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Protein

Pleckstrin homology-like domain family B member 2

Gene

PHLDB2

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

Functioni

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).By similarity1 Publication

GO - Biological processi

  • establishment of protein localization Source: UniProtKB
  • microtubule cytoskeleton organization Source: UniProtKB
  • negative regulation of focal adhesion assembly Source: UniProtKB
  • negative regulation of stress fiber assembly Source: UniProtKB
  • negative regulation of wound healing, spreading of epidermal cells Source: UniProtKB
  • positive regulation of basement membrane assembly involved in embryonic body morphogenesis Source: UniProtKB
  • regulation of epithelial to mesenchymal transition Source: UniProtKB
  • regulation of gastrulation Source: UniProtKB
  • regulation of microtubule cytoskeleton organization Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Pleckstrin homology-like domain family B member 2
Alternative name(s):
Protein LL5-beta
Gene namesi
Name:PHLDB2
Synonyms:LL5B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:29573. PHLDB2.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Membrane 1 Publication; Peripheral membrane protein 1 Publication

  • 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.

GO - Cellular componenti

  • basal cortex Source: UniProtKB
  • cell leading edge Source: UniProtKB
  • cytoplasm Source: HPA
  • intermediate filament cytoskeleton Source: HPA
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1162 – 11632KR → AA: Loss of binding to PtdIns(3,4,5)P3. 1 Publication

Organism-specific databases

PharmGKBiPA134884060.

Polymorphism and mutation databases

BioMutaiPHLDB2.
DMDMi84029396.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12531253Pleckstrin homology-like domain family B member 2PRO_0000053894Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei71 – 711PhosphoserineCombined sources
Modified residuei73 – 731PhosphoserineCombined sources
Modified residuei157 – 1571PhosphoserineCombined sources
Modified residuei204 – 2041PhosphoserineBy similarity
Modified residuei212 – 2121PhosphoserineCombined sources
Modified residuei242 – 2421PhosphoserineBy similarity
Modified residuei245 – 2451PhosphoserineBy similarity
Modified residuei330 – 3301PhosphoserineBy similarity
Modified residuei334 – 3341PhosphoserineCombined sources
Modified residuei348 – 3481PhosphoserineBy similarity
Modified residuei351 – 3511PhosphoserineCombined sources
Modified residuei384 – 3841PhosphoserineCombined sources
Modified residuei387 – 3871PhosphoserineCombined sources
Modified residuei415 – 4151PhosphoserineCombined sources
Modified residuei420 – 4201PhosphoserineCombined sources
Modified residuei468 – 4681PhosphoserineCombined sources
Modified residuei489 – 4891PhosphoserineCombined sources
Modified residuei501 – 5011PhosphoserineCombined sources
Modified residuei504 – 5041PhosphothreonineCombined sources
Modified residuei513 – 5131PhosphoserineCombined sources
Modified residuei550 – 5501PhosphothreonineCombined sources
Modified residuei574 – 5741PhosphothreonineCombined sources
Modified residuei898 – 8981PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ86SQ0.
MaxQBiQ86SQ0.
PaxDbiQ86SQ0.
PeptideAtlasiQ86SQ0.
PRIDEiQ86SQ0.

PTM databases

iPTMnetiQ86SQ0.
PhosphoSiteiQ86SQ0.

Expressioni

Gene expression databases

BgeeiQ86SQ0.
CleanExiHS_PHLDB2.
ExpressionAtlasiQ86SQ0. baseline and differential.
GenevisibleiQ86SQ0. HS.

Organism-specific databases

HPAiHPA035146.
HPA035147.

Interactioni

Subunit structurei

Interacts with FLNC.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FLNAP213333EBI-2798483,EBI-350432

Protein-protein interaction databases

BioGridi124661. 38 interactions.
DIPiDIP-42196N.
IntActiQ86SQ0. 37 interactions.
MINTiMINT-5289240.
STRINGi9606.ENSP00000377502.

Structurei

3D structure databases

ProteinModelPortaliQ86SQ0.
SMRiQ86SQ0. Positions 1148-1241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1143 – 1246104PHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili584 – 696113Sequence analysisAdd
BLAST
Coiled coili722 – 80786Sequence analysisAdd
BLAST
Coiled coili1032 – 109867Sequence analysisAdd
BLAST

Domaini

The PH domain mediates the binding to phosphoinositides.

Sequence similaritiesi

Contains 1 PH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFMW. Eukaryota.
ENOG4111JWX. LUCA.
GeneTreeiENSGT00530000063148.
HOVERGENiHBG082124.
InParanoidiQ86SQ0.
OMAiYLNSFHY.
OrthoDBiEOG779NX9.
PhylomeDBiQ86SQ0.
TreeFamiTF329165.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86SQ0-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MEEHSYIQKE LDLQNGSLEE DSVVHSVEND SQNMMESLSP KKYSSSLRFK
60 70 80 90 100
ANGDYSGSYL TLSQPVPAKR SPSPLGTSVR SSPSLAKIQG SKQFSYDGTD
110 120 130 140 150
KNIPMKPPTP LLNTTSSLSG YPLGRADFDH YTGRDSERAL RLSEKPPYSK
160 170 180 190 200
YSSRHKSHDN VYSLGGLEGR KASGSLLAMW NGSSLSDAGP PPISRSGAAS
210 220 230 240 250
MPSSPKQARK MSIQDSLALQ PKLTRHKELA SENINLRTRK YSSSSLSHMG
260 270 280 290 300
AYSRSLPRLY RATENQLTPL SLPPRNSLGN SKRTKLGEKD LPHSVIDNDN
310 320 330 340 350
YLNFSSLSSG ALPYKTSASE GNPYVSSTLS VPASPRVARK MLLASTSSCA
360 370 380 390 400
SDDFDQASYV GTNPSHSLLA GESDRVFATR RNFSCGSVEF DEADLESLRQ
410 420 430 440 450
ASGTPQPALR ERKSSISSIS GRDDLMDYHR RQREERLREQ EMERLERQRL
460 470 480 490 500
ETILSLCAEY TKPDSRLSTG TTVEDVQKIN KELEKLQLSD EESVFEEALM
510 520 530 540 550
SPDTRYRCHR KDSLPDADLA SCGSLSQSSA SFFTPRSTRN DELLSDLTRT
560 570 580 590 600
PPPPSSTFPK ASSESSYLSI LPKTPEGISE EQRSQELAAM EETRIVILNN
610 620 630 640 650
LEELKQKIKD INDQMDESFR ELDMECALLD GEQKSETTEL MKEKEILDHL
660 670 680 690 700
NRKIAELEKN IVGEKTKEKV KLDAEREKLE RLQELYSEQK TQLDNCPESM
710 720 730 740 750
REQLQQQLKR DADLLDVESK HFEDLEFQQL EHESRLDEEK ENLTQQLLRE
760 770 780 790 800
VAEYQRNIVS RKEKISALKK QANHIVQQAQ REQDHFVKEK NNLIMMLQRE
810 820 830 840 850
KENLCNLEKK YSSLSGGKGF PVNPNTLKEG YISVNEINEP CGNSTNLSPS
860 870 880 890 900
TQFPADADAV ATEPATAVLA SQPQSKEHFR SLEERKKQHK EGLYLSDTLP
910 920 930 940 950
RKKTTSSISP HFSSATMGRS ITPKAHLPLG QSNSCGSVLP PSLAAMAKDS
960 970 980 990 1000
ESRRMLRGYN HQQMSEGHRQ KSEFYNRTAS ESNVYLNSFH YPDHSYKDQA
1010 1020 1030 1040 1050
FDTLSLDSSD SMETSISACS PDNISSASTS NIARIEEMER LLKQAHAEKT
1060 1070 1080 1090 1100
RLLESREREM EAKKRALEEE KRRREILEKR LQEETSQRQK LIEKEVKIRE
1110 1120 1130 1140 1150
RQRAQARPLT RYLPVRKEDF DLRSHVETAG HNIDTCYHVS ITEKTCRGFL
1160 1170 1180 1190 1200
IKMGGKIKTW KKRWFVFDRN KRTFSYYADK HETKLKGVIY FQAIEEVYYD
1210 1220 1230 1240 1250
HLKNANKSPN PLLTFSVKTH DRIYYMVAPS PEAMRIWMDV IVTGAEGYTH

FLL
Length:1,253
Mass (Da):142,158
Last modified:December 20, 2005 - v2
Checksum:iD0950E96AEE1B020
GO
Isoform 2 (identifier: Q86SQ0-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,210
Mass (Da):136,886
Checksum:iD05881C68D0A811C
GO
Isoform 3 (identifier: Q86SQ0-3) [UniParc]FASTAAdd to basket

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

Show »
Length:1,237
Mass (Da):139,974
Checksum:iBF9C4AF0F1DEC613
GO

Sequence cautioni

The sequence AAH69194.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAD93140.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961Y → H in BAC04014 (PubMed:14702039).Curated
Sequence conflicti346 – 3461T → A in CAH18447 (PubMed:17974005).Curated
Sequence conflicti585 – 5851Q → E in CAD42711 (PubMed:12376540).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti941 – 9411P → S.1 Publication
Corresponds to variant rs3749298 [ dbSNP | Ensembl ].
VAR_024760

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MEEEDTKREVPKEDGVGDVQ HFDSSKIM in isoform 3. 1 PublicationVSP_016744
Alternative sequencei668 – 71043Missing in isoform 2 and isoform 3. 4 PublicationsVSP_016745Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2962.1. [Q86SQ0-2]
CCDS46885.1. [Q86SQ0-3]
CCDS46886.1. [Q86SQ0-1]
RefSeqiNP_001127909.1. NM_001134437.1. [Q86SQ0-3]
NP_001127910.1. NM_001134438.1. [Q86SQ0-1]
NP_001127911.1. NM_001134439.1. [Q86SQ0-1]
NP_665696.1. NM_145753.2. [Q86SQ0-2]
UniGeneiHs.603252.
Hs.679140.

Genome annotation databases

EnsembliENST00000393923; ENSP00000377500; ENSG00000144824. [Q86SQ0-3]
ENST00000393925; ENSP00000377502; ENSG00000144824. [Q86SQ0-1]
ENST00000412622; ENSP00000405292; ENSG00000144824. [Q86SQ0-2]
ENST00000431670; ENSP00000405405; ENSG00000144824. [Q86SQ0-1]
ENST00000481953; ENSP00000418319; ENSG00000144824. [Q86SQ0-2]
GeneIDi90102.
KEGGihsa:90102.
UCSCiuc003dyc.4. human. [Q86SQ0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2962.1. [Q86SQ0-2]
CCDS46885.1. [Q86SQ0-3]
CCDS46886.1. [Q86SQ0-1]
RefSeqiNP_001127909.1. NM_001134437.1. [Q86SQ0-3]
NP_001127910.1. NM_001134438.1. [Q86SQ0-1]
NP_001127911.1. NM_001134439.1. [Q86SQ0-1]
NP_665696.1. NM_145753.2. [Q86SQ0-2]
UniGeneiHs.603252.
Hs.679140.

3D structure databases

ProteinModelPortaliQ86SQ0.
SMRiQ86SQ0. Positions 1148-1241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124661. 38 interactions.
DIPiDIP-42196N.
IntActiQ86SQ0. 37 interactions.
MINTiMINT-5289240.
STRINGi9606.ENSP00000377502.

PTM databases

iPTMnetiQ86SQ0.
PhosphoSiteiQ86SQ0.

Polymorphism and mutation databases

BioMutaiPHLDB2.
DMDMi84029396.

Proteomic databases

EPDiQ86SQ0.
MaxQBiQ86SQ0.
PaxDbiQ86SQ0.
PeptideAtlasiQ86SQ0.
PRIDEiQ86SQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000393923; ENSP00000377500; ENSG00000144824. [Q86SQ0-3]
ENST00000393925; ENSP00000377502; ENSG00000144824. [Q86SQ0-1]
ENST00000412622; ENSP00000405292; ENSG00000144824. [Q86SQ0-2]
ENST00000431670; ENSP00000405405; ENSG00000144824. [Q86SQ0-1]
ENST00000481953; ENSP00000418319; ENSG00000144824. [Q86SQ0-2]
GeneIDi90102.
KEGGihsa:90102.
UCSCiuc003dyc.4. human. [Q86SQ0-1]

Organism-specific databases

CTDi90102.
GeneCardsiPHLDB2.
HGNCiHGNC:29573. PHLDB2.
HPAiHPA035146.
HPA035147.
MIMi610298. gene.
neXtProtiNX_Q86SQ0.
PharmGKBiPA134884060.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFMW. Eukaryota.
ENOG4111JWX. LUCA.
GeneTreeiENSGT00530000063148.
HOVERGENiHBG082124.
InParanoidiQ86SQ0.
OMAiYLNSFHY.
OrthoDBiEOG779NX9.
PhylomeDBiQ86SQ0.
TreeFamiTF329165.

Miscellaneous databases

ChiTaRSiPHLDB2. human.
GeneWikiiPHLDB2.
GenomeRNAii90102.
PROiQ86SQ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ86SQ0.
CleanExiHS_PHLDB2.
ExpressionAtlasiQ86SQ0. baseline and differential.
GenevisibleiQ86SQ0. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Fetal kidney.
  5. 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.
    , 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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-334; SER-415; SER-468 AND THR-898, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-384; SER-387; SER-420; SER-468 AND THR-550, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPHLB2_HUMAN
AccessioniPrimary (citable) accession number: Q86SQ0
Secondary accession number(s): A5PKZ3
, Q59EA8, Q68CY3, Q6NT98, Q8N8U8, Q8NAB1, Q8NCU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: July 6, 2016
This is version 114 of the entry and version 2 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.