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O75381

- PEX14_HUMAN

UniProt

O75381 - PEX14_HUMAN

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Protein

Peroxisomal membrane protein PEX14

Gene

PEX14

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

Functioni

Component of the peroxisomal translocation machinery with PEX13 and PEX17. Interacts with both the PTS1 and PTS2 receptors. Binds directly to PEX17.

GO - Molecular functioni

  1. beta-tubulin binding Source: UniProtKB
  2. microtubule binding Source: UniProtKB
  3. protein N-terminus binding Source: UniProtKB
  4. receptor binding Source: UniProtKB
  5. transcription corepressor activity Source: UniProtKB

GO - Biological processi

  1. microtubule anchoring Source: UniProtKB
  2. negative regulation of protein binding Source: UniProtKB
  3. negative regulation of protein homotetramerization Source: UniProtKB
  4. negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  5. negative regulation of transcription, DNA-templated Source: UniProtKB
  6. peroxisome organization Source: UniProtKB
  7. peroxisome transport along microtubule Source: UniProtKB
  8. protein complex assembly Source: UniProtKB
  9. protein homooligomerization Source: UniProtKB
  10. protein import into peroxisome matrix Source: UniProtKB
  11. protein import into peroxisome matrix, substrate release Source: UniProtKB
  12. protein import into peroxisome matrix, translocation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Protein family/group databases

TCDBi3.A.20.1.1. the peroxisomal protein importer (ppi) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal membrane protein PEX14
Alternative name(s):
PTS1 receptor-docking protein
Peroxin-14
Peroxisomal membrane anchor protein PEX14
Gene namesi
Name:PEX14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:8856. PEX14.

Subcellular locationi

Peroxisome membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
  2. intracellular Source: UniProtKB
  3. intracellular membrane-bounded organelle Source: HPA
  4. membrane Source: UniProtKB
  5. nucleolus Source: HPA
  6. nucleus Source: UniProtKB
  7. peroxisomal membrane Source: UniProtKB
  8. peroxisome Source: UniProtKB
  9. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Peroxisome

Pathology & Biotechi

Involvement in diseasei

Peroxisome biogenesis disorder complementation group K (PBD-CGK) [MIM:614887]: A peroxisomal disorder arising from a failure of protein import into the peroxisomal membrane or matrix. The peroxisome biogenesis disorders (PBD group) are genetically heterogeneous with at least 14 distinct genetic groups as concluded from complementation studies. Include disorders are: Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct from RCDP and constitute a clinical continuum of overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS).
Note: The disease is caused by mutations affecting the gene represented in this entry.
Peroxisome biogenesis disorder 13A (PBD13A) [MIM:614887]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521F → A or W: Reduced interaction with PEX19, minor effect on interaction with PEX5. 1 Publication
Mutagenesisi56 – 561K → A or E: Reduced interaction with PEX19, minor effect on interaction with PEX5. 1 Publication

Keywords - Diseasei

Peroxisome biogenesis disorder, Zellweger syndrome

Organism-specific databases

MIMi614887. phenotype.
Orphaneti772. Infantile Refsum disease.
44. Neonatal adrenoleukodystrophy.
912. Zellweger syndrome.
PharmGKBiPA33198.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 377376Peroxisomal membrane protein PEX14PRO_0000058325Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei34 – 341N6-acetyllysine1 Publication
Modified residuei335 – 3351Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO75381.
PaxDbiO75381.
PeptideAtlasiO75381.
PRIDEiO75381.

PTM databases

PhosphoSiteiO75381.

Expressioni

Gene expression databases

BgeeiO75381.
CleanExiHS_PEX14.
ExpressionAtlasiO75381. baseline and differential.
GenevestigatoriO75381.

Organism-specific databases

HPAiHPA046104.
HPA049231.

Interactioni

Subunit structurei

Interacts with PEX5 and PEX19.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PEX19P4085515EBI-594898,EBI-594747
PEX5P5054213EBI-594898,EBI-597835

Protein-protein interaction databases

BioGridi111218. 62 interactions.
IntActiO75381. 62 interactions.
MINTiMINT-241450.
STRINGi9606.ENSP00000349016.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 224
Helixi26 – 3611
Helixi41 – 433
Helixi46 – 5510
Helixi60 – 7011

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W84NMR-A16-80[»]
2W85NMR-A16-80[»]
4BXUNMR-A16-80[»]
ProteinModelPortaliO75381.
SMRiO75381. Positions 20-76.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75381.

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxin-14 family.Curated

Phylogenomic databases

eggNOGiNOG136629.
GeneTreeiENSGT00390000015047.
HOGENOMiHOG000220930.
HOVERGENiHBG053571.
InParanoidiO75381.
KOiK13343.
OMAiWQIPVKP.
OrthoDBiEOG7DFXD4.
PhylomeDBiO75381.
TreeFamiTF323535.

Family and domain databases

InterProiIPR025655. PEX14.
IPR006785. Pex14_N.
[Graphical view]
PANTHERiPTHR23058. PTHR23058. 1 hit.
PfamiPF04695. Pex14_N. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75381-1) [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
MASSEQAEQP SQPSSTPGSE NVLPREPLIA TAVKFLQNSR VRQSPLATRR
60 70 80 90 100
AFLKKKGLTD EEIDMAFQQS GTAADEPSSL GPATQVVPVQ PPHLISQPYS
110 120 130 140 150
PAGSRWRDYG ALAIIMAGIA FGFHQLYKKY LLPLILGGRE DRKQLERMEA
160 170 180 190 200
GLSELSGSVA QTVTQLQTTL ASVQELLIQQ QQKIQELAHE LAAAKATTST
210 220 230 240 250
NWILESQNIN ELKSEINSLK GLLLNRRQFP PSPSAPKIPS WQIPVKSPSP
260 270 280 290 300
SSPAAVNHHS SSDISPVSNE STSSSPGKEG HSPEGSTVTY HLLGPQEEGE
310 320 330 340 350
GVVDVKGQVR MEVQGEEEKR EDKEDEEDEE DDDVSHVDEE DCLGVQREDR
360 370
RGGDGQINEQ VEKLRRPEGA SNESERD
Length:377
Mass (Da):41,237
Last modified:November 1, 1998 - v1
Checksum:iFED28F62A0B94E7F
GO
Isoform 2 (identifier: O75381-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-100: Missing.

Note: No experimental confirmation available.

Show »
Length:334
Mass (Da):36,702
Checksum:i03B5FAF2B7892357
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti319 – 3191K → E in BAG51028. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti117 – 1171A → S.
Corresponds to variant rs12061667 [ dbSNP | Ensembl ].
VAR_051269
Natural varianti150 – 1501A → S.
Corresponds to variant rs11539793 [ dbSNP | Ensembl ].
VAR_051270
Natural varianti320 – 3201R → K.
Corresponds to variant rs12070353 [ dbSNP | Ensembl ].
VAR_051271

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei58 – 10043Missing in isoform 2. 1 PublicationVSP_037021Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF045186 mRNA. Translation: AAC39843.1.
AB017546 mRNA. Translation: BAA36837.1.
AK002194 mRNA. Translation: BAG51028.1.
AK293684 mRNA. Translation: BAH11568.1.
AK313046 mRNA. Translation: BAG35878.1.
CR450321 mRNA. Translation: CAG29317.1.
CR542083 mRNA. Translation: CAG46880.1.
AL139423, AL354956, AL591403 Genomic DNA. Translation: CAD20149.2.
AL354956, AL139423, AL591403 Genomic DNA. Translation: CAI19198.1.
AL591403, AL139423, AL354956 Genomic DNA. Translation: CAH70044.1.
CH471130 Genomic DNA. Translation: EAW71661.1.
BC006327 mRNA. Translation: AAH06327.1.
CCDSiCCDS30582.1. [O75381-1]
RefSeqiNP_004556.1. NM_004565.2. [O75381-1]
UniGeneiHs.149983.

Genome annotation databases

EnsembliENST00000356607; ENSP00000349016; ENSG00000142655. [O75381-1]
GeneIDi5195.
KEGGihsa:5195.
UCSCiuc001arn.3. human. [O75381-1]
uc010oan.2. human. [O75381-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF045186 mRNA. Translation: AAC39843.1 .
AB017546 mRNA. Translation: BAA36837.1 .
AK002194 mRNA. Translation: BAG51028.1 .
AK293684 mRNA. Translation: BAH11568.1 .
AK313046 mRNA. Translation: BAG35878.1 .
CR450321 mRNA. Translation: CAG29317.1 .
CR542083 mRNA. Translation: CAG46880.1 .
AL139423 , AL354956 , AL591403 Genomic DNA. Translation: CAD20149.2 .
AL354956 , AL139423 , AL591403 Genomic DNA. Translation: CAI19198.1 .
AL591403 , AL139423 , AL354956 Genomic DNA. Translation: CAH70044.1 .
CH471130 Genomic DNA. Translation: EAW71661.1 .
BC006327 mRNA. Translation: AAH06327.1 .
CCDSi CCDS30582.1. [O75381-1 ]
RefSeqi NP_004556.1. NM_004565.2. [O75381-1 ]
UniGenei Hs.149983.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2W84 NMR - A 16-80 [» ]
2W85 NMR - A 16-80 [» ]
4BXU NMR - A 16-80 [» ]
ProteinModelPortali O75381.
SMRi O75381. Positions 20-76.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111218. 62 interactions.
IntActi O75381. 62 interactions.
MINTi MINT-241450.
STRINGi 9606.ENSP00000349016.

Protein family/group databases

TCDBi 3.A.20.1.1. the peroxisomal protein importer (ppi) family.

PTM databases

PhosphoSitei O75381.

Proteomic databases

MaxQBi O75381.
PaxDbi O75381.
PeptideAtlasi O75381.
PRIDEi O75381.

Protocols and materials databases

DNASUi 5195.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356607 ; ENSP00000349016 ; ENSG00000142655 . [O75381-1 ]
GeneIDi 5195.
KEGGi hsa:5195.
UCSCi uc001arn.3. human. [O75381-1 ]
uc010oan.2. human. [O75381-2 ]

Organism-specific databases

CTDi 5195.
GeneCardsi GC01P010532.
GeneReviewsi PEX14.
HGNCi HGNC:8856. PEX14.
HPAi HPA046104.
HPA049231.
MIMi 601791. gene.
614887. phenotype.
neXtProti NX_O75381.
Orphaneti 772. Infantile Refsum disease.
44. Neonatal adrenoleukodystrophy.
912. Zellweger syndrome.
PharmGKBi PA33198.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG136629.
GeneTreei ENSGT00390000015047.
HOGENOMi HOG000220930.
HOVERGENi HBG053571.
InParanoidi O75381.
KOi K13343.
OMAi WQIPVKP.
OrthoDBi EOG7DFXD4.
PhylomeDBi O75381.
TreeFami TF323535.

Miscellaneous databases

ChiTaRSi PEX14. human.
EvolutionaryTracei O75381.
GeneWikii PEX14.
GenomeRNAii 5195.
NextBioi 20094.
PROi O75381.
SOURCEi Search...

Gene expression databases

Bgeei O75381.
CleanExi HS_PEX14.
ExpressionAtlasi O75381. baseline and differential.
Genevestigatori O75381.

Family and domain databases

InterProi IPR025655. PEX14.
IPR006785. Pex14_N.
[Graphical view ]
PANTHERi PTHR23058. PTHR23058. 1 hit.
Pfami PF04695. Pex14_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a human PTS1 receptor docking protein directly required for peroxisomal protein import."
    Fransen M., Terlecky S.R., Subramani S.
    Proc. Natl. Acad. Sci. U.S.A. 95:8087-8092(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The peroxin Pex14p. cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis."
    Shimizu N., Itoh R., Hirono Y., Otera H., Ghaedi K., Tateishi K., Tamura S., Okumoto K., Harano T., Mukai S., Fujiki Y.
    J. Biol. Chem. 274:12593-12604(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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] (ISOFORMS 1 AND 2).
    Tissue: Brain, Cerebellum and Placenta.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Muscle.
  8. Bienvenut W.V., Lempens A., Norman J.C.
    Submitted (OCT-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-34; 184-195 AND 352-363, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  9. "PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis."
    Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.
    J. Cell Biol. 148:931-944(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PEX19.
  10. "Identification of a new complementation group of the peroxisome biogenesis disorders and PEX14 as the mutated gene."
    Shimozawa N., Tsukamoto T., Nagase T., Takemoto Y., Koyama N., Suzuki Y., Komori M., Osumi T., Jeannette G., Wanders R.J., Kondo N.
    Hum. Mutat. 23:552-558(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PBD-CGK AND PBD13A.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Structural basis for competitive interactions of Pex14 with the import receptors Pex5 and Pex19."
    Neufeld C., Filipp F.V., Simon B., Neuhaus A., Schueller N., David C., Kooshapur H., Madl T., Erdmann R., Schliebs W., Wilmanns M., Sattler M.
    EMBO J. 28:745-754(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 16-80 IN COMPLEXES WITH PEX5 AND PEX19, MUTAGENESIS OF PHE-52 AND LYS-56, SUBCELLULAR LOCATION, INTERACTION WITH PEX5 AND PEX19.

Entry informationi

Entry nameiPEX14_HUMAN
AccessioniPrimary (citable) accession number: O75381
Secondary accession number(s): B2R7N1
, B3KML6, B7Z1N2, Q8WX51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: October 29, 2014
This is version 126 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3