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UniProtKB/Swiss-Prot entry Q13526


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PIN1_HUMAN
Primary accession number Q13526
Secondary accession number Q53X75
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 78)
Name and origin of the protein
Protein name Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
Synonyms EC 5.2.1.8
Rotamase Pin1
PPIase Pin1
Gene name
Name: PIN1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/380544a0; PubMed=8606777 [NCBI, ExPASy, EBI, Israel, Japan]
Lu K.P., Hanes S.D., Hunter T.;
"A human peptidyl-prolyl isomerase essential for regulation of mitosis.";
Nature 380:544-547(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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]
INTERACTION WITH MPHOSPH1, AND MUTAGENESIS OF TYR-23.
DOI=10.1074/jbc.M106207200; PubMed=11470801 [NCBI, ExPASy, EBI, Israel, Japan]
Kamimoto T., Zama T., Aoki R., Muro Y., Hagiwara M.;
"Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1.";
J. Biol. Chem. 276:37520-37528(2001).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[7]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
DOI=10.1016/S0092-8674(00)80273-1; PubMed=9200606 [NCBI, ExPASy, EBI, Israel, Japan]
Ranganathan R., Lu K.P., Hunter T., Noel J.P.;
"Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent.";
Cell 89:875-886(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U49070; AAC50492.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR407654; CAG28582.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019331; AAV38138.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002899; AAH02899.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S68520; S68520.
RefSeq NP_006212.1; -.
UniGene Hs.465849
3D structure databases
PDB
1F8A; X-ray; 1.84 A; B=1-163.[ExPASy / RCSB / EBI]
1I6C; NMR; -; A=6-44.[ExPASy / RCSB / EBI]
1I8G; NMR; -; B=6-44.[ExPASy / RCSB / EBI]
1I8H; NMR; -; B=6-44.[ExPASy / RCSB / EBI]
1NMV; NMR; -; A=1-163.[ExPASy / RCSB / EBI]
1NMW; NMR; -; A=50-163.[ExPASy / RCSB / EBI]
1PIN; X-ray; 1.35 A; A=1-163.[ExPASy / RCSB / EBI]
1ZCN; X-ray; 1.90 A; A=1-163.[ExPASy / RCSB / EBI]
2F21; X-ray; 1.50 A; A=1-163.[ExPASy / RCSB / EBI]
2ITK; X-ray; 1.45 A; A=1-163.[ExPASy / RCSB / EBI]
2Q5A; X-ray; 1.50 A; A=1-163.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1F8A; -.
1I6C; -.
1I8G; -.
1I8H; -.
1NMV; -.
1NMW; -.
1PIN; -.
1ZCN; -.
2F21; -.
2ITK; -.
2Q5A; -.
ModBase Q13526.
Protein-protein interaction databases
IntAct Q13526; -.
PTM databases
PhosphoSite Q13526; -.
Organism-specific databases
H-InvDB HIX0014730; -.
HGNC HGNC:8988; PIN1.
GenAtlas PIN1.
HPA CAB004528; -.
CAB009326; -.
MIM 601052; gene. [NCBI / EBI]
PharmGKB PA134978864; -.
GeneCards Q13526.
Gene expression databases
ArrayExpress Q13526; -.
CleanEx HS_PIN1; -.
GermOnline ENSG00000127445; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0007088; Biological process: regulation of mitosis (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000297; PPIase_PpiC.
IPR002349; WW.
IPR001202; WW_Rsp5_WWP.
Graphical view of domain structure.
Pfam PF00639; Rotamase; 1.
PF00397; WW; 1.
Pfam graphical view of domain structure.
PRINTS PR00403; WWDOMAIN.
SMART SM00456; WW; 1.
SMART graphical view of domain structure.
PROSITE PS01096; PPIC_PPIASE_1; 1.
PS50198; PPIC_PPIASE_2; 1.
PS01159; WW_DOMAIN_1; 1.
PS50020; WW_DOMAIN_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q13526.
Proteomic databases
PeptideAtlas Q13526; -.
Genome annotation databases
Ensembl ENSG00000127445; Homo sapiens. [Contig view]
GeneID 5300; -.
KEGG hsa:5300; -.
Phylogenomic databases
HOGENOM Q13526; -.
HOVERGEN Q13526; -.
Other
LinkHub Q13526; -.
SOURCE PIN1; Homo sapiens.
ProtoNet Q13526.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell cycle; Isomerase; Nucleus; Phosphoprotein; Rotamase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   163  163     Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1. PRO_0000193435
DOMAIN   5    39  35     WW. 
DOMAIN   52   163  112     PpiC. 
MOD_RES   108   108        Phosphoserine. 
MUTAGEN   23    23        Y->A: Reduced affinity for MPHOSPH1. 
STRAND   11    15  5      
STRAND   22    26  5      
TURN   27    29  3      
STRAND   32    35  4      
STRAND   55    62  8      
STRAND   67    69  3      
STRAND   75    77  3      
HELIX   82    98  17      
STRAND   99   101  3      
HELIX   103   110  8      
HELIX   114   118  5      
STRAND   121   125  5      
HELIX   132   140  9      
Sequence information
Length: 163 AA [This is the length of the unprocessed precursor] Molecular weight: 18243 Da [This is the MW of the unprocessed precursor] CRC64: 35391AF40B7D1E13 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG EPARVRCSHL 

        70         80         90        100        110        120 
LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG 

       130        140        150        160 
DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTE 

Q13526 in FASTA format

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View entry in raw text format (no links)
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