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O00459

- P85B_HUMAN

UniProt

O00459 - P85B_HUMAN

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Protein

Phosphatidylinositol 3-kinase regulatory subunit beta

Gene

PIK3R2

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

Functioni

Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane.

GO - Molecular functioni

  1. phosphatidylinositol 3-kinase regulator activity Source: InterPro
  2. receptor tyrosine kinase binding Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. epidermal growth factor receptor signaling pathway Source: Reactome
  3. Fc-epsilon receptor signaling pathway Source: Reactome
  4. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  5. fibroblast growth factor receptor signaling pathway Source: Reactome
  6. innate immune response Source: Reactome
  7. insulin receptor signaling pathway Source: Reactome
  8. leukocyte migration Source: Reactome
  9. neurotrophin TRK receptor signaling pathway Source: Reactome
  10. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  11. phosphatidylinositol biosynthetic process Source: Reactome
  12. phosphatidylinositol-mediated signaling Source: Reactome
  13. phospholipid metabolic process Source: Reactome
  14. regulation of small GTPase mediated signal transduction Source: Reactome
  15. small GTPase mediated signal transduction Source: Reactome
  16. small molecule metabolic process Source: Reactome
  17. T cell receptor signaling pathway Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000105647-MONOMER.
ReactomeiREACT_11051. Rho GTPase cycle.
REACT_111040. Signaling by SCF-KIT.
REACT_115529. Interleukin-7 signaling.
REACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_12464. PI3K/AKT activation.
REACT_12555. Downstream TCR signaling.
REACT_12621. Tie2 Signaling.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_147814. DAP12 signaling.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_1695. GPVI-mediated activation cascade.
REACT_17025. Downstream signal transduction.
REACT_18283. G alpha (q) signalling events.
REACT_18407. G alpha (12/13) signalling events.
REACT_19344. Costimulation by the CD28 family.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_23787. Regulation of signaling by CBL.
REACT_23832. Nephrin interactions.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23891. Interleukin receptor SHC signaling.
REACT_75829. PIP3 activates AKT signaling.
REACT_976. PI3K Cascade.
SignaLinkiO00459.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 3-kinase regulatory subunit beta
Short name:
PI3-kinase regulatory subunit beta
Short name:
PI3K regulatory subunit beta
Short name:
PtdIns-3-kinase regulatory subunit beta
Alternative name(s):
Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta
Short name:
PI3-kinase subunit p85-beta
Short name:
PtdIns-3-kinase regulatory subunit p85-beta
Gene namesi
Name:PIK3R2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:8980. PIK3R2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. phosphatidylinositol 3-kinase complex Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Megalencephaly-polymicrogyria-polydactyly-hydrocephalus syndrome (MPPH) [MIM:603387]: A syndrome characterized by megalencephaly, hydrocephalus, and polymicrogyria; polydactyly may also be seen. There is considerable phenotypic similarity between this disorder and the megalencephaly-capillary malformation syndrome.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti373 – 3731G → R in MPPH. 1 Publication
VAR_069262

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi603387. phenotype.
Orphaneti83473. Megalencephaly - polymicrogyria - postaxial polydactyly - hydrocephalus.
PharmGKBiPA33313.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 728728Phosphatidylinositol 3-kinase regulatory subunit betaPRO_0000080763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei464 – 4641Phosphotyrosine1 Publication
Modified residuei605 – 6051Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylated in response to signaling from activated receptor-type protein kinases. Dephosphorylated by PTPRJ.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00459.
PaxDbiO00459.
PRIDEiO00459.

PTM databases

PhosphoSiteiO00459.

Expressioni

Gene expression databases

BgeeiO00459.
CleanExiHS_PIK3R2.
ExpressionAtlasiO00459. baseline.
GenevestigatoriO00459.

Interactioni

Subunit structurei

Heterodimer of a regulatory subunit PIK3R2 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with AXL. Interacts with FLT1 (tyrosine-phosphorylated) and FLT4 (tyrosine-phosphorylated). Interacts with NYAP1, NYAP2 and MYO16.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARP1027514EBI-346930,EBI-608057
EGFRP005333EBI-346930,EBI-297353
ERBB2P046266EBI-346930,EBI-641062
ERBB3P2186016EBI-346930,EBI-720706
GAB1Q1348023EBI-346930,EBI-517684
GRB2P629934EBI-346930,EBI-401755
HTTP428586EBI-346930,EBI-466029
KITP1072119EBI-346930,EBI-1379503
METP0858111EBI-346930,EBI-1039152
NSP034968EBI-346930,EBI-2547442From a different organism.
PIK3CBP423383EBI-346930,EBI-2609540

Protein-protein interaction databases

BioGridi111314. 97 interactions.
IntActiO00459. 48 interactions.
MINTiMINT-1210047.
STRINGi9606.ENSP00000222254.

Structurei

Secondary structure

1
728
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Beta strandi30 – 345Combined sources
Helixi35 – 406Combined sources
Helixi47 – 493Combined sources
Helixi51 – 544Combined sources
Beta strandi56 – 616Combined sources
Turni62 – 643Combined sources
Beta strandi67 – 715Combined sources
Helixi72 – 743Combined sources
Beta strandi75 – 817Combined sources
Helixi114 – 1174Combined sources
Helixi126 – 13813Combined sources
Helixi144 – 1463Combined sources
Helixi162 – 1643Combined sources
Helixi167 – 18014Combined sources
Beta strandi181 – 1833Combined sources
Helixi188 – 19912Combined sources
Helixi206 – 2094Combined sources
Turni211 – 2133Combined sources
Helixi216 – 23520Combined sources
Helixi239 – 25517Combined sources
Helixi279 – 29315Combined sources
Helixi439 – 51274Combined sources
Helixi515 – 58369Combined sources
Helixi588 – 5947Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KT1NMR-A1-80[»]
2XS6X-ray2.09A108-298[»]
3MTTX-ray3.30A433-610[»]
3O5ZX-ray2.01A/B1-85[»]
ProteinModelPortaliO00459.
SMRiO00459. Positions 3-84, 109-294, 324-720.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00459.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 8077SH3PROSITE-ProRule annotationAdd
BLAST
Domaini109 – 295187Rho-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini330 – 42596SH2 1PROSITE-ProRule annotationAdd
BLAST
Domaini622 – 71695SH2 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PI3K p85 subunit family.Curated
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
Contains 2 SH2 domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG263689.
GeneTreeiENSGT00390000010431.
HOGENOMiHOG000008438.
HOVERGENiHBG082100.
InParanoidiO00459.
KOiK02649.
OMAiHCVIYKT.
PhylomeDBiO00459.
TreeFamiTF102033.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.30.505.10. 2 hits.
InterProiIPR001720. PI3kinase_P85.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10155. PTHR10155. 1 hit.
PfamiPF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view]
PRINTSiPR00678. PI3KINASEP85.
PR00401. SH2DOMAIN.
SMARTiSM00324. RhoGAP. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50238. RHOGAP. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00459 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGPEGFQYR ALYPFRRERP EDLELLPGDV LVVSRAALQA LGVAEGGERC
60 70 80 90 100
PQSVGWMPGL NERTRQRGDF PGTYVEFLGP VALARPGPRP RGPRPLPARP
110 120 130 140 150
RDGAPEPGLT LPDLPEQFSP PDVAPPLLVK LVEAIERTGL DSESHYRPEL
160 170 180 190 200
PAPRTDWSLS DVDQWDTAAL ADGIKSFLLA LPAPLVTPEA SAEARRALRE
210 220 230 240 250
AAGPVGPALE PPTLPLHRAL TLRFLLQHLG RVASRAPALG PAVRALGATF
260 270 280 290 300
GPLLLRAPPP PSSPPPGGAP DGSEPSPDFP ALLVEKLLQE HLEEQEVAPP
310 320 330 340 350
ALPPKPPKAK PASTVLANGG SPPSLQDAEW YWGDISREEV NEKLRDTPDG
360 370 380 390 400
TFLVRDASSK IQGEYTLTLR KGGNNKLIKV FHRDGHYGFS EPLTFCSVVD
410 420 430 440 450
LINHYRHESL AQYNAKLDTR LLYPVSKYQQ DQIVKEDSVE AVGAQLKVYH
460 470 480 490 500
QQYQDKSREY DQLYEEYTRT SQELQMKRTA IEAFNETIKI FEEQGQTQEK
510 520 530 540 550
CSKEYLERFR REGNEKEMQR ILLNSERLKS RIAEIHESRT KLEQQLRAQA
560 570 580 590 600
SDNREIDKRM NSLKPDLMQL RKIRDQYLVW LTQKGARQKK INEWLGIKNE
610 620 630 640 650
TEDQYALMED EDDLPHHEER TWYVGKINRT QAEEMLSGKR DGTFLIRESS
660 670 680 690 700
QRGCYACSVV VDGDTKHCVI YRTATGFGFA EPYNLYGSLK ELVLHYQHAS
710 720
LVQHNDALTV TLAHPVRAPG PGPPPAAR
Length:728
Mass (Da):81,545
Last modified:January 11, 2011 - v2
Checksum:iADAC3E4B61F3F44A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti234 – 2341S → R.3 Publications
Corresponds to variant rs2241088 [ dbSNP | Ensembl ].
VAR_030679
Natural varianti313 – 3131S → P.3 Publications
Corresponds to variant rs1011320 [ dbSNP | Ensembl ].
VAR_030680
Natural varianti373 – 3731G → R in MPPH. 1 Publication
VAR_069262

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80907 mRNA. Translation: CAA56868.1.
AC007192 Genomic DNA. Translation: AAD22671.1.
BC070082 mRNA. Translation: AAH70082.1.
BC090249 mRNA. Translation: AAH90249.1.
CCDSiCCDS12371.1.
PIRiH59435.
RefSeqiNP_005018.1. NM_005027.3.
UniGeneiHs.371344.

Genome annotation databases

EnsembliENST00000222254; ENSP00000222254; ENSG00000105647.
ENST00000617130; ENSP00000477864; ENSG00000105647.
GeneIDi5296.
KEGGihsa:5296.
UCSCiuc002nia.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80907 mRNA. Translation: CAA56868.1 .
AC007192 Genomic DNA. Translation: AAD22671.1 .
BC070082 mRNA. Translation: AAH70082.1 .
BC090249 mRNA. Translation: AAH90249.1 .
CCDSi CCDS12371.1.
PIRi H59435.
RefSeqi NP_005018.1. NM_005027.3.
UniGenei Hs.371344.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KT1 NMR - A 1-80 [» ]
2XS6 X-ray 2.09 A 108-298 [» ]
3MTT X-ray 3.30 A 433-610 [» ]
3O5Z X-ray 2.01 A/B 1-85 [» ]
ProteinModelPortali O00459.
SMRi O00459. Positions 3-84, 109-294, 324-720.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111314. 97 interactions.
IntActi O00459. 48 interactions.
MINTi MINT-1210047.
STRINGi 9606.ENSP00000222254.

Chemistry

BindingDBi O00459.
DrugBanki DB01064. Isoprenaline.

PTM databases

PhosphoSitei O00459.

Proteomic databases

MaxQBi O00459.
PaxDbi O00459.
PRIDEi O00459.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222254 ; ENSP00000222254 ; ENSG00000105647 .
ENST00000617130 ; ENSP00000477864 ; ENSG00000105647 .
GeneIDi 5296.
KEGGi hsa:5296.
UCSCi uc002nia.2. human.

Organism-specific databases

CTDi 5296.
GeneCardsi GC19P018263.
HGNCi HGNC:8980. PIK3R2.
MIMi 603157. gene.
603387. phenotype.
neXtProti NX_O00459.
Orphaneti 83473. Megalencephaly - polymicrogyria - postaxial polydactyly - hydrocephalus.
PharmGKBi PA33313.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG263689.
GeneTreei ENSGT00390000010431.
HOGENOMi HOG000008438.
HOVERGENi HBG082100.
InParanoidi O00459.
KOi K02649.
OMAi HCVIYKT.
PhylomeDBi O00459.
TreeFami TF102033.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000105647-MONOMER.
Reactomei REACT_11051. Rho GTPase cycle.
REACT_111040. Signaling by SCF-KIT.
REACT_115529. Interleukin-7 signaling.
REACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_12464. PI3K/AKT activation.
REACT_12555. Downstream TCR signaling.
REACT_12621. Tie2 Signaling.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_147814. DAP12 signaling.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_1695. GPVI-mediated activation cascade.
REACT_17025. Downstream signal transduction.
REACT_18283. G alpha (q) signalling events.
REACT_18407. G alpha (12/13) signalling events.
REACT_19344. Costimulation by the CD28 family.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_23787. Regulation of signaling by CBL.
REACT_23832. Nephrin interactions.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23891. Interleukin receptor SHC signaling.
REACT_75829. PIP3 activates AKT signaling.
REACT_976. PI3K Cascade.
SignaLinki O00459.

Miscellaneous databases

ChiTaRSi PIK3R2. human.
EvolutionaryTracei O00459.
GeneWikii PIK3R2.
GenomeRNAii 5296.
NextBioi 20470.
PROi O00459.
SOURCEi Search...

Gene expression databases

Bgeei O00459.
CleanExi HS_PIK3R2.
ExpressionAtlasi O00459. baseline.
Genevestigatori O00459.

Family and domain databases

Gene3Di 1.10.555.10. 1 hit.
3.30.505.10. 2 hits.
InterProi IPR001720. PI3kinase_P85.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR10155. PTHR10155. 1 hit.
Pfami PF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view ]
PRINTSi PR00678. PI3KINASEP85.
PR00401. SH2DOMAIN.
SMARTi SM00324. RhoGAP. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEi PS50238. RHOGAP. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Chromosomal localization of human p85 alpha, a subunit of phosphatidylinositol 3-kinase, and its homologue p85 beta."
    Volinia S., Patracchini P., Otsu M., Hiles I., Gout I., Calzolari E., Bernardi F., Rooke L., Waterfield M.D.
    Oncogene 7:789-793(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-234 AND PRO-313.
  2. "An oncogenic fusion product of the phosphatidylinositol 3-kinase p85beta subunit and HUMORF8, a putative deubiquitinating enzyme."
    Janssen J.W.G., Schleithhoff L., Bartram C.R., Schulz A.S.
    Oncogene 16:1767-1772(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-234 AND PRO-313.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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], VARIANTS ARG-234 AND PRO-313.
    Tissue: Brain and Placenta.
  5. "Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is mediated mainly by a multi-substrate docking-site."
    Braunger J., Schleithoff L., Schulz A.S., Kessler H., Lammers R., Ullrich A., Bartram C.R., Janssen J.W.
    Oncogene 14:2619-2631(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AXL.
  6. "Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2."
    Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.
    Biochem. Biophys. Res. Commun. 246:95-99(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT1.
  7. "Activation of vascular endothelial growth factor receptor-3 and its downstream signaling promote cell survival under oxidative stress."
    Wang J.F., Zhang X., Groopman J.E.
    J. Biol. Chem. 279:27088-27097(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT4.
  8. "The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase."
    Tsuboi N., Utsunomiya T., Roberts R.L., Ito H., Takahashi K., Noda M., Takahashi T.
    Biochem. J. 413:193-200(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPRJ.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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 TYR-605, 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 TYR-464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: VARIANT MPPH ARG-373.

Entry informationi

Entry nameiP85B_HUMAN
AccessioniPrimary (citable) accession number: O00459
Secondary accession number(s): Q5EAT5, Q9UPH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 149 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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