SubmitCancel

Skip Header

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

Q9NRF8

- PYRG2_HUMAN

UniProt

Q9NRF8 - PYRG2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
CTP synthase 2
Gene
CTPS2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides.2 Publications

Catalytic activityi

ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei399 – 3991For GATase activity By similarity
Active sitei526 – 5261For GATase activity By similarity
Active sitei528 – 5281For GATase activity By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. CTP synthase activity Source: Reactome
Complete GO annotation...

GO - Biological processi

  1. 'de novo' CTP biosynthetic process Source: UniProtKB-UniPathway
  2. glutamine metabolic process Source: UniProtKB-KW
  3. nucleobase-containing small molecule interconversion Source: Reactome
  4. nucleobase-containing small molecule metabolic process Source: Reactome
  5. pyrimidine nucleotide metabolic process Source: ProtInc
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00585-MONOMER.
BRENDAi6.3.4.2. 2681.
ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
UniPathwayiUPA00159; UER00277.

Names & Taxonomyi

Protein namesi
Recommended name:
CTP synthase 2 (EC:6.3.4.2)
Alternative name(s):
CTP synthetase 2
UTP--ammonia ligase 2
Gene namesi
Name:CTPS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:2520. CTPS2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27021.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 586586CTP synthase 2
PRO_0000247033Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei568 – 5681Phosphoserine3 Publications
Modified residuei571 – 5711Phosphoserine4 Publications
Modified residuei574 – 5741Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NRF8.
PaxDbiQ9NRF8.
PRIDEiQ9NRF8.

PTM databases

PhosphoSiteiQ9NRF8.

Expressioni

Gene expression databases

BgeeiQ9NRF8.
CleanExiHS_CTPS2.
GenevestigatoriQ9NRF8.

Organism-specific databases

HPAiHPA017437.

Interactioni

Protein-protein interaction databases

BioGridi121144. 23 interactions.
IntActiQ9NRF8. 6 interactions.
MINTiMINT-1443035.
STRINGi9606.ENSP00000352222.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87
Beta strandi10 – 156
Helixi16 – 2813
Turni29 – 313
Beta strandi34 – 407
Beta strandi87 – 893
Helixi90 – 10213
Turni103 – 1086
Helixi113 – 12917
Beta strandi141 – 1477
Helixi154 – 1563
Helixi157 – 16913
Helixi172 – 1743
Beta strandi175 – 1828
Turni187 – 1893
Helixi195 – 20612
Beta strandi212 – 2209
Helixi224 – 23310
Helixi238 – 2403
Beta strandi241 – 2455
Helixi252 – 2598
Helixi262 – 2709
Beta strandi297 – 30610
Helixi312 – 3143
Helixi315 – 32713
Beta strandi330 – 3389
Helixi339 – 3424
Helixi344 – 3496
Helixi351 – 36313
Beta strandi365 – 3695
Helixi378 – 39013
Beta strandi395 – 3984
Helixi400 – 41314
Beta strandi419 – 4224
Beta strandi429 – 4357
Beta strandi449 – 45810
Helixi463 – 4675
Beta strandi472 – 4809
Beta strandi482 – 4843
Helixi486 – 4883
Helixi490 – 4923
Beta strandi495 – 5039
Beta strandi508 – 51811
Beta strandi520 – 5267
Helixi527 – 5304
Helixi538 – 54811
Helixi551 – 5566

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4UX-ray2.30A297-562[»]
2VKTX-ray2.50A297-562[»]
3IHLX-ray2.80A/B1-275[»]
ProteinModelPortaliQ9NRF8.
SMRiQ9NRF8. Positions 1-273, 297-562.

Miscellaneous databases

EvolutionaryTraceiQ9NRF8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini300 – 554255Glutamine amidotransferase type-1
Add
BLAST

Sequence similaritiesi

Belongs to the CTP synthase family.

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0504.
HOGENOMiHOG000077514.
HOVERGENiHBG002243.
InParanoidiQ9NRF8.
KOiK01937.
OMAiCDIDKNA.
OrthoDBiEOG7M3HZZ.
PhylomeDBiQ9NRF8.
TreeFamiTF300379.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11550. PTHR11550. 1 hit.
PfamiPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00337. PyrG. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NRF8-1 [UniParc]FASTAAdd to Basket

« Hide

MKYILVTGGV ISGIGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF    50
SPYEHGEVFV LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQHVINK 100
ERRGDYLGKT VQVVPHITDA VQEWVMNQAK VPVDGNKEEP QICVIELGGT 150
IGDIEGMPFV EAFRQFQFKA KRENFCNIHV SLVPQLSATG EQKTKPTQNS 200
VRALRGLGLS PDLIVCRSST PIEMAVKEKI SMFCHVNPEQ VICIHDVSST 250
YRVPVLLEEQ SIVKYFKERL HLPIGDSASN LLFKWRNMAD RYERLQKICS 300
IALVGKYTKL RDCYASVFKA LEHSALAINH KLNLMYIDSI DLEKITETED 350
PVKFHEAWQK LCKADGILVP GGFGIRGTLG KLQAISWART KKIPFLGVCL 400
GMQLAVIEFA RNCLNLKDAD STEFRPNAPV PLVIDMPEHN PGNLGGTMRL 450
GIRRTVFKTE NSILRKLYGD VPFIEERHRH RFEVNPNLIK QFEQNDLSFV 500
GQDVDGDRME IIELANHPYF VGVQFHPEFS SRPMKPSPPY LGLLLAATGN 550
LNAYLQQGCK LSSSDRYSDA SDDSFSEPRI AELEIS 586
Length:586
Mass (Da):65,678
Last modified:October 1, 2000 - v1
Checksum:iAC1CF2E67D89741B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti220 – 2201T → S in BAB14814. 1 Publication
Sequence conflicti233 – 2331F → L in BAB14607. 1 Publication
Sequence conflicti304 – 3041V → A in BAB14607. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF226667 mRNA. Translation: AAF91241.1.
AK023549 mRNA. Translation: BAB14607.1.
AK024070 mRNA. Translation: BAB14814.1.
AK125332 mRNA. Translation: BAG54184.1.
AK125348 mRNA. Translation: BAG54188.1.
AL445467, AC073909 Genomic DNA. Translation: CAI40086.1.
CH471074 Genomic DNA. Translation: EAW98912.1.
BC006256 mRNA. Translation: AAH06256.2.
BC034986 mRNA. Translation: AAH34986.1.
CCDSiCCDS14175.1.
RefSeqiNP_001137474.1. NM_001144002.1.
NP_062831.3. NM_019857.4.
NP_787055.1. NM_175859.2.
XP_005274619.1. XM_005274562.1.
XP_006724566.1. XM_006724503.1.
UniGeneiHs.227049.

Genome annotation databases

EnsembliENST00000359276; ENSP00000352222; ENSG00000047230.
ENST00000380241; ENSP00000369590; ENSG00000047230.
ENST00000443824; ENSP00000401264; ENSG00000047230.
GeneIDi56474.
KEGGihsa:56474.
UCSCiuc004cxk.3. human.

Polymorphism databases

DMDMi74752919.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF226667 mRNA. Translation: AAF91241.1 .
AK023549 mRNA. Translation: BAB14607.1 .
AK024070 mRNA. Translation: BAB14814.1 .
AK125332 mRNA. Translation: BAG54184.1 .
AK125348 mRNA. Translation: BAG54188.1 .
AL445467 , AC073909 Genomic DNA. Translation: CAI40086.1 .
CH471074 Genomic DNA. Translation: EAW98912.1 .
BC006256 mRNA. Translation: AAH06256.2 .
BC034986 mRNA. Translation: AAH34986.1 .
CCDSi CCDS14175.1.
RefSeqi NP_001137474.1. NM_001144002.1.
NP_062831.3. NM_019857.4.
NP_787055.1. NM_175859.2.
XP_005274619.1. XM_005274562.1.
XP_006724566.1. XM_006724503.1.
UniGenei Hs.227049.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V4U X-ray 2.30 A 297-562 [» ]
2VKT X-ray 2.50 A 297-562 [» ]
3IHL X-ray 2.80 A/B 1-275 [» ]
ProteinModelPortali Q9NRF8.
SMRi Q9NRF8. Positions 1-273, 297-562.
ModBasei Search...

Protein-protein interaction databases

BioGridi 121144. 23 interactions.
IntActi Q9NRF8. 6 interactions.
MINTi MINT-1443035.
STRINGi 9606.ENSP00000352222.

PTM databases

PhosphoSitei Q9NRF8.

Polymorphism databases

DMDMi 74752919.

Proteomic databases

MaxQBi Q9NRF8.
PaxDbi Q9NRF8.
PRIDEi Q9NRF8.

Protocols and materials databases

DNASUi 56474.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359276 ; ENSP00000352222 ; ENSG00000047230 .
ENST00000380241 ; ENSP00000369590 ; ENSG00000047230 .
ENST00000443824 ; ENSP00000401264 ; ENSG00000047230 .
GeneIDi 56474.
KEGGi hsa:56474.
UCSCi uc004cxk.3. human.

Organism-specific databases

CTDi 56474.
GeneCardsi GC0XM016606.
HGNCi HGNC:2520. CTPS2.
HPAi HPA017437.
MIMi 300380. gene.
neXtProti NX_Q9NRF8.
PharmGKBi PA27021.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0504.
HOGENOMi HOG000077514.
HOVERGENi HBG002243.
InParanoidi Q9NRF8.
KOi K01937.
OMAi CDIDKNA.
OrthoDBi EOG7M3HZZ.
PhylomeDBi Q9NRF8.
TreeFami TF300379.

Enzyme and pathway databases

UniPathwayi UPA00159 ; UER00277 .
BioCyci MetaCyc:HS00585-MONOMER.
BRENDAi 6.3.4.2. 2681.
Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

EvolutionaryTracei Q9NRF8.
GeneWikii CTPS2.
GenomeRNAii 56474.
NextBioi 62001.
PROi Q9NRF8.
SOURCEi Search...

Gene expression databases

Bgeei Q9NRF8.
CleanExi HS_CTPS2.
Genevestigatori Q9NRF8.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
3.40.50.880. 1 hit.
InterProi IPR029062. Class_I_gatase-like.
IPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR11550. PTHR11550. 1 hit.
Pfami PF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view ]
SUPFAMi SSF52317. SSF52317. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00337. PyrG. 1 hit.
PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  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].
    Tissue: Placenta and Retinoblastoma.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [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].
    Tissue: Lung and Testis.
  6. "Expression of human CTP synthetase in Saccharomyces cerevisiae reveals phosphorylation by protein kinase A."
    Han G.-S., Sreenivas A., Choi M.-G., Chang Y.-F., Martin S.S., Baldwin E.P., Carman G.M.
    J. Biol. Chem. 280:38328-38336(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND SER-574, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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 SER-568; SER-571 AND SER-574, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-568 AND SER-571, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPYRG2_HUMAN
AccessioniPrimary (citable) accession number: Q9NRF8
Secondary accession number(s): B3KWM2
, Q9BRI0, Q9H809, Q9H8K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 116 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, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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