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Reviewed, UniProtKB/Swiss-Prot Q9HAU0 (PKHA5_HUMAN)

Last modified February 9, 2010. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pleckstrin homology domain-containing family A member 5
      Short name=PH domain-containing family A member 5
Alternative name(s):
    Phosphoinositol 3-phosphate-binding protein 2
      Short name=PEPP-2
Gene names
Name: PLEKHA5
Synonyms: KIAA1686, PEPP2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1116 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Tissue specificity

Highly expressed in heart and kidney. Ref.1

Sequence similarities

Contains 1 PH domain.

Contains 2 WW domains.

Sequence caution

The sequence BAA91742.1 differs from that shown. Reason: Frameshift at position 759.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   DomainRepeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Molecular functionphosphatidylinositol binding Ref.1

Non-traceable author statement. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HAU0-1)

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 2 (identifier: Q9HAU0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     615-615: T → TPEELTLLLIKLRRQQAELSSIREHTLAQLMQLKLEAHSPKNEILSHHLQRNTIYLDHQ
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9HAU0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     616-650: LSQDEGRGTLYKYRPEEVDIDAKLSRLCEQDKVVH → WGREKVATATGAAEAVASDTHLPRTGSSSPSLLCV
     651-1116: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9HAU0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     800-800: E → EEEEVVPPRPPLPRSYDFTEQPPIIPPLPSDSSSLLCYSRGPVHLPEEKKMYQVQGYPRNGSHC
Note: No experimental confirmation available.
Isoform 5 (identifier: Q9HAU0-5)

The sequence of this isoform differs from the canonical sequence as follows:
     785-840: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11161116Pleckstrin homology domain-containing family A member 5
PRO_0000053883

Regions

Domain10 – 4334WW 1
Domain56 – 8934WW 2
Domain169 – 268100PH

Amino acid modifications

Modified residue1281Phosphotyrosine Ref.7
Modified residue1341Phosphotyrosine Ref.7 Ref.14
Modified residue3531Phosphotyrosine Ref.14
Modified residue4101Phosphoserine Ref.13
Modified residue4381Phosphothreonine Ref.11
Modified residue4761Phosphothreonine Ref.11
Modified residue5681Phosphoserine Ref.13 Ref.9
Modified residue6071Phosphoserine Ref.13
Modified residue8551Phosphoserine Ref.8 Ref.10 Ref.12
Modified residue8571Phosphothreonine Ref.8
Modified residue9301Phosphoserine Ref.13
Modified residue9331Phosphoserine Ref.13 Ref.11 Ref.8 Ref.12 Ref.15
Modified residue9371Phosphoserine Ref.13 Ref.11 Ref.8 Ref.12

Natural variations

Alternative sequence6151T → TPEELTLLLIKLRRQQAELS SIREHTLAQLMQLKLEAHSP KNEILSHHLQRNTIYLDHQ in isoform 2.
VSP_009775
Alternative sequence616 – 65035LSQDE…DKVVH → WGREKVATATGAAEAVASDT HLPRTGSSSPSLLCV in isoform 3.
VSP_009776
Alternative sequence651 – 1116466Missing in isoform 3.
VSP_014595
Alternative sequence785 – 84056Missing in isoform 5.
VSP_009777
Alternative sequence8001E → EEEEVVPPRPPLPRSYDFTE QPPIIPPLPSDSSSLLCYSR GPVHLPEEKKMYQVQGYPRN GSHC in isoform 4.
VSP_009778

Experimental info

Sequence conflict6271K → R in BAB14419. Ref.6
Sequence conflict7361M → T in BAB14419. Ref.6
Sequence conflict9701P → S in BAA91742. Ref.6

Secondary structure

........................ 1116
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2001. Version 1.
Checksum: 327F792F644B9D48

FASTA1,116127,464
        10         20         30         40         50         60 
MAADLNLEWI SLPRSWTYGI TRGGRVFFIN EEAKSTTWLH PVTGEAVVTG HRRQSTDLPT 

        70         80         90        100        110        120 
GWEEAYTFEG ARYYINHNER KVTCKHPVTG QPSQDNCIFV VNEQTVATMT SEEKKERPIS 

       130        140        150        160        170        180 
MINEASNYNV TSDYAVHPMS PVGRTSRASK KVHNFGKRSN SIKRNPNAPV VRRGWLYKQD 

       190        200        210        220        230        240 
STGMKLWKKR WFVLSDLCLF YYRDEKEEGI LGSILLPSFQ IALLTSEDHI NRKYAFKAAH 

       250        260        270        280        290        300 
PNMRTYYFCT DTGKEMELWM KAMLDAALVQ TEPVKRVDKI TSENAPTKET NNIPNHRVLI 

       310        320        330        340        350        360 
KPEIQNNQKN KEMSKIEEKK ALEAEKYGFQ KDGQDRPLTK INSVKLNSLP SEYESGSACP 

       370        380        390        400        410        420 
AQTVHYRPIN LSSSENKIVN VSLADLRGGN RPNTGPLYTE ADRVIQRTNS MQQLEQWIKI 

       430        440        450        460        470        480 
QKGRGHEEET RGVISYQTLP RNMPSHRAQI MARYPEGYRT LPRNSKTRPE SICSVTPSTH 

       490        500        510        520        530        540 
DKTLGPGAEE KRRSMRDDTM WQLYEWQQRQ FYNKQSTLPR HSTLSSPKTM VNISDQTMHS 

       550        560        570        580        590        600 
IPTSPSHGSI AAYQGYSPQR TYRSEVSSPI QRGDVTIDRR HRAHHPKHVY VPDRRSVPAG 

       610        620        630        640        650        660 
LTLQSVSPQS LQGKTLSQDE GRGTLYKYRP EEVDIDAKLS RLCEQDKVVH ALEEKLQQLH 

       670        680        690        700        710        720 
KEKYTLEQAL LSASQEIEMH ADNPAAIQTV VLQRDDLQNG LLSTCRELSR ATAELERAWR 

       730        740        750        760        770        780 
EYDKLEYDVT VTRNQMQEQL DHLGEVQTES AGIQRAQIQK ELWRIQDVME GLSKHKQQRG 

       790        800        810        820        830        840 
TTEIGMIGSK PFSTVKYKNE GPDYRLYKSE PELTTVAEVD ESNGEEKSEP VSEIETSVVK 

       850        860        870        880        890        900 
GSHFPVGVVP PRAKSPTPES STIASYVTLR KTKKMMDLRT ERPRSAVEQL CLAESTRPRM 

       910        920        930        940        950        960 
TVEEQMERIR RHQQACLREK KKGLNVIGAS DQSPLQSPSN LRDNPFRTTQ TRRRDDKELD 

       970        980        990       1000       1010       1020 
TAIRENDVKP DHETPATEIV QLKETEPQNV DFSKELKKTE NISYEMLFEP EPNGVNSVEM 

      1030       1040       1050       1060       1070       1080 
MDKERNKDKM PEDVTFSPQD ETQTANHKPE EHPEENTKNS VDEQEETVIS YESTPEVSRG 

      1090       1100       1110 
NQTMAVKSLS PSPESSASPV PSTQPQLTEG SHFMCV 

« Hide

Isoform 2.

Checksum: B82D29C6F281D311
Show »

FASTA1,174134,323
Isoform 3.

Checksum: 98FCFC6BD6243232
Show »

FASTA65073,909
Isoform 4.

Checksum: A7E7827DDD2166DC
Show »

FASTA1,179134,593
Isoform 5.

Checksum: EC6B2DC66DC64F6A
Show »

FASTA1,060121,272

References

« Hide 'large scale' references
[1]"Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities."
Dowler S.J., Currie R.A., Campbell D.G., Deak M., Kular G., Downes C.P., Alessi D.R.
Biochem. J. 351:19-31(2000) [PubMed: 11001876] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
DNA Res. 7:347-355(2000) [PubMed: 11214970] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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: 12168954] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Amygdala.
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-1116 (ISOFORM 3).
Tissue: Placenta.
[6]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 625-1116 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 664-1116 (ISOFORM 5).
Tissue: Teratocarcinoma.
[7]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-128 AND TYR-134, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-855; THR-857; SER-933 AND SER-937, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568, MASS SPECTROMETRY.
Tissue: Epithelium.
[10]"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-855, MASS SPECTROMETRY.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-438; THR-476; SER-933 AND SER-937, MASS SPECTROMETRY.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-855; SER-933 AND SER-937, MASS SPECTROMETRY.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410; SER-568; SER-607; SER-930; SER-933 AND SER-937, MASS SPECTROMETRY.
[14]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-134 AND TYR-353, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-933, MASS SPECTROMETRY.
Tissue: T-cell.
[16]"Solution structure of the PH domain of pleckstrin homology domain-containing protein family A member 5 from human."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 156-271.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF302150 mRNA. Translation: AAG22817.1.
AB051473 mRNA. Translation: BAB21777.2. Different initiation.
AL834259 mRNA. Translation: CAD38934.1.
BC000969 mRNA. Translation: AAH00969.1.
BC013133 mRNA. Translation: AAH13133.3.
BC127092 mRNA. Translation: AAI27093.1.
AK001529 mRNA. Translation: BAA91742.1. Frameshift.
AK023127 mRNA. Translation: BAB14419.1. Different initiation.
IPIIPI00029515.
IPI00169401.
IPI00409581.
IPI00409582.
IPI00409583.
RefSeqNP_001137293.1.
NP_061885.2.
UniGeneHs.188614

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DKPNMR-A157-271[»]
SMRQ9HAU0. Positions 2-87.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9HAU0. 3 interactions.

PTM databases

PhosphoSiteQ9HAU0.

Proteomic databases

PRIDEQ9HAU0.

Genome annotation databases

EnsemblENST00000299275; ENSP00000299275; ENSG00000052126; Homo sapiens. [Genome view]
GeneID54477.
KEGGhsa:54477.
UCSCuc001rea.1. human.
uc001reb.1. human.

Organism-specific databases

CTD54477.
GeneCardsGC12P019174.
H-InvDBHIX0010473.
HGNCHGNC:30036. PLEKHA5.
MIM607770. gene.
PharmGKBPA134949896.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9HAU0.

Gene expression databases

ArrayExpressQ9HAU0.
BgeeQ9HAU0.
CleanExHS_PLEKHA5.
GenevestigatorQ9HAU0.
GermOnlineENSG00000052126. Homo sapiens.

Family and domain databases

InterProIPR011993. PH_type.
IPR001849. Pleckstrin_homology.
IPR001202. WW_Rsp5_WWP.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
PfamPF00169. PH. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00456. WW. 2 hits.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio56792.
SOURCESearch...

Entry information

Entry namePKHA5_HUMAN
AccessionPrimary (citable) accession number: Q9HAU0
Secondary accession number(s): A0JP03 expand/collapse secondary AC list , Q8N3K6, Q96DY9, Q9BVR4, Q9C0H7, Q9H924, Q9NVK8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 1, 2001
Last modified: February 9, 2010
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents