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Q9Y237

- PIN4_HUMAN

UniProt

Q9Y237 - PIN4_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4

Gene

PIN4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA.1 Publication
    Isoform 2 binds to double-stranded DNA.1 Publication

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).

    GO - Molecular functioni

    1. bent DNA binding Source: UniProtKB
    2. DNA binding Source: UniProtKB-KW
    3. double-stranded DNA binding Source: UniProtKB
    4. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW
    5. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. protein folding Source: UniProtKB-KW
    2. rRNA processing Source: UniProtKB

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (EC:5.2.1.8)
    Alternative name(s):
    Parvulin-14
    Short name:
    Par14
    Short name:
    hPar14
    Parvulin-17
    Short name:
    Par17
    Short name:
    hPar17
    Peptidyl-prolyl cis-trans isomerase Pin4
    Short name:
    PPIase Pin4
    Peptidyl-prolyl cis/trans isomerase EPVH
    Short name:
    hEPVH
    Rotamase Pin4
    Gene namesi
    Name:PIN4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:8992. PIN4.

    Subcellular locationi

    Isoform 1 : Nucleusnucleolus. Cytoplasmcytoskeletonspindle. Cytoplasm
    Note: Colocalizes in the nucleolus during interphase and on the spindle apparatus during mitosis with NPM1.
    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrial matrix Source: UniProtKB
    4. nucleolus Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. preribosome Source: UniProtKB
    7. spindle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 191S → A: Abolishes phosphorylation and reduces strongly nuclear localization. 1 Publication
    Mutagenesisi19 – 191S → E: Does not abolish nuclear localization and reduces DNA-binding ability. 1 Publication

    Organism-specific databases

    PharmGKBiPA33324.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 131131Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4PRO_0000193438Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Phosphoserine; by CK22 Publications

    Post-translational modificationi

    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.2 Publications
    Isoform 2 is sumoylated with SUMO2 and SUMO3.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y237.
    PaxDbiQ9Y237.
    PRIDEiQ9Y237.

    PTM databases

    PhosphoSiteiQ9Y237.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Gene expression databases

    ArrayExpressiQ9Y237.
    BgeeiQ9Y237.
    CleanExiHS_PIN4.
    GenevestigatoriQ9Y237.

    Organism-specific databases

    HPAiHPA054483.

    Interactioni

    Subunit structurei

    Isoform 1 is found in pre-ribosomal ribonucleoprotein (pre-rRNP) complexes.By similarity

    Protein-protein interaction databases

    BioGridi111320. 21 interactions.
    DIPiDIP-50838N.
    IntActiQ9Y237. 6 interactions.
    STRINGi9606.ENSP00000218432.

    Structurei

    Secondary structure

    1
    131
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi37 – 4711
    Helixi48 – 5912
    Helixi64 – 718
    Beta strandi73 – 753
    Helixi76 – 783
    Beta strandi81 – 866
    Helixi92 – 998
    Turni108 – 1103
    Beta strandi116 – 1183
    Beta strandi121 – 13010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EQ3NMR-A36-131[»]
    1FJDNMR-A28-131[»]
    3UI4X-ray0.80A36-131[»]
    3UI5X-ray1.40A36-131[»]
    3UI6X-ray0.89A36-131[»]
    ProteinModelPortaliQ9Y237.
    SMRiQ9Y237. Positions 36-131.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y237.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 12995PpiCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 4141Necessary for association with the pre-rRNP complexesAdd
    BLAST
    Regioni1 – 2525Necessary for nuclear localization and DNA-bindingAdd
    BLAST

    Domaini

    The PPIase domain enhances mitochondrial targeting.

    Sequence similaritiesi

    Contains 1 PpiC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0760.
    HOVERGENiHBG019150.
    InParanoidiQ9Y237.
    KOiK09579.
    OMAiSCKADES.
    PhylomeDBiQ9Y237.
    TreeFamiTF101102.

    Family and domain databases

    InterProiIPR000297. PPIase_PpiC.
    [Graphical view]
    PROSITEiPS50198. PPIC_PPIASE_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative promoter usage. Align

    Isoform 1 (identifier: Q9Y237-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPPKGKSGSG KAGKGGAASG SDSADKKAQG PKGGGNAVKV RHILCEKHGK    50
    IMEAMEKLKS GMRFNEVAAQ YSEDKARQGG DLGWMTRGSM VGPFQEAAFA 100
    LPVSGMDKPV FTDPPVKTKF GYHIIMVEGR K 131
    Length:131
    Mass (Da):13,810
    Last modified:November 1, 1999 - v1
    Checksum:i787C15BDB0701258
    GO
    Isoform 2 (identifier: Q9Y237-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MPMAGLLKGLVRQLERFSVQQQASKM

    Note: The first 25 amino acids are sufficient for mitochondrial targeting.2 Publications

    Show »
    Length:156
    Mass (Da):16,608
    Checksum:i8D4668D3ADB24740
    GO
    Isoform 3 (identifier: Q9Y237-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MPMAGLLKGLVRQLERFSVQQQASKM
         80-131: GDLGWMTRGS...YHIIMVEGRK → IPSLQQHAGHHRDLRSTLISLVSYLQTTP

    Note: No experimental confirmation available.

    Show »
    Length:133
    Mass (Da):14,179
    Checksum:iB217F63257D92D65
    GO

    Sequence cautioni

    The sequence AAH05234.2 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH70288.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAI04654.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAI11395.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAG54532.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 2 (identifier: Q9Y237-2)
    Natural varianti16 – 161R → Q.2 Publications
    Corresponds to variant rs6525589 [ dbSNP | Ensembl ].
    Natural varianti18 – 181S → R.2 Publications
    Corresponds to variant rs7058353 [ dbSNP | Ensembl ].

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MPMAGLLKGLVRQLERFSVQ QQASKM in isoform 2 and isoform 3. 2 PublicationsVSP_037754
    Alternative sequencei80 – 13152GDLGW…VEGRK → IPSLQQHAGHHRDLRSTLIS LVSYLQTTP in isoform 3. 1 PublicationVSP_046122Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF143096 mRNA. Translation: AAD27893.1.
    AB009690 mRNA. Translation: BAA82320.1.
    BX119917, AL135749 Genomic DNA. Translation: CAI39856.1.
    BC005234 mRNA. Translation: AAH05234.2. Different initiation.
    BC070288 mRNA. Translation: AAH70288.1. Different initiation.
    BC093700 mRNA. Translation: AAH93700.1.
    BC104653 mRNA. Translation: AAI04654.1. Different initiation.
    BC111394 mRNA. Translation: AAI11395.1. Different initiation.
    BC112281 mRNA. Translation: AAI12282.1.
    AM420633 Genomic DNA. Translation: CAM12362.1.
    AK127605 mRNA. Translation: BAG54532.1. Different initiation.
    CCDSiCCDS14417.1. [Q9Y237-2]
    CCDS55447.1. [Q9Y237-3]
    RefSeqiNP_001164218.1. NM_001170747.1. [Q9Y237-3]
    NP_006214.2. NM_006223.3. [Q9Y237-2]
    UniGeneiHs.655623.

    Genome annotation databases

    EnsembliENST00000373669; ENSP00000362773; ENSG00000102309. [Q9Y237-2]
    ENST00000423432; ENSP00000409154; ENSG00000102309. [Q9Y237-3]
    GeneIDi5303.
    KEGGihsa:5303.
    UCSCiuc004eam.3. human. [Q9Y237-2]

    Polymorphism databases

    DMDMi20139299.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF143096 mRNA. Translation: AAD27893.1 .
    AB009690 mRNA. Translation: BAA82320.1 .
    BX119917 , AL135749 Genomic DNA. Translation: CAI39856.1 .
    BC005234 mRNA. Translation: AAH05234.2 . Different initiation.
    BC070288 mRNA. Translation: AAH70288.1 . Different initiation.
    BC093700 mRNA. Translation: AAH93700.1 .
    BC104653 mRNA. Translation: AAI04654.1 . Different initiation.
    BC111394 mRNA. Translation: AAI11395.1 . Different initiation.
    BC112281 mRNA. Translation: AAI12282.1 .
    AM420633 Genomic DNA. Translation: CAM12362.1 .
    AK127605 mRNA. Translation: BAG54532.1 . Different initiation.
    CCDSi CCDS14417.1. [Q9Y237-2 ]
    CCDS55447.1. [Q9Y237-3 ]
    RefSeqi NP_001164218.1. NM_001170747.1. [Q9Y237-3 ]
    NP_006214.2. NM_006223.3. [Q9Y237-2 ]
    UniGenei Hs.655623.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EQ3 NMR - A 36-131 [» ]
    1FJD NMR - A 28-131 [» ]
    3UI4 X-ray 0.80 A 36-131 [» ]
    3UI5 X-ray 1.40 A 36-131 [» ]
    3UI6 X-ray 0.89 A 36-131 [» ]
    ProteinModelPortali Q9Y237.
    SMRi Q9Y237. Positions 36-131.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111320. 21 interactions.
    DIPi DIP-50838N.
    IntActi Q9Y237. 6 interactions.
    STRINGi 9606.ENSP00000218432.

    Chemistry

    BindingDBi Q9Y237.
    ChEMBLi CHEMBL4923.

    PTM databases

    PhosphoSitei Q9Y237.

    Polymorphism databases

    DMDMi 20139299.

    Proteomic databases

    MaxQBi Q9Y237.
    PaxDbi Q9Y237.
    PRIDEi Q9Y237.

    Protocols and materials databases

    DNASUi 5303.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373669 ; ENSP00000362773 ; ENSG00000102309 . [Q9Y237-2 ]
    ENST00000423432 ; ENSP00000409154 ; ENSG00000102309 . [Q9Y237-3 ]
    GeneIDi 5303.
    KEGGi hsa:5303.
    UCSCi uc004eam.3. human. [Q9Y237-2 ]

    Organism-specific databases

    CTDi 5303.
    GeneCardsi GC0XP071401.
    H-InvDB HIX0016866.
    HGNCi HGNC:8992. PIN4.
    HPAi HPA054483.
    MIMi 300252. gene.
    neXtProti NX_Q9Y237.
    PharmGKBi PA33324.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0760.
    HOVERGENi HBG019150.
    InParanoidi Q9Y237.
    KOi K09579.
    OMAi SCKADES.
    PhylomeDBi Q9Y237.
    TreeFami TF101102.

    Miscellaneous databases

    EvolutionaryTracei Q9Y237.
    GeneWikii PIN4.
    GenomeRNAii 5303.
    NextBioi 20496.
    PROi Q9Y237.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y237.
    Bgeei Q9Y237.
    CleanExi HS_PIN4.
    Genevestigatori Q9Y237.

    Family and domain databases

    InterProi IPR000297. PPIase_PpiC.
    [Graphical view ]
    PROSITEi PS50198. PPIC_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of eukaryotic parvulin homologues: a new subfamily of peptidylprolyl cis-trans isomerases."
      Rulten S.L., Thorpe J.R., Kay J.E.
      Biochem. Biophys. Res. Commun. 259:557-562(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase."
      Uchida T., Fujimori F., Tradler T., Fischer G., Rahfeld J.-U.
      FEBS Lett. 446:278-282(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    3. "The DNA sequence of the human X chromosome."
      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.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS GLN-16 AND ARG-18 (ISOFORM 2).
      Tissue: Brain, Prostate and Urinary bladder.
    5. "Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation."
      Mueller J.W., Kessler D., Neumann D., Stratmann T., Papatheodorou P., Hartmann-Fatu C., Bayer P.
      BMC Mol. Biol. 7:9-9(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-13 (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE PROMOTER USAGE, SUMOYLATION, TISSUE SPECIFICITY, VARIANTS GLN-16 AND ARG-18 (ISOFORM 2).
    6. "The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae."
      Kessler D., Papatheodorou P., Stratmann T., Dian E.A., Hartmann-Fatu C., Rassow J., Bayer P., Mueller J.W.
      BMC Biol. 5:37-37(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6 AND 48-72, ALTERNATIVE PROMOTER USAGE (ISOFORMS 1 AND 2), DNA-BINDING, SUBCELLULAR LOCATION.
    7. "Phosphorylation of the N-terminal domain regulates subcellular localization and DNA binding properties of the peptidyl-prolyl cis/trans isomerase hPar14."
      Reimer T., Weiwad M., Schierhorn A., Ruecknagel P.-K., Rahfeld J.-U., Bayer P., Fischer G.
      J. Mol. Biol. 330:955-966(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 15-25, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-19, MUTAGENESIS OF SER-19, SUBCELLULAR LOCATION.
    8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-131 (ISOFORM 3).
      Tissue: Brain.
    9. "The N-terminal basic domain of human parvulin hPar14 is responsible for the entry to the nucleus and high-affinity DNA-binding."
      Surmacz T.A., Bayer E., Rahfeld J.-U., Fischer G., Bayer P.
      J. Mol. Biol. 321:235-247(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, SUBCELLULAR LOCATION.
    10. "Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA processing factor that evolved in the metazoan lineage."
      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.
      Mol. Cell. Proteomics 8:1552-1565(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN PRE-RRNP COMPLEXES, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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."
      Sekerina E., Rahfeld J.-U., Mueller J., Fanghaenel J., Rascher C., Fischer G., Bayer P.
      J. Mol. Biol. 301:1003-1017(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 36-131.
    13. "Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14."
      Terada T., Shirouzu M., Fukumori Y., Fujimori F., Ito Y., Kigawa T., Yokoyama S., Uchida T.
      J. Mol. Biol. 305:917-926(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 28-131.

    Entry informationi

    Entry nameiPIN4_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y237
    Secondary accession number(s): A8E0G6
    , B3KXM0, F5H1P5, Q0D2H3, Q3MHV0, Q52M21, Q5HYW6, Q6IRW4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3