O14829 (PPE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	653 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion 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.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Calcium Iron Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	detection of stimulus involved in sensory perception Inferred from electronic annotation. Source: InterPro protein dephosphorylation Traceable author statement Ref.2. Source: ProtInc
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: InterPro protein serine/threonine phosphatase activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Calm3	P62204	2	EBI-2931238,EBI-397460	From 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 653	653	Serine/threonine-protein phosphatase with EF-hands 1		PRO_0000058899
Regions
	Domain	16 – 45	30	IQ
	Domain	483 – 518	36	EF-hand 1
	Domain	566 – 601	36	EF-hand 2
	Domain	606 – 641	36	EF-hand 3
	Calcium binding	579 – 590	12	1 Potential
	Calcium binding	619 – 630	12	2 Potential
	Region	121 – 455	335	Catalytic
Sites
	Active site	234	1	Proton donor By similarity
	Metal binding	172	1	Iron By similarity
	Metal binding	174	1	Iron By similarity
	Metal binding	201	1	Iron By similarity
	Metal binding	201	1	Manganese By similarity
	Metal binding	233	1	Manganese By similarity
	Metal binding	285	1	Manganese By similarity
	Metal binding	403	1	Manganese By similarity
Natural variations
	Alternative sequence	79 – 132	54	Missing in isoform 1A.		VSP_005098
	Alternative sequence	328 – 355	28	Missing in isoform 1B.		VSP_005099
	Alternative sequence	356 – 417	62	Missing in isoform 3.		VSP_005102
	Alternative sequence	356 – 376	21	IIDIL…PNTCR → SGYYGKQRHQDIKRESDFTK K in isoform 2.		VSP_005100
	Alternative sequence	377 – 653	277	Missing in isoform 2.		VSP_005101
	Natural variant	367	1	K → T. Ref.2 Corresponds to variant rs1065074 [ dbSNP | Ensembl ].		VAR_051736
	Natural variant	443	1	G → S. Corresponds to variant rs11796620 [ dbSNP | Ensembl ].		VAR_051737

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: DF7B78C444EE6484	FASTA	653	75,792
	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
	Isoform 1A [UniParc]. Checksum: CA3972CC029AE822	FASTA	599	69,376
	10 20 30 40 50 60 MGCSSSSTKT RRSDTSLRAA LIIQNWYRGY KARLKARQHY ALTIFQSIEY ADEQGQMQLS 70 80 90 100 110 120 TFFSFMLENY THIHKEELIL HAHYVLEVLF ETKKVLKQMP NFTHIQTSPS KEVTICGDLH 130 140 150 160 170 180 GKLDDLFLIF YKNGLPSERN PYVFNGDFVD RGKNSIEILM ILCVSFLVYP NDLHLNRGNH 190 200 210 220 230 240 EDFMMNLRYG FTKEILHKYK LHGKRILQIL EEFYAWLPIG TIVDNEILVI HGGISETTDL 250 260 270 280 290 300 NLLHRVERNK MKSVLIPPTE TNRDHDTDSK HNKVGVTFNA HGRIKTNGSP TEHLTEHEWE 310 320 330 340 350 360 QIIDILWSDP RGKNGCFPNT CRGGGCYFGP DVTSKILNKY QLKMLIRSHE CKPEGYEICH 370 380 390 400 410 420 DGKVVTIFSA SNYYEEGSNR GAYIKLCSGT TPRFFQYQVT KATCFQPLRQ RVDTMENSAI 430 440 450 460 470 480 KILRERVISR KSDLTRAFQL QDHRKSGKLS VSQWAFCMEN ILGLNLPWRS LSSNLVNIDQ 490 500 510 520 530 540 NGNVEYMSSF QNIRIEKPVQ EAHSTLVETL YRYRSDLEII FNAIDTDHSG LISVEEFRAM 550 560 570 580 590 WKLFSSHYNV HIDDSQVNKL ANIMDLNKDG SIDFNEFLKA FYVVHRYEDL MKPDVTNLG
	Isoform 1B [UniParc]. Checksum: DF86ABE8D0433ECE	FASTA	625	72,635
	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 TDSKHNKIID ILWSDPRGKN GCFPNTCRGG GCYFGPDVTS 370 380 390 400 410 420 KILNKYQLKM LIRSHECKPE GYEICHDGKV VTIFSASNYY EEGSNRGAYI KLCSGTTPRF 430 440 450 460 470 480 FQYQVTKATC FQPLRQRVDT MENSAIKILR ERVISRKSDL TRAFQLQDHR KSGKLSVSQW 490 500 510 520 530 540 AFCMENILGL NLPWRSLSSN LVNIDQNGNV EYMSSFQNIR IEKPVQEAHS TLVETLYRYR 550 560 570 580 590 600 SDLEIIFNAI DTDHSGLISV EEFRAMWKLF SSHYNVHIDD SQVNKLANIM DLNKDGSIDF 610 620 NEFLKAFYVV HRYEDLMKPD VTNLG
	Isoform 2 [UniParc]. Checksum: 0C0E1B327FC8C000	FASTA	376	44,019
	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 HEWEQSGYYG 370 KQRHQDIKRE SDFTKK
	Isoform 3 [UniParc]. Checksum: 920657F8E80D2C8B	FASTA	591	68,806
	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 HEWEQVVTIF 370 380 390 400 410 420 SASNYYEEGS NRGAYIKLCS GTTPRFFQYQ VTKATCFQPL RQRVDTMENS AIKILRERVI 430 440 450 460 470 480 SRKSDLTRAF QLQDHRKSGK LSVSQWAFCM ENILGLNLPW RSLSSNLVNI DQNGNVEYMS 490 500 510 520 530 540 SFQNIRIEKP VQEAHSTLVE TLYRYRSDLE IIFNAIDTDH SGLISVEEFR AMWKLFSSHY 550 560 570 580 590 NVHIDDSQVN KLANIMDLNK DGSIDFNEFL KAFYVVHRYE DLMKPDVTNL G

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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.
IPI	IPI00221149. IPI00221150. IPI00221151. IPI00513950. IPI00514326.
RefSeq	NP_006231.2. NM_006240.2. NP_689410.1. NM_152224.1. NP_689412.1. NM_152226.1.
UniGene	Hs.211589.
3D structure databases
ProteinModelPortal	O14829.
ModBase	Search...
Protein-protein interaction databases
IntAct	O14829. 1 interaction.
STRING	9606.ENSP00000354871.
PTM databases
PhosphoSite	O14829.
Proteomic databases
PaxDb	O14829.
PRIDE	O14829.
Protocols and materials databases
DNASU	5475.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000349874; ENSP00000341892; ENSG00000086717. ENST00000361511; ENSP00000354871; ENSG00000086717. ENST00000543630; ENSP00000437785; ENSG00000086717.
GeneID	5475.
KEGG	hsa:5475.
UCSC	uc004cyp.3. human. uc004cyq.3. human. uc004cyr.3. human.
Organism-specific databases
CTD	5475.
GeneCards	GC0XP018694.
HGNC	HGNC:9243. PPEF1.
HPA	HPA034577.
MIM	300109. gene.
neXtProt	NX_O14829.
PharmGKB	PA33564.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0639.
HOGENOM	HOG000006820.
HOVERGEN	HBG008238.
InParanoid	O14829.
KO	K01090.
OMA	WAFSMEN.
OrthoDB	EOG4255SB.
Gene expression databases
ArrayExpress	O14829.
Bgee	O14829.
CleanEx	HS_PPEF1.
Genevestigator	O14829.
GermOnline	ENSG00000086717. Homo sapiens.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR000048. IQ_motif_EF-hand-BS. IPR004843. Metallo_PEstase_dom. IPR013235. PPP_dom. IPR012008. Ser/Thr-Pase_EF-hand_contain. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00036. efhand. 1 hit. PF00612. IQ. 1 hit. PF00149. Metallophos. 1 hit. PF08321. PPP5. 1 hit. [Graphical view]
PIRSF	PIRSF000912. PPEF. 1 hit.
PRINTS	PR00114. STPHPHTASE.
SMART	SM00054. EFh. 3 hits. SM00015. IQ. 1 hit. SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 2 hits. PS50222. EF_HAND_2. 3 hits. PS50096. IQ. 1 hit. PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	5475.
NextBio	21194.
SOURCE	Search...

Entry information

Entry name

PPE1_HUMAN

Accession

Primary (citable) accession number: O14829
Secondary accession number(s): A6NHP4 , A8K348, O15253, Q9NU21, Q9UJH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.