Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

GMP synthase [glutamine-hydrolyzing]

Gene

GMPS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

Pathway: GMP biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes GMP from XMP (L-Gln route).
Proteins known to be involved in this subpathway in this organism are:
  1. GMP synthase [glutamine-hydrolyzing] (GMPS)
This subpathway is part of the pathway GMP biosynthesis, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes GMP from XMP (L-Gln route), the pathway GMP biosynthesis and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei104 – 1041For GATase activityPROSITE-ProRule annotation1 Publication
Active sitei190 – 1901For GATase activityPROSITE-ProRule annotation1 Publication
Active sitei192 – 1921For GATase activityPROSITE-ProRule annotation1 Publication
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

  • ATP binding Source: UniProtKB-KW
  • GMP synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
  • GMP synthase activity Source: ProtInc
  • pyrophosphatase activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.5.2. 2681.
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 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:4378. GMPS.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.

Chemistry

DrugBankiDB00130. L-Glutamine.

Polymorphism and mutation databases

BioMutaiGMPS.
DMDMi1708072.

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

BgeeiP49915.
CleanExiHS_GMPS.
GenevisibleiP49915. HS.

Organism-specific databases

HPAiHPA046630.
HPA050682.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi114360. 32 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 – 325Combined sources
Turni35 – 384Combined sources
Helixi39 – 479Combined sources
Beta strandi52 – 543Combined sources
Helixi61 – 677Combined sources
Beta strandi70 – 767Combined sources
Helixi91 – 944Combined sources
Beta strandi100 – 1045Combined sources
Helixi105 – 1139Combined sources
Beta strandi118 – 1236Combined sources
Beta strandi127 – 1337Combined sources
Helixi138 – 1403Combined sources
Beta strandi145 – 1517Combined sources
Beta strandi153 – 1597Combined sources
Beta strandi165 – 1706Combined sources
Beta strandi173 – 1797Combined sources
Turni180 – 1834Combined sources
Beta strandi184 – 1896Combined sources
Beta strandi193 – 1964Combined sources
Helixi199 – 2079Combined sources
Turni208 – 2114Combined sources
Helixi219 – 23416Combined sources
Beta strandi238 – 2425Combined sources
Helixi247 – 25913Combined sources
Helixi262 – 2643Combined sources
Beta strandi265 – 2717Combined sources
Helixi281 – 2899Combined sources
Beta strandi294 – 2985Combined sources
Helixi300 – 3045Combined sources
Helixi327 – 3293Combined sources
Helixi333 – 35422Combined sources
Beta strandi361 – 3655Combined sources
Helixi377 – 3826Combined sources
Helixi387 – 3893Combined sources
Helixi396 – 4038Combined sources
Helixi410 – 4134Combined sources
Helixi416 – 42510Combined sources
Helixi430 – 4334Combined sources
Helixi442 – 4465Combined sources
Beta strandi450 – 4523Combined sources
Helixi459 – 47012Combined sources
Helixi472 – 4754Combined sources
Helixi481 – 4899Combined sources
Helixi492 – 50413Combined sources
Beta strandi507 – 52014Combined sources
Beta strandi523 – 53614Combined sources
Helixi540 – 55314Combined sources
Beta strandi557 – 5637Combined sources
Helixi582 – 60120Combined sources
Helixi605 – 6073Combined sources
Beta strandi613 – 6175Combined sources
Helixi624 – 6263Combined sources
Beta strandi633 – 6375Combined sources
Beta strandi643 – 6497Combined sources
Turni654 – 6563Combined sources
Helixi659 – 67113Combined sources
Beta strandi675 – 6817Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000006591.
HOGENOMiHOG000223965.
HOVERGENiHBG005929.
InParanoidiP49915.
KOiK01951.
OMAiKNAKWLA.
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. AlignAdd to basket

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

        10         20         30         40         50
MALCNGDSKL ENAGGDLKDG HHHYEGAVVI LDAGAQYGKV IDRRVRELFV
60 70 80 90 100
QSEIFPLETP AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPV
110 120 130 140 150
LGICYGMQMM NKVFGGTVHK KSVREDGVFN ISVDNTCSLF RGLQKEEVVL
160 170 180 190 200
LTHGDSVDKV ADGFKVVARS GNIVAGIANE SKKLYGAQFH PEVGLTENGK
210 220 230 240 250
VILKNFLYDI AGCSGTFTVQ NRELECIREI KERVGTSKVL VLLSGGVDST
260 270 280 290 300
VCTALLNRAL NQEQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA
310 320 330 340 350
HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE
360 370 380 390 400
VIGEMNLKPE EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK
410 420 430 440 450
LREEGKVIEP LKDFHKDEVR ILGRELGLPE ELVSRHPFPG PGLAIRVICA
460 470 480 490 500
EEPYICKDFP ETNNILKIVA DFSASVKKPH TLLQRVKACT TEEDQEKLMQ
510 520 530 540 550
ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW ESLIFLARLI
560 570 580 590 600
PRMCHNVNRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR
610 620 630 640 650
ESGYAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGIP
660 670 680 690
ATPGNEIPVE VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE
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:
EMBLi
GenBanki
DDBJi
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]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi114360. 32 interactions.
IntActiP49915. 13 interactions.
MINTiMINT-5004310.
STRINGi9606.ENSP00000419851.

Chemistry

ChEMBLiCHEMBL5721.
DrugBankiDB00130. L-Glutamine.

Protein family/group databases

MEROPSiC26.950.

PTM databases

PhosphoSiteiP49915.

Polymorphism and mutation databases

BioMutaiGMPS.
DMDMi1708072.

2D gel databases

REPRODUCTION-2DPAGEIPI00029079.

Proteomic databases

MaxQBiP49915.
PaxDbiP49915.
PeptideAtlasiP49915.
PRIDEiP49915.

Protocols and materials databases

DNASUi8833.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8833.
GeneCardsiGC03P155588.
HGNCiHGNC:4378. GMPS.
HPAiHPA046630.
HPA050682.
MIMi600358. gene.
neXtProtiNX_P49915.
PharmGKBiPA28763.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0519.
GeneTreeiENSGT00390000006591.
HOGENOMiHOG000223965.
HOVERGENiHBG005929.
InParanoidiP49915.
KOiK01951.
OMAiKNAKWLA.
OrthoDBiEOG7J17Z9.
PhylomeDBiP49915.
TreeFamiTF106132.

Enzyme and pathway databases

UniPathwayiUPA00189; UER00296.
BRENDAi6.3.5.2. 2681.
ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

ChiTaRSiGMPS. human.
EvolutionaryTraceiP49915.
GeneWikiiGMP_synthase.
GenomeRNAii8833.
NextBioi33152.
PROiP49915.
SOURCEiSearch...

Gene expression databases

BgeeiP49915.
CleanExiHS_GMPS.
GenevisibleiP49915. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], CLEAVAGE OF INITIATOR METHIONINE [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: June 24, 2015
This is version 159 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.