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P49915

- GUAA_HUMAN

UniProt

P49915 - GUAA_HUMAN

Protein

GMP synthase [glutamine-hydrolyzing]

Gene

GMPS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division.

    Catalytic activityi

    ATP + XMP + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei104 – 1041For GATase activity1 PublicationPROSITE-ProRule annotation
    Active sitei190 – 1901For GATase activity1 PublicationPROSITE-ProRule annotation
    Active sitei192 – 1921For GATase activity1 PublicationPROSITE-ProRule annotation
    Binding sitei337 – 3371Substrate
    Binding sitei522 – 5221Substrate
    Binding sitei610 – 6101Substrate
    Binding sitei685 – 6851Substrate
    Binding sitei691 – 6911Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi244 – 2507ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. GMP synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
    3. GMP synthase activity Source: ProtInc
    4. pyrophosphatase activity Source: InterPro

    GO - Biological processi

    1. glutamine metabolic process Source: UniProtKB-KW
    2. nucleobase-containing small molecule metabolic process Source: Reactome
    3. purine nucleobase biosynthetic process Source: ProtInc
    4. purine nucleobase metabolic process Source: Reactome
    5. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    UniPathwayiUPA00189; UER00296.

    Protein family/group databases

    MEROPSiC26.950.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GMP synthase [glutamine-hydrolyzing] (EC:6.3.5.2)
    Alternative name(s):
    GMP synthetase
    Glutamine amidotransferase
    Gene namesi
    Name:GMPS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:4378. GMPS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving GMPS is found in acute myeloid leukemias. Translocation t(3,11)(q25,q23) with KMT2A/MLL1.

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA28763.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 693692GMP synthase [glutamine-hydrolyzing]PRO_0000140257Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei9 – 91N6-acetyllysine1 Publication
    Modified residuei318 – 3181Phosphothreonine1 Publication
    Modified residuei332 – 3321Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP49915.
    PaxDbiP49915.
    PeptideAtlasiP49915.
    PRIDEiP49915.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00029079.

    PTM databases

    PhosphoSiteiP49915.

    Expressioni

    Gene expression databases

    ArrayExpressiP49915.
    BgeeiP49915.
    CleanExiHS_GMPS.
    GenevestigatoriP49915.

    Organism-specific databases

    HPAiHPA046630.
    HPA050682.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi114360. 30 interactions.
    IntActiP49915. 13 interactions.
    MINTiMINT-5004310.
    STRINGi9606.ENSP00000419851.

    Structurei

    Secondary structure

    1
    693
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 325
    Turni35 – 384
    Helixi39 – 479
    Beta strandi52 – 543
    Helixi61 – 677
    Beta strandi70 – 767
    Helixi91 – 944
    Beta strandi100 – 1045
    Helixi105 – 1139
    Beta strandi118 – 1236
    Beta strandi127 – 1337
    Helixi138 – 1403
    Beta strandi145 – 1517
    Beta strandi153 – 1597
    Beta strandi165 – 1706
    Beta strandi173 – 1797
    Turni180 – 1834
    Beta strandi184 – 1896
    Beta strandi193 – 1964
    Helixi199 – 2079
    Turni208 – 2114
    Helixi219 – 23416
    Beta strandi238 – 2425
    Helixi247 – 25913
    Helixi262 – 2643
    Beta strandi265 – 2717
    Helixi281 – 2899
    Beta strandi294 – 2985
    Helixi300 – 3045
    Helixi327 – 3293
    Helixi333 – 35422
    Beta strandi361 – 3655
    Helixi377 – 3826
    Helixi387 – 3893
    Helixi396 – 4038
    Helixi410 – 4134
    Helixi416 – 42510
    Helixi430 – 4334
    Helixi442 – 4465
    Beta strandi450 – 4523
    Helixi459 – 47012
    Helixi472 – 4754
    Helixi481 – 4899
    Helixi492 – 50413
    Beta strandi507 – 52014
    Beta strandi523 – 53614
    Helixi540 – 55314
    Beta strandi557 – 5637
    Helixi582 – 60120
    Helixi605 – 6073
    Beta strandi613 – 6175
    Helixi624 – 6263
    Beta strandi633 – 6375
    Beta strandi643 – 6497
    Turni654 – 6563
    Helixi659 – 67113
    Beta strandi675 – 6817

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VPIX-ray2.40A/B25-219[»]
    2VXOX-ray2.50A/B20-693[»]
    ProteinModelPortaliP49915.
    SMRiP49915. Positions 23-693.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49915.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 216190Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd
    BLAST
    Domaini217 – 435219GMPS ATP-PPasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 glutamine amidotransferase type-1 domain.PROSITE-ProRule annotation
    Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiCOG0519.
    HOGENOMiHOG000223965.
    HOVERGENiHBG005929.
    InParanoidiP49915.
    KOiK01951.
    OMAiKIYGLQF.
    OrthoDBiEOG7J17Z9.
    PhylomeDBiP49915.
    TreeFamiTF106132.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR001674. GMP_synth_C.
    IPR004739. GMP_synth_N.
    IPR025777. GMPS_ATP_PPase_dom.
    IPR022310. NAD/GMP_synthase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF00117. GATase. 1 hit.
    PF00958. GMP_synt_C. 1 hit.
    PF02540. NAD_synthase. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR00888. guaA_Nterm. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    PS51553. GMPS_ATP_PPASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49915-1) [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

    MALCNGDSKL ENAGGDLKDG HHHYEGAVVI LDAGAQYGKV IDRRVRELFV    50
    QSEIFPLETP AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPV 100
    LGICYGMQMM NKVFGGTVHK KSVREDGVFN ISVDNTCSLF RGLQKEEVVL 150
    LTHGDSVDKV ADGFKVVARS GNIVAGIANE SKKLYGAQFH PEVGLTENGK 200
    VILKNFLYDI AGCSGTFTVQ NRELECIREI KERVGTSKVL VLLSGGVDST 250
    VCTALLNRAL NQEQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA 300
    HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE 350
    VIGEMNLKPE EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK 400
    LREEGKVIEP LKDFHKDEVR ILGRELGLPE ELVSRHPFPG PGLAIRVICA 450
    EEPYICKDFP ETNNILKIVA DFSASVKKPH TLLQRVKACT TEEDQEKLMQ 500
    ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW ESLIFLARLI 550
    PRMCHNVNRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR 600
    ESGYAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGIP 650
    ATPGNEIPVE VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE 693
    Length:693
    Mass (Da):76,715
    Last modified:October 1, 1996 - v1
    Checksum:i1CDA0DD3B244728D
    GO
    Isoform 2 (identifier: P49915-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         10-108: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:594
    Mass (Da):65,929
    Checksum:i376D7F0A7E3F8C07
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti261 – 2611N → D in BAG63519. (PubMed:14702039)Curated
    Sequence conflicti415 – 4151H → I AA sequence (PubMed:8089153)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei10 – 10899Missing in isoform 2. 1 PublicationVSP_053933Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10860 mRNA. Translation: AAA60331.1.
    AK291504 mRNA. Translation: BAF84193.1.
    AK302148 mRNA. Translation: BAG63519.1.
    AK315832 mRNA. Translation: BAF98723.1.
    AC067721 Genomic DNA. No translation available.
    AC104472 Genomic DNA. No translation available.
    AC140753 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78741.1.
    BC012178 mRNA. Translation: AAH12178.1.
    CCDSiCCDS46941.1. [P49915-1]
    PIRiA54847.
    RefSeqiNP_003866.1. NM_003875.2. [P49915-1]
    UniGeneiHs.591314.

    Genome annotation databases

    EnsembliENST00000295920; ENSP00000295920; ENSG00000163655. [P49915-2]
    ENST00000496455; ENSP00000419851; ENSG00000163655. [P49915-1]
    GeneIDi8833.
    KEGGihsa:8833.
    UCSCiuc003faq.3. human. [P49915-1]

    Polymorphism databases

    DMDMi1708072.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10860 mRNA. Translation: AAA60331.1 .
    AK291504 mRNA. Translation: BAF84193.1 .
    AK302148 mRNA. Translation: BAG63519.1 .
    AK315832 mRNA. Translation: BAF98723.1 .
    AC067721 Genomic DNA. No translation available.
    AC104472 Genomic DNA. No translation available.
    AC140753 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78741.1 .
    BC012178 mRNA. Translation: AAH12178.1 .
    CCDSi CCDS46941.1. [P49915-1 ]
    PIRi A54847.
    RefSeqi NP_003866.1. NM_003875.2. [P49915-1 ]
    UniGenei Hs.591314.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VPI X-ray 2.40 A/B 25-219 [» ]
    2VXO X-ray 2.50 A/B 20-693 [» ]
    ProteinModelPortali P49915.
    SMRi P49915. Positions 23-693.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114360. 30 interactions.
    IntActi P49915. 13 interactions.
    MINTi MINT-5004310.
    STRINGi 9606.ENSP00000419851.

    Chemistry

    ChEMBLi CHEMBL5721.
    DrugBanki DB00142. L-Glutamic Acid.
    DB00130. L-Glutamine.

    Protein family/group databases

    MEROPSi C26.950.

    PTM databases

    PhosphoSitei P49915.

    Polymorphism databases

    DMDMi 1708072.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00029079.

    Proteomic databases

    MaxQBi P49915.
    PaxDbi P49915.
    PeptideAtlasi P49915.
    PRIDEi P49915.

    Protocols and materials databases

    DNASUi 8833.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295920 ; ENSP00000295920 ; ENSG00000163655 . [P49915-2 ]
    ENST00000496455 ; ENSP00000419851 ; ENSG00000163655 . [P49915-1 ]
    GeneIDi 8833.
    KEGGi hsa:8833.
    UCSCi uc003faq.3. human. [P49915-1 ]

    Organism-specific databases

    CTDi 8833.
    GeneCardsi GC03P155588.
    HGNCi HGNC:4378. GMPS.
    HPAi HPA046630.
    HPA050682.
    MIMi 600358. gene.
    neXtProti NX_P49915.
    PharmGKBi PA28763.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0519.
    HOGENOMi HOG000223965.
    HOVERGENi HBG005929.
    InParanoidi P49915.
    KOi K01951.
    OMAi KIYGLQF.
    OrthoDBi EOG7J17Z9.
    PhylomeDBi P49915.
    TreeFami TF106132.

    Enzyme and pathway databases

    UniPathwayi UPA00189 ; UER00296 .
    Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.

    Miscellaneous databases

    ChiTaRSi GMPS. human.
    EvolutionaryTracei P49915.
    GeneWikii GMP_synthase.
    GenomeRNAii 8833.
    NextBioi 33152.
    PROi P49915.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49915.
    Bgeei P49915.
    CleanExi HS_GMPS.
    Genevestigatori P49915.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    3.40.50.880. 1 hit.
    InterProi IPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR001674. GMP_synth_C.
    IPR004739. GMP_synth_N.
    IPR025777. GMPS_ATP_PPase_dom.
    IPR022310. NAD/GMP_synthase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF00117. GATase. 1 hit.
    PF00958. GMP_synt_C. 1 hit.
    PF02540. NAD_synthase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52317. SSF52317. 1 hit.
    TIGRFAMsi TIGR00888. guaA_Nterm. 1 hit.
    PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
    PS51553. GMPS_ATP_PPASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA."
      Hirst M., Haliday E., Nakamura J., Lou L.
      J. Biol. Chem. 269:23830-23837(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    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 AND 2).
      Tissue: Testis.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [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 1).
      Tissue: Placenta.
    6. "t(3;11) translocation in treatment-related acute myeloid leukemia fuses MLL with the GMPS (guanosine 5-prime monophosphate synthetase) gene."
      Pegram L.D., Megonigal M.D., Lange B.J., Nowell P.C., Rowley J.D., Rappaport E.F., Felix C.A.
      Blood 96:4360-4362(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318 AND SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-693, SUBSTRATE-BINDING SITES, ACTIVE SITE, SUBUNIT.

    Entry informationi

    Entry nameiGUAA_HUMAN
    AccessioniPrimary (citable) accession number: P49915
    Secondary accession number(s): A8K639, B4DXV7, F8W720
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 152 of the entry and version 1 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3