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(Top) 1 References 2 Further reading

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4

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PIN4

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
1EQ3, 1FJD, 3UI4, 3UI5, 3UI6

Identifiers

Aliases

PIN4, EPVH, PAR14, PAR17, peptidylprolyl cis/trans isomerase, NIMA-interacting 4

External IDs

OMIM: 300252; MGI: 1916963; HomoloGene: 121907; GeneCards: PIN4; OMA:PIN4 - orthologs

Gene location (Human)

Chr.	X chromosome (human)^[1]

Band	Xq13.1	Start	72,181,353 bp^[1]
Band	Xq13.1	End	72,302,926 bp^[1]

Gene location (Mouse)

Chr.	X chromosome (mouse)^[2]

Band	X\|X D	Start	102,119,447 bp^[2]
Band	X\|X D	End	102,127,669 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

tendon of biceps brachii

gingival epithelium

amniotic fluid

germinal epithelium

buccal mucosa cell

hair follicle

pancreatic epithelial cell

pancreatic ductal cell

palpebral conjunctiva

kidney tubule

Top expressed in

yolk sac

lens

epiblast

embryo

duodenum

morula

bone marrow

urinary bladder

embryo

dentate gyrus of hippocampal formation granule cell

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	DNA binding double-stranded DNA binding protein binding bent DNA binding isomerase activity peptidyl-prolyl cis-trans isomerase activity RNA binding
Cellular component	cytoplasm mitochondrial matrix spindle preribosome nucleolus extracellular exosome cytoskeleton mitochondrion nucleus
Biological process	rRNA processing protein peptidyl-prolyl isomerization
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


5303


69713

Ensembl


ENSG00000102309


ENSMUSG00000079480

UniProt


Q9Y237


Q9CWW6

RefSeq (mRNA)


NM_001170747 NM_006223


NM_027181

RefSeq (protein)


NP_001164218 NP_006214


NP_081457 NP_001352019

Location (UCSC)

Chr X: 72.18 – 72.3 Mb

Chr X: 102.12 – 102.13 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 is an enzyme that in humans is encoded by the PIN4 gene.^[5]^[6]^[7]

References[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000102309 – Ensembl, May 2017

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000079480 – Ensembl, May 2017

^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ Mueller JW, Kessler D, Neumann D, Stratmann T, Papatheodorou P, Hartmann-Fatu C, Bayer P (Mar 2006). "Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation". BMC Mol Biol. 7: 9. doi:10.1186/1471-2199-7-9. PMC 1420321. PMID 16522211.

^ Kessler D, Papatheodorou P, Stratmann T, Dian EA, Hartmann-Fatu C, Rassow J, Bayer P, Mueller JW (Oct 2007). "The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae". BMC Biol. 5: 37. doi:10.1186/1741-7007-5-37. PMC 2031878. PMID 17875217.

^ "Entrez Gene: PIN4 protein (peptidylprolyl cis/trans isomerase) NIMA-interacting, 4 (parvulin)".

Further reading[edit]

Uchida T, Fujimori F, Tradler T, et al. (1999). "Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase". FEBS Lett. 446 (2–3): 278–82. Bibcode:1999FEBSL.446..278U. doi:10.1016/S0014-5793(99)00239-2. PMID 10100858. S2CID 45172611.

Rulten S, Thorpe J, Kay J (1999). "Identification of eukaryotic parvulin homologues: a new subfamily of peptidylprolyl cis-trans isomerases". Biochem. Biophys. Res. Commun. 259 (3): 557–62. doi:10.1006/bbrc.1999.0828. PMID 10364457.

Sekerina E, Rahfeld JU, Müller J, et al. (2000). "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". J. Mol. Biol. 301 (4): 1003–17. doi:10.1006/jmbi.2000.4013. PMID 10966801.

Terada T, Shirouzu M, Fukumori Y, et al. (2001). "Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14". J. Mol. Biol. 305 (4): 917–26. doi:10.1006/jmbi.2000.4293. PMID 11162102.

Suzuki Y, Tsunoda T, Sese J, et al. (2001). "Identification and characterization of the potential promoter regions of 1031 kinds of human genes". Genome Res. 11 (5): 677–84. doi:10.1101/gr.gr-1640r. PMC 311086. PMID 11337467.

Fujiyama S, Yanagida M, Hayano T, et al. (2002). "Isolation and proteomic characterization of human Parvulin-associating preribosomal ribonucleoprotein complexes". J. Biol. Chem. 277 (26): 23773–80. doi:10.1074/jbc.M201181200. PMID 11960984.

Surmacz TA, Bayer E, Rahfeld JU, et al. (2002). "The N-terminal basic domain of human parvulin hPar14 is responsible for the entry to the nucleus and high-affinity DNA-binding". J. Mol. Biol. 321 (2): 235–47. doi:10.1016/S0022-2836(02)00615-0. PMID 12144781.

Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.

Reimer T, Weiwad M, Schierhorn A, et al. (2003). "Phosphorylation of the N-terminal domain regulates subcellular localization and DNA binding properties of the peptidyl-prolyl cis/trans isomerase hPar14". J. Mol. Biol. 330 (5): 955–66. doi:10.1016/S0022-2836(03)00713-7. PMID 12860119.

Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

v t e PDB gallery
1eq3: NMR STRUCTURE OF HUMAN PARVULIN HPAR14 1fjd: HUMAN PARVULIN-LIKE PEPTIDYL PROLYL CIS/TRANS ISOMERASE, HPAR14

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