ID PIN1_HUMAN Reviewed; 163 AA. AC Q13526; Q53X75; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 07-JUL-2009, entry version 91. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; DE EC=5.2.1.8; DE AltName: Full=Rotamase Pin1; DE AltName: Full=PPIase Pin1; GN Name=PIN1; 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]. RX MEDLINE=96195064; 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 RT 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 RT vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP INTERACTION WITH MPHOSPH1, AND MUTAGENESIS OF TYR-23. RX MEDLINE=21463052; 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 RT for mitotic peptidyl-prolyl isomerase Pin1."; RL J. Biol. Chem. 276:37520-37528(2001). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASS RP SPECTROMETRY. RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., 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 [7] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [8] RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS). RX MEDLINE=97344079; 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 RT suggests substrate recognition is phosphorylation dependent."; RL Cell 89:875-886(1997). CC -!- FUNCTION: Essential PPIase that regulates mitosis presumably by CC interacting with NIMA and attenuating its mitosis-promoting CC activity. Displays a preference for an acidic residue N-terminal CC to the isomerized proline bond. Catalyzing pSer/Thr-Pro cis/trans CC isomerizations. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- SUBUNIT: Interacts with STIL (By similarity). Interacts with CC MPHOSPH1. CC -!- INTERACTION: CC Q9HC98:NEK6; NbExp=2; IntAct=EBI-714158, EBI-740364; CC P40337:VHL; NbExp=1; IntAct=EBI-714158, EBI-301246; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- DOMAIN: The WW domain is required for the interaction with STIL CC and MPHOSPH1. CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. CC -!- SIMILARITY: Contains 1 PpiC domain. CC -!- SIMILARITY: Contains 1 WW domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U49070; AAC50492.1; -; mRNA. DR EMBL; CR407654; CAG28582.1; -; mRNA. DR EMBL; BT019331; AAV38138.1; -; mRNA. DR EMBL; BC002899; AAH02899.1; -; mRNA. DR IPI; IPI00013723; -. DR PIR; S68520; S68520. DR RefSeq; NP_006212.1; -. DR UniGene; Hs.465849; -. 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; 2KCF; NMR; -; A=6-39. DR PDB; 2Q5A; X-ray; 1.50 A; 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; 2KCF; -. DR PDBsum; 2Q5A; -. DR IntAct; Q13526; 30. DR PhosphoSite; Q13526; -. DR PeptideAtlas; Q13526; -. DR PRIDE; Q13526; -. DR Ensembl; ENSG00000127445; Homo sapiens. DR GeneID; 5300; -. DR KEGG; hsa:5300; -. DR UCSC; uc002mml.1; human. DR GeneCards; GC19P009806; -. DR H-InvDB; HIX0014730; -. DR HGNC; HGNC:8988; PIN1. DR HPA; CAB004528; -. DR HPA; CAB009326; -. DR MIM; 601052; gene. DR PharmGKB; PA134978864; -. DR HOGENOM; Q13526; -. DR HOVERGEN; Q13526; -. DR OMA; Q13526; NGQGEPT. DR BRENDA; 5.2.1.8; 247. DR NextBio; 20486; -. DR ArrayExpress; Q13526; -. DR Bgee; Q13526; -. DR CleanEx; HS_PIN1; -. DR GermOnline; ENSG00000127445; Homo sapiens. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB. DR GO; GO:0050815; F:phosphoserine binding; IDA:UniProtKB. DR GO; GO:0050816; F:phosphothreonine binding; IDA:UniProtKB. DR GO; GO:0070412; F:R-SMAD binding; IPI:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0030512; P:negative regulation of transforming growth ...; IDA:UniProtKB. DR GO; GO:0051443; P:positive regulation of ubiquitin-protein li...; IDA:UniProtKB. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW. DR GO; GO:0007088; P:regulation of mitosis; TAS:ProtInc. DR GO; GO:0060393; P:regulation of pathway-restricted SMAD prote...; IDA:UniProtKB. DR InterPro; IPR000297; PPIase_PpiC. DR InterPro; IPR001202; WW_Rsp5_WWP. DR Pfam; PF00639; Rotamase; 1. DR Pfam; PF00397; WW; 1. DR SMART; SM00456; WW; 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; Cell cycle; Complete proteome; Isomerase; Nucleus; KW Phosphoprotein; Rotamase. FT CHAIN 1 163 Peptidyl-prolyl cis-trans isomerase NIMA- FT interacting 1. FT /FTId=PRO_0000193435. FT DOMAIN 5 39 WW. FT DOMAIN 52 163 PpiC. FT MOD_RES 108 108 Phosphoserine. FT MUTAGEN 23 23 Y->A: Reduced affinity for MPHOSPH1. FT STRAND 11 15 FT STRAND 22 26 FT TURN 27 29 FT STRAND 32 35 FT STRAND 55 62 FT STRAND 67 69 FT STRAND 75 77 FT HELIX 82 98 FT STRAND 99 101 FT HELIX 103 110 FT HELIX 114 118 FT STRAND 121 125 FT HELIX 132 140 FT STRAND 156 163 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 //