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Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2

Gene

PFKFB2

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

Functioni

Synthesis and degradation of fructose 2,6-bisphosphate.

Catalytic activityi

Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate.

Enzyme regulationi

Phosphorylation results in the activation of the kinase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781Fructose 6-phosphateBy similarity
Binding sitei102 – 1021Fructose 6-phosphateBy similarity
Active sitei128 – 1281Sequence Analysis
Binding sitei130 – 1301Fructose 6-phosphateBy similarity
Binding sitei136 – 1361Fructose 6-phosphateBy similarity
Active sitei158 – 1581Sequence Analysis
Binding sitei172 – 1721Fructose 6-phosphateBy similarity
Binding sitei193 – 1931Fructose 6-phosphateBy similarity
Binding sitei197 – 1971Fructose 6-phosphateBy similarity
Binding sitei256 – 2561Fructose 2,6-bisphosphateBy similarity
Active sitei257 – 2571Tele-phosphohistidine intermediateBy similarity
Binding sitei263 – 2631Fructose 2,6-bisphosphateBy similarity
Binding sitei269 – 2691Fructose 2,6-bisphosphate; via amide nitrogenBy similarity
Binding sitei306 – 3061Fructose 2,6-bisphosphateBy similarity
Active sitei326 – 3261Proton donor/acceptorBy similarity
Binding sitei337 – 3371Fructose 2,6-bisphosphateBy similarity
Binding sitei351 – 3511Fructose 2,6-bisphosphateBy similarity
Binding sitei355 – 3551Fructose 2,6-bisphosphateBy similarity
Binding sitei366 – 3661Fructose 2,6-bisphosphateBy similarity
Active sitei391 – 3911Proton donor/acceptorBy similarity
Binding sitei392 – 3921Fructose 2,6-bisphosphateBy similarity
Binding sitei396 – 3961Fructose 2,6-bisphosphateBy similarity
Binding sitei428 – 4281ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi45 – 539ATPBy similarity
Nucleotide bindingi167 – 1726ATPBy similarity
Nucleotide bindingi348 – 3514ATPBy similarity
Nucleotide bindingi392 – 3965ATPBy similarity

GO - Molecular functioni

  • 6-phosphofructo-2-kinase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • fructose-2,6-bisphosphate 2-phosphatase activity Source: UniProtKB-EC
  • protein kinase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.105. 2681.
3.1.3.46. 2681.
ReactomeiREACT_1383. Glycolysis.
SABIO-RKO60825.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
Short name:
6PF-2-K/Fru-2,6-P2ase 2
Short name:
PFK/FBPase 2
Alternative name(s):
6PF-2-K/Fru-2,6-P2ase heart-type isozyme
Including the following 2 domains:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
Gene namesi
Name:PFKFB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:8873. PFKFB2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi466 – 4661S → E: Constitutively active mutant that cannot be phosphorylated and further activated by AMPK. 1 Publication

Organism-specific databases

PharmGKBiPA33212.

Polymorphism and mutation databases

BioMutaiPFKFB2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 5055046-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2PRO_0000179964Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei29 – 291Phosphoserine; by PKABy similarity
Modified residuei466 – 4661Phosphoserine; by AMPK4 Publications
Modified residuei468 – 4681Phosphothreonine1 Publication
Modified residuei475 – 4751Phosphothreonine; by PKCBy similarity
Modified residuei483 – 4831Phosphoserine2 Publications
Modified residuei493 – 4931Phosphoserine2 Publications

Post-translational modificationi

Phosphorylation by AMPK stimulates activity.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO60825.
PaxDbiO60825.
PRIDEiO60825.

PTM databases

DEPODiO60825.
PhosphoSiteiO60825.

Expressioni

Tissue specificityi

Heart.

Gene expression databases

BgeeiO60825.
CleanExiHS_PFKFB2.
ExpressionAtlasiO60825. baseline and differential.
GenevisibleiO60825. HS.

Organism-specific databases

HPAiHPA049975.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi111229. 7 interactions.
IntActiO60825. 4 interactions.
MINTiMINT-3000455.
STRINGi9606.ENSP00000356047.

Structurei

3D structure databases

ProteinModelPortaliO60825.
SMRiO60825. Positions 37-448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2482476-phosphofructo-2-kinaseAdd
BLAST
Regioni249 – 505257Fructose-2,6-bisphosphataseAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the phosphoglycerate mutase family.Curated

Phylogenomic databases

eggNOGiCOG0406.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiO60825.
KOiK19029.
OMAiEKQYPEE.
OrthoDBiEOG7M3J03.
PhylomeDBiO60825.
TreeFamiTF313541.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PANTHERiPTHR10606. PTHR10606. 1 hit.
PfamiPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiPS00175. PG_MUTASE. 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: O60825-1) [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
MSGASSSEQN NNSYETKTPN LRMSEKKCSW ASYMTNSPTL IVMIGLPARG
60 70 80 90 100
KTYVSKKLTR YLNWIGVPTK VFNLGVYRRE AVKSYKSYDF FRHDNEEAMK
110 120 130 140 150
IRKQCALVAL EDVKAYLTEE NGQIAVFDAT NTTRERRDMI LNFAEQNSFK
160 170 180 190 200
VFFVESVCDD PDVIAANILE VKVSSPDYPE RNRENVMEDF LKRIECYKVT
210 220 230 240 250
YRPLDPDNYD KDLSFIKVIN VGQRFLVNRV QDYIQSKIVY YLMNIHVQPR
260 270 280 290 300
TIYLCRHGES EFNLLGKIGG DSGLSVRGKQ FAQALRKFLE EQEITDLKVW
310 320 330 340 350
TSQLKRTIQT AESLGVPYEQ WKILNEIDAG VCEEMTYAEI EKRYPEEFAL
360 370 380 390 400
RDQEKYLYRY PGGESYQDLV QRLEPVIMEL ERQGNVLVIS HQAVMRCLLA
410 420 430 440 450
YFLDKGADEL PYLRCPLHTI FKLTPVAYGC KVETIKLNVE AVNTHRDKPT
460 470 480 490 500
NNFPKNQTPV RMRRNSFTPL SSSNTIRRPR NYSVGSRPLK PLSPLRAQDM

QEGAD
Length:505
Mass (Da):58,477
Last modified:January 24, 2001 - v2
Checksum:i5CD6A933A7EBF604
GO
Isoform 2 (identifier: O60825-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     451-505: NNFPKNQTPV...RAQDMQEGAD → AAETTLAVRRRPSAASLMLPC

Show »
Length:471
Mass (Da):54,406
Checksum:i2B9C8957889F4D61
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281Missing in CAA06605 (PubMed:9652401).Curated
Sequence conflicti303 – 3042QL → HV in CAA06606 (PubMed:9652401).Curated
Sequence conflicti372 – 3721R → L in CAA06606 (PubMed:9652401).Curated
Sequence conflicti396 – 3961R → H in CAA06606 (PubMed:9652401).Curated
Sequence conflicti406 – 4061G → D in CAA06606 (PubMed:9652401).Curated
Sequence conflicti427 – 4271A → T in CAA06606 (PubMed:9652401).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei451 – 50555NNFPK…QEGAD → AAETTLAVRRRPSAASLMLP C in isoform 2. 3 PublicationsVSP_004675Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005577 Genomic DNA. Translation: CAA06605.1.
AJ005578 mRNA. Translation: CAA06606.1.
AB044805 mRNA. Translation: BAB19681.1.
AF470623 mRNA. Translation: AAL99386.1.
AK292883 mRNA. Translation: BAF85572.1.
AL445493 Genomic DNA. Translation: CAH70777.1.
AL445493 Genomic DNA. Translation: CAH70778.1.
CH471100 Genomic DNA. Translation: EAW93508.1.
BC069350 mRNA. Translation: AAH69350.1.
BC069385 mRNA. Translation: AAH69385.1.
BC069583 mRNA. Translation: AAH69583.1.
BC069586 mRNA. Translation: AAH69586.1.
BC069600 mRNA. Translation: AAH69600.1.
BC075075 mRNA. Translation: AAH75075.1.
BC075076 mRNA. Translation: AAH75076.1.
BC112103 mRNA. Translation: AAI12104.1.
BC112105 mRNA. Translation: AAI12106.1.
CCDSiCCDS31003.1. [O60825-2]
CCDS31004.1. [O60825-1]
RefSeqiNP_001018063.1. NM_001018053.1. [O60825-2]
NP_006203.2. NM_006212.2. [O60825-1]
XP_011507927.1. XM_011509625.1. [O60825-1]
XP_011507928.1. XM_011509626.1. [O60825-1]
XP_011507929.1. XM_011509627.1. [O60825-1]
XP_011507930.1. XM_011509628.1. [O60825-1]
UniGeneiHs.282702.

Genome annotation databases

EnsembliENST00000367079; ENSP00000356046; ENSG00000123836. [O60825-2]
ENST00000367080; ENSP00000356047; ENSG00000123836.
GeneIDi5208.
KEGGihsa:5208.
UCSCiuc001hfg.3. human. [O60825-1]
uc001hfh.3. human. [O60825-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005577 Genomic DNA. Translation: CAA06605.1.
AJ005578 mRNA. Translation: CAA06606.1.
AB044805 mRNA. Translation: BAB19681.1.
AF470623 mRNA. Translation: AAL99386.1.
AK292883 mRNA. Translation: BAF85572.1.
AL445493 Genomic DNA. Translation: CAH70777.1.
AL445493 Genomic DNA. Translation: CAH70778.1.
CH471100 Genomic DNA. Translation: EAW93508.1.
BC069350 mRNA. Translation: AAH69350.1.
BC069385 mRNA. Translation: AAH69385.1.
BC069583 mRNA. Translation: AAH69583.1.
BC069586 mRNA. Translation: AAH69586.1.
BC069600 mRNA. Translation: AAH69600.1.
BC075075 mRNA. Translation: AAH75075.1.
BC075076 mRNA. Translation: AAH75076.1.
BC112103 mRNA. Translation: AAI12104.1.
BC112105 mRNA. Translation: AAI12106.1.
CCDSiCCDS31003.1. [O60825-2]
CCDS31004.1. [O60825-1]
RefSeqiNP_001018063.1. NM_001018053.1. [O60825-2]
NP_006203.2. NM_006212.2. [O60825-1]
XP_011507927.1. XM_011509625.1. [O60825-1]
XP_011507928.1. XM_011509626.1. [O60825-1]
XP_011507929.1. XM_011509627.1. [O60825-1]
XP_011507930.1. XM_011509628.1. [O60825-1]
UniGeneiHs.282702.

3D structure databases

ProteinModelPortaliO60825.
SMRiO60825. Positions 37-448.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111229. 7 interactions.
IntActiO60825. 4 interactions.
MINTiMINT-3000455.
STRINGi9606.ENSP00000356047.

PTM databases

DEPODiO60825.
PhosphoSiteiO60825.

Polymorphism and mutation databases

BioMutaiPFKFB2.

Proteomic databases

MaxQBiO60825.
PaxDbiO60825.
PRIDEiO60825.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367079; ENSP00000356046; ENSG00000123836. [O60825-2]
ENST00000367080; ENSP00000356047; ENSG00000123836.
GeneIDi5208.
KEGGihsa:5208.
UCSCiuc001hfg.3. human. [O60825-1]
uc001hfh.3. human. [O60825-2]

Organism-specific databases

CTDi5208.
GeneCardsiGC01P207226.
HGNCiHGNC:8873. PFKFB2.
HPAiHPA049975.
MIMi171835. gene.
neXtProtiNX_O60825.
PharmGKBiPA33212.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0406.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiO60825.
KOiK19029.
OMAiEKQYPEE.
OrthoDBiEOG7M3J03.
PhylomeDBiO60825.
TreeFamiTF313541.

Enzyme and pathway databases

BRENDAi2.7.1.105. 2681.
3.1.3.46. 2681.
ReactomeiREACT_1383. Glycolysis.
SABIO-RKO60825.

Miscellaneous databases

ChiTaRSiPFKFB2. human.
GeneWikiiPFKFB2.
GenomeRNAii5208.
NextBioi20140.
PROiO60825.
SOURCEiSearch...

Gene expression databases

BgeeiO60825.
CleanExiHS_PFKFB2.
ExpressionAtlasiO60825. baseline and differential.
GenevisibleiO60825. HS.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PANTHERiPTHR10606. PTHR10606. 1 hit.
PfamiPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and structure of the human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase heart isoform gene (PFKFB2)."
    Heine-Suner D., Diaz-Guillen M.A., Lange A.J., Rodriguez de Cordoba S.
    Eur. J. Biochem. 254:103-110(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Heart.
  3. "Human insulinoma PFK2/F26DPase."
    Matsutani A.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  4. "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] (ISOFORM 2).
    Tissue: Trachea.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Brain.
  8. "Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia."
    Marsin A.S., Bertrand L., Rider M.H., Deprez J., Beauloye C., Vincent M.F., Van den Berghe G., Carling D., Hue L.
    Curr. Biol. 10:1247-1255(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-466, MUTAGENESIS OF SER-466.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-468; SER-483 AND SER-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "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.
  12. "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-466; SER-483 AND SER-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-466, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiF262_HUMAN
AccessioniPrimary (citable) accession number: O60825
Secondary accession number(s): O60824
, Q5VVQ3, Q5VVQ4, Q9H3P1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 24, 2001
Last modified: July 22, 2015
This is version 152 of the entry and version 2 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

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. 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.