ID   PURA1_HUMAN             Reviewed;         457 AA.
AC   Q8N142; Q86TT6; Q8N714;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   07-JUL-2009, entry version 68.
DE   RecName: Full=Adenylosuccinate synthetase isozyme 1;
DE            Short=AMPSase 1;
DE            Short=AdSS 1;
DE            EC=6.3.4.4;
DE   AltName: Full=IMP--aspartate ligase 1;
GN   Name=ADSSL1; Synonyms=ADSS1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Bone marrow stroma;
RX   PubMed=15786719; DOI=10.1007/s11010-005-2539-9;
RA   Sun H., Li N., Wang X., Chen T., Shi L., Zhang L., Wang J., Wan T.,
RA   Cao X.;
RT   "Molecular cloning and characterization of a novel muscle
RT   adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal
RT   cells.";
RL   Mol. Cell. Biochem. 269:85-94(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Heart;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-388, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18083107; DOI=10.1016/j.cell.2007.11.025;
RA   Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,
RA   Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,
RA   Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,
RA   Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,
RA   Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
RT   "Global survey of phosphotyrosine signaling identifies oncogenic
RT   kinases in lung cancer.";
RL   Cell 131:1190-1203(2007).
CC   -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC       nucleotide biosynthesis (By similarity).
CC   -!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate +
CC       N(6)-(1,2-dicarboxyethyl)-AMP.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 1/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8N142-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N142-2; Sequence=VSP_008421;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and
CC       heart, as well as in several hematopoietic cell lines and solid
CC       tumors.
CC   -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH32039.1; Type=Frameshift; Positions=1;
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DR   EMBL; AY037159; AAK67646.1; -; mRNA.
DR   EMBL; AK095921; BAC04649.1; -; mRNA.
DR   EMBL; BX248286; CAD62614.1; ALT_INIT; mRNA.
DR   EMBL; BC032039; AAH32039.1; ALT_FRAME; mRNA.
DR   EMBL; BC047904; AAH47904.1; -; mRNA.
DR   IPI; IPI00167065; -.
DR   IPI; IPI00170914; -.
DR   RefSeq; NP_689541.1; -.
DR   RefSeq; NP_954634.1; -.
DR   UniGene; Hs.592327; -.
DR   PDB; 2GJO; Model; -; A=27-457.
DR   PDBsum; 2GJO; -.
DR   SMR; Q8N142; 27-457.
DR   PhosphoSite; Q8N142; -.
DR   PRIDE; Q8N142; -.
DR   Ensembl; ENSG00000185100; Homo sapiens.
DR   GeneID; 122622; -.
DR   KEGG; hsa:122622; -.
DR   NMPDR; fig|9606.3.peg.10250; -.
DR   UCSC; uc001ypd.1; human.
DR   UCSC; uc001ype.1; human.
DR   GeneCards; GC14P104261; -.
DR   HGNC; HGNC:20093; ADSSL1.
DR   MIM; 612498; gene.
DR   PharmGKB; PA134974111; -.
DR   HOVERGEN; Q8N142; -.
DR   OMA; Q8N142; KAQNYIR.
DR   BRENDA; 6.3.4.4; 247.
DR   Reactome; REACT_1698; Metablism of nucleotides.
DR   DrugBank; DB00128; L-Aspartic Acid.
DR   NextBio; 80937; -.
DR   ArrayExpress; Q8N142; -.
DR   Bgee; Q8N142; -.
DR   CleanEx; HS_ADSSL1; -.
DR   GermOnline; ENSG00000185100; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0004019; F:adenylosuccinate synthase activity; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042301; F:phosphate binding; NAS:UniProtKB.
DR   GO; GO:0006167; P:AMP biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0002376; P:immune system process; NAS:UniProtKB.
DR   InterPro; IPR018220; Adenylosuccinate_synthase_AS.
DR   InterPro; IPR001114; Adenylosuccinate_synthetase.
DR   PANTHER; PTHR11846; Asucc_synthtase; 1.
DR   Pfam; PF00709; Adenylsucc_synt; 1.
DR   ProDom; PD001188; Asucc_synthtase; 1.
DR   SMART; SM00788; Adenylsucc_synt; 1.
DR   TIGRFAMs; TIGR00184; purA; 1.
DR   PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR   PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW   GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Purine biosynthesis.
FT   CHAIN         1    457       Adenylosuccinate synthetase isozyme 1.
FT                                /FTId=PRO_0000095132.
FT   NP_BIND      42     48       GTP (Potential).
FT   ACT_SITE    174    174       By similarity.
FT   ACT_SITE    181    181       By similarity.
FT   METAL        43     43       Magnesium (By similarity).
FT   METAL        70     70       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   MOD_RES     388    388       Phosphotyrosine.
FT   VAR_SEQ       1     64       MSGTRASNDRPPGAGGVKRGRLQQEAAATGSRVTVVLGAQW
FT                                GDEGKGKVVDLLATDADIISRCQ -> MVGRSCGVATQRQG
FT                                GGQRPTNLALTLSSSPAHSTALPWLPPRSLQLLSGHSVPAQ
FT                                PTPHLPSACGGPTRVTLGEERAWRSHGSNAGGHTCLPRRTA
FT                                GAGSLTPGGER (in isoform 2).
FT                                /FTId=VSP_008421.
SQ   SEQUENCE   457 AA;  50208 MW;  387341D49721B2EF CRC64;
     MSGTRASNDR PPGAGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV DLLATDADII
     SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN GVVIHLPGLF EEAEKNEKKG
     LKDWEKRLII SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTKKGIGPT YSSKAARTGL
     RICDLLSDFD EFSSRFKNLA HQHQSMFPTL EIDIEGQLKR LKGFAERIRP MVRDGVYFMY
     EALHGPPKKI LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA
     YTTRVGIGAF PTEQINEIGG LLQTRGHEWG VTTGRKRRCG WLDLMILRYA HMVNGFTALA
     LTKLDILDVL GEVKVGVSYK LNGKRIPYFP ANQEMLQKVE VEYETLPGWK ADTTGARRWE
     DLPPQAQNYI RFVENHVGVA VKWVGVGKSR ESMIQLF
//