Full text data of PIN4
PIN4
[Confidence: high (present in two of the MS resources)]
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4; 5.2.1.8 (Parvulin-14; Par14; hPar14; Parvulin-17; Par17; hPar17; Peptidyl-prolyl cis-trans isomerase Pin4; PPIase Pin4; Peptidyl-prolyl cis/trans isomerase EPVH; hEPVH; Rotamase Pin4)
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4; 5.2.1.8 (Parvulin-14; Par14; hPar14; Parvulin-17; Par17; hPar17; Peptidyl-prolyl cis-trans isomerase Pin4; PPIase Pin4; Peptidyl-prolyl cis/trans isomerase EPVH; hEPVH; Rotamase Pin4)
hRBCD
IPI00006658
IPI00006658 protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting, 4 (parvulin) protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting, 4 (parvulin) membrane n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a mitochondrial matrix n/a expected molecular weight found in band < 14 kDa
IPI00006658 protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting, 4 (parvulin) protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting, 4 (parvulin) membrane n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a mitochondrial matrix n/a expected molecular weight found in band < 14 kDa
UniProt
Q9Y237
ID PIN4_HUMAN Reviewed; 131 AA.
AC Q9Y237; A8E0G6; B3KXM0; F5H1P5; Q0D2H3; Q3MHV0; Q52M21; Q5HYW6;
read moreAC Q6IRW4;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4;
DE EC=5.2.1.8;
DE AltName: Full=Parvulin-14;
DE Short=Par14;
DE Short=hPar14;
DE AltName: Full=Parvulin-17;
DE Short=Par17;
DE Short=hPar17;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin4;
DE Short=PPIase Pin4;
DE AltName: Full=Peptidyl-prolyl cis/trans isomerase EPVH;
DE Short=hEPVH;
DE AltName: Full=Rotamase Pin4;
GN Name=PIN4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=10364457; DOI=10.1006/bbrc.1999.0828;
RA Rulten S.L., Thorpe J.R., Kay J.E.;
RT "Identification of eukaryotic parvulin homologues: a new subfamily of
RT peptidylprolyl cis-trans isomerases.";
RL Biochem. Biophys. Res. Commun. 259:557-562(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=10100858; DOI=10.1016/S0014-5793(99)00239-2;
RA Uchida T., Fujimori F., Tradler T., Fischer G., Rahfeld J.-U.;
RT "Identification and characterization of a 14 kDa human protein as a
RT novel parvulin-like peptidyl prolyl cis/trans isomerase.";
RL FEBS Lett. 446:278-282(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP VARIANTS GLN-16 AND ARG-18 (ISOFORM 2).
RC TISSUE=Brain, Prostate, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-13 (ISOFORM 1), PARTIAL NUCLEOTIDE
RP SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE PROMOTER USAGE, SUMOYLATION,
RP TISSUE SPECIFICITY, AND VARIANTS GLN-16 AND ARG-18 (ISOFORM 2).
RX PubMed=16522211; DOI=10.1186/1471-2199-7-9;
RA Mueller J.W., Kessler D., Neumann D., Stratmann T., Papatheodorou P.,
RA Hartmann-Fatu C., Bayer P.;
RT "Characterization of novel elongated Parvulin isoforms that are
RT ubiquitously expressed in human tissues and originate from alternative
RT transcription initiation.";
RL BMC Mol. Biol. 7:9-9(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6 AND 48-72, ALTERNATIVE
RP PROMOTER USAGE (ISOFORMS 1 AND 2), DNA-BINDING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17875217; DOI=10.1186/1741-7007-5-37;
RA Kessler D., Papatheodorou P., Stratmann T., Dian E.A.,
RA Hartmann-Fatu C., Rassow J., Bayer P., Mueller J.W.;
RT "The DNA binding parvulin Par17 is targeted to the mitochondrial
RT matrix by a recently evolved prepeptide uniquely present in
RT Hominidae.";
RL BMC Biol. 5:37-37(2007).
RN [7]
RP PROTEIN SEQUENCE OF 15-25, IDENTIFICATION BY MASS SPECTROMETRY,
RP PHOSPHORYLATION AT SER-19, MUTAGENESIS OF SER-19, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12860119; DOI=10.1016/S0022-2836(03)00713-7;
RA Reimer T., Weiwad M., Schierhorn A., Ruecknagel P.-K., Rahfeld J.-U.,
RA Bayer P., Fischer G.;
RT "Phosphorylation of the N-terminal domain regulates subcellular
RT localization and DNA binding properties of the peptidyl-prolyl
RT cis/trans isomerase hPar14.";
RL J. Mol. Biol. 330:955-966(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-131 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP DNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=12144781; DOI=10.1016/S0022-2836(02)00615-0;
RA Surmacz T.A., Bayer E., Rahfeld J.-U., Fischer G., Bayer P.;
RT "The N-terminal basic domain of human parvulin hPar14 is responsible
RT for the entry to the nucleus and high-affinity DNA-binding.";
RL J. Mol. Biol. 321:235-247(2002).
RN [10]
RP FUNCTION, IDENTIFICATION IN PRE-RRNP COMPLEXES, PHOSPHORYLATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19369196; DOI=10.1074/mcp.M900147-MCP200;
RA Fujiyama-Nakamura S., Yoshikawa H., Homma K., Hayano T.,
RA Tsujimura-Takahashi T., Izumikawa K., Ishikawa H., Miyazawa N.,
RA Yanagida M., Miura Y., Shinkawa T., Yamauchi Y., Isobe T.,
RA Takahashi N.;
RT "Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel
RT rRNA processing factor that evolved in the metazoan lineage.";
RL Mol. Cell. Proteomics 8:1552-1565(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP STRUCTURE BY NMR OF 36-131.
RX PubMed=10966801; DOI=10.1006/jmbi.2000.4013;
RA Sekerina E., Rahfeld J.-U., Mueller J., Fanghaenel J., Rascher C.,
RA Fischer G., Bayer P.;
RT "NMR solution structure of hPar14 reveals similarity to the peptidyl
RT prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but
RT indicates a different functionality of the protein.";
RL J. Mol. Biol. 301:1003-1017(2000).
RN [13]
RP STRUCTURE BY NMR OF 28-131.
RX PubMed=11162102; DOI=10.1006/jmbi.2000.4293;
RA Terada T., Shirouzu M., Fukumori Y., Fujimori F., Ito Y., Kigawa T.,
RA Yokoyama S., Uchida T.;
RT "Solution structure of the human parvulin-like peptidyl prolyl
RT cis/trans isomerase, hPar14.";
RL J. Mol. Biol. 305:917-926(2001).
CC -!- FUNCTION: Isoform 1 is involved as a ribosomal RNA processing
CC factor in ribosome biogenesis. Binds to tightly bent AT-rich
CC stretches of double-stranded DNA.
CC -!- FUNCTION: Isoform 2 binds to double-stranded DNA.
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- SUBUNIT: Isoform 1 is found in pre-ribosomal ribonucleoprotein
CC (pre-rRNP) complexes (By similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus. Cytoplasm,
CC cytoskeleton, spindle. Cytoplasm. Note=Colocalizes in the
CC nucleolus during interphase and on the spindle apparatus during
CC mitosis with NPM1.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Mitochondrion. Mitochondrion
CC matrix. Note=Imported in a time- and membrane potential-dependent
CC manner to the mitochondrial matrix, but without concomitant
CC processing of the protein. Directed to mitochondria by a novel N-
CC terminal domain that functions as non-cleavable mitochondrial
CC targeting peptide.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y237-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y237-2; Sequence=VSP_037754;
CC Note=The first 25 amino acids are sufficient for mitochondrial
CC targeting. Variant in position: 16:R->Q (in dbSNP:rs6525589).
CC Variant in position: 18:S->R (in dbSNP:rs7058353);
CC Name=3;
CC IsoId=Q9Y237-3; Sequence=VSP_037754, VSP_046122;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Isoform 2 is much more stable than isoform 1
CC (at protein level). Ubiquitous. Isoform 1 and isoform 2 are
CC expressed in kidney, liver, blood vessel, brain, mammary gland,
CC skeletal muscle, small intestine and submandibularis. Isoform 1
CC transcripts are much more abundant than isoform 2 in each tissue
CC analyzed.
CC -!- DOMAIN: The PPIase domain enhances mitochondrial targeting.
CC -!- PTM: Phosphorylated. Isoform 1 phosphorylation occurs both in the
CC nucleus and the cytoplasm. Isoform 1 phosphorylation at Ser-19
CC does not affect its PPIase activity but is required for nuclear
CC localization, and the dephosphorylation is a prerequisite for the
CC binding to DNA. The unphosphorylated isoform 1 associates with the
CC pre-rRNP complexes in the nucleus.
CC -!- PTM: Isoform 2 is sumoylated with SUMO2 and SUMO3.
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4
CC subfamily.
CC -!- SIMILARITY: Contains 1 PpiC domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05234.2; Type=Erroneous initiation;
CC Sequence=AAH70288.1; Type=Erroneous initiation;
CC Sequence=AAI04654.1; Type=Erroneous initiation;
CC Sequence=AAI11395.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAG54532.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF143096; AAD27893.1; -; mRNA.
DR EMBL; AB009690; BAA82320.1; -; mRNA.
DR EMBL; BX119917; CAI39856.1; -; Genomic_DNA.
DR EMBL; AL135749; CAI39856.1; JOINED; Genomic_DNA.
DR EMBL; BC005234; AAH05234.2; ALT_INIT; mRNA.
DR EMBL; BC070288; AAH70288.1; ALT_INIT; mRNA.
DR EMBL; BC093700; AAH93700.1; -; mRNA.
DR EMBL; BC104653; AAI04654.1; ALT_INIT; mRNA.
DR EMBL; BC111394; AAI11395.1; ALT_INIT; mRNA.
DR EMBL; BC112281; AAI12282.1; -; mRNA.
DR EMBL; AM420633; CAM12362.1; -; Genomic_DNA.
DR EMBL; AK127605; BAG54532.1; ALT_INIT; mRNA.
DR RefSeq; NP_001164218.1; NM_001170747.1.
DR RefSeq; NP_006214.2; NM_006223.3.
DR UniGene; Hs.655623; -.
DR PDB; 1EQ3; NMR; -; A=36-131.
DR PDB; 1FJD; NMR; -; A=30-131.
DR PDB; 3UI4; X-ray; 0.80 A; A=36-131.
DR PDB; 3UI5; X-ray; 1.40 A; A=36-131.
DR PDB; 3UI6; X-ray; 0.89 A; A=36-131.
DR PDBsum; 1EQ3; -.
DR PDBsum; 1FJD; -.
DR PDBsum; 3UI4; -.
DR PDBsum; 3UI5; -.
DR PDBsum; 3UI6; -.
DR ProteinModelPortal; Q9Y237; -.
DR SMR; Q9Y237; 36-131.
DR DIP; DIP-50838N; -.
DR IntAct; Q9Y237; 6.
DR STRING; 9606.ENSP00000218432; -.
DR BindingDB; Q9Y237; -.
DR ChEMBL; CHEMBL4923; -.
DR PhosphoSite; Q9Y237; -.
DR DMDM; 20139299; -.
DR PaxDb; Q9Y237; -.
DR PRIDE; Q9Y237; -.
DR DNASU; 5303; -.
DR Ensembl; ENST00000373669; ENSP00000362773; ENSG00000102309.
DR Ensembl; ENST00000423432; ENSP00000409154; ENSG00000102309.
DR GeneID; 5303; -.
DR KEGG; hsa:5303; -.
DR UCSC; uc004eao.2; human.
DR CTD; 5303; -.
DR GeneCards; GC0XP071401; -.
DR H-InvDB; HIX0016866; -.
DR HGNC; HGNC:8992; PIN4.
DR HPA; HPA054483; -.
DR MIM; 300252; gene.
DR neXtProt; NX_Q9Y237; -.
DR PharmGKB; PA33324; -.
DR eggNOG; COG0760; -.
DR HOVERGEN; HBG019150; -.
DR InParanoid; Q9Y237; -.
DR KO; K09579; -.
DR OMA; KSGMKFN; -.
DR EvolutionaryTrace; Q9Y237; -.
DR GeneWiki; PIN4; -.
DR GenomeRNAi; 5303; -.
DR NextBio; 20496; -.
DR PRO; PR:Q9Y237; -.
DR ArrayExpress; Q9Y237; -.
DR Bgee; Q9Y237; -.
DR CleanEx; HS_PIN4; -.
DR Genevestigator; Q9Y237; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0030684; C:preribosome; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0003681; F:bent DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR InterPro; IPR000297; PPIase_PpiC.
DR PROSITE; PS01096; PPIC_PPIASE_1; FALSE_NEG.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Complete proteome;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; DNA-binding;
KW Isomerase; Mitochondrion; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Rotamase; Ubl conjugation.
FT CHAIN 1 131 Peptidyl-prolyl cis-trans isomerase NIMA-
FT interacting 4.
FT /FTId=PRO_0000193438.
FT DOMAIN 35 129 PpiC.
FT REGION 1 41 Necessary for association with the pre-
FT rRNP complexes.
FT REGION 1 25 Necessary for nuclear localization and
FT DNA-binding.
FT MOD_RES 19 19 Phosphoserine; by CK2.
FT VAR_SEQ 1 1 M -> MPMAGLLKGLVRQLERFSVQQQASKM (in
FT isoform 2 and isoform 3).
FT /FTId=VSP_037754.
FT VAR_SEQ 80 131 GDLGWMTRGSMVGPFQEAAFALPVSGMDKPVFTDPPVKTKF
FT GYHIIMVEGRK -> IPSLQQHAGHHRDLRSTLISLVSYLQ
FT TTP (in isoform 3).
FT /FTId=VSP_046122.
FT MUTAGEN 19 19 S->A: Abolishes phosphorylation and
FT reduces strongly nuclear localization.
FT MUTAGEN 19 19 S->E: Does not abolish nuclear
FT localization and reduces DNA-binding
FT ability.
FT STRAND 37 47
FT HELIX 48 59
FT HELIX 64 71
FT STRAND 73 75
FT HELIX 76 78
FT STRAND 81 86
FT HELIX 92 99
FT TURN 108 110
FT STRAND 116 118
FT STRAND 121 130
SQ SEQUENCE 131 AA; 13810 MW; 787C15BDB0701258 CRC64;
MPPKGKSGSG KAGKGGAASG SDSADKKAQG PKGGGNAVKV RHILCEKHGK IMEAMEKLKS
GMRFNEVAAQ YSEDKARQGG DLGWMTRGSM VGPFQEAAFA LPVSGMDKPV FTDPPVKTKF
GYHIIMVEGR K
//
ID PIN4_HUMAN Reviewed; 131 AA.
AC Q9Y237; A8E0G6; B3KXM0; F5H1P5; Q0D2H3; Q3MHV0; Q52M21; Q5HYW6;
read moreAC Q6IRW4;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4;
DE EC=5.2.1.8;
DE AltName: Full=Parvulin-14;
DE Short=Par14;
DE Short=hPar14;
DE AltName: Full=Parvulin-17;
DE Short=Par17;
DE Short=hPar17;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin4;
DE Short=PPIase Pin4;
DE AltName: Full=Peptidyl-prolyl cis/trans isomerase EPVH;
DE Short=hEPVH;
DE AltName: Full=Rotamase Pin4;
GN Name=PIN4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=10364457; DOI=10.1006/bbrc.1999.0828;
RA Rulten S.L., Thorpe J.R., Kay J.E.;
RT "Identification of eukaryotic parvulin homologues: a new subfamily of
RT peptidylprolyl cis-trans isomerases.";
RL Biochem. Biophys. Res. Commun. 259:557-562(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=10100858; DOI=10.1016/S0014-5793(99)00239-2;
RA Uchida T., Fujimori F., Tradler T., Fischer G., Rahfeld J.-U.;
RT "Identification and characterization of a 14 kDa human protein as a
RT novel parvulin-like peptidyl prolyl cis/trans isomerase.";
RL FEBS Lett. 446:278-282(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP VARIANTS GLN-16 AND ARG-18 (ISOFORM 2).
RC TISSUE=Brain, Prostate, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-13 (ISOFORM 1), PARTIAL NUCLEOTIDE
RP SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE PROMOTER USAGE, SUMOYLATION,
RP TISSUE SPECIFICITY, AND VARIANTS GLN-16 AND ARG-18 (ISOFORM 2).
RX PubMed=16522211; DOI=10.1186/1471-2199-7-9;
RA Mueller J.W., Kessler D., Neumann D., Stratmann T., Papatheodorou P.,
RA Hartmann-Fatu C., Bayer P.;
RT "Characterization of novel elongated Parvulin isoforms that are
RT ubiquitously expressed in human tissues and originate from alternative
RT transcription initiation.";
RL BMC Mol. Biol. 7:9-9(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6 AND 48-72, ALTERNATIVE
RP PROMOTER USAGE (ISOFORMS 1 AND 2), DNA-BINDING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17875217; DOI=10.1186/1741-7007-5-37;
RA Kessler D., Papatheodorou P., Stratmann T., Dian E.A.,
RA Hartmann-Fatu C., Rassow J., Bayer P., Mueller J.W.;
RT "The DNA binding parvulin Par17 is targeted to the mitochondrial
RT matrix by a recently evolved prepeptide uniquely present in
RT Hominidae.";
RL BMC Biol. 5:37-37(2007).
RN [7]
RP PROTEIN SEQUENCE OF 15-25, IDENTIFICATION BY MASS SPECTROMETRY,
RP PHOSPHORYLATION AT SER-19, MUTAGENESIS OF SER-19, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12860119; DOI=10.1016/S0022-2836(03)00713-7;
RA Reimer T., Weiwad M., Schierhorn A., Ruecknagel P.-K., Rahfeld J.-U.,
RA Bayer P., Fischer G.;
RT "Phosphorylation of the N-terminal domain regulates subcellular
RT localization and DNA binding properties of the peptidyl-prolyl
RT cis/trans isomerase hPar14.";
RL J. Mol. Biol. 330:955-966(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-131 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP DNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=12144781; DOI=10.1016/S0022-2836(02)00615-0;
RA Surmacz T.A., Bayer E., Rahfeld J.-U., Fischer G., Bayer P.;
RT "The N-terminal basic domain of human parvulin hPar14 is responsible
RT for the entry to the nucleus and high-affinity DNA-binding.";
RL J. Mol. Biol. 321:235-247(2002).
RN [10]
RP FUNCTION, IDENTIFICATION IN PRE-RRNP COMPLEXES, PHOSPHORYLATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19369196; DOI=10.1074/mcp.M900147-MCP200;
RA Fujiyama-Nakamura S., Yoshikawa H., Homma K., Hayano T.,
RA Tsujimura-Takahashi T., Izumikawa K., Ishikawa H., Miyazawa N.,
RA Yanagida M., Miura Y., Shinkawa T., Yamauchi Y., Isobe T.,
RA Takahashi N.;
RT "Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel
RT rRNA processing factor that evolved in the metazoan lineage.";
RL Mol. Cell. Proteomics 8:1552-1565(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP STRUCTURE BY NMR OF 36-131.
RX PubMed=10966801; DOI=10.1006/jmbi.2000.4013;
RA Sekerina E., Rahfeld J.-U., Mueller J., Fanghaenel J., Rascher C.,
RA Fischer G., Bayer P.;
RT "NMR solution structure of hPar14 reveals similarity to the peptidyl
RT prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but
RT indicates a different functionality of the protein.";
RL J. Mol. Biol. 301:1003-1017(2000).
RN [13]
RP STRUCTURE BY NMR OF 28-131.
RX PubMed=11162102; DOI=10.1006/jmbi.2000.4293;
RA Terada T., Shirouzu M., Fukumori Y., Fujimori F., Ito Y., Kigawa T.,
RA Yokoyama S., Uchida T.;
RT "Solution structure of the human parvulin-like peptidyl prolyl
RT cis/trans isomerase, hPar14.";
RL J. Mol. Biol. 305:917-926(2001).
CC -!- FUNCTION: Isoform 1 is involved as a ribosomal RNA processing
CC factor in ribosome biogenesis. Binds to tightly bent AT-rich
CC stretches of double-stranded DNA.
CC -!- FUNCTION: Isoform 2 binds to double-stranded DNA.
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- SUBUNIT: Isoform 1 is found in pre-ribosomal ribonucleoprotein
CC (pre-rRNP) complexes (By similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus. Cytoplasm,
CC cytoskeleton, spindle. Cytoplasm. Note=Colocalizes in the
CC nucleolus during interphase and on the spindle apparatus during
CC mitosis with NPM1.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Mitochondrion. Mitochondrion
CC matrix. Note=Imported in a time- and membrane potential-dependent
CC manner to the mitochondrial matrix, but without concomitant
CC processing of the protein. Directed to mitochondria by a novel N-
CC terminal domain that functions as non-cleavable mitochondrial
CC targeting peptide.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y237-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y237-2; Sequence=VSP_037754;
CC Note=The first 25 amino acids are sufficient for mitochondrial
CC targeting. Variant in position: 16:R->Q (in dbSNP:rs6525589).
CC Variant in position: 18:S->R (in dbSNP:rs7058353);
CC Name=3;
CC IsoId=Q9Y237-3; Sequence=VSP_037754, VSP_046122;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Isoform 2 is much more stable than isoform 1
CC (at protein level). Ubiquitous. Isoform 1 and isoform 2 are
CC expressed in kidney, liver, blood vessel, brain, mammary gland,
CC skeletal muscle, small intestine and submandibularis. Isoform 1
CC transcripts are much more abundant than isoform 2 in each tissue
CC analyzed.
CC -!- DOMAIN: The PPIase domain enhances mitochondrial targeting.
CC -!- PTM: Phosphorylated. Isoform 1 phosphorylation occurs both in the
CC nucleus and the cytoplasm. Isoform 1 phosphorylation at Ser-19
CC does not affect its PPIase activity but is required for nuclear
CC localization, and the dephosphorylation is a prerequisite for the
CC binding to DNA. The unphosphorylated isoform 1 associates with the
CC pre-rRNP complexes in the nucleus.
CC -!- PTM: Isoform 2 is sumoylated with SUMO2 and SUMO3.
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4
CC subfamily.
CC -!- SIMILARITY: Contains 1 PpiC domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05234.2; Type=Erroneous initiation;
CC Sequence=AAH70288.1; Type=Erroneous initiation;
CC Sequence=AAI04654.1; Type=Erroneous initiation;
CC Sequence=AAI11395.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAG54532.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF143096; AAD27893.1; -; mRNA.
DR EMBL; AB009690; BAA82320.1; -; mRNA.
DR EMBL; BX119917; CAI39856.1; -; Genomic_DNA.
DR EMBL; AL135749; CAI39856.1; JOINED; Genomic_DNA.
DR EMBL; BC005234; AAH05234.2; ALT_INIT; mRNA.
DR EMBL; BC070288; AAH70288.1; ALT_INIT; mRNA.
DR EMBL; BC093700; AAH93700.1; -; mRNA.
DR EMBL; BC104653; AAI04654.1; ALT_INIT; mRNA.
DR EMBL; BC111394; AAI11395.1; ALT_INIT; mRNA.
DR EMBL; BC112281; AAI12282.1; -; mRNA.
DR EMBL; AM420633; CAM12362.1; -; Genomic_DNA.
DR EMBL; AK127605; BAG54532.1; ALT_INIT; mRNA.
DR RefSeq; NP_001164218.1; NM_001170747.1.
DR RefSeq; NP_006214.2; NM_006223.3.
DR UniGene; Hs.655623; -.
DR PDB; 1EQ3; NMR; -; A=36-131.
DR PDB; 1FJD; NMR; -; A=30-131.
DR PDB; 3UI4; X-ray; 0.80 A; A=36-131.
DR PDB; 3UI5; X-ray; 1.40 A; A=36-131.
DR PDB; 3UI6; X-ray; 0.89 A; A=36-131.
DR PDBsum; 1EQ3; -.
DR PDBsum; 1FJD; -.
DR PDBsum; 3UI4; -.
DR PDBsum; 3UI5; -.
DR PDBsum; 3UI6; -.
DR ProteinModelPortal; Q9Y237; -.
DR SMR; Q9Y237; 36-131.
DR DIP; DIP-50838N; -.
DR IntAct; Q9Y237; 6.
DR STRING; 9606.ENSP00000218432; -.
DR BindingDB; Q9Y237; -.
DR ChEMBL; CHEMBL4923; -.
DR PhosphoSite; Q9Y237; -.
DR DMDM; 20139299; -.
DR PaxDb; Q9Y237; -.
DR PRIDE; Q9Y237; -.
DR DNASU; 5303; -.
DR Ensembl; ENST00000373669; ENSP00000362773; ENSG00000102309.
DR Ensembl; ENST00000423432; ENSP00000409154; ENSG00000102309.
DR GeneID; 5303; -.
DR KEGG; hsa:5303; -.
DR UCSC; uc004eao.2; human.
DR CTD; 5303; -.
DR GeneCards; GC0XP071401; -.
DR H-InvDB; HIX0016866; -.
DR HGNC; HGNC:8992; PIN4.
DR HPA; HPA054483; -.
DR MIM; 300252; gene.
DR neXtProt; NX_Q9Y237; -.
DR PharmGKB; PA33324; -.
DR eggNOG; COG0760; -.
DR HOVERGEN; HBG019150; -.
DR InParanoid; Q9Y237; -.
DR KO; K09579; -.
DR OMA; KSGMKFN; -.
DR EvolutionaryTrace; Q9Y237; -.
DR GeneWiki; PIN4; -.
DR GenomeRNAi; 5303; -.
DR NextBio; 20496; -.
DR PRO; PR:Q9Y237; -.
DR ArrayExpress; Q9Y237; -.
DR Bgee; Q9Y237; -.
DR CleanEx; HS_PIN4; -.
DR Genevestigator; Q9Y237; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0030684; C:preribosome; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0003681; F:bent DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR InterPro; IPR000297; PPIase_PpiC.
DR PROSITE; PS01096; PPIC_PPIASE_1; FALSE_NEG.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Complete proteome;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; DNA-binding;
KW Isomerase; Mitochondrion; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Rotamase; Ubl conjugation.
FT CHAIN 1 131 Peptidyl-prolyl cis-trans isomerase NIMA-
FT interacting 4.
FT /FTId=PRO_0000193438.
FT DOMAIN 35 129 PpiC.
FT REGION 1 41 Necessary for association with the pre-
FT rRNP complexes.
FT REGION 1 25 Necessary for nuclear localization and
FT DNA-binding.
FT MOD_RES 19 19 Phosphoserine; by CK2.
FT VAR_SEQ 1 1 M -> MPMAGLLKGLVRQLERFSVQQQASKM (in
FT isoform 2 and isoform 3).
FT /FTId=VSP_037754.
FT VAR_SEQ 80 131 GDLGWMTRGSMVGPFQEAAFALPVSGMDKPVFTDPPVKTKF
FT GYHIIMVEGRK -> IPSLQQHAGHHRDLRSTLISLVSYLQ
FT TTP (in isoform 3).
FT /FTId=VSP_046122.
FT MUTAGEN 19 19 S->A: Abolishes phosphorylation and
FT reduces strongly nuclear localization.
FT MUTAGEN 19 19 S->E: Does not abolish nuclear
FT localization and reduces DNA-binding
FT ability.
FT STRAND 37 47
FT HELIX 48 59
FT HELIX 64 71
FT STRAND 73 75
FT HELIX 76 78
FT STRAND 81 86
FT HELIX 92 99
FT TURN 108 110
FT STRAND 116 118
FT STRAND 121 130
SQ SEQUENCE 131 AA; 13810 MW; 787C15BDB0701258 CRC64;
MPPKGKSGSG KAGKGGAASG SDSADKKAQG PKGGGNAVKV RHILCEKHGK IMEAMEKLKS
GMRFNEVAAQ YSEDKARQGG DLGWMTRGSM VGPFQEAAFA LPVSGMDKPV FTDPPVKTKF
GYHIIMVEGR K
//
MIM
300252
*RECORD*
*FIELD* NO
300252
*FIELD* TI
*300252 PEPTIDYL-PROLYL CIS/TRANS ISOMERASE, NIMA-INTERACTING, 4; PIN4
;;PARVULIN 14; PAR14;;
read moreEPVH
*FIELD* TX
The peptidyl-prolyl cis/trans isomerase protein family (PPIases)
consists of the cyclophilin (e.g., PPIA; 123840), FK506-binding protein
(FKBPs, e.g., FKBP1A; 186945), and parvulin subfamilies. PPIases have
diverse functions, but in general they are implicated in the folding,
transport, or assembly of proteins. The human parvulin PIN1 (601052) is
implicated in the regulation of mitosis through interaction with CDC25
(157680) and polo-like kinase-1 (PLX1; see 602098).
CLONING
By searching an EST database using human PIN1 and E. coli parvulin
sequences as probes, followed by screening a lung cDNA library, Uchida
et al. (1999) isolated a cDNA encoding PIN4, which they called PAR14
(parvulin-14). Using a similar method, Rulten et al. (1999) isolated a
cDNA encoding PIN4, which they called EPVH (eukaryotic parvulin
homolog). Sequence analysis predicted that the 131-amino acid PIN4
protein contains a PPIase domain preceded by a 40-amino acid glycine-
and lysine-rich N-terminal sequence. PIN4, however, lacks a WW domain, a
nuclear localization motif, and residues required for phosphoprotein
interactions. Multiple-tissue Northern blot analysis detected variable
expression of an approximately 1.0-kb PIN4 transcript in all tissues
tested, with notably lower expression in neuronal tissue. Transmission
electron microscopy demonstrated preferential localization of PIN4 in
the mitochondrial matrix. Functional analysis failed to show PPIase
activity, possibly due to proteolytic degradation or different substrate
requirements.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PIN4
gene to Xq13 (TMAP sts-H61973).
*FIELD* RF
1. Rulten, S.; Thorpe, J.; Kay, J.: Identification of eukaryotic
parvulin homologues: a new subfamily of peptidylprolyl cis-trans isomerases. Biochem.
Biophys. Res. Commun. 259: 557-562, 1999.
2. Uchida, T.; Fujimori, F.; Tradler, T.; Fischer, G.; Rahfeld, J.-U.
: Identification and characterization of a 14 kDa human protein as
a novel parvulin-like peptidyl prolyl cis/trans isomerase. FEBS Lett. 446:
278-282, 1999.
*FIELD* CD
Paul J. Converse: 7/3/2000
*FIELD* ED
carol: 07/10/2001
mgross: 7/3/2000
*RECORD*
*FIELD* NO
300252
*FIELD* TI
*300252 PEPTIDYL-PROLYL CIS/TRANS ISOMERASE, NIMA-INTERACTING, 4; PIN4
;;PARVULIN 14; PAR14;;
read moreEPVH
*FIELD* TX
The peptidyl-prolyl cis/trans isomerase protein family (PPIases)
consists of the cyclophilin (e.g., PPIA; 123840), FK506-binding protein
(FKBPs, e.g., FKBP1A; 186945), and parvulin subfamilies. PPIases have
diverse functions, but in general they are implicated in the folding,
transport, or assembly of proteins. The human parvulin PIN1 (601052) is
implicated in the regulation of mitosis through interaction with CDC25
(157680) and polo-like kinase-1 (PLX1; see 602098).
CLONING
By searching an EST database using human PIN1 and E. coli parvulin
sequences as probes, followed by screening a lung cDNA library, Uchida
et al. (1999) isolated a cDNA encoding PIN4, which they called PAR14
(parvulin-14). Using a similar method, Rulten et al. (1999) isolated a
cDNA encoding PIN4, which they called EPVH (eukaryotic parvulin
homolog). Sequence analysis predicted that the 131-amino acid PIN4
protein contains a PPIase domain preceded by a 40-amino acid glycine-
and lysine-rich N-terminal sequence. PIN4, however, lacks a WW domain, a
nuclear localization motif, and residues required for phosphoprotein
interactions. Multiple-tissue Northern blot analysis detected variable
expression of an approximately 1.0-kb PIN4 transcript in all tissues
tested, with notably lower expression in neuronal tissue. Transmission
electron microscopy demonstrated preferential localization of PIN4 in
the mitochondrial matrix. Functional analysis failed to show PPIase
activity, possibly due to proteolytic degradation or different substrate
requirements.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PIN4
gene to Xq13 (TMAP sts-H61973).
*FIELD* RF
1. Rulten, S.; Thorpe, J.; Kay, J.: Identification of eukaryotic
parvulin homologues: a new subfamily of peptidylprolyl cis-trans isomerases. Biochem.
Biophys. Res. Commun. 259: 557-562, 1999.
2. Uchida, T.; Fujimori, F.; Tradler, T.; Fischer, G.; Rahfeld, J.-U.
: Identification and characterization of a 14 kDa human protein as
a novel parvulin-like peptidyl prolyl cis/trans isomerase. FEBS Lett. 446:
278-282, 1999.
*FIELD* CD
Paul J. Converse: 7/3/2000
*FIELD* ED
carol: 07/10/2001
mgross: 7/3/2000