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Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (EC 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)

 PIN4_HUMAN              Reviewed;         131 AA.
Q9Y237; A8E0G6; B3KXM0; F5H1P5; Q0D2H3; Q3MHV0; Q52M21; Q5HYW6;
Q6IRW4;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-OCT-2017, entry version 151.
RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4;
EC=5.2.1.8;
AltName: Full=Parvulin-14;
Short=Par14;
Short=hPar14;
AltName: Full=Parvulin-17;
Short=Par17;
Short=hPar17;
AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin4;
Short=PPIase Pin4;
AltName: Full=Peptidyl-prolyl cis/trans isomerase EPVH;
Short=hEPVH;
AltName: Full=Rotamase Pin4;
Name=PIN4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=10364457; DOI=10.1006/bbrc.1999.0828;
Rulten S.L., Thorpe J.R., Kay J.E.;
"Identification of eukaryotic parvulin homologues: a new subfamily of
peptidylprolyl cis-trans isomerases.";
Biochem. Biophys. Res. Commun. 259:557-562(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=10100858; DOI=10.1016/S0014-5793(99)00239-2;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS GLN-16 AND ARG-18 (ISOFORM 2).
TISSUE=Brain, Prostate, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-13 (ISOFORM 1), PARTIAL NUCLEOTIDE
SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE PROMOTER USAGE, SUMOYLATION,
TISSUE SPECIFICITY, AND VARIANTS GLN-16 AND ARG-18 (ISOFORM 2).
PubMed=16522211; DOI=10.1186/1471-2199-7-9;
Mueller J.W., Kessler D., Neumann D., Stratmann T., Papatheodorou P.,
Hartmann-Fatu C., Bayer P.;
"Characterization of novel elongated Parvulin isoforms that are
ubiquitously expressed in human tissues and originate from alternative
transcription initiation.";
BMC Mol. Biol. 7:9-9(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6 AND 48-72, ALTERNATIVE
PROMOTER USAGE (ISOFORMS 1 AND 2), DNA-BINDING, AND SUBCELLULAR
LOCATION.
PubMed=17875217; DOI=10.1186/1741-7007-5-37;
Kessler D., Papatheodorou P., Stratmann T., Dian E.A.,
Hartmann-Fatu C., Rassow J., Bayer P., Mueller J.W.;
"The DNA binding parvulin Par17 is targeted to the mitochondrial
matrix by a recently evolved prepeptide uniquely present in
Hominidae.";
BMC Biol. 5:37-37(2007).
[7]
PROTEIN SEQUENCE OF 15-25, IDENTIFICATION BY MASS SPECTROMETRY,
PHOSPHORYLATION AT SER-19, MUTAGENESIS OF SER-19, AND SUBCELLULAR
LOCATION.
PubMed=12860119; DOI=10.1016/S0022-2836(03)00713-7;
Reimer T., Weiwad M., Schierhorn A., Ruecknagel P.-K., Rahfeld J.-U.,
Bayer P., Fischer G.;
"Phosphorylation of the N-terminal domain regulates subcellular
localization and DNA binding properties of the peptidyl-prolyl
cis/trans isomerase hPar14.";
J. Mol. Biol. 330:955-966(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-131 (ISOFORM 3).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
DNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=12144781; DOI=10.1016/S0022-2836(02)00615-0;
Surmacz T.A., Bayer E., Rahfeld J.-U., Fischer G., Bayer P.;
"The N-terminal basic domain of human parvulin hPar14 is responsible
for the entry to the nucleus and high-affinity DNA-binding.";
J. Mol. Biol. 321:235-247(2002).
[10]
FUNCTION, IDENTIFICATION IN PRE-RRNP COMPLEXES, PHOSPHORYLATION, AND
SUBCELLULAR LOCATION.
PubMed=19369196; DOI=10.1074/mcp.M900147-MCP200;
Fujiyama-Nakamura S., Yoshikawa H., Homma K., Hayano T.,
Tsujimura-Takahashi T., Izumikawa K., Ishikawa H., Miyazawa N.,
Yanagida M., Miura Y., Shinkawa T., Yamauchi Y., Isobe T.,
Takahashi N.;
"Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel
rRNA processing factor that evolved in the metazoan lineage.";
Mol. Cell. Proteomics 8:1552-1565(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
STRUCTURE BY NMR OF 36-131.
PubMed=10966801; DOI=10.1006/jmbi.2000.4013;
Sekerina E., Rahfeld J.-U., Mueller J., Fanghaenel J., Rascher C.,
Fischer G., Bayer P.;
"NMR solution structure of hPar14 reveals similarity to the peptidyl
prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but
indicates a different functionality of the protein.";
J. Mol. Biol. 301:1003-1017(2000).
[14]
STRUCTURE BY NMR OF 28-131.
PubMed=11162102; DOI=10.1006/jmbi.2000.4293;
Terada T., Shirouzu M., Fukumori Y., Fujimori F., Ito Y., Kigawa T.,
Yokoyama S., Uchida T.;
"Solution structure of the human parvulin-like peptidyl prolyl
cis/trans isomerase, hPar14.";
J. Mol. Biol. 305:917-926(2001).
-!- FUNCTION: Isoform 1 is involved as a ribosomal RNA processing
factor in ribosome biogenesis. Binds to tightly bent AT-rich
stretches of double-stranded DNA. {ECO:0000269|PubMed:19369196}.
-!- FUNCTION: Isoform 2 binds to double-stranded DNA.
{ECO:0000269|PubMed:19369196}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- SUBUNIT: Isoform 1 is found in pre-ribosomal ribonucleoprotein
(pre-rRNP) complexes. {ECO:0000250}.
-!- INTERACTION:
Q9P209:CEP72; NbExp=3; IntAct=EBI-714599, EBI-739498;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-714599, EBI-10175124;
Q969F0:FATE1; NbExp=3; IntAct=EBI-714599, EBI-743099;
P43364-2:MAGEA11; NbExp=3; IntAct=EBI-714599, EBI-10178634;
Q8ND90:PNMA1; NbExp=3; IntAct=EBI-714599, EBI-302345;
Q96C00:ZBTB9; NbExp=3; IntAct=EBI-714599, EBI-395708;
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus. Cytoplasm,
cytoskeleton, spindle. Cytoplasm. Note=Colocalizes in the
nucleolus during interphase and on the spindle apparatus during
mitosis with NPM1.
-!- SUBCELLULAR LOCATION: Isoform 2: Mitochondrion. Mitochondrion
matrix. Note=Imported in a time- and membrane potential-dependent
manner to the mitochondrial matrix, but without concomitant
processing of the protein. Directed to mitochondria by a novel N-
terminal domain that functions as non-cleavable mitochondrial
targeting peptide.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=3;
Name=1;
IsoId=Q9Y237-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y237-2; Sequence=VSP_037754;
Note=The first 25 amino acids are sufficient for mitochondrial
targeting. Variant in position: 16:R->Q (in dbSNP:rs6525589).
Variant in position: 18:S->R (in dbSNP:rs7058353).
{ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16522211};
Name=3;
IsoId=Q9Y237-3; Sequence=VSP_037754, VSP_046122;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 2 is much more stable than isoform 1
(at protein level). Ubiquitous. Isoform 1 and isoform 2 are
expressed in kidney, liver, blood vessel, brain, mammary gland,
skeletal muscle, small intestine and submandibularis. Isoform 1
transcripts are much more abundant than isoform 2 in each tissue
analyzed. {ECO:0000269|PubMed:10100858,
ECO:0000269|PubMed:10364457, ECO:0000269|PubMed:16522211}.
-!- DOMAIN: The PPIase domain enhances mitochondrial targeting.
-!- PTM: Phosphorylated. Isoform 1 phosphorylation occurs both in the
nucleus and the cytoplasm. Isoform 1 phosphorylation at Ser-19
does not affect its PPIase activity but is required for nuclear
localization, and the dephosphorylation is a prerequisite for the
binding to DNA. The unphosphorylated isoform 1 associates with the
pre-rRNP complexes in the nucleus. {ECO:0000269|PubMed:12860119,
ECO:0000269|PubMed:19369196}.
-!- PTM: Isoform 2 is sumoylated with SUMO2 and SUMO3.
{ECO:0000269|PubMed:16522211}.
-!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH05234.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH70288.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAI04654.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAI11395.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAG54532.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF143096; AAD27893.1; -; mRNA.
EMBL; AB009690; BAA82320.1; -; mRNA.
EMBL; BX119917; CAI39856.1; -; Genomic_DNA.
EMBL; AL135749; CAI39856.1; JOINED; Genomic_DNA.
EMBL; BC005234; AAH05234.2; ALT_INIT; mRNA.
EMBL; BC070288; AAH70288.1; ALT_INIT; mRNA.
EMBL; BC093700; AAH93700.1; -; mRNA.
EMBL; BC104653; AAI04654.1; ALT_INIT; mRNA.
EMBL; BC111394; AAI11395.1; ALT_INIT; mRNA.
EMBL; BC112281; AAI12282.1; -; mRNA.
EMBL; AM420633; CAM12362.1; -; Genomic_DNA.
EMBL; AK127605; BAG54532.1; ALT_INIT; mRNA.
CCDS; CCDS14417.1; -. [Q9Y237-2]
CCDS; CCDS55447.1; -. [Q9Y237-3]
RefSeq; NP_001164218.1; NM_001170747.1. [Q9Y237-3]
RefSeq; NP_006214.2; NM_006223.3. [Q9Y237-2]
UniGene; Hs.655623; -.
PDB; 1EQ3; NMR; -; A=36-131.
PDB; 1FJD; NMR; -; A=28-131.
PDB; 3UI4; X-ray; 0.80 A; A=36-131.
PDB; 3UI5; X-ray; 1.40 A; A=36-131.
PDB; 3UI6; X-ray; 0.89 A; A=36-131.
PDBsum; 1EQ3; -.
PDBsum; 1FJD; -.
PDBsum; 3UI4; -.
PDBsum; 3UI5; -.
PDBsum; 3UI6; -.
ProteinModelPortal; Q9Y237; -.
SMR; Q9Y237; -.
BioGrid; 111320; 33.
CORUM; Q9Y237; -.
DIP; DIP-50838N; -.
IntAct; Q9Y237; 16.
STRING; 9606.ENSP00000362773; -.
BindingDB; Q9Y237; -.
ChEMBL; CHEMBL4923; -.
iPTMnet; Q9Y237; -.
PhosphoSitePlus; Q9Y237; -.
DMDM; 20139299; -.
EPD; Q9Y237; -.
PaxDb; Q9Y237; -.
PeptideAtlas; Q9Y237; -.
PRIDE; Q9Y237; -.
TopDownProteomics; Q9Y237-1; -. [Q9Y237-1]
TopDownProteomics; Q9Y237-2; -. [Q9Y237-2]
DNASU; 5303; -.
Ensembl; ENST00000373669; ENSP00000362773; ENSG00000102309. [Q9Y237-2]
Ensembl; ENST00000423432; ENSP00000409154; ENSG00000102309. [Q9Y237-3]
GeneID; 5303; -.
KEGG; hsa:5303; -.
UCSC; uc004eam.4; human. [Q9Y237-1]
CTD; 5303; -.
DisGeNET; 5303; -.
EuPathDB; HostDB:ENSG00000102309.12; -.
GeneCards; PIN4; -.
H-InvDB; HIX0016866; -.
HGNC; HGNC:8992; PIN4.
HPA; HPA054483; -.
HPA; HPA064504; -.
MIM; 300252; gene.
neXtProt; NX_Q9Y237; -.
OpenTargets; ENSG00000102309; -.
PharmGKB; PA33324; -.
eggNOG; KOG3258; Eukaryota.
eggNOG; COG0760; LUCA.
GeneTree; ENSGT00510000047029; -.
HOVERGEN; HBG019150; -.
InParanoid; Q9Y237; -.
KO; K09579; -.
OMA; LGWKTKG; -.
OrthoDB; EOG091G0Z6N; -.
PhylomeDB; Q9Y237; -.
TreeFam; TF101102; -.
ChiTaRS; PIN4; human.
EvolutionaryTrace; Q9Y237; -.
GeneWiki; PIN4; -.
GenomeRNAi; 5303; -.
PRO; PR:Q9Y237; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102309; -.
CleanEx; HS_PIN4; -.
ExpressionAtlas; Q9Y237; baseline and differential.
Genevisible; Q9Y237; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0030684; C:preribosome; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0003681; F:bent DNA binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
InterPro; IPR000297; PPIase_PpiC.
PROSITE; PS50198; PPIC_PPIASE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; DNA-binding;
Isomerase; Mitochondrion; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Rotamase; Ubl conjugation.
CHAIN 1 131 Peptidyl-prolyl cis-trans isomerase NIMA-
interacting 4.
/FTId=PRO_0000193438.
DOMAIN 35 129 PpiC. {ECO:0000255|PROSITE-
ProRule:PRU00278}.
REGION 1 41 Necessary for association with the pre-
rRNP complexes.
REGION 1 25 Necessary for nuclear localization and
DNA-binding.
MOD_RES 19 19 Phosphoserine; by CK2.
{ECO:0000269|PubMed:12860119}.
VAR_SEQ 1 1 M -> MPMAGLLKGLVRQLERFSVQQQASKM (in
isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_037754.
VAR_SEQ 80 131 GDLGWMTRGSMVGPFQEAAFALPVSGMDKPVFTDPPVKTKF
GYHIIMVEGRK -> IPSLQQHAGHHRDLRSTLISLVSYLQ
TTP (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046122.
MUTAGEN 19 19 S->A: Abolishes phosphorylation and
reduces strongly nuclear localization.
{ECO:0000269|PubMed:12860119}.
MUTAGEN 19 19 S->E: Does not abolish nuclear
localization and reduces DNA-binding
ability. {ECO:0000269|PubMed:12860119}.
STRAND 37 47 {ECO:0000244|PDB:3UI4}.
HELIX 48 59 {ECO:0000244|PDB:3UI4}.
HELIX 64 71 {ECO:0000244|PDB:3UI4}.
STRAND 73 75 {ECO:0000244|PDB:3UI4}.
HELIX 76 78 {ECO:0000244|PDB:3UI4}.
STRAND 81 86 {ECO:0000244|PDB:3UI4}.
HELIX 92 99 {ECO:0000244|PDB:3UI4}.
TURN 108 110 {ECO:0000244|PDB:1EQ3}.
STRAND 116 118 {ECO:0000244|PDB:3UI4}.
STRAND 121 130 {ECO:0000244|PDB:3UI4}.
SEQUENCE 131 AA; 13810 MW; 787C15BDB0701258 CRC64;
MPPKGKSGSG KAGKGGAASG SDSADKKAQG PKGGGNAVKV RHILCEKHGK IMEAMEKLKS
GMRFNEVAAQ YSEDKARQGG DLGWMTRGSM VGPFQEAAFA LPVSGMDKPV FTDPPVKTKF
GYHIIMVEGR K


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