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O60346 (PHLP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PH domain leucine-rich repeat-containing protein phosphatase 1

EC=3.1.3.16
Alternative name(s):
Pleckstrin homology domain-containing family E member 1
Short name=PH domain-containing family E member 1
Suprachiasmatic nucleus circadian oscillatory protein
Short name=hSCOP
Gene names
Name:PHLPP1
Synonyms:KIAA0606, PHLPP, PLEKHE1, SCOP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1717 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein phosphatase that mediates dephosphorylation of 'Ser-473' of AKT1, 'Ser-660' of PRKCB isoform beta-IIand 'Ser-657' of PRKCA. AKT1 regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of AKT1 triggers apoptosis and suppression of tumor growth. Controls the phosphorylation of AKT2 and AKT3 more efficiently than that of AKT1. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Inhibits cancer cell proliferation and may act as a tumor suppressor. May act as a negative regulator of K-Ras signaling in membrane rafts. Ref.6 Ref.8 Ref.9 Ref.10

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.6

Cofactor

Binds 2 manganese ions per subunit By similarity. Ref.6

Enzyme regulation

Insensitive to okadaic acid. Ref.6

Subunit structure

Interacts with the nucleotide free form of K-Ras (KRAS) via its LRR repeats By similarity. Interacts with AKT2, AKT3 and PRKCB isoform beta-II Ref.8 Ref.9

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Nucleus. Note: In colorectal cancer tissue, expression is concentrated at the lateral membrane of epithelial cells. Ref.8 Ref.10

Tissue specificity

In colorectal cancer tissue, expression is highest in the surface epithelium of normal colonic mucosa adjacent to the cancer tissue but is largely excluded from the crypt bases. Expression is lost or significantly decreased in 78% of tested tumors (at protein level). Ubiquitously expressed in non-cancerous tissues. Ref.6 Ref.10

Domain

The PH domain is required for interaction with PRKCB and its dephosphorylation.

Sequence similarities

Contains 21 LRR (leucine-rich) repeats.

Contains 1 PH domain.

Contains 1 PP2C-like domain.

Sequence caution

The sequence AAH14927.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH82244.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAI26278.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA91980.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseTumor suppressor
   DomainLeucine-rich repeat
Repeat
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

entrainment of circadian clock

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.9PubMed 19615732PubMed 21701506. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRKCBP05771-25EBI-2511516,EBI-5774511
SCRIBQ141602EBI-2511516,EBI-357345
ScribQ80U722EBI-2511516,EBI-1766028From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17171717PH domain leucine-rich repeat-containing protein phosphatase 1
PRO_0000057781

Regions

Domain536 – 636101PH
Repeat638 – 65922LRR 1
Repeat661 – 68222LRR 2
Repeat692 – 71221LRR 3
Repeat715 – 73622LRR 4
Repeat738 – 76023LRR 5
Repeat761 – 78323LRR 6
Repeat784 – 80421LRR 7
Repeat808 – 83124LRR 8
Repeat832 – 85322LRR 9
Repeat873 – 89422LRR 10
Repeat895 – 91622LRR 11
Repeat918 – 93922LRR 12
Repeat941 – 96222LRR 13
Repeat963 – 98422LRR 14
Repeat987 – 100822LRR 15
Repeat1013 – 103321LRR 16
Repeat1037 – 105822LRR 17
Repeat1061 – 108222LRR 18
Repeat1084 – 110522LRR 19
Repeat1106 – 112722LRR 20
Repeat1129 – 115022LRR 21
Domain1165 – 1420256PP2C-like
Motif1715 – 17173PDZ-binding
Compositional bias4 – 74Poly-Ala
Compositional bias21 – 4525Poly-Ala
Compositional bias132 – 1376Poly-Ala
Compositional bias138 – 1447Poly-Ser
Compositional bias145 – 1484Poly-Ala
Compositional bias254 – 2574Poly-Ala
Compositional bias463 – 4697Poly-Pro
Compositional bias1682 – 16898Poly-Gln

Sites

Metal binding12101Manganese 1 By similarity
Metal binding12101Manganese 2 By similarity
Metal binding12111Manganese 1; via carbonyl oxygen By similarity
Metal binding13741Manganese 2 By similarity
Metal binding14131Manganese 2 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11

Natural variations

Natural variant11181S → T.
Corresponds to variant rs9950585 [ dbSNP | Ensembl ].
VAR_056725

Experimental info

Mutagenesis1715 – 17173Missing: Loss of function in vivo, but does not abolishes intrinsic phosphatase activity. Ref.6
Sequence conflict6911T → A in BAA91980. Ref.5
Sequence conflict10621L → F in AAH47653. Ref.4
Sequence conflict10831R → S in BAA25532. Ref.2
Sequence conflict12271D → V in BAA91980. Ref.5
Sequence conflict14901V → M in AAH47653. Ref.4
Sequence conflict15801Missing in AAH63519. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O60346 [UniParc].

Last modified June 7, 2005. Version 3.
Checksum: A4AB53F334EA8AB6

FASTA1,717184,672
        10         20         30         40         50         60 
MEPAAAATVQ RLPELGREDR ASAPAAAAAA AAAAAAAAAA LAAAAGGGRS PEPALTPAAP 

        70         80         90        100        110        120 
SGGNGSGSGA REEAPGEAPP GPLPGRAGGA GRRRRRGAPQ PIAGGAAPVP GAGGGANSLL 

       130        140        150        160        170        180 
LRRGRLKRNL SAAAAAASSS SSSSAAAASH SPGAAGLPAS CSASASLCTR SLDRKTLLLK 

       190        200        210        220        230        240 
HRQTLQLQPS DRDWVRHQLQ RGCVHVFDRH MASTYLRPVL CTLDTTAGEV AARLLQLGHK 

       250        260        270        280        290        300 
GGGVVKVLGQ GPGAAAAREP AEPPPEAGPR LAPPEPRDSE VPPARSAPGA FGGPPRAPPA 

       310        320        330        340        350        360 
DLPLPVGGPG GWSRRASPAP SDSSPGEPFV GGPVSSPRAP RPVVSDTESF SLSPSAESVS 

       370        380        390        400        410        420 
DRLDPYSSGG GSSSSSEELE ADAASAPTGV PGQPRRPGHP AQPLPLPQTA SSPQPQQKAP 

       430        440        450        460        470        480 
RAIDSPGGAV REGSCEEKAA AAVAPGGLQS TPGRSGVTAE KAPPPPPPPT LYVQLHGETT 

       490        500        510        520        530        540 
RRLEAEEKPL QIQNDYLFQL GFGELWRVQE EGMDSEIGCL IRFYAGKPHS TGSSERIQLS 

       550        560        570        580        590        600 
GMYNVRKGKM QLPVNRWTRR QVILCGTCLI VSSVKDSLTG KMHVLPLIGG KVEEVKKHQH 

       610        620        630        640        650        660 
CLAFSSSGPQ SQTYYICFDT FTEYLRWLRQ VSKVASQRIS SVDLSCCSLE HLPANLFYSQ 

       670        680        690        700        710        720 
DLTHLNLKQN FLRQNPSLPA ARGLNELQRF TKLKSLNLSN NHLGDFPLAV CSIPTLAELN 

       730        740        750        760        770        780 
VSCNALRSVP AAVGVMHNLQ TFLLDGNFLQ SLPAELENMK QLSYLGLSFN EFTDIPEVLE 

       790        800        810        820        830        840 
KLTAVDKLCM SGNCVETLRL QALRKMPHIK HVDLRLNVIR KLIADEVDFL QHVTQLDLRD 

       850        860        870        880        890        900 
NKLGDLDAMI FNNIEVLHCE RNQLVTLDIC GYFLKALYAS SNELVQLDVY PVPNYLSYMD 

       910        920        930        940        950        960 
VSRNRLENVP EWVCESRKLE VLDIGHNQIC ELPARLFCNS SLRKLLAGHN QLARLPERLE 

       970        980        990       1000       1010       1020 
RTSVEVLDVQ HNQLLELPPN LLMKADSLRF LNASANKLES LPPATLSEET NSILQELYLT 

      1030       1040       1050       1060       1070       1080 
NNSLTDKCVP LLTGHPHLKI LHMAYNRLQS FPASKMAKLE ELEEIDLSGN KLKAIPTTIM 

      1090       1100       1110       1120       1130       1140 
NCRRMHTVIA HSNCIEVFPE VMQLPEIKCV DLSCNELSEV TLPENLPPKL QELDLTGNPR 

      1150       1160       1170       1180       1190       1200 
LVLDHKTLEL LNNIRCFKID QPSTGDASGA PAVWSHGYTE ASGVKNKLCV AALSVNNFCD 

      1210       1220       1230       1240       1250       1260 
NREALYGVFD GDRNVEVPYL LQCTMSDILA EELQKTKNEE EYMVNTFIVM QRKLGTAGQK 

      1270       1280       1290       1300       1310       1320 
LGGAAVLCHI KHDPVDPGGS FTLTSANVGK CQTVLCRNGK PLPLSRSYIM SCEEELKRIK 

      1330       1340       1350       1360       1370       1380 
QHKAIITEDG KVNGVTESTR ILGYTFLHPS VVPRPHVQSV LLTPQDEFFI LGSKGLWDSL 

      1390       1400       1410       1420       1430       1440 
SVEEAVEAVR NVPDALAAAK KLCTLAQSYG CHDSISAVVV QLSVTEDSFC CCELSAGGAV 

      1450       1460       1470       1480       1490       1500 
PPPSPGIFPP SVNMVIKDRP SDGLGVPSSS SGMASEISSE LSTSEMSSEV GSTASDEPPP 

      1510       1520       1530       1540       1550       1560 
GALSENSPAY PSEQRCMLHP ICLSNSFQRQ LSSATFSSAF SDNGLDSDDE EPIEGVFTNG 

      1570       1580       1590       1600       1610       1620 
SRVEVEVDIH CSRAKEKEKQ QHLLQVPAEA SDEGIVISAN EDEPGLPRKA DFSAVGTIGR 

      1630       1640       1650       1660       1670       1680 
RRANGSVAPQ ERSHNVIEVA TDAPLRKPGG YFAAPAQPDP DDQFIIPPEL EEEVKEIMKH 

      1690       1700       1710 
HQEQQQQQQP PPPPQLQPQL PRHYQLDQLP DYYDTPL 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-1717.
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"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] OF 475-1717.
Tissue: Cerebellum, Hippocampus, Lymphoma, Melanoma and Retinoblastoma.
[5]"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] OF 495-1233.
Tissue: Placenta.
[6]"PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth."
Gao T., Furnari F., Newton A.C.
Mol. Cell 18:13-24(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY, COFACTOR, ENZYME REGULATION, TISSUE SPECIFICITY, MUTAGENESIS OF 1715-THR--LEU-1717.
[7]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms."
Brognard J., Sierecki E., Gao T., Newton A.C.
Mol. Cell 25:917-931(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AKT2 AND AKT3.
[9]"The phosphatase PHLPP controls the cellular levels of protein kinase C."
Gao T., Brognard J., Newton A.C.
J. Biol. Chem. 283:6300-6311(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRKCB.
[10]"Loss of PHLPP expression in colon cancer: role in proliferation and tumorigenesis."
Liu J., Weiss H.L., Rychahou P., Jackson L.N., Evers B.M., Gao T.
Oncogene 28:994-1004(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC015989 Genomic DNA. No translation available.
AC022046 Genomic DNA. No translation available.
AC027553 Genomic DNA. No translation available.
AB011178 mRNA. Translation: BAA25532.2.
BC010706 mRNA. Translation: AAH10706.1.
BC014927 mRNA. Translation: AAH14927.3. Different initiation.
BC047653 mRNA. Translation: AAH47653.1.
BC063519 mRNA. Translation: AAH63519.1.
BC082244 mRNA. Translation: AAH82244.1. Sequence problems.
BC126277 mRNA. Translation: AAI26278.1. Different initiation.
AK001924 mRNA. Translation: BAA91980.1. Different initiation.
CCDSCCDS45881.2.
PIRT00258.
RefSeqNP_919431.2. NM_194449.3.
UniGeneHs.465337.

3D structure databases

ProteinModelPortalO60346.
SMRO60346. Positions 626-1160, 1205-1422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116843. 23 interactions.
IntActO60346. 20 interactions.
MINTMINT-2796653.
STRING9606.ENSP00000393405.

PTM databases

PhosphoSiteO60346.

Proteomic databases

MaxQBO60346.
PaxDbO60346.
PeptideAtlasO60346.
PRIDEO60346.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262719; ENSP00000262719; ENSG00000081913.
ENST00000400316; ENSP00000383170; ENSG00000081913.
GeneID23239.
KEGGhsa:23239.
UCSCuc021ule.1. human.

Organism-specific databases

CTD23239.
GeneCardsGC18P060382.
H-InvDBHIX0014494.
HIX0174202.
HGNCHGNC:20610. PHLPP1.
HPAHPA020200.
MIM609396. gene.
neXtProtNX_O60346.
PharmGKBPA165429055.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
InParanoidO60346.
KOK16340.
OMAFTNGSRV.
OrthoDBEOG7RFTGK.
PhylomeDBO60346.
TreeFamTF315993.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

BgeeO60346.
CleanExHS_PHLPP.
GenevestigatorO60346.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.60.40.10. 1 hit.
InterProIPR001611. Leu-rich_rpt.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR001932. PP2C-like_dom.
[Graphical view]
PfamPF00560. LRR_1. 2 hits.
PF13855. LRR_8. 2 hits.
PF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 1 hit.
PROSITEPS51450. LRR. 17 hits.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPHLPP1. human.
GeneWikiPHLPP_(gene).
GenomeRNAi23239.
NextBio44894.
PROO60346.
SOURCESearch...

Entry information

Entry namePHLP1_HUMAN
AccessionPrimary (citable) accession number: O60346
Secondary accession number(s): A1A4F5 expand/collapse secondary AC list , Q641Q7, Q6P4C4, Q6PJI6, Q86TN6, Q96FK2, Q9NUY1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: July 9, 2014
This is version 135 of the entry and version 3 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 18

Human chromosome 18: entries, gene names and cross-references to MIM