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Protein

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4

Gene

Pin4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

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
Peptidyl-prolyl cis-trans isomerase Pin4
Short name:
PPIase Pin4
Rotamase Pin4
Gene namesi
Name:Pin4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1916963. Pin4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 131131Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4PRO_0000193439Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine; by CK2By similarity

Post-translational modificationi

Phosphorylated. Phosphorylation occurs both in the nucleus and the cytoplasm. 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 form associates with the pre-rRNP complexes in the nucleus (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9CWW6.
MaxQBiQ9CWW6.
PaxDbiQ9CWW6.
PeptideAtlasiQ9CWW6.
PRIDEiQ9CWW6.

PTM databases

iPTMnetiQ9CWW6.
PhosphoSiteiQ9CWW6.

Expressioni

Gene expression databases

BgeeiQ9CWW6.
GenevisibleiQ9CWW6. MM.

Interactioni

Subunit structurei

Found in pre-ribosomal ribonucleoprotein (pre-rRNP) complexes.1 Publication

Protein-protein interaction databases

IntActiQ9CWW6. 1 interaction.
STRINGi10090.ENSMUSP00000109257.

Structurei

3D structure databases

ProteinModelPortaliQ9CWW6.
SMRiQ9CWW6. Positions 30-131.
ModBaseiSearch...
MobiDBiSearch...

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 complexesBy similarityAdd
BLAST
Regioni1 – 2525Necessary for nuclear localization and DNA-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 PpiC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3258. Eukaryota.
COG0760. LUCA.
GeneTreeiENSGT00510000047029.
HOGENOMiHOG000275330.
HOVERGENiHBG019150.
InParanoidiQ9CWW6.
KOiK09579.
OMAiLGWKTKG.
OrthoDBiEOG7WT43M.
PhylomeDBiQ9CWW6.
TreeFamiTF101102.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9CWW6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPKGKSGSG KGGKGGAASG SDSADKKSQG PKGGGNAVKV RHILCEKHGK
60 70 80 90 100
IMEAMEKLKS GMRFSEVATQ YSEDKARQGG DLGWMTRGSM VGPFQEAAFA
110 120 130
LPVSGMDKPV FTDPPVKTKF GYHIIMVEGR K
Length:131
Mass (Da):13,815
Last modified:June 1, 2001 - v1
Checksum:i290BDEF72DC69CA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010338 mRNA. Translation: BAB26863.1.
AL807784 Genomic DNA. Translation: CAM24632.1.
CH466564 Genomic DNA. Translation: EDL14129.1.
BC119355 mRNA. Translation: AAI19356.1.
BC119357 mRNA. Translation: AAI19358.1.
CCDSiCCDS41082.1.
RefSeqiNP_081457.1. NM_027181.1.
XP_011249230.1. XM_011250928.1.
UniGeneiMm.371635.

Genome annotation databases

EnsembliENSMUST00000113627; ENSMUSP00000109257; ENSMUSG00000079480.
GeneIDi105247253.
69713.
KEGGimmu:105247253.
mmu:69713.
UCSCiuc009tyj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010338 mRNA. Translation: BAB26863.1.
AL807784 Genomic DNA. Translation: CAM24632.1.
CH466564 Genomic DNA. Translation: EDL14129.1.
BC119355 mRNA. Translation: AAI19356.1.
BC119357 mRNA. Translation: AAI19358.1.
CCDSiCCDS41082.1.
RefSeqiNP_081457.1. NM_027181.1.
XP_011249230.1. XM_011250928.1.
UniGeneiMm.371635.

3D structure databases

ProteinModelPortaliQ9CWW6.
SMRiQ9CWW6. Positions 30-131.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CWW6. 1 interaction.
STRINGi10090.ENSMUSP00000109257.

PTM databases

iPTMnetiQ9CWW6.
PhosphoSiteiQ9CWW6.

Proteomic databases

EPDiQ9CWW6.
MaxQBiQ9CWW6.
PaxDbiQ9CWW6.
PeptideAtlasiQ9CWW6.
PRIDEiQ9CWW6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000113627; ENSMUSP00000109257; ENSMUSG00000079480.
GeneIDi105247253.
69713.
KEGGimmu:105247253.
mmu:69713.
UCSCiuc009tyj.1. mouse.

Organism-specific databases

CTDi5303.
MGIiMGI:1916963. Pin4.

Phylogenomic databases

eggNOGiKOG3258. Eukaryota.
COG0760. LUCA.
GeneTreeiENSGT00510000047029.
HOGENOMiHOG000275330.
HOVERGENiHBG019150.
InParanoidiQ9CWW6.
KOiK09579.
OMAiLGWKTKG.
OrthoDBiEOG7WT43M.
PhylomeDBiQ9CWW6.
TreeFamiTF101102.

Miscellaneous databases

PROiQ9CWW6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CWW6.
GenevisibleiQ9CWW6. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic stem cell.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    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].
    Tissue: Brain.
  5. "Isolation and proteomic characterization of human Parvulin-associating pre-ribosomal ribonucleoprotein complexes."
    Fujiyama S., Yanagida M., Hayano T., Miura Y., Isobe T., Fujimori F., Uchida T., Takahashi N.
    J. Biol. Chem. 277:23773-23780(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN PRE-RRNP COMPLEXES.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPIN4_MOUSE
AccessioniPrimary (citable) accession number: Q9CWW6
Secondary accession number(s): Q0VE57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.