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Q9Y237

- PIN4_HUMAN

UniProt

Q9Y237 - PIN4_HUMAN

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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

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
Complete GO annotation...

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. cytoskeleton Source: UniProtKB-KW
  3. extracellular vesicular exosome Source: UniProt
  4. mitochondrial matrix Source: UniProtKB
  5. mitochondrion Source: UniProtKB-KW
  6. nucleolus Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. preribosome Source: UniProtKB
  9. spindle Source: UniProtKB
Complete GO annotation...

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 CK21 Publication

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

BgeeiQ9Y237.
CleanExiHS_PIN4.
ExpressionAtlasiQ9Y237. baseline and differential.
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 – 4711Combined sources
Helixi48 – 5912Combined sources
Helixi64 – 718Combined sources
Beta strandi73 – 753Combined sources
Helixi76 – 783Combined sources
Beta strandi81 – 866Combined sources
Helixi92 – 998Combined sources
Turni108 – 1103Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi121 – 13010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00510000047029.
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

        10         20         30         40         50
MPPKGKSGSG KAGKGGAASG SDSADKKAQG PKGGGNAVKV RHILCEKHGK
60 70 80 90 100
IMEAMEKLKS GMRFNEVAAQ YSEDKARQGG DLGWMTRGSM VGPFQEAAFA
110 120 130
LPVSGMDKPV FTDPPVKTKF GYHIIMVEGR K
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. Curated
The sequence AAH70288.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAI04654.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAI11395.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAG54532.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00510000047029.
HOVERGENi HBG019150.
InParanoidi Q9Y237.
KOi K09579.
OMAi SCKADES.
PhylomeDBi Q9Y237.
TreeFami TF101102.

Miscellaneous databases

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

Gene expression databases

Bgeei Q9Y237.
CleanExi HS_PIN4.
ExpressionAtlasi Q9Y237. baseline and differential.
Genevestigatori Q9Y237.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: November 26, 2014
This is version 124 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