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P49915

- GUAA_HUMAN

UniProt

P49915 - GUAA_HUMAN

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Protein
GMP synthase [glutamine-hydrolyzing]
Gene
GMPS
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei104 – 1041For GATase activity1 Publication
Active sitei190 – 1901For GATase activity1 Publication
Active sitei192 – 1921For GATase activity1 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 – 2507ATP By similarity

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
Complete GO annotation...

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
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
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

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.

Miscellaneous databases

EvolutionaryTraceiP49915.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 216190Glutamine amidotransferase type-1
Add
BLAST
Domaini217 – 435219GMPS ATP-PPase
Add
BLAST

Sequence similaritiesi

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei10 – 10899Missing in isoform 2.
VSP_053933Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti261 – 2611N → D in BAG63519. 1 Publication
Sequence conflicti415 – 4151H → I AA sequence 1 Publication

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.
ENST00000496455; ENSP00000419851; ENSG00000163655.
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 .
ENST00000496455 ; ENSP00000419851 ; ENSG00000163655 .
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

« 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].
  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: September 3, 2014
This is version 151 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

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