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O14829

- PPE1_HUMAN

UniProt

O14829 - PPE1_HUMAN

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Protein

Serine/threonine-protein phosphatase with EF-hands 1

Gene

PPEF1

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

Functioni

May have a role in the recovery or adaptation response of photoreceptors. May have a role in development.

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Protein has several cofactor binding sites:
  • Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity
  • Mg2+By similarity

Enzyme regulationi

Activated by calcium.

pH dependencei

Optimum pH is 8.0.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi172 – 1721Manganese 1By similarity
Metal bindingi174 – 1741Manganese 1By similarity
Metal bindingi201 – 2011Manganese 1By similarity
Metal bindingi201 – 2011Manganese 2By similarity
Metal bindingi233 – 2331Manganese 2By similarity
Active sitei234 – 2341Proton donorBy similarity
Metal bindingi285 – 2851Manganese 2By similarity
Metal bindingi403 – 4031Manganese 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi579 – 590121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi619 – 630122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. manganese ion binding Source: InterPro
  4. protein serine/threonine phosphatase activity Source: Reactome

GO - Biological processi

  1. detection of stimulus involved in sensory perception Source: InterPro
  2. phototransduction, visible light Source: Reactome
  3. protein dephosphorylation Source: ProtInc
  4. regulation of rhodopsin mediated signaling pathway Source: Reactome
  5. rhodopsin mediated signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calcium, Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase with EF-hands 1 (EC:3.1.3.16)
Short name:
PPEF-1
Alternative name(s):
Protein phosphatase with EF calcium-binding domain
Short name:
PPEF
Serine/threonine-protein phosphatase 7
Short name:
PP7
Gene namesi
Name:PPEF1
Synonyms:PPEF, PPP7C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:9243. PPEF1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33564.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 653653Serine/threonine-protein phosphatase with EF-hands 1PRO_0000058899Add
BLAST

Proteomic databases

PaxDbiO14829.
PRIDEiO14829.

PTM databases

PhosphoSiteiO14829.

Expressioni

Tissue specificityi

Detected in retina and retinal derived Y-79 retinoblastoma cells. Also found in fetal brain.

Gene expression databases

BgeeiO14829.
CleanExiHS_PPEF1.
ExpressionAtlasiO14829. baseline and differential.
GenevestigatoriO14829.

Organism-specific databases

HPAiHPA034577.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Calm3P622042EBI-2931238,EBI-397460From a different organism.

Protein-protein interaction databases

BioGridi111471. 1 interaction.
IntActiO14829. 1 interaction.
STRINGi9606.ENSP00000354871.

Structurei

3D structure databases

ProteinModelPortaliO14829.
SMRiO14829. Positions 107-451, 464-638.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 4530IQPROSITE-ProRule annotationAdd
BLAST
Domaini483 – 51836EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini566 – 60136EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini606 – 64136EF-hand 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni121 – 455335CatalyticAdd
BLAST

Sequence similaritiesi

Belongs to the PPP phosphatase family.Curated
Contains 3 EF-hand domains.PROSITE-ProRule annotation
Contains 1 IQ domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063173.
HOGENOMiHOG000006820.
HOVERGENiHBG008238.
InParanoidiO14829.
KOiK13807.
OMAiMMNLRYG.
OrthoDBiEOG7KH9J7.
PhylomeDBiO14829.
TreeFamiTF313342.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
3.60.21.10. 2 hits.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR029052. Metallo-depent_PP-like.
IPR013235. PPP_dom.
IPR012008. Ser/Thr-Pase_EF-hand_contain.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00036. EF-hand_1. 1 hit.
PF00612. IQ. 1 hit.
PF00149. Metallophos. 1 hit.
PF08321. PPP5. 1 hit.
[Graphical view]
PIRSFiPIRSF000912. PPEF. 1 hit.
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00054. EFh. 3 hits.
SM00015. IQ. 1 hit.
SM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 2 hits.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS50096. IQ. 1 hit.
PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O14829-1) [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
MGCSSSSTKT RRSDTSLRAA LIIQNWYRGY KARLKARQHY ALTIFQSIEY
60 70 80 90 100
ADEQGQMQLS TFFSFMLENY THIHKEELEL RNQSLESEQD MRDRWDYVDS
110 120 130 140 150
IDVPDSYNGP RLQFPLTCTD IDLLLEAFKE QQILHAHYVL EVLFETKKVL
160 170 180 190 200
KQMPNFTHIQ TSPSKEVTIC GDLHGKLDDL FLIFYKNGLP SERNPYVFNG
210 220 230 240 250
DFVDRGKNSI EILMILCVSF LVYPNDLHLN RGNHEDFMMN LRYGFTKEIL
260 270 280 290 300
HKYKLHGKRI LQILEEFYAW LPIGTIVDNE ILVIHGGISE TTDLNLLHRV
310 320 330 340 350
ERNKMKSVLI PPTETNRDHD TDSKHNKVGV TFNAHGRIKT NGSPTEHLTE
360 370 380 390 400
HEWEQIIDIL WSDPRGKNGC FPNTCRGGGC YFGPDVTSKI LNKYQLKMLI
410 420 430 440 450
RSHECKPEGY EICHDGKVVT IFSASNYYEE GSNRGAYIKL CSGTTPRFFQ
460 470 480 490 500
YQVTKATCFQ PLRQRVDTME NSAIKILRER VISRKSDLTR AFQLQDHRKS
510 520 530 540 550
GKLSVSQWAF CMENILGLNL PWRSLSSNLV NIDQNGNVEY MSSFQNIRIE
560 570 580 590 600
KPVQEAHSTL VETLYRYRSD LEIIFNAIDT DHSGLISVEE FRAMWKLFSS
610 620 630 640 650
HYNVHIDDSQ VNKLANIMDL NKDGSIDFNE FLKAFYVVHR YEDLMKPDVT

NLG
Length:653
Mass (Da):75,792
Last modified:January 1, 1998 - v1
Checksum:iDF7B78C444EE6484
GO
Isoform 1A (identifier: O14829-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     79-132: Missing.

Show »
Length:599
Mass (Da):69,376
Checksum:iCA3972CC029AE822
GO
Isoform 1B (identifier: O14829-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     328-355: Missing.

Show »
Length:625
Mass (Da):72,635
Checksum:iDF86ABE8D0433ECE
GO
Isoform 2 (identifier: O14829-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     356-376: IIDILWSDPRGKNGCFPNTCR → SGYYGKQRHQDIKRESDFTKK
     377-653: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:376
Mass (Da):44,019
Checksum:i0C0E1B327FC8C000
GO
Isoform 3 (identifier: O14829-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     356-417: Missing.

Note: May have no functional significance.

Show »
Length:591
Mass (Da):68,806
Checksum:i920657F8E80D2C8B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti367 – 3671K → T.1 Publication
Corresponds to variant rs1065074 [ dbSNP | Ensembl ].
VAR_051736
Natural varianti443 – 4431G → S.
Corresponds to variant rs11796620 [ dbSNP | Ensembl ].
VAR_051737

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei79 – 13254Missing in isoform 1A. CuratedVSP_005098Add
BLAST
Alternative sequencei328 – 35528Missing in isoform 1B. CuratedVSP_005099Add
BLAST
Alternative sequencei356 – 41762Missing in isoform 3. CuratedVSP_005102Add
BLAST
Alternative sequencei356 – 37621IIDIL…PNTCR → SGYYGKQRHQDIKRESDFTK K in isoform 2. CuratedVSP_005100Add
BLAST
Alternative sequencei377 – 653277Missing in isoform 2. CuratedVSP_005101Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023455 mRNA. Translation: AAB82795.1.
X97867 mRNA. Translation: CAA66461.1.
AF027977 mRNA. Translation: AAC05825.1.
AK290463 mRNA. Translation: BAF83152.1.
AL096700, Z94056 Genomic DNA. Translation: CAI42857.1.
Z94056, AL096700 Genomic DNA. Translation: CAI42777.1.
CH471074 Genomic DNA. Translation: EAW98944.1.
BC036026 mRNA. Translation: AAH36026.1.
CCDSiCCDS14188.1. [O14829-1]
CCDS43920.1. [O14829-5]
RefSeqiNP_006231.2. NM_006240.2. [O14829-1]
NP_689410.1. NM_152224.1. [O14829-3]
NP_689412.1. NM_152226.1. [O14829-5]
XP_005274610.1. XM_005274553.1. [O14829-1]
UniGeneiHs.211589.

Genome annotation databases

EnsembliENST00000349874; ENSP00000341892; ENSG00000086717. [O14829-5]
ENST00000361511; ENSP00000354871; ENSG00000086717. [O14829-1]
GeneIDi5475.
KEGGihsa:5475.
UCSCiuc004cyp.3. human. [O14829-3]
uc004cyq.3. human. [O14829-1]
uc004cyr.3. human. [O14829-5]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023455 mRNA. Translation: AAB82795.1 .
X97867 mRNA. Translation: CAA66461.1 .
AF027977 mRNA. Translation: AAC05825.1 .
AK290463 mRNA. Translation: BAF83152.1 .
AL096700 , Z94056 Genomic DNA. Translation: CAI42857.1 .
Z94056 , AL096700 Genomic DNA. Translation: CAI42777.1 .
CH471074 Genomic DNA. Translation: EAW98944.1 .
BC036026 mRNA. Translation: AAH36026.1 .
CCDSi CCDS14188.1. [O14829-1 ]
CCDS43920.1. [O14829-5 ]
RefSeqi NP_006231.2. NM_006240.2. [O14829-1 ]
NP_689410.1. NM_152224.1. [O14829-3 ]
NP_689412.1. NM_152226.1. [O14829-5 ]
XP_005274610.1. XM_005274553.1. [O14829-1 ]
UniGenei Hs.211589.

3D structure databases

ProteinModelPortali O14829.
SMRi O14829. Positions 107-451, 464-638.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111471. 1 interaction.
IntActi O14829. 1 interaction.
STRINGi 9606.ENSP00000354871.

PTM databases

PhosphoSitei O14829.

Proteomic databases

PaxDbi O14829.
PRIDEi O14829.

Protocols and materials databases

DNASUi 5475.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000349874 ; ENSP00000341892 ; ENSG00000086717 . [O14829-5 ]
ENST00000361511 ; ENSP00000354871 ; ENSG00000086717 . [O14829-1 ]
GeneIDi 5475.
KEGGi hsa:5475.
UCSCi uc004cyp.3. human. [O14829-3 ]
uc004cyq.3. human. [O14829-1 ]
uc004cyr.3. human. [O14829-5 ]

Organism-specific databases

CTDi 5475.
GeneCardsi GC0XP018694.
HGNCi HGNC:9243. PPEF1.
HPAi HPA034577.
MIMi 300109. gene.
neXtProti NX_O14829.
PharmGKBi PA33564.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00530000063173.
HOGENOMi HOG000006820.
HOVERGENi HBG008238.
InParanoidi O14829.
KOi K13807.
OMAi MMNLRYG.
OrthoDBi EOG7KH9J7.
PhylomeDBi O14829.
TreeFami TF313342.

Enzyme and pathway databases

Reactomei REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

ChiTaRSi PPEF1. human.
GeneWikii PPEF1.
GenomeRNAii 5475.
NextBioi 21194.
PROi O14829.
SOURCEi Search...

Gene expression databases

Bgeei O14829.
CleanExi HS_PPEF1.
ExpressionAtlasi O14829. baseline and differential.
Genevestigatori O14829.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
3.60.21.10. 2 hits.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR029052. Metallo-depent_PP-like.
IPR013235. PPP_dom.
IPR012008. Ser/Thr-Pase_EF-hand_contain.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00036. EF-hand_1. 1 hit.
PF00612. IQ. 1 hit.
PF00149. Metallophos. 1 hit.
PF08321. PPP5. 1 hit.
[Graphical view ]
PIRSFi PIRSF000912. PPEF. 1 hit.
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00054. EFh. 3 hits.
SM00015. IQ. 1 hit.
SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 2 hits.
PROSITEi PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS50096. IQ. 1 hit.
PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a conserved family of protein serine/threonine phosphatases homologous to Drosophila retinal degeneration C."
    Sherman P.M., Sun H., Macke J.P., Williams J., Smallwood P.M., Nathans J.
    Proc. Natl. Acad. Sci. U.S.A. 94:11639-11644(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  2. "A novel human serine-threonine phosphatase related to the Drosophila retinal degeneration C (rdgC) gene is selectively expressed in sensory neurons of neural crest origin."
    Montini E., Rugarli E.I., van de Vosse E., Andolfi G., Mariani M., Puca A.A., Consales G.G., den Dunnen J.T., Ballabio A., Franco B.
    Hum. Mol. Genet. 6:1137-1145(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, VARIANT THR-367.
    Tissue: Fetal brain.
  3. "Molecular cloning, expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC)."
    Huang X., Honkanen R.E.
    J. Biol. Chem. 273:1462-1468(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  4. "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].
    Tissue: Brain.
  5. "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].
  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: Testis.
  8. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).

Entry informationi

Entry nameiPPE1_HUMAN
AccessioniPrimary (citable) accession number: O14829
Secondary accession number(s): A6NHP4
, A8K348, O15253, Q9NU21, Q9UJH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 156 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3