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Protein

Protein phosphatase 1 regulatory subunit 29

Gene

ELFN2

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

Functioni

Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes.1 Publication

GO - Molecular functioni

  • phosphatase binding Source: UniProtKB
  • protein phosphatase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

  • negative regulation of phosphatase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Protein phosphatase inhibitor

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 1 regulatory subunit 29
Alternative name(s):
Extracellular leucine-rich repeat and fibronectin type III domain-containing protein 2
Leucine-rich repeat and fibronectin type-III domain-containing protein 6
Leucine-rich repeat-containing protein 62
Gene namesi
Name:ELFN2
Synonyms:KIAA1904, LRRC62, PPP1R29
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:29396. ELFN2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 397375ExtracellularSequence analysisAdd
BLAST
Transmembranei398 – 41821HelicalSequence analysisAdd
BLAST
Topological domaini419 – 820402CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular space Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162385040.

Polymorphism and mutation databases

BioMutaiELFN2.
DMDMi74755895.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 820798Protein phosphatase 1 regulatory subunit 29PRO_0000256138Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi54 – 541N-linked (GlcNAc...)Sequence analysis
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence analysis
Glycosylationi85 – 851N-linked (GlcNAc...)Sequence analysis
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence analysis
Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence analysis
Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence analysis
Modified residuei619 – 6191PhosphoserineCombined sources
Modified residuei668 – 6681PhosphoserineBy similarity
Modified residuei672 – 6721PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ5R3F8.
MaxQBiQ5R3F8.
PaxDbiQ5R3F8.
PeptideAtlasiQ5R3F8.
PRIDEiQ5R3F8.

PTM databases

iPTMnetiQ5R3F8.
PhosphoSiteiQ5R3F8.

Expressioni

Gene expression databases

BgeeiQ5R3F8.
CleanExiHS_ELFN2.
GenevisibleiQ5R3F8. HS.

Organism-specific databases

HPAiHPA000781.

Interactioni

Subunit structurei

Interacts with PPP1CA.1 Publication

GO - Molecular functioni

  • phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi125356. 1 interaction.
IntActiQ5R3F8. 1 interaction.
STRINGi9606.ENSP00000300147.

Structurei

3D structure databases

ProteinModelPortaliQ5R3F8.
SMRiQ5R3F8. Positions 7-247.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati56 – 7722LRR 1Add
BLAST
Repeati80 – 10122LRR 2Add
BLAST
Repeati104 – 12522LRR 3Add
BLAST
Repeati128 – 14922LRR 4Add
BLAST
Repeati152 – 17322LRR 5Add
BLAST
Domaini185 – 24763LRRCTAdd
BLAST
Domaini292 – 37988Fibronectin type-IIIAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi583 – 5875Poly-Ala
Compositional biasi683 – 69311Poly-GlyAdd
BLAST

Sequence similaritiesi

Contains 1 fibronectin type-III domain.Curated
Contains 5 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IHCP. Eukaryota.
ENOG4110NB3. LUCA.
GeneTreeiENSGT00790000122963.
HOGENOMiHOG000112354.
HOVERGENiHBG056941.
InParanoidiQ5R3F8.
KOiK17568.
OMAiRPVSHPT.
OrthoDBiEOG7SFHW4.
PhylomeDBiQ5R3F8.
TreeFamiTF332887.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR019931. LPXTG_anchor.
[Graphical view]
PfamiPF13855. LRR_8. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 4 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5R3F8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRLGLCAAA LLCVCRPGAV RADCWLIEGD KGYVWLAICS QNQPPYETIP
60 70 80 90 100
QHINSTVHDL RLNENKLKAV LYSSLNRFGN LTDLNLTKNE ISYIEDGAFL
110 120 130 140 150
GQSSLQVLQL GYNKLSNLTE GMLRGMSRLQ FLFVQHNLIE VVTPTAFSEC
160 170 180 190 200
PSLISIDLSS NRLSRLDGAT FASLASLMVC ELAGNPFNCE CDLFGFLAWL
210 220 230 240 250
VVFNNVTKNY DRLQCESPRE FAGYPLLVPR PYHSLNAITV LQAKCRNGSL
260 270 280 290 300
PARPVSHPTP YSTDAQREPD ENSGFNPDEI LSVEPPASST TDASAGPAIK
310 320 330 340 350
LHHVTFTSAT LVVIIPHPYS KMYILVQYNN SYFSDVMTLK NKKEIVTLDK
360 370 380 390 400
LRAHTEYTFC VTSLRNSRRF NHTCLTFTTR DPVPGDLAPS TSTTTHYIMT
410 420 430 440 450
ILGCLFGMVI VLGAVYYCLR KRRMQEEKQK SVNVKKTILE MRYGADVDAG
460 470 480 490 500
SIVHAAQKLG EPPVLPVSRM ASIPSMIGEK LPTAKGLEAG LDTPKVATKG
510 520 530 540 550
NYIEVRTGAG GDGLARPEDD LPDLENGQGS AAEISTIAKE VDKVNQIINN
560 570 580 590 600
CIDALKLDSA SFLGGGSSSG DPELAFECQS LPAAAAASSA TGPGALERPS
610 620 630 640 650
FLSPPYKESS HHPLQRQLSA DAAVTRKTCS VSSSGSIKSA KVFSLDVPDH
660 670 680 690 700
PAATGLAKGD SKYIEKGSPL NSPLDRLPLV PAGSGGGSGG GGGIHHLEVK
710 720 730 740 750
PAYHCSEHRH SFPALYYEEG ADSLSQRVSF LKPLTRSKRD STYSQLSPRH
760 770 780 790 800
YYSGYSSSPE YSSESTHKIW ERFRPYKKHH REEVYMAAGH ALRKKVQFAK
810 820
DEDLHDILDY WKGVSAQQKL
Length:820
Mass (Da):89,687
Last modified:December 21, 2004 - v1
Checksum:i18BCDBDEC0F21212
GO

Sequence cautioni

The sequence BAB67797.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391T → I in BAB67797 (PubMed:11572484).Curated
Sequence conflicti605 – 6051P → S in BAB67797 (PubMed:11572484).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB067491 mRNA. Translation: BAB67797.1. Different initiation.
Z94160 Genomic DNA. Translation: CAI22122.1.
CCDSiCCDS33642.1.
RefSeqiNP_443138.2. NM_052906.4.
UniGeneiHs.344170.
Hs.660812.

Genome annotation databases

EnsembliENST00000402918; ENSP00000385277; ENSG00000166897.
ENST00000613079; ENSP00000480338; ENSG00000166897.
GeneIDi114794.
KEGGihsa:114794.
UCSCiuc003asq.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB067491 mRNA. Translation: BAB67797.1. Different initiation.
Z94160 Genomic DNA. Translation: CAI22122.1.
CCDSiCCDS33642.1.
RefSeqiNP_443138.2. NM_052906.4.
UniGeneiHs.344170.
Hs.660812.

3D structure databases

ProteinModelPortaliQ5R3F8.
SMRiQ5R3F8. Positions 7-247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125356. 1 interaction.
IntActiQ5R3F8. 1 interaction.
STRINGi9606.ENSP00000300147.

PTM databases

iPTMnetiQ5R3F8.
PhosphoSiteiQ5R3F8.

Polymorphism and mutation databases

BioMutaiELFN2.
DMDMi74755895.

Proteomic databases

EPDiQ5R3F8.
MaxQBiQ5R3F8.
PaxDbiQ5R3F8.
PeptideAtlasiQ5R3F8.
PRIDEiQ5R3F8.

Protocols and materials databases

DNASUi114794.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000402918; ENSP00000385277; ENSG00000166897.
ENST00000613079; ENSP00000480338; ENSG00000166897.
GeneIDi114794.
KEGGihsa:114794.
UCSCiuc003asq.4. human.

Organism-specific databases

CTDi114794.
GeneCardsiELFN2.
H-InvDBHIX0016443.
HGNCiHGNC:29396. ELFN2.
HPAiHPA000781.
neXtProtiNX_Q5R3F8.
PharmGKBiPA162385040.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHCP. Eukaryota.
ENOG4110NB3. LUCA.
GeneTreeiENSGT00790000122963.
HOGENOMiHOG000112354.
HOVERGENiHBG056941.
InParanoidiQ5R3F8.
KOiK17568.
OMAiRPVSHPT.
OrthoDBiEOG7SFHW4.
PhylomeDBiQ5R3F8.
TreeFamiTF332887.

Miscellaneous databases

GenomeRNAii114794.
NextBioi79223.
PROiQ5R3F8.

Gene expression databases

BgeeiQ5R3F8.
CleanExiHS_ELFN2.
GenevisibleiQ5R3F8. HS.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR019931. LPXTG_anchor.
[Graphical view]
PfamiPF13855. LRR_8. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 4 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins."
    Nagase T., Kikuno R., Ohara O.
    DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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-619, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. "Docking motif-guided mapping of the interactome of protein phosphatase-1."
    Hendrickx A., Beullens M., Ceulemans H., Den Abt T., Van Eynde A., Nicolaescu E., Lesage B., Bollen M.
    Chem. Biol. 16:365-371(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPP1CA.

Entry informationi

Entry nameiPPR29_HUMAN
AccessioniPrimary (citable) accession number: Q5R3F8
Secondary accession number(s): Q96PY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: December 21, 2004
Last modified: May 11, 2016
This is version 106 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 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.