PIN4_HUMAN
ID PIN4_HUMAN Reviewed; 131 AA.
AC Q9Y237; A8E0G6; B3KXM0; F5H1P5; Q0D2H3; Q3MHV0; Q52M21; Q5HYW6; Q6IRW4;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 179.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP 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 TISSUE
RP 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 novel
RT 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., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., 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., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., 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., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., 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., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., 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., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA 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 VARIANTS
RP 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 project:
RT 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 SEQUENCE
RP [MRNA] (ISOFORM 2), ALTERNATIVE PROMOTER USAGE, SUMOYLATION, TISSUE
RP 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 PROMOTER
RP USAGE (ISOFORMS 1 AND 2), DNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=17875217; DOI=10.1186/1741-7007-5-37;
RA Kessler D., Papatheodorou P., Stratmann T., Dian E.A., Hartmann-Fatu C.,
RA Rassow J., Bayer P., Mueller J.W.;
RT "The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by
RT a recently evolved prepeptide uniquely present in 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 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 cis/trans
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 for
RT 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., Takahashi N.;
RT "Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA
RT 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., Buerckstuemmer T.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
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 prolyl
RT cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a
RT different functionality of the protein.";
RL J. Mol. Biol. 301:1003-1017(2000).
RN [14]
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 cis/trans
RT isomerase, hPar14.";
RL J. Mol. Biol. 305:917-926(2001).
CC -!- FUNCTION: Isoform 1 is involved as a ribosomal RNA processing factor in
CC ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-
CC stranded DNA. {ECO:0000269|PubMed:19369196}.
CC -!- FUNCTION: Isoform 2 binds to double-stranded DNA.
CC {ECO:0000269|PubMed:19369196}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBUNIT: Isoform 1 is found in pre-ribosomal ribonucleoprotein (pre-
CC rRNP) complexes. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y237; Q9P209: CEP72; NbExp=4; IntAct=EBI-714599, EBI-739498;
CC Q9Y237; Q8IZU0: FAM9B; NbExp=4; IntAct=EBI-714599, EBI-10175124;
CC Q9Y237; Q969F0: FATE1; NbExp=3; IntAct=EBI-714599, EBI-743099;
CC Q9Y237; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-714599, EBI-10178634;
CC Q9Y237; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-714599, EBI-302345;
CC Q9Y237; Q96C00: ZBTB9; NbExp=4; IntAct=EBI-714599, EBI-395708;
CC Q9Y237-2; P43364: MAGEA11; NbExp=3; IntAct=EBI-11749201, EBI-739552;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus. Cytoplasm,
CC cytoskeleton, spindle. Cytoplasm. Note=Colocalizes in the nucleolus
CC during interphase and on the spindle apparatus during mitosis with
CC NPM1.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion. Mitochondrion matrix.
CC Note=Imported in a time- and membrane potential-dependent manner to the
CC mitochondrial matrix, but without concomitant processing of the
CC protein. Directed to mitochondria by a novel N-terminal domain that
CC functions as non-cleavable mitochondrial 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 Name=3;
CC IsoId=Q9Y237-3; Sequence=VSP_037754, VSP_046122;
CC -!- TISSUE SPECIFICITY: Isoform 2 is much more stable than isoform 1 (at
CC protein level). Ubiquitous. Isoform 1 and isoform 2 are expressed in
CC kidney, liver, blood vessel, brain, mammary gland, skeletal muscle,
CC small intestine and submandibularis. Isoform 1 transcripts are much
CC more abundant than isoform 2 in each tissue analyzed.
CC {ECO:0000269|PubMed:10100858, ECO:0000269|PubMed:10364457,
CC ECO:0000269|PubMed:16522211}.
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 does not
CC affect its PPIase activity but is required for nuclear localization,
CC and the dephosphorylation is a prerequisite for the binding to DNA. The
CC unphosphorylated isoform 1 associates with the pre-rRNP complexes in
CC the nucleus. {ECO:0000269|PubMed:12860119,
CC ECO:0000269|PubMed:19369196}.
CC -!- PTM: Isoform 2 is sumoylated with SUMO2 and SUMO3.
CC {ECO:0000269|PubMed:16522211}.
CC -!- MISCELLANEOUS: [Isoform 2]: The first 25 amino acids are sufficient for
CC mitochondrial targeting. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05234.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH70288.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI04654.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI11395.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG54532.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF143096; AAD27893.1; -; mRNA.
DR EMBL; AB009690; BAA82320.1; -; mRNA.
DR EMBL; AL135749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX119917; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS14417.1; -. [Q9Y237-1]
DR CCDS; CCDS55447.1; -. [Q9Y237-3]
DR RefSeq; NP_001164218.1; NM_001170747.1. [Q9Y237-3]
DR RefSeq; NP_006214.2; NM_006223.3. [Q9Y237-1]
DR PDB; 1EQ3; NMR; -; A=36-131.
DR PDB; 1FJD; NMR; -; A=28-131.
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 AlphaFoldDB; Q9Y237; -.
DR BMRB; Q9Y237; -.
DR SMR; Q9Y237; -.
DR BioGRID; 111320; 49.
DR CORUM; Q9Y237; -.
DR DIP; DIP-50838N; -.
DR IntAct; Q9Y237; 21.
DR MINT; Q9Y237; -.
DR STRING; 9606.ENSP00000362773; -.
DR BindingDB; Q9Y237; -.
DR ChEMBL; CHEMBL4923; -.
DR GlyGen; Q9Y237; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y237; -.
DR PhosphoSitePlus; Q9Y237; -.
DR BioMuta; PIN4; -.
DR DMDM; 20139299; -.
DR EPD; Q9Y237; -.
DR jPOST; Q9Y237; -.
DR MassIVE; Q9Y237; -.
DR MaxQB; Q9Y237; -.
DR PaxDb; Q9Y237; -.
DR PeptideAtlas; Q9Y237; -.
DR PRIDE; Q9Y237; -.
DR ProteomicsDB; 25719; -.
DR ProteomicsDB; 85631; -. [Q9Y237-1]
DR ProteomicsDB; 85632; -. [Q9Y237-2]
DR TopDownProteomics; Q9Y237-1; -. [Q9Y237-1]
DR TopDownProteomics; Q9Y237-2; -. [Q9Y237-2]
DR Antibodypedia; 27865; 219 antibodies from 25 providers.
DR DNASU; 5303; -.
DR Ensembl; ENST00000373669.8; ENSP00000362773.3; ENSG00000102309.15. [Q9Y237-1]
DR Ensembl; ENST00000423432.6; ENSP00000409154.2; ENSG00000102309.15. [Q9Y237-3]
DR Ensembl; ENST00000664196.1; ENSP00000499466.1; ENSG00000102309.15. [Q9Y237-2]
DR GeneID; 5303; -.
DR KEGG; hsa:5303; -.
DR MANE-Select; ENST00000373669.8; ENSP00000362773.3; NM_006223.4; NP_006214.3.
DR UCSC; uc004eam.4; human. [Q9Y237-1]
DR CTD; 5303; -.
DR DisGeNET; 5303; -.
DR GeneCards; PIN4; -.
DR HGNC; HGNC:8992; PIN4.
DR HPA; ENSG00000102309; Low tissue specificity.
DR MIM; 300252; gene.
DR neXtProt; NX_Q9Y237; -.
DR OpenTargets; ENSG00000102309; -.
DR PharmGKB; PA33324; -.
DR VEuPathDB; HostDB:ENSG00000102309; -.
DR eggNOG; KOG3258; Eukaryota.
DR GeneTree; ENSGT00510000047029; -.
DR HOGENOM; CLU_090028_5_0_1; -.
DR InParanoid; Q9Y237; -.
DR OrthoDB; 1413648at2759; -.
DR PhylomeDB; Q9Y237; -.
DR TreeFam; TF101102; -.
DR PathwayCommons; Q9Y237; -.
DR SignaLink; Q9Y237; -.
DR SIGNOR; Q9Y237; -.
DR BioGRID-ORCS; 5303; 34 hits in 707 CRISPR screens.
DR ChiTaRS; PIN4; human.
DR EvolutionaryTrace; Q9Y237; -.
DR GeneWiki; PIN4; -.
DR GenomeRNAi; 5303; -.
DR Pharos; Q9Y237; Tbio.
DR PRO; PR:Q9Y237; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9Y237; protein.
DR Bgee; ENSG00000102309; Expressed in tendon of biceps brachii and 207 other tissues.
DR ExpressionAtlas; Q9Y237; baseline and differential.
DR Genevisible; Q9Y237; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
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:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; 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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR043323; PIN4.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR PANTHER; PTHR45995; PTHR45995; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; DNA-binding; Isomerase; Mitochondrion; Nucleus;
KW Phosphoprotein; Reference proteome; Rotamase; Ubl conjugation.
FT CHAIN 1..131
FT /note="Peptidyl-prolyl cis-trans isomerase NIMA-interacting
FT 4"
FT /id="PRO_0000193438"
FT DOMAIN 35..129
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT REGION 1..41
FT /note="Necessary for association with the pre-rRNP
FT complexes"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..25
FT /note="Necessary for nuclear localization and DNA-binding"
FT MOD_RES 19
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:12860119"
FT VAR_SEQ 1
FT /note="M -> MPMAGLLKGLVRQLERFSVQQQASKM (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_037754"
FT VAR_SEQ 80..131
FT /note="GDLGWMTRGSMVGPFQEAAFALPVSGMDKPVFTDPPVKTKFGYHIIMVEGRK
FT -> IPSLQQHAGHHRDLRSTLISLVSYLQTTP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046122"
FT MUTAGEN 19
FT /note="S->A: Abolishes phosphorylation and reduces strongly
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:12860119"
FT MUTAGEN 19
FT /note="S->E: Does not abolish nuclear localization and
FT reduces DNA-binding ability."
FT /evidence="ECO:0000269|PubMed:12860119"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:3UI4"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:3UI4"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:3UI4"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3UI4"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:3UI4"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3UI4"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:3UI4"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1EQ3"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3UI4"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:3UI4"
FT VARIANT Q9Y237-2:16
FT /note="R -> Q (in dbSNP:rs6525589)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16522211"
FT /id="VAR_082896"
FT VARIANT Q9Y237-2:18
FT /note="S -> R (in dbSNP:rs7058353)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16522211"
FT /id="VAR_082897"
SQ SEQUENCE 131 AA; 13810 MW; 787C15BDB0701258 CRC64;
MPPKGKSGSG KAGKGGAASG SDSADKKAQG PKGGGNAVKV RHILCEKHGK IMEAMEKLKS
GMRFNEVAAQ YSEDKARQGG DLGWMTRGSM VGPFQEAAFA LPVSGMDKPV FTDPPVKTKF
GYHIIMVEGR K
