PEX14_HUMAN
ID PEX14_HUMAN Reviewed; 377 AA.
AC O75381; B2R7N1; B3KML6; B7Z1N2; Q8WX51;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Peroxisomal membrane protein PEX14;
DE AltName: Full=PTS1 receptor-docking protein;
DE AltName: Full=Peroxin-14;
DE AltName: Full=Peroxisomal membrane anchor protein PEX14;
GN Name=PEX14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PEX5 AND PEX13,
RP AND FUNCTION.
RX PubMed=9653144; DOI=10.1073/pnas.95.14.8087;
RA Fransen M., Terlecky S.R., Subramani S.;
RT "Identification of a human PTS1 receptor docking protein directly required
RT for peroxisomal protein import.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8087-8092(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10212238; DOI=10.1074/jbc.274.18.12593;
RA Shimizu N., Itoh R., Hirono Y., Otera H., Ghaedi K., Tateishi K.,
RA Tamura S., Okumoto K., Harano T., Mukai S., Fujiki Y.;
RT "The peroxin Pex14p. cDNA cloning by functional complementation on a
RT Chinese hamster ovary cell mutant, characterization, and functional
RT analysis.";
RL J. Biol. Chem. 274:12593-12604(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Cerebellum, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-34; 184-195 AND 352-363, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lempens A., Norman J.C.;
RL Submitted (OCT-2009) to UniProtKB.
RN [9]
RP INTERACTION WITH PEX19.
RX PubMed=10704444; DOI=10.1083/jcb.148.5.931;
RA Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.;
RT "PEX19 binds multiple peroxisomal membrane proteins, is predominantly
RT cytoplasmic, and is required for peroxisome membrane synthesis.";
RL J. Cell Biol. 148:931-944(2000).
RN [10]
RP INVOLVEMENT IN PBD-CGK AND PBD13A.
RX PubMed=15146459; DOI=10.1002/humu.20032;
RA Shimozawa N., Tsukamoto T., Nagase T., Takemoto Y., Koyama N., Suzuki Y.,
RA Komori M., Osumi T., Jeannette G., Wanders R.J., Kondo N.;
RT "Identification of a new complementation group of the peroxisome biogenesis
RT disorders and PEX14 as the mutated gene.";
RL Hum. Mutat. 23:552-558(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP STRUCTURE BY NMR OF 16-80 IN COMPLEXES WITH PEX5 AND PEX19, MUTAGENESIS OF
RP PHE-52 AND LYS-56, SUBCELLULAR LOCATION, AND INTERACTION WITH PEX5 AND
RP PEX19.
RX PubMed=19197237; DOI=10.1038/emboj.2009.7;
RA Neufeld C., Filipp F.V., Simon B., Neuhaus A., Schueller N., David C.,
RA Kooshapur H., Madl T., Erdmann R., Schliebs W., Wilmanns M., Sattler M.;
RT "Structural basis for competitive interactions of Pex14 with the import
RT receptors Pex5 and Pex19.";
RL EMBO J. 28:745-754(2009).
RN [21]
RP FUNCTION, AND INTERACTION WITH TUBULIN.
RX PubMed=21525035; DOI=10.1242/jcs.079368;
RA Bharti P., Schliebs W., Schievelbusch T., Neuhaus A., David C., Kock K.,
RA Herrmann C., Meyer H.E., Wiese S., Warscheid B., Theiss C., Erdmann R.;
RT "PEX14 is required for microtubule-based peroxisome motility in human
RT cells.";
RL J. Cell Sci. 124:1759-1768(2011).
CC -!- FUNCTION: Peroxisome membrane protein that is an essential component of
CC the peroxisomal import machinery. Functions as a docking factor for the
CC predominantly cytoplasmic PTS1 receptor (PEX5). Plays a key role for
CC peroxisome movement through a direct interaction with tubulin.
CC {ECO:0000269|PubMed:21525035, ECO:0000269|PubMed:9653144}.
CC -!- SUBUNIT: Interacts with PEX5, PEX13 and PEX19. Interacts with tubulin.
CC {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:19197237,
CC ECO:0000269|PubMed:21525035, ECO:0000269|PubMed:9653144}.
CC -!- INTERACTION:
CC O75381; Q9Y6Y1: CAMTA1; NbExp=2; IntAct=EBI-594898, EBI-1222733;
CC O75381; Q9BS16: CENPK; NbExp=3; IntAct=EBI-594898, EBI-6871750;
CC O75381; Q8TDI0: CHD5; NbExp=2; IntAct=EBI-594898, EBI-1042816;
CC O75381; Q9BT78: COPS4; NbExp=3; IntAct=EBI-594898, EBI-742413;
CC O75381; Q14204: DYNC1H1; NbExp=4; IntAct=EBI-594898, EBI-356015;
CC O75381; Q8IYM0: FAM186B; NbExp=2; IntAct=EBI-594898, EBI-6269645;
CC O75381; O43681: GET3; NbExp=3; IntAct=EBI-594898, EBI-2515857;
CC O75381; Q9Y4F3: MARF1; NbExp=3; IntAct=EBI-594898, EBI-5235902;
CC O75381; Q14511: NEDD9; NbExp=2; IntAct=EBI-594898, EBI-2108053;
CC O75381; P40855: PEX19; NbExp=26; IntAct=EBI-594898, EBI-594747;
CC O75381; P50542: PEX5; NbExp=13; IntAct=EBI-594898, EBI-597835;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:19197237}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19197237}; Cytoplasmic side
CC {ECO:0000269|PubMed:19197237}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75381-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75381-2; Sequence=VSP_037021;
CC -!- DISEASE: Peroxisome biogenesis disorder complementation group K (PBD-
CC CGK) [MIM:614887]: A peroxisomal disorder arising from a failure of
CC protein import into the peroxisomal membrane or matrix. The peroxisome
CC biogenesis disorders (PBD group) are genetically heterogeneous with at
CC least 14 distinct genetic groups as concluded from complementation
CC studies. Include disorders are: Zellweger syndrome (ZWS), neonatal
CC adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and
CC classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and
CC IRD are distinct from RCDP and constitute a clinical continuum of
CC overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS).
CC {ECO:0000269|PubMed:15146459}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Peroxisome biogenesis disorder 13A (PBD13A) [MIM:614887]: A
CC fatal peroxisome biogenesis disorder belonging to the Zellweger disease
CC spectrum and clinically characterized by severe neurologic dysfunction
CC with profound psychomotor retardation, severe hypotonia and neonatal
CC seizures, craniofacial abnormalities, liver dysfunction, and
CC biochemically by the absence of peroxisomes. Additional features
CC include cardiovascular and skeletal defects, renal cysts, ocular
CC abnormalities, and hearing impairment. Most severely affected
CC individuals with the classic form of the disease (classic Zellweger
CC syndrome) die within the first year of life.
CC {ECO:0000269|PubMed:15146459}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peroxin-14 family. {ECO:0000305}.
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DR EMBL; AF045186; AAC39843.1; -; mRNA.
DR EMBL; AB017546; BAA36837.1; -; mRNA.
DR EMBL; AK002194; BAG51028.1; -; mRNA.
DR EMBL; AK293684; BAH11568.1; -; mRNA.
DR EMBL; AK313046; BAG35878.1; -; mRNA.
DR EMBL; CR450321; CAG29317.1; -; mRNA.
DR EMBL; CR542083; CAG46880.1; -; mRNA.
DR EMBL; AL139423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71661.1; -; Genomic_DNA.
DR EMBL; BC006327; AAH06327.1; -; mRNA.
DR CCDS; CCDS30582.1; -. [O75381-1]
DR RefSeq; NP_004556.1; NM_004565.2. [O75381-1]
DR RefSeq; XP_011539882.1; XM_011541580.1. [O75381-2]
DR PDB; 2W84; NMR; -; A=16-80.
DR PDB; 2W85; NMR; -; A=16-80.
DR PDB; 4BXU; NMR; -; A=16-80.
DR PDBsum; 2W84; -.
DR PDBsum; 2W85; -.
DR PDBsum; 4BXU; -.
DR AlphaFoldDB; O75381; -.
DR BMRB; O75381; -.
DR SMR; O75381; -.
DR BioGRID; 111218; 214.
DR CORUM; O75381; -.
DR ELM; O75381; -.
DR IntAct; O75381; 217.
DR MINT; O75381; -.
DR STRING; 9606.ENSP00000349016; -.
DR BindingDB; O75381; -.
DR ChEMBL; CHEMBL4523152; -.
DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family.
DR iPTMnet; O75381; -.
DR PhosphoSitePlus; O75381; -.
DR BioMuta; PEX14; -.
DR EPD; O75381; -.
DR jPOST; O75381; -.
DR MassIVE; O75381; -.
DR MaxQB; O75381; -.
DR PaxDb; O75381; -.
DR PeptideAtlas; O75381; -.
DR PRIDE; O75381; -.
DR ProteomicsDB; 49953; -. [O75381-1]
DR ProteomicsDB; 49954; -. [O75381-2]
DR TopDownProteomics; O75381-2; -. [O75381-2]
DR Antibodypedia; 27930; 312 antibodies from 33 providers.
DR DNASU; 5195; -.
DR Ensembl; ENST00000356607.9; ENSP00000349016.4; ENSG00000142655.13. [O75381-1]
DR GeneID; 5195; -.
DR KEGG; hsa:5195; -.
DR MANE-Select; ENST00000356607.9; ENSP00000349016.4; NM_004565.3; NP_004556.1.
DR UCSC; uc001arn.5; human. [O75381-1]
DR CTD; 5195; -.
DR DisGeNET; 5195; -.
DR GeneCards; PEX14; -.
DR GeneReviews; PEX14; -.
DR HGNC; HGNC:8856; PEX14.
DR HPA; ENSG00000142655; Low tissue specificity.
DR MalaCards; PEX14; -.
DR MIM; 601791; gene.
DR MIM; 614887; phenotype.
DR neXtProt; NX_O75381; -.
DR OpenTargets; ENSG00000142655; -.
DR Orphanet; 772; Infantile Refsum disease.
DR Orphanet; 44; Neonatal adrenoleukodystrophy.
DR Orphanet; 912; Zellweger syndrome.
DR PharmGKB; PA33198; -.
DR VEuPathDB; HostDB:ENSG00000142655; -.
DR eggNOG; KOG2629; Eukaryota.
DR GeneTree; ENSGT00390000015047; -.
DR HOGENOM; CLU_065928_0_0_1; -.
DR InParanoid; O75381; -.
DR OMA; RRDWRDW; -.
DR OrthoDB; 1033073at2759; -.
DR PhylomeDB; O75381; -.
DR TreeFam; TF323535; -.
DR PathwayCommons; O75381; -.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import.
DR SignaLink; O75381; -.
DR SIGNOR; O75381; -.
DR BioGRID-ORCS; 5195; 36 hits in 1085 CRISPR screens.
DR ChiTaRS; PEX14; human.
DR EvolutionaryTrace; O75381; -.
DR GeneWiki; PEX14; -.
DR GenomeRNAi; 5195; -.
DR Pharos; O75381; Tbio.
DR PRO; PR:O75381; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75381; protein.
DR Bgee; ENSG00000142655; Expressed in bronchial epithelial cell and 194 other tissues.
DR ExpressionAtlas; O75381; baseline and differential.
DR Genevisible; O75381; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0034453; P:microtubule anchoring; IDA:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
DR GO; GO:0036250; P:peroxisome transport along microtubule; IDA:UniProtKB.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:UniProtKB.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IBA:GO_Central.
DR GO; GO:0044721; P:protein import into peroxisome matrix, substrate release; IDA:UniProtKB.
DR GO; GO:0016561; P:protein import into peroxisome matrix, translocation; IDA:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR025655; PEX14.
DR InterPro; IPR006785; Pex14_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR23058; PTHR23058; 1.
DR Pfam; PF04695; Pex14_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Membrane; Peroxisome; Peroxisome biogenesis disorder; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport;
KW Zellweger syndrome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..377
FT /note="Peroxisomal membrane protein PEX14"
FT /id="PRO_0000058325"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..338
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q642G4"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT VAR_SEQ 58..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037021"
FT VARIANT 117
FT /note="A -> S (in dbSNP:rs12061667)"
FT /id="VAR_051269"
FT VARIANT 150
FT /note="A -> S (in dbSNP:rs11539793)"
FT /id="VAR_051270"
FT VARIANT 320
FT /note="R -> K (in dbSNP:rs12070353)"
FT /id="VAR_051271"
FT MUTAGEN 52
FT /note="F->A,W: Reduced interaction with PEX19, minor effect
FT on interaction with PEX5."
FT /evidence="ECO:0000269|PubMed:19197237"
FT MUTAGEN 56
FT /note="K->A,E: Reduced interaction with PEX19, minor effect
FT on interaction with PEX5."
FT /evidence="ECO:0000269|PubMed:19197237"
FT CONFLICT 319
FT /note="K -> E (in Ref. 3; BAG51028)"
FT /evidence="ECO:0000305"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:4BXU"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:2W84"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2W84"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:2W84"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:2W84"
SQ SEQUENCE 377 AA; 41237 MW; FED28F62A0B94E7F CRC64;
MASSEQAEQP SQPSSTPGSE NVLPREPLIA TAVKFLQNSR VRQSPLATRR AFLKKKGLTD
EEIDMAFQQS GTAADEPSSL GPATQVVPVQ PPHLISQPYS PAGSRWRDYG ALAIIMAGIA
FGFHQLYKKY LLPLILGGRE DRKQLERMEA GLSELSGSVA QTVTQLQTTL ASVQELLIQQ
QQKIQELAHE LAAAKATTST NWILESQNIN ELKSEINSLK GLLLNRRQFP PSPSAPKIPS
WQIPVKSPSP SSPAAVNHHS SSDISPVSNE STSSSPGKEG HSPEGSTVTY HLLGPQEEGE
GVVDVKGQVR MEVQGEEEKR EDKEDEEDEE DDDVSHVDEE DCLGVQREDR RGGDGQINEQ
VEKLRRPEGA SNESERD
