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O14829 (PPE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase with EF-hands 1

Short name=PPEF-1
EC=3.1.3.16
Alternative name(s):
Protein phosphatase with EF calcium-binding domain
Short name=PPEF
Serine/threonine-protein phosphatase 7
Short name=PP7
Gene names
Name:PPEF1
Synonyms:PPEF, PPP7C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length653 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 2 manganese ions per subunit By similarity.

Magnesium By similarity.

Enzyme regulation

Activated by calcium.

Tissue specificity

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

Sequence similarities

Belongs to the PPP phosphatase family.

Contains 3 EF-hand domains.

Contains 1 IQ domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.0.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Calm3P622042EBI-2931238,EBI-397460From a different organism.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14829-1)

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.
Isoform 1A (identifier: O14829-2)

The sequence of this isoform differs from the canonical sequence as follows:
     79-132: Missing.
Isoform 1B (identifier: O14829-3)

The sequence of this isoform differs from the canonical sequence as follows:
     328-355: Missing.
Isoform 2 (identifier: O14829-4)

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.
Isoform 3 (identifier: O14829-5)

The sequence of this isoform differs from the canonical sequence as follows:
     356-417: Missing.
Note: May have no functional significance.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 653653Serine/threonine-protein phosphatase with EF-hands 1
PRO_0000058899

Regions

Domain16 – 4530IQ
Domain483 – 51836EF-hand 1
Domain566 – 60136EF-hand 2
Domain606 – 64136EF-hand 3
Calcium binding579 – 590121 Potential
Calcium binding619 – 630122 Potential
Region121 – 455335Catalytic

Sites

Active site2341Proton donor By similarity
Metal binding1721Manganese 1 By similarity
Metal binding1741Manganese 1 By similarity
Metal binding2011Manganese 1 By similarity
Metal binding2011Manganese 2 By similarity
Metal binding2331Manganese 2 By similarity
Metal binding2851Manganese 2 By similarity
Metal binding4031Manganese 2 By similarity

Natural variations

Alternative sequence79 – 13254Missing in isoform 1A.
VSP_005098
Alternative sequence328 – 35528Missing in isoform 1B.
VSP_005099
Alternative sequence356 – 41762Missing in isoform 3.
VSP_005102
Alternative sequence356 – 37621IIDIL…PNTCR → SGYYGKQRHQDIKRESDFTK K in isoform 2.
VSP_005100
Alternative sequence377 – 653277Missing in isoform 2.
VSP_005101
Natural variant3671K → T. Ref.2
Corresponds to variant rs1065074 [ dbSNP | Ensembl ].
VAR_051736
Natural variant4431G → S.
Corresponds to variant rs11796620 [ dbSNP | Ensembl ].
VAR_051737

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: DF7B78C444EE6484

FASTA65375,792
        10         20         30         40         50         60 
MGCSSSSTKT RRSDTSLRAA LIIQNWYRGY KARLKARQHY ALTIFQSIEY ADEQGQMQLS 

        70         80         90        100        110        120 
TFFSFMLENY THIHKEELEL RNQSLESEQD MRDRWDYVDS IDVPDSYNGP RLQFPLTCTD 

       130        140        150        160        170        180 
IDLLLEAFKE QQILHAHYVL EVLFETKKVL KQMPNFTHIQ TSPSKEVTIC GDLHGKLDDL 

       190        200        210        220        230        240 
FLIFYKNGLP SERNPYVFNG DFVDRGKNSI EILMILCVSF LVYPNDLHLN RGNHEDFMMN 

       250        260        270        280        290        300 
LRYGFTKEIL HKYKLHGKRI LQILEEFYAW LPIGTIVDNE ILVIHGGISE TTDLNLLHRV 

       310        320        330        340        350        360 
ERNKMKSVLI PPTETNRDHD TDSKHNKVGV TFNAHGRIKT NGSPTEHLTE HEWEQIIDIL 

       370        380        390        400        410        420 
WSDPRGKNGC FPNTCRGGGC YFGPDVTSKI LNKYQLKMLI RSHECKPEGY EICHDGKVVT 

       430        440        450        460        470        480 
IFSASNYYEE GSNRGAYIKL CSGTTPRFFQ YQVTKATCFQ PLRQRVDTME NSAIKILRER 

       490        500        510        520        530        540 
VISRKSDLTR AFQLQDHRKS GKLSVSQWAF CMENILGLNL PWRSLSSNLV NIDQNGNVEY 

       550        560        570        580        590        600 
MSSFQNIRIE KPVQEAHSTL VETLYRYRSD LEIIFNAIDT DHSGLISVEE FRAMWKLFSS 

       610        620        630        640        650 
HYNVHIDDSQ VNKLANIMDL NKDGSIDFNE FLKAFYVVHR YEDLMKPDVT NLG 

« Hide

Isoform 1A [UniParc].

Checksum: CA3972CC029AE822
Show »

FASTA59969,376
Isoform 1B [UniParc].

Checksum: DF86ABE8D0433ECE
Show »

FASTA62572,635
Isoform 2 [UniParc].

Checksum: 0C0E1B327FC8C000
Show »

FASTA37644,019
Isoform 3 [UniParc].

Checksum: 920657F8E80D2C8B
Show »

FASTA59168,806

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14188.1. [O14829-1]
CCDS43920.1. [O14829-5]
RefSeqNP_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]
UniGeneHs.211589.

3D structure databases

ProteinModelPortalO14829.
SMRO14829. Positions 107-451, 483-639.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111471. 1 interaction.
IntActO14829. 1 interaction.
STRING9606.ENSP00000354871.

PTM databases

PhosphoSiteO14829.

Proteomic databases

PaxDbO14829.
PRIDEO14829.

Protocols and materials databases

DNASU5475.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000349874; ENSP00000341892; ENSG00000086717. [O14829-5]
ENST00000361511; ENSP00000354871; ENSG00000086717. [O14829-1]
ENST00000543630; ENSP00000437785; ENSG00000086717. [O14829-4]
GeneID5475.
KEGGhsa:5475.
UCSCuc004cyp.3. human. [O14829-3]
uc004cyq.3. human. [O14829-1]
uc004cyr.3. human. [O14829-5]

Organism-specific databases

CTD5475.
GeneCardsGC0XP018694.
HGNCHGNC:9243. PPEF1.
HPAHPA034577.
MIM300109. gene.
neXtProtNX_O14829.
PharmGKBPA33564.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000006820.
HOVERGENHBG008238.
InParanoidO14829.
KOK13807.
OMAMMNLRYG.
OrthoDBEOG7KH9J7.
PhylomeDBO14829.
TreeFamTF313342.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressO14829.
BgeeO14829.
CleanExHS_PPEF1.
GenevestigatorO14829.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
3.60.21.10. 2 hits.
InterProIPR004843. 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]
PfamPF00036. EF-hand_1. 1 hit.
PF00612. IQ. 1 hit.
PF00149. Metallophos. 1 hit.
PF08321. PPP5. 1 hit.
[Graphical view]
PIRSFPIRSF000912. PPEF. 1 hit.
PRINTSPR00114. STPHPHTASE.
SMARTSM00054. EFh. 3 hits.
SM00015. IQ. 1 hit.
SM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 2 hits.
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS50096. IQ. 1 hit.
PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPPEF1.
GenomeRNAi5475.
NextBio21194.
PROO14829.
SOURCESearch...

Entry information

Entry namePPE1_HUMAN
AccessionPrimary (citable) accession number: O14829
Secondary accession number(s): A6NHP4 expand/collapse secondary AC list , A8K348, O15253, Q9NU21, Q9UJH0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM