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Protein

Protein prune homolog

Gene

PRUNE

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

Functioni

Phosphodiesterase (PDE) that has higher activity toward cAMP than cGMP, as substrate. Plays a role in cell proliferation, is able to induce cell motility and acts as a negative regulator of NME1.5 Publications

Catalytic activityi

Diphosphate + H2O = 2 phosphate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Enzyme regulationi

Activated by magnesium ions and inhibited by manganese ions. Inhibited by dipyridamole, moderately sensitive to IBMX and inhibited by vinpocetine.1 Publication

Kineticsi

  1. KM=0.91 µM for cAMP2 Publications
  2. KM=2.3 µM for cGMP2 Publications
  1. Vmax=12.8 pmol/min/µg enzyme with cAMP as substrate2 Publications
  2. Vmax=0.8 pmol/min/µg enzyme with cGMP as substrate2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi28 – 281Manganese 1By similarity
Metal bindingi30 – 301Manganese 2By similarity
Metal bindingi106 – 1061Manganese 1By similarity
Metal bindingi106 – 1061Manganese 2By similarity
Metal bindingi179 – 1791Manganese 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein prune homolog (EC:3.6.1.1)
Short name:
hPrune
Alternative name(s):
Drosophila-related expressed sequence 17
Short name:
DRES-17
Short name:
DRES17
HTcD37
Gene namesi
Name:PRUNE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:13420. PRUNE.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi28 – 281D → A: Partial loss of cAMP PDE activity. Partial loss of cAMP PDE activity; when associated with D-106. Partial loss of cAMP PDE activity; when associated with D-106 and D-179. 1 Publication
Mutagenesisi106 – 1061D → A: No change in cAMP PDE activity. Partial loss of cAMP PDE activity; when associated with D-28. Partial loss of cAMP PDE activity; when associated with D-28 and D-179. 1 Publication
Mutagenesisi126 – 1294DHRP → AAAA: Partial loss of cAMP PDE activity. 1 Publication
Mutagenesisi179 – 1791D → A: Partial loss of cAMP PDE activity. Partial loss of cAMP PDE activity; when associated with D-28 and D-106. 1 Publication

Organism-specific databases

PharmGKBiPA134939749.

Polymorphism and mutation databases

BioMutaiPRUNE.
DMDMi229462737.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453Protein prune homologPRO_0000337987Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ86TP1.
PaxDbiQ86TP1.
PRIDEiQ86TP1.

PTM databases

PhosphoSiteiQ86TP1.

Expressioni

Tissue specificityi

Ubiquitously expressed. Seems to be overexpressed in aggressive sarcoma subtypes, such as leiomyosarcomas and malignant fibrous histiocytomas (MFH) as well as in the less malignant liposarcomas.3 Publications

Gene expression databases

BgeeiQ86TP1.
CleanExiHS_PRUNE.
ExpressionAtlasiQ86TP1. baseline and differential.
GenevisibleiQ86TP1. HS.

Organism-specific databases

HPAiHPA028411.

Interactioni

Subunit structurei

Homooligomer. Able to homodimerize via its C-terminal domain. Interacts with NME1. Interacts with GSK3; at focal adhesion complexes where paxillin and vinculin are colocalized.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NME1P155312EBI-2127112,EBI-741141

Protein-protein interaction databases

BioGridi121827. 8 interactions.
IntActiQ86TP1. 2 interactions.
STRINGi9606.ENSP00000271620.

Structurei

3D structure databases

ProteinModelPortaliQ86TP1.
SMRiQ86TP1. Positions 18-360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni393 – 42028Essential for homodimerizationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi106 – 1083DHH motif

Sequence similaritiesi

Belongs to the PPase class C family. Prune subfamily.Curated

Phylogenomic databases

eggNOGiCOG1227.
GeneTreeiENSGT00450000040262.
HOVERGENiHBG058142.
InParanoidiQ86TP1.
KOiK01514.
OMAiALRTTIC.
PhylomeDBiQ86TP1.
TreeFamiTF323914.

Family and domain databases

InterProiIPR001667. DDH_dom.
IPR004097. DHHA2.
[Graphical view]
PfamiPF01368. DHH. 1 hit.
PF02833. DHHA2. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86TP1-1) [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
MEDYLQGCRA ALQESRPLHV VLGNEACDLD STVSALALAF YLAKTTEAEE
60 70 80 90 100
VFVPVLNIKR SELPLRGDIV FFLQKVHIPE SILIFRDEID LHALYQAGQL
110 120 130 140 150
TLILVDHHIL SKSDTALEEA VAEVLDHRPI EPKHCPPCHV SVELVGSCAT
160 170 180 190 200
LVTERILQGA PEILDRQTAA LLHGTIILDC VNMDLKIGKA TPKDSKYVEK
210 220 230 240 250
LEALFPDLPK RNDIFDSLQK AKFDVSGLTT EQMLRKDQKT IYRQGVKVAI
260 270 280 290 300
SAIYMDLEAF LQRSNLLADL HAFCQAHSYD VLVAMTIFFN THNEPVRQLA
310 320 330 340 350
IFCPHVALQT TICEVLERSH SPPLKLTPAS STHPNLHAYL QGNTQVSRKK
360 370 380 390 400
LLPLLQEALS AYFDSMKIPS GQPETADVSR EQVDKELDRA SNSLISGLSQ
410 420 430 440 450
DEEDPPLPPT PMNSLVDECP LDQGLPKLSA EAVFEKCSQI SLSQSTTASL

SKK
Length:453
Mass (Da):50,200
Last modified:May 5, 2009 - v2
Checksum:i34BE1909AB89DBD5
GO
Isoform 2 (identifier: Q86TP1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     45-112: TTEAEEVFVPVLNIKRSELPLRGDIVFFLQKVHIPESILIFRDEIDLHALYQAGQLTLILVDHHILSK → A

Note: No experimental confirmation available.
Show »
Length:386
Mass (Da):42,456
Checksum:i6E3355352353B0A5
GO
Isoform 3 (identifier: Q86TP1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-182: Missing.

Note: No experimental confirmation available.
Show »
Length:271
Mass (Da):30,127
Checksum:iEADC5693A59D308F
GO
Isoform 4 (identifier: Q86TP1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     15-174: Missing.
     259-311: Missing.

Note: No experimental confirmation available.
Show »
Length:240
Mass (Da):26,611
Checksum:i7D8897402A2B3136
GO
Isoform 5 (identifier: Q86TP1-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-182: Missing.
     259-311: Missing.

Note: No experimental confirmation available.
Show »
Length:218
Mass (Da):24,131
Checksum:iDC0632A96FDD07EE
GO
Isoform 6 (identifier: Q86TP1-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-232: Missing.
     259-311: Missing.

Note: No experimental confirmation available.
Show »
Length:168
Mass (Da):18,478
Checksum:i54405F7EA079B5C2
GO
Isoform 7 (identifier: Q86TP1-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-232: Missing.

Show »
Length:221
Mass (Da):24,475
Checksum:i108DE09A66C5F957
GO

Sequence cautioni

The sequence BAB55423.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAG60534.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141E → A in AAK00592 (Ref. 2) Curated
Sequence conflicti19 – 224HVVL → AWHE in AAF04914 (PubMed:10524757).Curated
Sequence conflicti221 – 2211A → V in AAC95290 (PubMed:10602478).Curated
Sequence conflicti221 – 2211A → V in AAF04914 (PubMed:10524757).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti397 – 3971G → R.
Corresponds to variant rs3738477 [ dbSNP | Ensembl ].
VAR_059559
Natural varianti397 – 3971G → S.
Corresponds to variant rs3738477 [ dbSNP | Ensembl ].
VAR_043728

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 232232Missing in isoform 6 and isoform 7. 2 PublicationsVSP_034013Add
BLAST
Alternative sequencei1 – 182182Missing in isoform 3 and isoform 5. 2 PublicationsVSP_034014Add
BLAST
Alternative sequencei15 – 174160Missing in isoform 4. 1 PublicationVSP_034015Add
BLAST
Alternative sequencei45 – 11268TTEAE…HILSK → A in isoform 2. 1 PublicationVSP_034016Add
BLAST
Alternative sequencei259 – 31153Missing in isoform 4, isoform 5 and isoform 6. 3 PublicationsVSP_034017Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051907 mRNA. Translation: AAC95290.1.
AF123538 mRNA. Translation: AAK00592.1.
AF123539 mRNA. Translation: AAK00593.1.
AK027875 mRNA. Translation: BAB55423.1. Different initiation.
AK294154 mRNA. Translation: BAG57478.1.
AK298273 mRNA. Translation: BAG60534.1. Different initiation.
AK315120 mRNA. Translation: BAG37575.1.
AL590133 Genomic DNA. Translation: CAI13338.1.
AL590133 Genomic DNA. Translation: CAI13341.1.
AL590133 Genomic DNA. Translation: CAI13342.1.
AL590133 Genomic DNA. Translation: CAI13343.1.
CH471121 Genomic DNA. Translation: EAW53486.1.
CH471121 Genomic DNA. Translation: EAW53488.1.
CH471121 Genomic DNA. Translation: EAW53489.1.
BC014886 mRNA. Translation: AAH14886.1.
BC025304 mRNA. Translation: AAH25304.1.
BC063481 mRNA. Translation: AAH63481.1.
U67085 mRNA. Translation: AAF04914.1.
AL122054 mRNA. Translation: CAH56396.1.
CCDSiCCDS76211.1. [Q86TP1-3]
CCDS977.1. [Q86TP1-1]
RefSeqiNP_001290158.1. NM_001303229.1. [Q86TP1-3]
NP_001290171.1. NM_001303242.1.
NP_001290172.1. NM_001303243.1.
NP_067045.1. NM_021222.2. [Q86TP1-1]
XP_005245454.1. XM_005245397.3. [Q86TP1-3]
XP_011508134.1. XM_011509832.1. [Q86TP1-3]
UniGeneiHs.78524.

Genome annotation databases

EnsembliENST00000271620; ENSP00000271620; ENSG00000143363.
ENST00000368934; ENSP00000357930; ENSG00000143363. [Q86TP1-5]
ENST00000368935; ENSP00000357931; ENSG00000143363. [Q86TP1-6]
ENST00000368936; ENSP00000357932; ENSG00000143363. [Q86TP1-3]
ENST00000368937; ENSP00000357933; ENSG00000143363. [Q86TP1-5]
GeneIDi58497.
KEGGihsa:58497.
UCSCiuc001ewh.1. human. [Q86TP1-1]
uc001ewj.1. human. [Q86TP1-6]
uc001ewk.1. human. [Q86TP1-5]
uc010pco.1. human. [Q86TP1-7]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051907 mRNA. Translation: AAC95290.1.
AF123538 mRNA. Translation: AAK00592.1.
AF123539 mRNA. Translation: AAK00593.1.
AK027875 mRNA. Translation: BAB55423.1. Different initiation.
AK294154 mRNA. Translation: BAG57478.1.
AK298273 mRNA. Translation: BAG60534.1. Different initiation.
AK315120 mRNA. Translation: BAG37575.1.
AL590133 Genomic DNA. Translation: CAI13338.1.
AL590133 Genomic DNA. Translation: CAI13341.1.
AL590133 Genomic DNA. Translation: CAI13342.1.
AL590133 Genomic DNA. Translation: CAI13343.1.
CH471121 Genomic DNA. Translation: EAW53486.1.
CH471121 Genomic DNA. Translation: EAW53488.1.
CH471121 Genomic DNA. Translation: EAW53489.1.
BC014886 mRNA. Translation: AAH14886.1.
BC025304 mRNA. Translation: AAH25304.1.
BC063481 mRNA. Translation: AAH63481.1.
U67085 mRNA. Translation: AAF04914.1.
AL122054 mRNA. Translation: CAH56396.1.
CCDSiCCDS76211.1. [Q86TP1-3]
CCDS977.1. [Q86TP1-1]
RefSeqiNP_001290158.1. NM_001303229.1. [Q86TP1-3]
NP_001290171.1. NM_001303242.1.
NP_001290172.1. NM_001303243.1.
NP_067045.1. NM_021222.2. [Q86TP1-1]
XP_005245454.1. XM_005245397.3. [Q86TP1-3]
XP_011508134.1. XM_011509832.1. [Q86TP1-3]
UniGeneiHs.78524.

3D structure databases

ProteinModelPortaliQ86TP1.
SMRiQ86TP1. Positions 18-360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121827. 8 interactions.
IntActiQ86TP1. 2 interactions.
STRINGi9606.ENSP00000271620.

Chemistry

BindingDBiQ86TP1.
ChEMBLiCHEMBL2079850.

PTM databases

PhosphoSiteiQ86TP1.

Polymorphism and mutation databases

BioMutaiPRUNE.
DMDMi229462737.

Proteomic databases

MaxQBiQ86TP1.
PaxDbiQ86TP1.
PRIDEiQ86TP1.

Protocols and materials databases

DNASUi58497.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000271620; ENSP00000271620; ENSG00000143363.
ENST00000368934; ENSP00000357930; ENSG00000143363. [Q86TP1-5]
ENST00000368935; ENSP00000357931; ENSG00000143363. [Q86TP1-6]
ENST00000368936; ENSP00000357932; ENSG00000143363. [Q86TP1-3]
ENST00000368937; ENSP00000357933; ENSG00000143363. [Q86TP1-5]
GeneIDi58497.
KEGGihsa:58497.
UCSCiuc001ewh.1. human. [Q86TP1-1]
uc001ewj.1. human. [Q86TP1-6]
uc001ewk.1. human. [Q86TP1-5]
uc010pco.1. human. [Q86TP1-7]

Organism-specific databases

CTDi58497.
GeneCardsiGC01P150980.
H-InvDBHIX0001042.
HGNCiHGNC:13420. PRUNE.
HPAiHPA028411.
neXtProtiNX_Q86TP1.
PharmGKBiPA134939749.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1227.
GeneTreeiENSGT00450000040262.
HOVERGENiHBG058142.
InParanoidiQ86TP1.
KOiK01514.
OMAiALRTTIC.
PhylomeDBiQ86TP1.
TreeFamiTF323914.

Miscellaneous databases

ChiTaRSiPRUNE. human.
GenomeRNAii58497.
NextBioi64992.
PROiQ86TP1.

Gene expression databases

BgeeiQ86TP1.
CleanExiHS_PRUNE.
ExpressionAtlasiQ86TP1. baseline and differential.
GenevisibleiQ86TP1. HS.

Family and domain databases

InterProiIPR001667. DDH_dom.
IPR004097. DHHA2.
[Graphical view]
PfamiPF01368. DHH. 1 hit.
PF02833. DHHA2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Evidence for interaction between human PRUNE and nm23-H1 NDPKinase."
    Reymond A., Volorio S., Merla G., Al-Maghtheh M., Zuffardi O., Bulfone A., Ballabio A., Zollo M.
    Oncogene 18:7244-7252(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH NME1, SUBCELLULAR LOCATION, FUNCTION.
  2. "Human Prune homolog."
    Zollo M., Volorio S.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4).
  3. "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; 5 AND 7), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 211-453 (ISOFORMS 1/3).
    Tissue: Brain cortex, Kidney and Thyroid.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1; 3 AND 6).
    Tissue: Blood and Brain.
  7. "Sequencing analysis of forty-eight human image cDNA clones similar to Drosophila mutant protein."
    Volorio S., Simon G., Repetto M., Cucciardi M., Banfi S., Borsani G., Ballabio A., Zollo M.
    DNA Seq. 9:307-315(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-453 (ISOFORM 1).
    Tissue: Brain.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-453 (ISOFORMS 1/2/3/4/5/6/7).
    Tissue: Testis.
  9. Cited for: TISSUE SPECIFICITY, FUNCTION.
  10. Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH NME1, ENZYME REGULATION, MUTAGENESIS OF ASP-28; ASP-106; 126-ASP--PRO-129 AND ASP-179.
  11. "Overexpression of h-prune in breast cancer is correlated with advanced disease status."
    Zollo M., Andre A., Cossu A., Sini M.C., D'Angelo A., Marino N., Budroni M., Tanda F., Arrigoni G., Palmieri G.
    Clin. Cancer Res. 11:199-205(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  12. "Glycogen synthase kinase 3 and h-prune regulate cell migration by modulating focal adhesions."
    Kobayashi T., Hino S., Oue N., Asahara T., Zollo M., Yasui W., Kikuchi A.
    Mol. Cell. Biol. 26:898-911(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GSK3B, SUBCELLULAR LOCATION, FUNCTION.
  13. "Domain mapping on the human metastasis regulator protein h-Prune reveals a C-terminal dimerization domain."
    Middelhaufe S., Garzia L., Ohndorf U.M., Kachholz B., Zollo M., Steegborn C.
    Biochem. J. 407:199-205(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NME1, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  14. "Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility."
    Garzia L., D'Angelo A., Amoresano A., Knauer S.K., Cirulli C., Campanella C., Stauber R.H., Steegborn C., Iolascon A., Zollo M.
    Oncogene 27:1853-1864(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NME1, FUNCTION.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPRUNE_HUMAN
AccessioniPrimary (citable) accession number: Q86TP1
Secondary accession number(s): B2RCH8
, B4DFL7, Q5SZF9, Q659E5, Q6P4E0, Q8N654, Q96JU5, Q9C071, Q9C072, Q9UIV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: May 5, 2009
Last modified: July 22, 2015
This is version 98 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. 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.