMDM

37537958.

Proteomic databases

PaxDb

Q8N142.

PRIDE

Q8N142.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000330877; ENSP00000331260; ENSG00000185100.
ENST00000332972; ENSP00000333019; ENSG00000185100.

GeneID

122622.

KEGG

hsa:122622.

UCSC

uc001ypd.3. human.
uc001ype.3. human.

Organism-specific databases

CTD

122622.

GeneCards

GC14P105190.

HGNC

HGNC:20093. ADSSL1.

MIM

612498. gene.

neXtProt

NX_Q8N142.

PharmGKB

PA134974111.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0104.

HOGENOM

HOG000260959.

HOVERGEN

HBG053768.

KO

K01939.

OMA

LDYYNFQ.

OrthoDB

EOG4P5K90.

Enzyme and pathway databases

BRENDA

6.3.4.4. 2681.

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00075; UER00335.

Gene expression databases

ArrayExpress

Q8N142.

Bgee

Q8N142.

CleanEx

HS_ADSSL1.

Genevestigator

Q8N142.

GermOnline

ENSG00000185100. Homo sapiens.

Family and domain databases

HAMAP

MF_03126. Adenylosucc_synth_vert_basic.

InterPro

IPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]

PANTHER

PTHR11846. PTHR11846. 1 hit.

Pfam

PF00709. Adenylsucc_synt. 1 hit.
[Graphical view]

SMART

SM00788. Adenylsucc_synt. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00184. purA. 1 hit.

PROSITE

PS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00128. L-Aspartic Acid.

GenomeRNAi

122622.

NextBio

80937.

SOURCE

Search...

Entry information

Entry name

PURA1_HUMAN

Accession

Primary (citable) accession number: Q8N142
Secondary accession number(s): Q86TT6, Q8N714

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 105 of the entry and version 1 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.