PIN1_HUMAN
ID PIN1_HUMAN Reviewed; 163 AA.
AC Q13526; A8K4V9; Q53X75;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1;
DE EC=5.2.1.8 {ECO:0000269|PubMed:21497122, ECO:0000269|PubMed:23623683, ECO:0000269|PubMed:29686383};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1;
DE Short=PPIase Pin1;
DE AltName: Full=Rotamase Pin1;
GN Name=PIN1;
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].
RX PubMed=8606777; DOI=10.1038/380544a0;
RA Lu K.P., Hanes S.D., Hunter T.;
RT "A human peptidyl-prolyl isomerase essential for regulation of mitosis.";
RL Nature 380:544-547(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [7]
RP INTERACTION WITH KIF20B, AND MUTAGENESIS OF TYR-23.
RX PubMed=11470801; DOI=10.1074/jbc.m106207200;
RA Kamimoto T., Zama T., Aoki R., Muro Y., Hagiwara M.;
RT "Identification of a novel kinesin-related protein, KRMP1, as a target for
RT mitotic peptidyl-prolyl isomerase Pin1.";
RL J. Biol. Chem. 276:37520-37528(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH RAF1.
RX PubMed=15664191; DOI=10.1016/j.molcel.2004.11.055;
RA Dougherty M.K., Muller J., Ritt D.A., Zhou M., Zhou X.Z., Copeland T.D.,
RA Conrads T.P., Veenstra T.D., Lu K.P., Morrison D.K.;
RT "Regulation of Raf-1 by direct feedback phosphorylation.";
RL Mol. Cell 17:215-224(2005).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NEK6.
RX PubMed=16476580; DOI=10.1016/j.bbrc.2005.12.228;
RA Chen J., Li L., Zhang Y., Yang H., Wei Y., Zhang L., Liu X., Yu L.;
RT "Interaction of Pin1 with Nek6 and characterization of their expression
RT correlation in Chinese hepatocellular carcinoma patients.";
RL Biochem. Biophys. Res. Commun. 341:1059-1065(2006).
RN [10]
RP INTERACTION WITH BTK, AND FUNCTION.
RX PubMed=16644721; DOI=10.1074/jbc.m603090200;
RA Yu L., Mohamed A.J., Vargas L., Berglof A., Finn G., Lu K.P., Smith C.I.;
RT "Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase
RT Pin1.";
RL J. Biol. Chem. 281:18201-18207(2006).
RN [11]
RP FUNCTION IN BCL6 STABILITY REGULATION, INTERACTION WITH BCL6, AND TISSUE
RP SPECIFICITY.
RX PubMed=17828269; DOI=10.1038/ni1508;
RA Phan R.T., Saito M., Kitagawa Y., Means A.R., Dalla-Favera R.;
RT "Genotoxic stress regulates expression of the proto-oncogene Bcl6 in
RT germinal center B cells.";
RL Nat. Immunol. 8:1132-1139(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP INTERACTION WITH ATCAY.
RX PubMed=18628984; DOI=10.1371/journal.pone.0002686;
RA Buschdorf J.P., Chew L.L., Soh U.J., Liou Y.C., Low B.C.;
RT "Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-
RT H/Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating
RT neurons.";
RL PLoS ONE 3:E2686-E2686(2008).
RN [14]
RP INTERACTION WITH PRKX.
RX PubMed=19367327; DOI=10.1038/ki.2009.95;
RA Li X., Hyink D.P., Radbill B., Sudol M., Zhang H., Zheleznova N.N.,
RA Wilson P.D.;
RT "Protein kinase-X interacts with Pin-1 and Polycystin-1 during mouse kidney
RT development.";
RL Kidney Int. 76:54-62(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
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 [17]
RP FUNCTION, AND INTERACTION WITH PML.
RX PubMed=22033920; DOI=10.1074/jbc.m111.289512;
RA Lim J.H., Liu Y., Reineke E., Kao H.Y.;
RT "Mitogen-activated protein kinase extracellular signal-regulated kinase 2
RT phosphorylates and promotes Pin1 protein-dependent promyelocytic leukemia
RT protein turnover.";
RL J. Biol. Chem. 286:44403-44411(2011).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-71, INTERACTION WITH
RP DAPK1, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-71, AND TISSUE SPECIFICITY.
RX PubMed=21497122; DOI=10.1016/j.molcel.2011.03.005;
RA Lee T.H., Chen C.H., Suizu F., Huang P., Schiene-Fischer C., Daum S.,
RA Zhang Y.J., Goate A., Chen R.H., Zhou X.Z., Lu K.P.;
RT "Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its
RT prolyl isomerase activity and cellular function.";
RL Mol. Cell 42:147-159(2011).
RN [19]
RP FUNCTION, INTERACTION WITH FBXW7, AND MUTAGENESIS OF TRP-34 AND LYS-63.
RX PubMed=22608923; DOI=10.1016/j.molcel.2012.04.012;
RA Min S.H., Lau A.W., Lee T.H., Inuzuka H., Wei S., Huang P., Shaik S.,
RA Lee D.Y., Finn G., Balastik M., Chen C.H., Luo M., Tron A.E.,
RA Decaprio J.A., Zhou X.Z., Wei W., Lu K.P.;
RT "Negative regulation of the stability and tumor suppressor function of Fbw7
RT by the Pin1 prolyl isomerase.";
RL Mol. Cell 46:771-783(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RBBP8, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF TRP-34 AND CYS-113.
RX PubMed=23623683; DOI=10.1016/j.molcel.2013.03.023;
RA Steger M., Murina O., Huehn D., Ferretti L.P., Walser R., Haenggi K.,
RA Lafranchi L., Neugebauer C., Paliwal S., Janscak P., Gerrits B.,
RA Del Sal G., Zerbe O., Sartori A.A.;
RT "Prolyl isomerase PIN1 regulates DNA double-strand break repair by
RT counteracting DNA end resection.";
RL Mol. Cell 50:333-343(2013).
RN [22]
RP FUNCTION.
RX PubMed=27561354; DOI=10.1038/ncomms12628;
RA Ferretti L.P., Himmels S.F., Trenner A., Walker C., von Aesch C.,
RA Eggenschwiler A., Murina O., Enchev R.I., Peter M., Freire R., Porro A.,
RA Sartori A.A.;
RT "Cullin3-KLHL15 ubiquitin ligase mediates CtIP protein turnover to fine-
RT tune DNA-end resection.";
RL Nat. Commun. 7:12628-12628(2016).
RN [23]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH IRAK3, TISSUE SPECIFICITY,
RP PHOSPHORYLATION AT SER-71, AND MUTAGENESIS OF TRP-34 AND LYS-63.
RX PubMed=29686383; DOI=10.1038/s41467-018-03886-6;
RA Nechama M., Kwon J., Wei S., Kyi A.T., Welner R.S., Ben-Dov I.Z.,
RA Arredouani M.S., Asara J.M., Chen C.H., Tsai C.Y., Nelson K.F.,
RA Kobayashi K.S., Israel E., Zhou X.Z., Nicholson L.K., Lu K.P.;
RT "The IL-33-PIN1-IRAK-M axis is critical for type 2 immunity in IL-33-
RT induced allergic airway inflammation.";
RL Nat. Commun. 9:1603-1603(2018).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
RX PubMed=9200606; DOI=10.1016/s0092-8674(00)80273-1;
RA Ranganathan R., Lu K.P., Hunter T., Noel J.P.;
RT "Structural and functional analysis of the mitotic rotamase Pin1 suggests
RT substrate recognition is phosphorylation dependent.";
RL Cell 89:875-886(1997).
CC -!- FUNCTION: Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to
CC and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro)
CC motifs (PubMed:21497122, PubMed:23623683, PubMed:29686383). By inducing
CC conformational changes in a subset of phosphorylated proteins, acts as
CC a molecular switch in multiple cellular processes (PubMed:21497122,
CC PubMed:22033920, PubMed:23623683). Displays a preference for acidic
CC residues located N-terminally to the proline bond to be isomerized.
CC Regulates mitosis presumably by interacting with NIMA and attenuating
CC its mitosis-promoting activity. Down-regulates kinase activity of BTK
CC (PubMed:16644721). Can transactivate multiple oncogenes and induce
CC centrosome amplification, chromosome instability and cell
CC transformation. Required for the efficient dephosphorylation and
CC recycling of RAF1 after mitogen activation (PubMed:15664191). Binds and
CC targets PML and BCL6 for degradation in a phosphorylation-dependent
CC manner (PubMed:17828269). Acts as a regulator of JNK cascade by binding
CC to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting
CC FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to
CC subsequent stabilization of JUN (PubMed:22608923). May facilitate the
CC ubiquitination and proteasomal degradation of RBBP8/CtIP through
CC CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA
CC double-strand repair through error-prone non-homologous end joining
CC (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR)
CC (PubMed:23623683, PubMed:27561354). Upon IL33-induced lung
CC inflammation, catalyzes cis-trans isomerization of phosphorylated
CC IRAK3/IRAK-M, inducing IRAK3 stabilization, nuclear translocation and
CC expression of pro-inflammatory genes in dendritic cells
CC (PubMed:29686383). {ECO:0000269|PubMed:15664191,
CC ECO:0000269|PubMed:16644721, ECO:0000269|PubMed:17828269,
CC ECO:0000269|PubMed:21497122, ECO:0000269|PubMed:22033920,
CC ECO:0000269|PubMed:22608923, ECO:0000269|PubMed:23623683,
CC ECO:0000269|PubMed:27561354, ECO:0000269|PubMed:29686383}.
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; Evidence={ECO:0000269|PubMed:21497122,
CC ECO:0000269|PubMed:23623683, ECO:0000269|PubMed:29686383};
CC -!- SUBUNIT: Interacts with STIL (By similarity). Interacts with KIF20B
CC (PubMed:11470801). Interacts with NEK6 (PubMed:16476580). Interacts
CC (via WW domain) with PRKX (PubMed:19367327). Interacts with BTK
CC (PubMed:16644721). Interacts (via PpiC domain) with DAPK1
CC (PubMed:21497122). Interacts with the phosphorylated form of RAF1
CC (PubMed:15664191). Interacts (via WW domain) with ATCAY; upon NGF
CC stimulation (PubMed:18628984). Interacts with PML (isoform PML-4)
CC (PubMed:22033920). Interacts with BCL6 (PubMed:17828269). Interacts
CC with FBXW7, disrupting FBXW7 dimerization and promoting FBXW7
CC autoubiquitination and degradation (PubMed:22608923). Directly
CC interacts with RBBP8/CtIP; this interaction depends upon RBBP8
CC phosphorylation (PubMed:23623683). Interacts (via WW domain) with
CC IRAK3/IRAK-M (when phosphorylated at 'Ser-110') in response to IL33-
CC mediated (but not TLR4 ligand LPS) dendritic cell stimulation
CC (PubMed:29686383). {ECO:0000250|UniProtKB:Q9QUR7,
CC ECO:0000269|PubMed:11470801, ECO:0000269|PubMed:15664191,
CC ECO:0000269|PubMed:16476580, ECO:0000269|PubMed:16644721,
CC ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:18628984,
CC ECO:0000269|PubMed:19367327, ECO:0000269|PubMed:21497122,
CC ECO:0000269|PubMed:22033920, ECO:0000269|PubMed:22608923,
CC ECO:0000269|PubMed:23623683, ECO:0000269|PubMed:29686383}.
CC -!- INTERACTION:
CC Q13526; Q9NYB9: ABI2; NbExp=5; IntAct=EBI-714158, EBI-743598;
CC Q13526; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-714158, EBI-11096309;
CC Q13526; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-714158, EBI-10173507;
CC Q13526; P78563: ADARB1; NbExp=12; IntAct=EBI-714158, EBI-2967304;
CC Q13526; Q96IF1: AJUBA; NbExp=3; IntAct=EBI-714158, EBI-949782;
CC Q13526; A2BDD9: AMOT; NbExp=3; IntAct=EBI-714158, EBI-17286414;
CC Q13526; Q4VCS5-2: AMOT; NbExp=3; IntAct=EBI-714158, EBI-3891843;
CC Q13526; Q6AI12: ANKRD40; NbExp=6; IntAct=EBI-714158, EBI-2838246;
CC Q13526; P05067: APP; NbExp=4; IntAct=EBI-714158, EBI-77613;
CC Q13526; P05067-4: APP; NbExp=2; IntAct=EBI-714158, EBI-302641;
CC Q13526; P85298-4: ARHGAP8; NbExp=25; IntAct=EBI-714158, EBI-9523517;
CC Q13526; D3DTR7: ARHGEF15; NbExp=3; IntAct=EBI-714158, EBI-10176602;
CC Q13526; Q03989: ARID5A; NbExp=3; IntAct=EBI-714158, EBI-948603;
CC Q13526; Q86V38: ATN1; NbExp=3; IntAct=EBI-714158, EBI-11954292;
CC Q13526; Q99728-1: BARD1; NbExp=4; IntAct=EBI-714158, EBI-21498323;
CC Q13526; Q9H165-2: BCL11A; NbExp=3; IntAct=EBI-714158, EBI-10183342;
CC Q13526; P38398-1: BRCA1; NbExp=4; IntAct=EBI-714158, EBI-21498346;
CC Q13526; Q9H0E9-2: BRD8; NbExp=3; IntAct=EBI-714158, EBI-10304361;
CC Q13526; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-714158, EBI-18036948;
CC Q13526; P35520: CBS; NbExp=4; IntAct=EBI-714158, EBI-740135;
CC Q13526; Q8NA61: CBY2; NbExp=3; IntAct=EBI-714158, EBI-741724;
CC Q13526; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-714158, EBI-11524851;
CC Q13526; Q494R4-2: CCDC153; NbExp=3; IntAct=EBI-714158, EBI-11974185;
CC Q13526; Q52MB2: CCDC184; NbExp=6; IntAct=EBI-714158, EBI-10179526;
CC Q13526; Q16204: CCDC6; NbExp=6; IntAct=EBI-714158, EBI-1045350;
CC Q13526; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-714158, EBI-347573;
CC Q13526; Q15131: CDK10; NbExp=5; IntAct=EBI-714158, EBI-1646959;
CC Q13526; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-714158, EBI-747776;
CC Q13526; Q8TAP6: CEP76; NbExp=6; IntAct=EBI-714158, EBI-742887;
CC Q13526; Q969H4: CNKSR1; NbExp=6; IntAct=EBI-714158, EBI-741671;
CC Q13526; O75553: DAB1; NbExp=3; IntAct=EBI-714158, EBI-7875264;
CC Q13526; O75553-5: DAB1; NbExp=3; IntAct=EBI-714158, EBI-12133006;
CC Q13526; Q16254: E2F4; NbExp=3; IntAct=EBI-714158, EBI-448943;
CC Q13526; O43281-2: EFS; NbExp=3; IntAct=EBI-714158, EBI-11525448;
CC Q13526; P41212: ETV6; NbExp=3; IntAct=EBI-714158, EBI-1372759;
CC Q13526; O00167-2: EYA2; NbExp=3; IntAct=EBI-714158, EBI-12807776;
CC Q13526; Q5TD97: FHL5; NbExp=3; IntAct=EBI-714158, EBI-750641;
CC Q13526; P01100: FOS; NbExp=3; IntAct=EBI-714158, EBI-852851;
CC Q13526; P15407: FOSL1; NbExp=3; IntAct=EBI-714158, EBI-744510;
CC Q13526; Q12951-2: FOXI1; NbExp=3; IntAct=EBI-714158, EBI-12018822;
CC Q13526; O15353: FOXN1; NbExp=3; IntAct=EBI-714158, EBI-11319000;
CC Q13526; O15409: FOXP2; NbExp=6; IntAct=EBI-714158, EBI-983612;
CC Q13526; Q9BTY2: FUCA2; NbExp=3; IntAct=EBI-714158, EBI-9050116;
CC Q13526; P08151: GLI1; NbExp=3; IntAct=EBI-714158, EBI-308084;
CC Q13526; Q9UKD1: GMEB2; NbExp=3; IntAct=EBI-714158, EBI-948296;
CC Q13526; Q08379: GOLGA2; NbExp=6; IntAct=EBI-714158, EBI-618309;
CC Q13526; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-714158, EBI-5916454;
CC Q13526; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-714158, EBI-13345167;
CC Q13526; Q96MH2: HEXIM2; NbExp=6; IntAct=EBI-714158, EBI-5460660;
CC Q13526; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-714158, EBI-10172004;
CC Q13526; P49639: HOXA1; NbExp=5; IntAct=EBI-714158, EBI-740785;
CC Q13526; Q13422: IKZF1; NbExp=3; IntAct=EBI-714158, EBI-745305;
CC Q13526; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-714158, EBI-11522367;
CC Q13526; Q9UKT9: IKZF3; NbExp=8; IntAct=EBI-714158, EBI-747204;
CC Q13526; Q8NBZ0: INO80E; NbExp=3; IntAct=EBI-714158, EBI-769401;
CC Q13526; P51617: IRAK1; NbExp=10; IntAct=EBI-714158, EBI-358664;
CC Q13526; Q96AA8: JAKMIP2; NbExp=4; IntAct=EBI-714158, EBI-752007;
CC Q13526; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-714158, EBI-11954971;
CC Q13526; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-714158, EBI-14069005;
CC Q13526; Q15323: KRT31; NbExp=6; IntAct=EBI-714158, EBI-948001;
CC Q13526; O76011: KRT34; NbExp=3; IntAct=EBI-714158, EBI-1047093;
CC Q13526; O76014: KRT37; NbExp=3; IntAct=EBI-714158, EBI-1045716;
CC Q13526; O76015: KRT38; NbExp=6; IntAct=EBI-714158, EBI-1047263;
CC Q13526; Q6A162: KRT40; NbExp=3; IntAct=EBI-714158, EBI-10171697;
CC Q13526; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-714158, EBI-12012928;
CC Q13526; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-714158, EBI-10172290;
CC Q13526; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-714158, EBI-10171774;
CC Q13526; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-714158, EBI-10172052;
CC Q13526; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-714158, EBI-10172511;
CC Q13526; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-714158, EBI-3958099;
CC Q13526; P80188: LCN2; NbExp=3; IntAct=EBI-714158, EBI-11911016;
CC Q13526; Q02750: MAP2K1; NbExp=5; IntAct=EBI-714158, EBI-492564;
CC Q13526; P41279: MAP3K8; NbExp=8; IntAct=EBI-714158, EBI-354900;
CC Q13526; Q99750: MDFI; NbExp=7; IntAct=EBI-714158, EBI-724076;
CC Q13526; P50221: MEOX1; NbExp=3; IntAct=EBI-714158, EBI-2864512;
CC Q13526; P50222: MEOX2; NbExp=3; IntAct=EBI-714158, EBI-748397;
CC Q13526; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-714158, EBI-16439278;
CC Q13526; P55198: MLLT6; NbExp=3; IntAct=EBI-714158, EBI-740216;
CC Q13526; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-714158, EBI-742948;
CC Q13526; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-714158, EBI-11522433;
CC Q13526; P01106: MYC; NbExp=5; IntAct=EBI-714158, EBI-447544;
CC Q13526; P13349: MYF5; NbExp=3; IntAct=EBI-714158, EBI-17491620;
CC Q13526; Q15742: NAB2; NbExp=6; IntAct=EBI-714158, EBI-8641936;
CC Q13526; Q9NZQ3-3: NCKIPSD; NbExp=3; IntAct=EBI-714158, EBI-10963850;
CC Q13526; Q9HC98: NEK6; NbExp=3; IntAct=EBI-714158, EBI-740364;
CC Q13526; Q9H3P2: NELFA; NbExp=3; IntAct=EBI-714158, EBI-5461341;
CC Q13526; Q9HD90: NEUROD4; NbExp=3; IntAct=EBI-714158, EBI-3917781;
CC Q13526; Q15233: NONO; NbExp=4; IntAct=EBI-714158, EBI-350527;
CC Q13526; Q15233-2: NONO; NbExp=3; IntAct=EBI-714158, EBI-10203843;
CC Q13526; P46531: NOTCH1; NbExp=9; IntAct=EBI-714158, EBI-636374;
CC Q13526; Q92570: NR4A3; NbExp=3; IntAct=EBI-714158, EBI-13644623;
CC Q13526; Q8NFH5: NUP35; NbExp=5; IntAct=EBI-714158, EBI-9050429;
CC Q13526; P37198: NUP62; NbExp=6; IntAct=EBI-714158, EBI-347978;
CC Q13526; P26367: PAX6; NbExp=3; IntAct=EBI-714158, EBI-747278;
CC Q13526; P40424: PBX1; NbExp=3; IntAct=EBI-714158, EBI-301611;
CC Q13526; Q9NR12: PDLIM7; NbExp=3; IntAct=EBI-714158, EBI-350517;
CC Q13526; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-714158, EBI-2876622;
CC Q13526; Q9H7P9: PLEKHG2; NbExp=3; IntAct=EBI-714158, EBI-2797213;
CC Q13526; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-714158, EBI-302345;
CC Q13526; Q96M27: PRRC1; NbExp=3; IntAct=EBI-714158, EBI-2560879;
CC Q13526; P04049: RAF1; NbExp=2; IntAct=EBI-714158, EBI-365996;
CC Q13526; Q7Z5J4: RAI1; NbExp=4; IntAct=EBI-714158, EBI-743815;
CC Q13526; Q99708-2: RBBP8; NbExp=3; IntAct=EBI-714158, EBI-10203615;
CC Q13526; Q8NC74: RBBP8NL; NbExp=3; IntAct=EBI-714158, EBI-11322432;
CC Q13526; Q93062: RBPMS; NbExp=4; IntAct=EBI-714158, EBI-740322;
CC Q13526; Q9H0X6: RNF208; NbExp=3; IntAct=EBI-714158, EBI-751555;
CC Q13526; Q13950: RUNX2; NbExp=7; IntAct=EBI-714158, EBI-976402;
CC Q13526; Q8N9R8: SCAI; NbExp=3; IntAct=EBI-714158, EBI-4395514;
CC Q13526; Q96KG9-4: SCYL1; NbExp=3; IntAct=EBI-714158, EBI-12023020;
CC Q13526; P59797: SELENOV; NbExp=3; IntAct=EBI-714158, EBI-10216195;
CC Q13526; Q13342: SP140; NbExp=4; IntAct=EBI-714158, EBI-2865100;
CC Q13526; Q9BWW4: SSBP3; NbExp=6; IntAct=EBI-714158, EBI-2902395;
CC Q13526; Q9BWG4: SSBP4; NbExp=4; IntAct=EBI-714158, EBI-744719;
CC Q13526; A1L4H1: SSC5D; NbExp=3; IntAct=EBI-714158, EBI-10172867;
CC Q13526; Q9BR01: SULT4A1; NbExp=4; IntAct=EBI-714158, EBI-6690555;
CC Q13526; O00267: SUPT5H; NbExp=4; IntAct=EBI-714158, EBI-710464;
CC Q13526; Q8N5C8: TAB3; NbExp=3; IntAct=EBI-714158, EBI-359964;
CC Q13526; Q99081-3: TCF12; NbExp=3; IntAct=EBI-714158, EBI-11952764;
CC Q13526; P15884: TCF4; NbExp=3; IntAct=EBI-714158, EBI-533224;
CC Q13526; P0C1Z6: TFPT; NbExp=3; IntAct=EBI-714158, EBI-1245626;
CC Q13526; Q9BT49: THAP7; NbExp=5; IntAct=EBI-714158, EBI-741350;
CC Q13526; Q15025: TNIP1; NbExp=7; IntAct=EBI-714158, EBI-357849;
CC Q13526; Q63HR2: TNS2; NbExp=3; IntAct=EBI-714158, EBI-949753;
CC Q13526; P04637: TP53; NbExp=12; IntAct=EBI-714158, EBI-366083;
CC Q13526; Q9H3D4: TP63; NbExp=3; IntAct=EBI-714158, EBI-2337775;
CC Q13526; Q13077: TRAF1; NbExp=3; IntAct=EBI-714158, EBI-359224;
CC Q13526; Q12933: TRAF2; NbExp=7; IntAct=EBI-714158, EBI-355744;
CC Q13526; P14373: TRIM27; NbExp=3; IntAct=EBI-714158, EBI-719493;
CC Q13526; Q15654: TRIP6; NbExp=3; IntAct=EBI-714158, EBI-742327;
CC Q13526; Q9Y3Q8: TSC22D4; NbExp=7; IntAct=EBI-714158, EBI-739485;
CC Q13526; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-714158, EBI-947187;
CC Q13526; Q14CS0: UBXN2B; NbExp=3; IntAct=EBI-714158, EBI-1993619;
CC Q13526; O43829: ZBTB14; NbExp=3; IntAct=EBI-714158, EBI-10176632;
CC Q13526; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-714158, EBI-2515601;
CC Q13526; O15209: ZBTB22; NbExp=3; IntAct=EBI-714158, EBI-723574;
CC Q13526; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-714158, EBI-12287587;
CC Q13526; O15156: ZBTB7B; NbExp=3; IntAct=EBI-714158, EBI-740434;
CC Q13526; Q96C00: ZBTB9; NbExp=6; IntAct=EBI-714158, EBI-395708;
CC Q13526; Q8NF64: ZMIZ2; NbExp=4; IntAct=EBI-714158, EBI-745786;
CC Q13526; Q8NF64-2: ZMIZ2; NbExp=3; IntAct=EBI-714158, EBI-10182121;
CC Q13526; Q8NF64-3: ZMIZ2; NbExp=3; IntAct=EBI-714158, EBI-12011330;
CC Q13526; Q9NWS9-2: ZNF446; NbExp=6; IntAct=EBI-714158, EBI-740232;
CC Q13526; Q6P9G9: ZNF449; NbExp=3; IntAct=EBI-714158, EBI-10215956;
CC Q13526; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-714158, EBI-11035148;
CC Q13526; Q9H5H4: ZNF768; NbExp=5; IntAct=EBI-714158, EBI-1210580;
CC Q13526; Q6ZMS7-2: ZNF783; NbExp=3; IntAct=EBI-714158, EBI-17789949;
CC Q13526; A0A384NQ31; NbExp=3; IntAct=EBI-714158, EBI-12903728;
CC Q13526; P31424-2: Grm5; Xeno; NbExp=3; IntAct=EBI-714158, EBI-8830305;
CC Q13526; Q3UVX5: Grm5; Xeno; NbExp=2; IntAct=EBI-714158, EBI-8795045;
CC Q13526; P31938: Map2k1; Xeno; NbExp=4; IntAct=EBI-714158, EBI-298860;
CC Q13526; Q63932: Map2k2; Xeno; NbExp=12; IntAct=EBI-714158, EBI-397724;
CC Q13526; Q80Z64-1: Nanog; Xeno; NbExp=2; IntAct=EBI-714158, EBI-15699014;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16476580,
CC ECO:0000269|PubMed:23623683}. Nucleus speckle
CC {ECO:0000269|PubMed:21497122}. Cytoplasm {ECO:0000269|PubMed:21497122}.
CC Note=Colocalizes with NEK6 in the nucleus (PubMed:16476580). Mainly
CC localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results
CC in inhibition of its nuclear localization (PubMed:21497122).
CC {ECO:0000269|PubMed:16476580}.
CC -!- TISSUE SPECIFICITY: Expressed in immune cells in the lung (at protein
CC level) (PubMed:29686383). The phosphorylated form at Ser-71 is
CC expressed in normal breast tissue cells but not in breast cancer cells.
CC {ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:21497122,
CC ECO:0000269|PubMed:29686383}.
CC -!- DOMAIN: The WW domain is required for the interaction with STIL and
CC KIF20B.
CC -!- PTM: Phosphorylation at Ser-71 by DAPK1 results in inhibition of its
CC catalytic activity, nuclear localization, and its ability to induce
CC centrosome amplification, chromosome instability and cell
CC transformation (PubMed:21497122). Ser-71 is dephosphorylated upon IL33-
CC stimulation of dendritic cells (By similarity).
CC {ECO:0000250|UniProtKB:Q9QUR7, ECO:0000269|PubMed:21497122}.
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DR EMBL; U49070; AAC50492.1; -; mRNA.
DR EMBL; CR407654; CAG28582.1; -; mRNA.
DR EMBL; BT019331; AAV38138.1; -; mRNA.
DR EMBL; AK291074; BAF83763.1; -; mRNA.
DR EMBL; CH471106; EAW84057.1; -; Genomic_DNA.
DR EMBL; BC002899; AAH02899.1; -; mRNA.
DR CCDS; CCDS12220.1; -.
DR PIR; S68520; S68520.
DR RefSeq; NP_006212.1; NM_006221.3.
DR PDB; 1F8A; X-ray; 1.84 A; B=1-163.
DR PDB; 1I6C; NMR; -; A=6-44.
DR PDB; 1I8G; NMR; -; B=6-44.
DR PDB; 1I8H; NMR; -; B=6-44.
DR PDB; 1NMV; NMR; -; A=1-163.
DR PDB; 1NMW; NMR; -; A=50-163.
DR PDB; 1PIN; X-ray; 1.35 A; A=1-163.
DR PDB; 1ZCN; X-ray; 1.90 A; A=1-161.
DR PDB; 2F21; X-ray; 1.50 A; A=1-162.
DR PDB; 2ITK; X-ray; 1.45 A; A=1-163.
DR PDB; 2KBU; NMR; -; A=6-39.
DR PDB; 2KCF; NMR; -; A=6-39.
DR PDB; 2LB3; NMR; -; A=6-41.
DR PDB; 2M8I; NMR; -; A=1-39.
DR PDB; 2M8J; NMR; -; A=1-39.
DR PDB; 2M9E; NMR; -; A=6-15, A=22-39.
DR PDB; 2M9F; NMR; -; A=6-15, A=22-39.
DR PDB; 2M9I; NMR; -; A=6-39.
DR PDB; 2M9J; NMR; -; A=6-39.
DR PDB; 2N1O; NMR; -; A=7-39.
DR PDB; 2Q5A; X-ray; 1.50 A; A=1-163.
DR PDB; 2RUC; NMR; -; A=51-163.
DR PDB; 2RUD; NMR; -; A=51-163.
DR PDB; 2RUQ; NMR; -; A=51-163.
DR PDB; 2RUR; NMR; -; A=51-163.
DR PDB; 2XP3; X-ray; 2.00 A; A=1-163.
DR PDB; 2XP4; X-ray; 1.80 A; A=1-163.
DR PDB; 2XP5; X-ray; 1.90 A; A=1-163.
DR PDB; 2XP6; X-ray; 1.90 A; A=1-163.
DR PDB; 2XP7; X-ray; 2.00 A; A=1-163.
DR PDB; 2XP8; X-ray; 2.10 A; A=1-163.
DR PDB; 2XP9; X-ray; 1.90 A; A=1-163.
DR PDB; 2XPA; X-ray; 1.90 A; A=1-163.
DR PDB; 2XPB; X-ray; 2.00 A; A=1-163.
DR PDB; 2ZQS; X-ray; 1.90 A; A=1-163.
DR PDB; 2ZQT; X-ray; 1.46 A; A=1-163.
DR PDB; 2ZQU; X-ray; 2.50 A; A=1-163.
DR PDB; 2ZQV; X-ray; 2.50 A; A=1-163.
DR PDB; 2ZR4; X-ray; 2.00 A; A=1-163.
DR PDB; 2ZR5; X-ray; 2.60 A; A=1-163.
DR PDB; 2ZR6; X-ray; 3.20 A; A=1-163.
DR PDB; 3I6C; X-ray; 1.30 A; A/B=45-163.
DR PDB; 3IK8; X-ray; 1.85 A; A/B=45-163.
DR PDB; 3IKD; X-ray; 2.00 A; A/B=45-163.
DR PDB; 3IKG; X-ray; 1.86 A; A/B=45-163.
DR PDB; 3JYJ; X-ray; 1.87 A; A/B=45-163.
DR PDB; 3KAB; X-ray; 2.19 A; A=1-163.
DR PDB; 3KAC; X-ray; 2.00 A; A/B=45-163.
DR PDB; 3KAD; X-ray; 1.95 A; A=1-163.
DR PDB; 3KAF; X-ray; 2.30 A; A=1-163.
DR PDB; 3KAG; X-ray; 1.90 A; A=1-163.
DR PDB; 3KAH; X-ray; 2.30 A; A=1-163.
DR PDB; 3KAI; X-ray; 1.90 A; A=1-163.
DR PDB; 3KCE; X-ray; 1.90 A; A=1-163.
DR PDB; 3NTP; X-ray; 1.76 A; A=1-163.
DR PDB; 3ODK; X-ray; 2.30 A; A=1-163.
DR PDB; 3OOB; X-ray; 1.89 A; A=1-163.
DR PDB; 3TC5; X-ray; 1.40 A; A=1-163.
DR PDB; 3TCZ; X-ray; 2.10 A; A=6-163.
DR PDB; 3TDB; X-ray; 2.27 A; A=6-163.
DR PDB; 3WH0; X-ray; 1.60 A; A=1-163.
DR PDB; 4GWT; X-ray; 2.25 A; A=6-39.
DR PDB; 4GWV; X-ray; 3.05 A; A=6-39.
DR PDB; 4QIB; X-ray; 1.86 A; A=7-163.
DR PDB; 4TNS; X-ray; 1.33 A; A/B=43-163.
DR PDB; 4TYO; X-ray; 1.75 A; A/B=45-163.
DR PDB; 4U84; X-ray; 1.78 A; A=1-163.
DR PDB; 4U85; X-ray; 1.70 A; A=1-163.
DR PDB; 4U86; X-ray; 1.60 A; A=1-163.
DR PDB; 5B3W; X-ray; 2.40 A; A/B=5-15.
DR PDB; 5B3X; X-ray; 2.40 A; A=5-15.
DR PDB; 5B3Y; X-ray; 1.90 A; A=5-23.
DR PDB; 5B3Z; X-ray; 2.30 A; A/B/C/D=5-39.
DR PDB; 5BMY; X-ray; 2.00 A; A=5-29.
DR PDB; 5GPH; NMR; -; A=51-163.
DR PDB; 5UY9; X-ray; 1.85 A; A=1-163.
DR PDB; 5VTI; X-ray; 1.80 A; A=6-39.
DR PDB; 5VTJ; X-ray; 1.50 A; A=6-39.
DR PDB; 5VTK; X-ray; 1.99 A; A=6-39.
DR PDB; 6DUN; X-ray; 1.59 A; A/B=46-163.
DR PDB; 6O33; X-ray; 1.74 A; A=1-163.
DR PDB; 6O34; X-ray; 1.57 A; A=1-163.
DR PDB; 6SVC; NMR; -; A=6-39.
DR PDB; 6SVE; NMR; -; A=6-39.
DR PDB; 6SVH; NMR; -; A=6-39.
DR PDB; 6VAJ; X-ray; 1.42 A; A=1-163.
DR PDB; 7AOG; X-ray; 1.50 A; P=61-77.
DR PDB; 7AXN; X-ray; 1.40 A; P=61-77.
DR PDB; 7AYF; X-ray; 1.75 A; P=61-77.
DR PDB; 7AZ1; X-ray; 1.15 A; P=61-77.
DR PDB; 7AZ2; X-ray; 1.08 A; P=61-77.
DR PDB; 7BDP; X-ray; 1.75 A; P=61-77.
DR PDB; 7BDT; X-ray; 1.75 A; P=61-77.
DR PDB; 7BDY; X-ray; 1.80 A; P=61-77.
DR PDB; 7BFW; X-ray; 1.80 A; P=61-77.
DR PDB; 7BG3; X-ray; 1.40 A; P=61-77.
DR PDB; 7BGQ; X-ray; 1.75 A; P=61-77.
DR PDB; 7BGR; X-ray; 1.80 A; P=61-77.
DR PDB; 7BGV; X-ray; 1.68 A; P=61-77.
DR PDB; 7BGW; X-ray; 1.90 A; P=61-77.
DR PDB; 7EFJ; X-ray; 1.99 A; A=1-163.
DR PDB; 7EFX; X-ray; 2.41 A; A=1-163.
DR PDB; 7EKV; X-ray; 1.95 A; A=1-163.
DR PDB; 7F0M; X-ray; 1.90 A; A/B/C/D=1-163.
DR PDB; 7NIF; X-ray; 1.71 A; P=61-77.
DR PDB; 7NIG; X-ray; 1.90 A; P=61-77.
DR PDB; 7NJ6; X-ray; 1.59 A; P=61-77.
DR PDB; 7NJ8; X-ray; 1.80 A; P=61-77.
DR PDB; 7NJA; X-ray; 1.75 A; P=61-77.
DR PDB; 7NRK; X-ray; 1.75 A; P=61-77.
DR PDB; 7NRL; X-ray; 1.80 A; P=61-77.
DR PDB; 7SA5; NMR; -; A=1-163.
DR PDBsum; 1F8A; -.
DR PDBsum; 1I6C; -.
DR PDBsum; 1I8G; -.
DR PDBsum; 1I8H; -.
DR PDBsum; 1NMV; -.
DR PDBsum; 1NMW; -.
DR PDBsum; 1PIN; -.
DR PDBsum; 1ZCN; -.
DR PDBsum; 2F21; -.
DR PDBsum; 2ITK; -.
DR PDBsum; 2KBU; -.
DR PDBsum; 2KCF; -.
DR PDBsum; 2LB3; -.
DR PDBsum; 2M8I; -.
DR PDBsum; 2M8J; -.
DR PDBsum; 2M9E; -.
DR PDBsum; 2M9F; -.
DR PDBsum; 2M9I; -.
DR PDBsum; 2M9J; -.
DR PDBsum; 2N1O; -.
DR PDBsum; 2Q5A; -.
DR PDBsum; 2RUC; -.
DR PDBsum; 2RUD; -.
DR PDBsum; 2RUQ; -.
DR PDBsum; 2RUR; -.
DR PDBsum; 2XP3; -.
DR PDBsum; 2XP4; -.
DR PDBsum; 2XP5; -.
DR PDBsum; 2XP6; -.
DR PDBsum; 2XP7; -.
DR PDBsum; 2XP8; -.
DR PDBsum; 2XP9; -.
DR PDBsum; 2XPA; -.
DR PDBsum; 2XPB; -.
DR PDBsum; 2ZQS; -.
DR PDBsum; 2ZQT; -.
DR PDBsum; 2ZQU; -.
DR PDBsum; 2ZQV; -.
DR PDBsum; 2ZR4; -.
DR PDBsum; 2ZR5; -.
DR PDBsum; 2ZR6; -.
DR PDBsum; 3I6C; -.
DR PDBsum; 3IK8; -.
DR PDBsum; 3IKD; -.
DR PDBsum; 3IKG; -.
DR PDBsum; 3JYJ; -.
DR PDBsum; 3KAB; -.
DR PDBsum; 3KAC; -.
DR PDBsum; 3KAD; -.
DR PDBsum; 3KAF; -.
DR PDBsum; 3KAG; -.
DR PDBsum; 3KAH; -.
DR PDBsum; 3KAI; -.
DR PDBsum; 3KCE; -.
DR PDBsum; 3NTP; -.
DR PDBsum; 3ODK; -.
DR PDBsum; 3OOB; -.
DR PDBsum; 3TC5; -.
DR PDBsum; 3TCZ; -.
DR PDBsum; 3TDB; -.
DR PDBsum; 3WH0; -.
DR PDBsum; 4GWT; -.
DR PDBsum; 4GWV; -.
DR PDBsum; 4QIB; -.
DR PDBsum; 4TNS; -.
DR PDBsum; 4TYO; -.
DR PDBsum; 4U84; -.
DR PDBsum; 4U85; -.
DR PDBsum; 4U86; -.
DR PDBsum; 5B3W; -.
DR PDBsum; 5B3X; -.
DR PDBsum; 5B3Y; -.
DR PDBsum; 5B3Z; -.
DR PDBsum; 5BMY; -.
DR PDBsum; 5GPH; -.
DR PDBsum; 5UY9; -.
DR PDBsum; 5VTI; -.
DR PDBsum; 5VTJ; -.
DR PDBsum; 5VTK; -.
DR PDBsum; 6DUN; -.
DR PDBsum; 6O33; -.
DR PDBsum; 6O34; -.
DR PDBsum; 6SVC; -.
DR PDBsum; 6SVE; -.
DR PDBsum; 6SVH; -.
DR PDBsum; 6VAJ; -.
DR PDBsum; 7AOG; -.
DR PDBsum; 7AXN; -.
DR PDBsum; 7AYF; -.
DR PDBsum; 7AZ1; -.
DR PDBsum; 7AZ2; -.
DR PDBsum; 7BDP; -.
DR PDBsum; 7BDT; -.
DR PDBsum; 7BDY; -.
DR PDBsum; 7BFW; -.
DR PDBsum; 7BG3; -.
DR PDBsum; 7BGQ; -.
DR PDBsum; 7BGR; -.
DR PDBsum; 7BGV; -.
DR PDBsum; 7BGW; -.
DR PDBsum; 7EFJ; -.
DR PDBsum; 7EFX; -.
DR PDBsum; 7EKV; -.
DR PDBsum; 7F0M; -.
DR PDBsum; 7NIF; -.
DR PDBsum; 7NIG; -.
DR PDBsum; 7NJ6; -.
DR PDBsum; 7NJ8; -.
DR PDBsum; 7NJA; -.
DR PDBsum; 7NRK; -.
DR PDBsum; 7NRL; -.
DR PDBsum; 7SA5; -.
DR AlphaFoldDB; Q13526; -.
DR BMRB; Q13526; -.
DR SMR; Q13526; -.
DR BioGRID; 111317; 366.
DR CORUM; Q13526; -.
DR DIP; DIP-29306N; -.
DR ELM; Q13526; -.
DR IntAct; Q13526; 209.
DR MINT; Q13526; -.
DR STRING; 9606.ENSP00000247970; -.
DR BindingDB; Q13526; -.
DR ChEMBL; CHEMBL2288; -.
DR DrugBank; DB06867; 3,6,9,12,15,18-HEXAOXAICOSANE.
DR DrugBank; DB01766; Beta-(2-Naphthyl)-Alanine.
DR GuidetoPHARMACOLOGY; 3171; -.
DR iPTMnet; Q13526; -.
DR MetOSite; Q13526; -.
DR PhosphoSitePlus; Q13526; -.
DR BioMuta; PIN1; -.
DR DMDM; 3024406; -.
DR EPD; Q13526; -.
DR jPOST; Q13526; -.
DR MassIVE; Q13526; -.
DR MaxQB; Q13526; -.
DR PaxDb; Q13526; -.
DR PeptideAtlas; Q13526; -.
DR PRIDE; Q13526; -.
DR ProteomicsDB; 59519; -.
DR Antibodypedia; 3867; 769 antibodies from 44 providers.
DR DNASU; 5300; -.
DR Ensembl; ENST00000247970.9; ENSP00000247970.5; ENSG00000127445.14.
DR Ensembl; ENST00000588695.5; ENSP00000466962.1; ENSG00000127445.14.
DR GeneID; 5300; -.
DR KEGG; hsa:5300; -.
DR MANE-Select; ENST00000247970.9; ENSP00000247970.5; NM_006221.4; NP_006212.1.
DR UCSC; uc002mml.3; human.
DR CTD; 5300; -.
DR DisGeNET; 5300; -.
DR GeneCards; PIN1; -.
DR HGNC; HGNC:8988; PIN1.
DR HPA; ENSG00000127445; Low tissue specificity.
DR MIM; 601052; gene.
DR neXtProt; NX_Q13526; -.
DR OpenTargets; ENSG00000127445; -.
DR PharmGKB; PA33320; -.
DR VEuPathDB; HostDB:ENSG00000127445; -.
DR eggNOG; KOG3259; Eukaryota.
DR GeneTree; ENSGT00640000091578; -.
DR HOGENOM; CLU_090028_0_1_1; -.
DR InParanoid; Q13526; -.
DR OMA; DEVQCLH; -.
DR OrthoDB; 1437969at2759; -.
DR PhylomeDB; Q13526; -.
DR TreeFam; TF101101; -.
DR BRENDA; 5.2.1.8; 2681.
DR PathwayCommons; Q13526; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR SignaLink; Q13526; -.
DR SIGNOR; Q13526; -.
DR BioGRID-ORCS; 5300; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; PIN1; human.
DR EvolutionaryTrace; Q13526; -.
DR GeneWiki; PIN1; -.
DR GenomeRNAi; 5300; -.
DR Pharos; Q13526; Tchem.
DR PRO; PR:Q13526; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q13526; protein.
DR Bgee; ENSG00000127445; Expressed in right frontal lobe and 191 other tissues.
DR ExpressionAtlas; Q13526; baseline and differential.
DR Genevisible; Q13526; HS.
DR GO; GO:0036064; C:ciliary basal body; IDA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030496; C:midbody; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:0008013; F:beta-catenin binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0016859; F:cis-trans isomerase activity; IMP:UniProtKB.
DR GO; GO:0003774; F:cytoskeletal motor activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:BHF-UCL.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:BHF-UCL.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; ISS:ARUK-UCL.
DR GO; GO:0050815; F:phosphoserine residue binding; IDA:BHF-UCL.
DR GO; GO:0050816; F:phosphothreonine residue binding; IDA:BHF-UCL.
DR GO; GO:0048156; F:tau protein binding; NAS:ARUK-UCL.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IMP:UniProtKB.
DR GO; GO:2000146; P:negative regulation of cell motility; IDA:BHF-UCL.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0030182; P:neuron differentiation; ISS:ParkinsonsUK-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:BHF-UCL.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:ARUK-UCL.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; TAS:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IDA:BHF-UCL.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IDA:ARUK-UCL.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; TAS:ProtInc.
DR GO; GO:0060393; P:regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IDA:ARUK-UCL.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR GO; GO:0050808; P:synapse organization; ISS:ParkinsonsUK-UCL.
DR CDD; cd00201; WW; 1.
DR DisProt; DP02727; -.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00639; Rotamase; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cytoplasm; Isomerase; Nucleus;
KW Phosphoprotein; Reference proteome; Rotamase.
FT CHAIN 1..163
FT /note="Peptidyl-prolyl cis-trans isomerase NIMA-interacting
FT 1"
FT /id="PRO_0000193435"
FT DOMAIN 5..39
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 52..163
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT REGION 33..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 46
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 71
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000269|PubMed:21497122,
FT ECO:0000269|PubMed:29686383"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MUTAGEN 23
FT /note="Y->A: Reduced affinity for KIF20B."
FT /evidence="ECO:0000269|PubMed:11470801"
FT MUTAGEN 34
FT /note="W->A: Loss of binding to phosphorylated target
FT proteins, including to phosphorylated RBBP8/CtIP; decrease
FT in DNA repair of double-strand breaks by homologous
FT recombination less efficient than that observed with wild-
FT type protein. Abolishes interaction with IRAK3/IRAK-M.
FT Abolishes IL33-mediated increase of IRAK3/IRAK-M protein
FT levels."
FT /evidence="ECO:0000269|PubMed:22608923,
FT ECO:0000269|PubMed:23623683, ECO:0000269|PubMed:29686383"
FT MUTAGEN 63
FT /note="K->A: Loss of peptidyl-prolyl cis/trans isomerase
FT activity. No effect on the interaction with IRAK3/IRAK-M.
FT Abolishes IL33-mediated increase of IRAK3/IRAK-M protein
FT levels."
FT /evidence="ECO:0000269|PubMed:22608923,
FT ECO:0000269|PubMed:29686383"
FT MUTAGEN 71
FT /note="S->D,E: Loss of peptidyl-prolyl cis/trans isomerase
FT activity, nuclear localization and cellular function."
FT /evidence="ECO:0000269|PubMed:21497122"
FT MUTAGEN 113
FT /note="C->A: Loss of peptidyl-prolyl cis/trans isomerase
FT activity; decrease in DNA repair of double-strand breaks by
FT homologous recombination slightly less efficient than that
FT observed with wild-type protein. No effect on RBBP8/CtIP."
FT /evidence="ECO:0000269|PubMed:23623683"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:7SA5"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:1PIN"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:3TC5"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:1PIN"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1PIN"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1PIN"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1I6C"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:3I6C"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3I6C"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3I6C"
FT HELIX 82..98
FT /evidence="ECO:0007829|PDB:3I6C"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3I6C"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:3I6C"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:3I6C"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3I6C"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2RUD"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:3I6C"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3I6C"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:3I6C"
SQ SEQUENCE 163 AA; 18243 MW; 35391AF40B7D1E13 CRC64;
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG EPARVRCSHL
LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG
DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTE
