Q86TP1 (PRUNE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Evidence 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 junction › focal 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 component	Cell junction Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	inorganic diphosphatase activity Inferred from electronic annotation. Source: EC manganese ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NME1	P15531	2	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 453	453	Protein prune homolog		PRO_0000337987
Regions
	Region	393 – 420	28	Essential for homodimerization
	Motif	106 – 108	3	DHH motif
Sites
	Metal binding	28	1	Manganese 1 By similarity
	Metal binding	30	1	Manganese 2 By similarity
	Metal binding	106	1	Manganese 1 By similarity
	Metal binding	106	1	Manganese 2 By similarity
	Metal binding	179	1	Manganese 2 By similarity
Natural variations
	Alternative sequence	1 – 232	232	Missing in isoform 6 and isoform 7.		VSP_034013
	Alternative sequence	1 – 182	182	Missing in isoform 3 and isoform 5.		VSP_034014
	Alternative sequence	15 – 174	160	Missing in isoform 4.		VSP_034015
	Alternative sequence	45 – 112	68	TTEAE…HILSK → A in isoform 2.		VSP_034016
	Alternative sequence	259 – 311	53	Missing in isoform 4, isoform 5 and isoform 6.		VSP_034017
	Natural variant	397	1	G → R. Corresponds to variant rs3738477 [ dbSNP | Ensembl ].		VAR_059559
	Natural variant	397	1	G → S. Corresponds to variant rs3738477 [ dbSNP | Ensembl ].		VAR_043728
Experimental info
	Mutagenesis	28	1	D → 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
	Mutagenesis	106	1	D → 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
	Mutagenesis	126 – 129	4	DHRP → AAAA: Partial loss of cAMP PDE activity. Ref.10
	Mutagenesis	179	1	D → A: Partial loss of cAMP PDE activity. Partial loss of cAMP PDE activity; when associated with D-28 and D-106. Ref.10
	Sequence conflict	14	1	E → A in AAK00592. Ref.2
	Sequence conflict	19 – 22	4	HVVL → AWHE in AAF04914. Ref.7
	Sequence conflict	221	1	A → V in AAC95290. Ref.1
	Sequence conflict	221	1	A → V in AAF04914. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 34BE1909AB89DBD5	FASTA	453	50,200
	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
	Isoform 2 [UniParc]. Checksum: 6E3355352353B0A5	FASTA	386	42,456
	10 20 30 40 50 60 MEDYLQGCRA ALQESRPLHV VLGNEACDLD STVSALALAF YLAKASDTAL EEAVAEVLDH 70 80 90 100 110 120 RPIEPKHCPP CHVSVELVGS CATLVTERIL QGAPEILDRQ TAALLHGTII LDCVNMDLKI 130 140 150 160 170 180 GKATPKDSKY VEKLEALFPD LPKRNDIFDS LQKAKFDVSG LTTEQMLRKD QKTIYRQGVK 190 200 210 220 230 240 VAISAIYMDL EAFLQRSNLL ADLHAFCQAH SYDVLVAMTI FFNTHNEPVR QLAIFCPHVA 250 260 270 280 290 300 LQTTICEVLE RSHSPPLKLT PASSTHPNLH AYLQGNTQVS RKKLLPLLQE ALSAYFDSMK 310 320 330 340 350 360 IPSGQPETAD VSREQVDKEL DRASNSLISG LSQDEEDPPL PPTPMNSLVD ECPLDQGLPK 370 380 LSAEAVFEKC SQISLSQSTT ASLSKK
	Isoform 3 [UniParc]. Checksum: EADC5693A59D308F	FASTA	271	30,127
	10 20 30 40 50 60 MDLKIGKATP KDSKYVEKLE ALFPDLPKRN DIFDSLQKAK FDVSGLTTEQ MLRKDQKTIY 70 80 90 100 110 120 RQGVKVAISA IYMDLEAFLQ RSNLLADLHA FCQAHSYDVL VAMTIFFNTH NEPVRQLAIF 130 140 150 160 170 180 CPHVALQTTI CEVLERSHSP PLKLTPASST HPNLHAYLQG NTQVSRKKLL PLLQEALSAY 190 200 210 220 230 240 FDSMKIPSGQ PETADVSREQ VDKELDRASN SLISGLSQDE EDPPLPPTPM NSLVDECPLD 250 260 270 QGLPKLSAEA VFEKCSQISL SQSTTASLSK K
	Isoform 4 [UniParc]. Checksum: 7D8897402A2B3136	FASTA	240	26,611
	10 20 30 40 50 60 MEDYLQGCRA ALQETIILDC VNMDLKIGKA TPKDSKYVEK LEALFPDLPK RNDIFDSLQK 70 80 90 100 110 120 AKFDVSGLTT EQMLRKDQKT IYRQGVKVAI SAIYMDLEIC EVLERSHSPP LKLTPASSTH 130 140 150 160 170 180 PNLHAYLQGN TQVSRKKLLP LLQEALSAYF DSMKIPSGQP ETADVSREQV DKELDRASNS 190 200 210 220 230 240 LISGLSQDEE DPPLPPTPMN SLVDECPLDQ GLPKLSAEAV FEKCSQISLS QSTTASLSKK
	Isoform 5 [UniParc]. Checksum: DC0632A96FDD07EE	FASTA	218	24,131
	10 20 30 40 50 60 MDLKIGKATP KDSKYVEKLE ALFPDLPKRN DIFDSLQKAK FDVSGLTTEQ MLRKDQKTIY 70 80 90 100 110 120 RQGVKVAISA IYMDLEICEV LERSHSPPLK LTPASSTHPN LHAYLQGNTQ VSRKKLLPLL 130 140 150 160 170 180 QEALSAYFDS MKIPSGQPET ADVSREQVDK ELDRASNSLI SGLSQDEEDP PLPPTPMNSL 190 200 210 VDECPLDQGL PKLSAEAVFE KCSQISLSQS TTASLSKK
	Isoform 6 [UniParc]. Checksum: 54405F7EA079B5C2	FASTA	168	18,478
	10 20 30 40 50 60 MLRKDQKTIY RQGVKVAISA IYMDLEICEV LERSHSPPLK LTPASSTHPN LHAYLQGNTQ 70 80 90 100 110 120 VSRKKLLPLL QEALSAYFDS MKIPSGQPET ADVSREQVDK ELDRASNSLI SGLSQDEEDP 130 140 150 160 PLPPTPMNSL VDECPLDQGL PKLSAEAVFE KCSQISLSQS TTASLSKK
	Isoform 7 [UniParc]. Checksum: 108DE09A66C5F957	FASTA	221	24,475
	10 20 30 40 50 60 MLRKDQKTIY RQGVKVAISA IYMDLEAFLQ RSNLLADLHA FCQAHSYDVL VAMTIFFNTH 70 80 90 100 110 120 NEPVRQLAIF CPHVALQTTI CEVLERSHSP PLKLTPASST HPNLHAYLQG NTQVSRKKLL 130 140 150 160 170 180 PLLQEALSAY FDSMKIPSGQ PETADVSREQ VDKELDRASN SLISGLSQDE EDPPLPPTPM 190 200 210 220 NSLVDECPLD QGLPKLSAEA VFEKCSQISL SQSTTASLSK K

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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. , 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].

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.
IPI	IPI00028177. IPI00155261. IPI00166931. IPI00645747. IPI00895809. IPI00895854. IPI00929544.
RefSeq	NP_067045.1. NM_021222.1.
UniGene	Hs.78524.
3D structure databases
ProteinModelPortal	Q86TP1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q86TP1. 2 interactions.
PTM databases
PhosphoSite	Q86TP1.
Polymorphism databases
DMDM	229462737.
Proteomic databases
PaxDb	Q86TP1.
PRIDE	Q86TP1.
Protocols and materials databases
DNASU	58497.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000271620; ENSP00000271620; ENSG00000143363. ENST00000368934; ENSP00000357930; ENSG00000143363. ENST00000368935; ENSP00000357931; ENSG00000143363. ENST00000368936; ENSP00000357932; ENSG00000143363. ENST00000368937; ENSP00000357933; ENSG00000143363.
GeneID	58497.
KEGG	hsa:58497.
UCSC	uc001ewh.1. human. uc001ewj.1. human. uc001ewk.1. human. uc010pco.1. human.
Organism-specific databases
CTD	58497.
GeneCards	GC01P150980.
H-InvDB	HIX0001042.
HGNC	HGNC:13420. PRUNE.
HPA	HPA028411.
neXtProt	NX_Q86TP1.
PharmGKB	PA134939749.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1227.
HOVERGEN	HBG058142.
InParanoid	Q86TP1.
KO	K01514.
OMA	IYMDLEA.
OrthoDB	EOG46Q6SG.
PhylomeDB	Q86TP1.
Gene expression databases
ArrayExpress	Q86TP1.
Bgee	Q86TP1.
CleanEx	HS_PRUNE.
Genevestigator	Q86TP1.
Family and domain databases
InterPro	IPR004097. DHHA2. IPR001667. Pesterase_RecJ. [Graphical view]
Pfam	PF01368. DHH. 1 hit. PF02833. DHHA2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	58497.
NextBio	64992.

Entry information

Entry name

PRUNE_HUMAN

Accession

Primary (citable) accession number: Q86TP1
Secondary accession number(s): B2RCH8 , 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:	May 1, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.