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Q86TP1 (PRUNE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein prune homolog

Short name=hPrune
EC=3.6.1.1
Alternative name(s):
Drosophila-related expressed sequence 17
Short name=DRES-17
Short name=DRES17
HTcD37
Gene names
Name:PRUNE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.9 Ref.10 Ref.12 Ref.14

Catalytic activity

Diphosphate + H2O = 2 phosphate.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Enzyme regulation

Activated by magnesium ions and inhibited by manganese ions. Inhibited by dipyridamole, moderately sensitive to IBMX and inhibited by vinpocetine. Ref.10

Subunit structure

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. Ref.1 Ref.10 Ref.12 Ref.13 Ref.14

Subcellular location

Cytoplasm. Nucleus. Cell junctionfocal adhesion. Note: In some transfected cells a nuclear staining is also observed. Ref.1 Ref.11 Ref.12

Tissue specificity

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. Ref.1 Ref.9 Ref.11

Sequence similarities

Belongs to the PPase class C family. Prune subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.91 µM for cAMP Ref.10 Ref.13

KM=2.3 µM for cGMP

Vmax=12.8 pmol/min/µg enzyme with cAMP as substrate

Vmax=0.8 pmol/min/µg enzyme with cGMP as substrate

Sequence caution

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

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

Ontologies

Keywords
   Cellular componentCell junction
Cytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioninorganic diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

manganese ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.1. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NME1P155312EBI-2127112,EBI-741141

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86TP1-1)

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.
Isoform 2 (identifier: Q86TP1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     45-112: TTEAEEVFVPVLNIKRSELPLRGDIVFFLQKVHIPESILIFRDEIDLHALYQAGQLTLILVDHHILSK → A
Note: No experimental confirmation available.
Isoform 3 (identifier: Q86TP1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-182: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q86TP1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     15-174: Missing.
     259-311: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q86TP1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-182: Missing.
     259-311: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q86TP1-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-232: Missing.
     259-311: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q86TP1-7)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 453453Protein prune homolog
PRO_0000337987

Regions

Region393 – 42028Essential for homodimerization
Motif106 – 1083DHH motif

Sites

Metal binding281Manganese 1 By similarity
Metal binding301Manganese 2 By similarity
Metal binding1061Manganese 1 By similarity
Metal binding1061Manganese 2 By similarity
Metal binding1791Manganese 2 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16

Natural variations

Alternative sequence1 – 232232Missing in isoform 6 and isoform 7.
VSP_034013
Alternative sequence1 – 182182Missing in isoform 3 and isoform 5.
VSP_034014
Alternative sequence15 – 174160Missing in isoform 4.
VSP_034015
Alternative sequence45 – 11268TTEAE…HILSK → A in isoform 2.
VSP_034016
Alternative sequence259 – 31153Missing in isoform 4, isoform 5 and isoform 6.
VSP_034017
Natural variant3971G → R.
Corresponds to variant rs3738477 [ dbSNP | Ensembl ].
VAR_059559
Natural variant3971G → S.
Corresponds to variant rs3738477 [ dbSNP | Ensembl ].
VAR_043728

Experimental info

Mutagenesis281D → 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. Ref.10
Mutagenesis1061D → 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. Ref.10
Mutagenesis126 – 1294DHRP → AAAA: Partial loss of cAMP PDE activity. Ref.10
Mutagenesis1791D → A: Partial loss of cAMP PDE activity. Partial loss of cAMP PDE activity; when associated with D-28 and D-106. Ref.10
Sequence conflict141E → A in AAK00592. Ref.2
Sequence conflict19 – 224HVVL → AWHE in AAF04914. Ref.7
Sequence conflict2211A → V in AAC95290. Ref.1
Sequence conflict2211A → V in AAF04914. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 34BE1909AB89DBD5

FASTA45350,200
        10         20         30         40         50         60 
MEDYLQGCRA ALQESRPLHV VLGNEACDLD STVSALALAF YLAKTTEAEE VFVPVLNIKR 

        70         80         90        100        110        120 
SELPLRGDIV FFLQKVHIPE SILIFRDEID LHALYQAGQL TLILVDHHIL SKSDTALEEA 

       130        140        150        160        170        180 
VAEVLDHRPI EPKHCPPCHV SVELVGSCAT LVTERILQGA PEILDRQTAA LLHGTIILDC 

       190        200        210        220        230        240 
VNMDLKIGKA TPKDSKYVEK LEALFPDLPK RNDIFDSLQK AKFDVSGLTT EQMLRKDQKT 

       250        260        270        280        290        300 
IYRQGVKVAI SAIYMDLEAF LQRSNLLADL HAFCQAHSYD VLVAMTIFFN THNEPVRQLA 

       310        320        330        340        350        360 
IFCPHVALQT TICEVLERSH SPPLKLTPAS STHPNLHAYL QGNTQVSRKK LLPLLQEALS 

       370        380        390        400        410        420 
AYFDSMKIPS GQPETADVSR EQVDKELDRA SNSLISGLSQ DEEDPPLPPT PMNSLVDECP 

       430        440        450 
LDQGLPKLSA EAVFEKCSQI SLSQSTTASL SKK 

« Hide

Isoform 2 [UniParc].

Checksum: 6E3355352353B0A5
Show »

FASTA38642,456
Isoform 3 [UniParc].

Checksum: EADC5693A59D308F
Show »

FASTA27130,127
Isoform 4 [UniParc].

Checksum: 7D8897402A2B3136
Show »

FASTA24026,611
Isoform 5 [UniParc].

Checksum: DC0632A96FDD07EE
Show »

FASTA21824,131
Isoform 6 [UniParc].

Checksum: 54405F7EA079B5C2
Show »

FASTA16818,478
Isoform 7 [UniParc].

Checksum: 108DE09A66C5F957
Show »

FASTA22124,475

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-453 (ISOFORMS 1/2/3/4/5/6/7).
Tissue: Testis.
[9]"Amplification and overexpression of PRUNE in human sarcomas and breast carcinomas-a possible mechanism for altering the nm23-H1 activity."
Forus A., D'Angelo A., Henriksen J., Merla G., Maelandsmo G.M., Floerenes V.A., Olivieri S., Bjerkehagen B., Meza-Zepeda L.A., del Vecchio Blanco F., Mueller C., Sanvito F., Kononen J., Nesland J.M., Fodstad O., Reymond A., Kallioniemi O.-P., Arrigoni G. expand/collapse author list , Ballabio A., Myklebost O., Zollo M.
Oncogene 20:6881-6890(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, FUNCTION.
[10]"Prune cAMP phosphodiesterase binds nm23-H1 and promotes cancer metastasis."
D'Angelo A., Garzia L., Andre A., Carotenuto P., Aglio V., Guardiola O., Arrigoni G., Cossu A., Palmieri G., Aravind L., Zollo M.
Cancer Cell 5:137-149(2004) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS977.1. [Q86TP1-1]
RefSeqNP_067045.1. NM_021222.1. [Q86TP1-1]
XP_005245453.1. XM_005245396.1. [Q86TP1-3]
XP_005245454.1. XM_005245397.2. [Q86TP1-3]
UniGeneHs.78524.

3D structure databases

ProteinModelPortalQ86TP1.
SMRQ86TP1. Positions 18-360.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121827. 4 interactions.
IntActQ86TP1. 2 interactions.

Chemistry

ChEMBLCHEMBL2079850.

PTM databases

PhosphoSiteQ86TP1.

Polymorphism databases

DMDM229462737.

Proteomic databases

MaxQBQ86TP1.
PaxDbQ86TP1.
PRIDEQ86TP1.

Protocols and materials databases

DNASU58497.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000271620; ENSP00000271620; ENSG00000143363. [Q86TP1-1]
ENST00000368934; ENSP00000357930; ENSG00000143363. [Q86TP1-5]
ENST00000368935; ENSP00000357931; ENSG00000143363. [Q86TP1-6]
ENST00000368936; ENSP00000357932; ENSG00000143363. [Q86TP1-3]
ENST00000368937; ENSP00000357933; ENSG00000143363. [Q86TP1-5]
GeneID58497.
KEGGhsa:58497.
UCSCuc001ewh.1. human. [Q86TP1-1]
uc001ewj.1. human. [Q86TP1-6]
uc001ewk.1. human. [Q86TP1-5]
uc010pco.1. human. [Q86TP1-7]

Organism-specific databases

CTD58497.
GeneCardsGC01P150980.
H-InvDBHIX0001042.
HGNCHGNC:13420. PRUNE.
HPAHPA028411.
neXtProtNX_Q86TP1.
PharmGKBPA134939749.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1227.
HOVERGENHBG058142.
InParanoidQ86TP1.
KOK01514.
OMAIYMDLEA.
PhylomeDBQ86TP1.
TreeFamTF323914.

Gene expression databases

ArrayExpressQ86TP1.
BgeeQ86TP1.
CleanExHS_PRUNE.
GenevestigatorQ86TP1.

Family and domain databases

InterProIPR004097. DHHA2.
IPR001667. Pesterase_RecJ.
[Graphical view]
PfamPF01368. DHH. 1 hit.
PF02833. DHHA2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi58497.
NextBio64992.
PROQ86TP1.

Entry information

Entry namePRUNE_HUMAN
AccessionPrimary (citable) accession number: Q86TP1
Secondary accession number(s): B2RCH8 expand/collapse secondary AC list , B4DFL7, Q5SZF9, Q659E5, Q6P4E0, Q8N654, Q96JU5, Q9C071, Q9C072, Q9UIV0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM