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Q86SQ0 (PHLB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. 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:
Pleckstrin homology-like domain family B member 2
Alternative name(s):
Protein LL5-beta
Gene names
Name:PHLDB2
Synonyms:LL5B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1253 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to be involved in the assembly of the postsynaptic apparatus. May play a role in acetyl-choline receptor (AChR) aggregation in the postsynaptic membrane By similarity. Ref.1

Subunit structure

Interacts with FLNC. Ref.1

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Note: Translocates to the plasma membrane at high levels of PtdIns(3,4,5)P3. At low levels of PtdIns(3,4,5)P3 is translocated to vesicular compartments. Ref.1

Domain

The PH domain mediates the binding to phosphoinositides.

Sequence similarities

Contains 1 PH domain.

Sequence caution

The sequence AAH69194.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAD93140.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

intermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionphospholipid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FLNAP213332EBI-2798483,EBI-350432

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86SQ0-1)

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: Q86SQ0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     668-710: Missing.
Isoform 3 (identifier: Q86SQ0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEEEDTKREVPKEDGVGDVQHFDSSKIM
     668-710: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12531253Pleckstrin homology-like domain family B member 2
PRO_0000053894

Regions

Domain1143 – 1246104PH
Coiled coil584 – 696113 Potential
Coiled coil722 – 80786 Potential
Coiled coil1032 – 109867 Potential

Amino acid modifications

Modified residue711Phosphoserine Ref.10
Modified residue731Phosphoserine Ref.10
Modified residue1571Phosphoserine Ref.10 Ref.11 Ref.14
Modified residue2121Phosphoserine Ref.10
Modified residue3341Phosphoserine Ref.10
Modified residue3511Phosphoserine Ref.10
Modified residue3841Phosphoserine Ref.10
Modified residue3871Phosphoserine Ref.10
Modified residue4151Phosphoserine Ref.10
Modified residue4681Phosphoserine Ref.10
Modified residue4891Phosphoserine Ref.10 Ref.12
Modified residue5011Phosphoserine Ref.10 Ref.12
Modified residue5041Phosphothreonine Ref.12
Modified residue5131Phosphoserine Ref.10
Modified residue5501Phosphothreonine Ref.10
Modified residue5741Phosphothreonine Ref.10
Modified residue8981Phosphothreonine Ref.10
Modified residue9801Phosphoserine By similarity

Natural variations

Alternative sequence11M → MEEEDTKREVPKEDGVGDVQ HFDSSKIM in isoform 3.
VSP_016744
Alternative sequence668 – 71043Missing in isoform 2 and isoform 3.
VSP_016745
Natural variant9411P → S. Ref.6
Corresponds to variant rs3749298 [ dbSNP | Ensembl ].
VAR_024760

Experimental info

Mutagenesis1162 – 11632KR → AA: Loss of binding to PtdIns(3,4,5)P3. Ref.1
Sequence conflict961Y → H in BAC04014. Ref.7
Sequence conflict3461T → A in CAH18447. Ref.4
Sequence conflict5851Q → E in CAD42711. Ref.1

Sequences

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

Last modified December 20, 2005. Version 2.
Checksum: D0950E96AEE1B020

FASTA1,253142,158
        10         20         30         40         50         60 
MEEHSYIQKE LDLQNGSLEE DSVVHSVEND SQNMMESLSP KKYSSSLRFK ANGDYSGSYL 

        70         80         90        100        110        120 
TLSQPVPAKR SPSPLGTSVR SSPSLAKIQG SKQFSYDGTD KNIPMKPPTP LLNTTSSLSG 

       130        140        150        160        170        180 
YPLGRADFDH YTGRDSERAL RLSEKPPYSK YSSRHKSHDN VYSLGGLEGR KASGSLLAMW 

       190        200        210        220        230        240 
NGSSLSDAGP PPISRSGAAS MPSSPKQARK MSIQDSLALQ PKLTRHKELA SENINLRTRK 

       250        260        270        280        290        300 
YSSSSLSHMG AYSRSLPRLY RATENQLTPL SLPPRNSLGN SKRTKLGEKD LPHSVIDNDN 

       310        320        330        340        350        360 
YLNFSSLSSG ALPYKTSASE GNPYVSSTLS VPASPRVARK MLLASTSSCA SDDFDQASYV 

       370        380        390        400        410        420 
GTNPSHSLLA GESDRVFATR RNFSCGSVEF DEADLESLRQ ASGTPQPALR ERKSSISSIS 

       430        440        450        460        470        480 
GRDDLMDYHR RQREERLREQ EMERLERQRL ETILSLCAEY TKPDSRLSTG TTVEDVQKIN 

       490        500        510        520        530        540 
KELEKLQLSD EESVFEEALM SPDTRYRCHR KDSLPDADLA SCGSLSQSSA SFFTPRSTRN 

       550        560        570        580        590        600 
DELLSDLTRT PPPPSSTFPK ASSESSYLSI LPKTPEGISE EQRSQELAAM EETRIVILNN 

       610        620        630        640        650        660 
LEELKQKIKD INDQMDESFR ELDMECALLD GEQKSETTEL MKEKEILDHL NRKIAELEKN 

       670        680        690        700        710        720 
IVGEKTKEKV KLDAEREKLE RLQELYSEQK TQLDNCPESM REQLQQQLKR DADLLDVESK 

       730        740        750        760        770        780 
HFEDLEFQQL EHESRLDEEK ENLTQQLLRE VAEYQRNIVS RKEKISALKK QANHIVQQAQ 

       790        800        810        820        830        840 
REQDHFVKEK NNLIMMLQRE KENLCNLEKK YSSLSGGKGF PVNPNTLKEG YISVNEINEP 

       850        860        870        880        890        900 
CGNSTNLSPS TQFPADADAV ATEPATAVLA SQPQSKEHFR SLEERKKQHK EGLYLSDTLP 

       910        920        930        940        950        960 
RKKTTSSISP HFSSATMGRS ITPKAHLPLG QSNSCGSVLP PSLAAMAKDS ESRRMLRGYN 

       970        980        990       1000       1010       1020 
HQQMSEGHRQ KSEFYNRTAS ESNVYLNSFH YPDHSYKDQA FDTLSLDSSD SMETSISACS 

      1030       1040       1050       1060       1070       1080 
PDNISSASTS NIARIEEMER LLKQAHAEKT RLLESREREM EAKKRALEEE KRRREILEKR 

      1090       1100       1110       1120       1130       1140 
LQEETSQRQK LIEKEVKIRE RQRAQARPLT RYLPVRKEDF DLRSHVETAG HNIDTCYHVS 

      1150       1160       1170       1180       1190       1200 
ITEKTCRGFL IKMGGKIKTW KKRWFVFDRN KRTFSYYADK HETKLKGVIY FQAIEEVYYD 

      1210       1220       1230       1240       1250 
HLKNANKSPN PLLTFSVKTH DRIYYMVAPS PEAMRIWMDV IVTGAEGYTH FLL 

« Hide

Isoform 2 [UniParc].

Checksum: D05881C68D0A811C
Show »

FASTA1,210136,886
Isoform 3 [UniParc].

Checksum: BF9C4AF0F1DEC613
Show »

FASTA1,237139,974

References

« Hide 'large scale' references
[1]"LL5beta is a phosphatidylinositol (3,4,5)-trisphosphate sensor that can bind the cytoskeletal adaptor, gamma-filamin."
Paranavitane V., Coadwell W.J., Eguinoa A., Hawkins P.T., Stephens L.
J. Biol. Chem. 278:1328-1335(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH FLNC, BINDING TO PTDINS(3,4,5)P3, MUTAGENESIS OF 1162-LYS-ARG-1163.
[2]Guo J.H., Yu L.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Aortic endothelium.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Fetal kidney.
[5]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1156 (ISOFORM 2), VARIANT SER-941.
Tissue: Lung.
[7]"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 1-788 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-787 (ISOFORM 1).
Tissue: Spleen.
[8]"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] [Europe PMC] [Abstract]
Cited for: BINDING TO PHOSPHOINOSITIDES.
[9]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-73; SER-157; SER-212; SER-334; SER-351; SER-384; SER-387; SER-415; SER-468; SER-489; SER-501; SER-513; THR-550; THR-574 AND THR-898, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489; SER-501 AND THR-504, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ496194 mRNA. Translation: CAD42711.1.
AF506820 mRNA. Translation: AAM33634.1.
AB209903 mRNA. Translation: BAD93140.1. Different initiation.
CR749654 mRNA. Translation: CAH18447.1.
CH471052 Genomic DNA. Translation: EAW79690.1.
BC069194 mRNA. Translation: AAH69194.1. Sequence problems.
BC142678 mRNA. Translation: AAI42679.1.
BC150210 mRNA. Translation: AAI50211.1.
AK092996 mRNA. Translation: BAC04014.1.
AK096151 mRNA. Translation: BAC04713.1.
IPIIPI00168459.
IPI00410259.
IPI00657763.
RefSeqNP_001127909.1. NM_001134437.1.
NP_001127910.1. NM_001134438.1.
NP_001127911.1. NM_001134439.1.
NP_665696.1. NM_145753.2.
UniGeneHs.603252.
Hs.679140.

3D structure databases

ProteinModelPortalQ86SQ0.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-42196N.
IntActQ86SQ0. 6 interactions.
STRING9606.ENSP00000377502.

PTM databases

PhosphoSiteQ86SQ0.

Polymorphism databases

DMDM84029396.

Proteomic databases

PaxDbQ86SQ0.
PRIDEQ86SQ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393923; ENSP00000377500; ENSG00000144824.
ENST00000393925; ENSP00000377502; ENSG00000144824.
ENST00000412622; ENSP00000405292; ENSG00000144824.
ENST00000431670; ENSP00000405405; ENSG00000144824.
ENST00000481953; ENSP00000418319; ENSG00000144824.
GeneID90102.
KEGGhsa:90102.
UCSCuc003dyc.3. human.
uc003dyd.3. human.
uc003dyg.3. human.

Organism-specific databases

CTD90102.
GeneCardsGC03P111451.
HGNCHGNC:29573. PHLDB2.
HPAHPA035146.
MIM610298. gene.
neXtProtNX_Q86SQ0.
PharmGKBPA134884060.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG86245.
HOVERGENHBG082124.
InParanoidQ86SQ0.
OMALNSFHYP.
PhylomeDBQ86SQ0.

Gene expression databases

ArrayExpressQ86SQ0.
BgeeQ86SQ0.
CleanExHS_PHLDB2.
GenevestigatorQ86SQ0.
GermOnlineENSG00000144824. Homo sapiens.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF00169. PH. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPHLDB2. human.
GenomeRNAi90102.
NextBio76517.
SOURCESearch...

Entry information

Entry namePHLB2_HUMAN
AccessionPrimary (citable) accession number: Q86SQ0
Secondary accession number(s): A5PKZ3 expand/collapse secondary AC list , Q59EA8, Q68CY3, Q6NT98, Q8N8U8, Q8NAB1, Q8NCU5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 1, 2013
This is version 86 of the entry and version 2 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

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families