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PH-interacting protein (PHIP) (IRS-1 PH domain-binding protein) (WD repeat-containing protein 11)

 PHIP_HUMAN              Reviewed;        1821 AA.
Q8WWQ0; A7J992; B2RPK4; Q05CQ9; Q5VVH4; Q66I29; Q69YV1; Q8NBZ5;
Q96H52; Q96ME2; Q9H261;
21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 2.
13-FEB-2019, entry version 149.
RecName: Full=PH-interacting protein;
Short=PHIP;
AltName: Full=DDB1- and CUL4-associated factor 14;
AltName: Full=IRS-1 PH domain-binding protein;
AltName: Full=WD repeat-containing protein 11;
Name=PHIP; Synonyms=DCAF14, WDR11;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-663.
PubMed=17636024; DOI=10.1128/MCB.02409-06;
Podcheko A., Northcott P., Bikopoulos G., Lee A., Bommareddi S.R.,
Kushner J.A., Farhang-Fallah J., Rozakis-Adcock M.;
"Identification of a WD40 repeat-containing isoform of PHIP as a novel
regulator of beta-cell growth and survival.";
Mol. Cell. Biol. 27:6484-6496(2007).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-663.
Antonarakis S.E.;
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-663.
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., 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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-663; ILE-874
AND PRO-1093.
TISSUE=Brain, Lymph, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-912, NUCLEOTIDE SEQUENCE
[LARGE SCALE MRNA] OF 1230-1821, AND VARIANT GLY-663.
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 905-1821, AND VARIANT
PRO-1093.
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 960-1821, AND TISSUE SPECIFICITY.
PubMed=11018022; DOI=10.1074/jbc.C000611200;
Farhang-Fallah J., Yin X., Trentin G., Cheng A.M., Rozakis-Adcock M.;
"Cloning and characterization of PHIP, a novel insulin receptor
substrate-1 pleckstrin homology domain interacting protein.";
J. Biol. Chem. 275:40492-40497(2000).
[9]
FUNCTION.
PubMed=12242307; DOI=10.1128/MCB.22.20.7325-7336.2002;
Farhang-Fallah J., Randhawa V.K., Nimnual A., Klip A., Bar-Sagi D.,
Rozakis-Adcock M.;
"The pleckstrin homology (PH) domain-interacting protein couples the
insulin receptor substrate 1 PH domain to insulin signaling pathways
leading to mitogenesis and GLUT4 translocation.";
Mol. Cell. Biol. 22:7325-7336(2002).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-1281; SER-1283;
SER-1296; SER-1405; SER-1479 AND SER-1783, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281; SER-1283; SER-1315
AND SER-1783, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1497 AND LYS-1533, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-659; SER-692;
SER-911; SER-1315; THR-1359; SER-1405; SER-1525; SER-1651; SER-1762
AND SER-1783, VARIANT [LARGE SCALE ANALYSIS] GLY-663, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
FUNCTION.
PubMed=21834987; DOI=10.1186/1741-7007-9-54;
Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
"Identification and characterization of a set of conserved and new
regulators of cytoskeletal organisation, cell morphology and
migration.";
BMC Biol. 9:54-54(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683; SER-692; SER-879;
SER-880; SER-881; SER-911; SER-1315 AND SER-1783, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-677; SER-683;
SER-911; SER-1281; SER-1283; SER-1315; SER-1525; SER-1560; SER-1762
AND SER-1783, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1315, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1470, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-421 AND LYS-1470, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-421; LYS-1470; LYS-1644 AND
LYS-1670, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[24]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1302-1434, AND SUBUNIT.
PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
Gingras A.C., Arrowsmith C.H., Knapp S.;
"Histone recognition and large-scale structural analysis of the human
bromodomain family.";
Cell 149:214-231(2012).
[25]
VARIANTS [LARGE SCALE ANALYSIS] ILE-469 AND ILE-1767.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[26]
INVOLVEMENT IN DIDOD, AND VARIANT DIDOD 1149-TYR--TRP-1821 DEL.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
[27]
INVOLVEMENT IN DIDOD, AND VARIANT DIDOD SER-17.
PubMed=27900362; DOI=10.1101/mcs.a001172;
Webster E., Cho M.T., Alexander N., Desai S., Naidu S.,
Bekheirnia M.R., Lewis A., Retterer K., Juusola J., Chung W.K.;
"De novo PHIP-predicted deleterious variants are associated with
developmental delay, intellectual disability, obesity, and dysmorphic
features.";
Cold Spring Harb. Mol. Case Stud. 2:A001172-A001172(2016).
[28]
INVOLVEMENT IN DIDOD, AND VARIANTS DIDOD CYS-110; SER-110;
274-GLN--TRP-1821 DEL; 555-GLN--TRP-1821 DEL; 634-GLN--TRP-1821 DEL;
968-ARG--TRP-1821 DEL; 1149-TYR--TRP-1821 DEL; 1191-GLN--TRP-1821 DEL;
GLU-1263; 1298-ARG--TRP-1821 DEL AND 1354-ARG--TRP-1821 DEL.
PubMed=29209020; DOI=10.1038/s41431-017-0039-5;
Jansen S., Hoischen A., Coe B.P., Carvill G.L., Van Esch H.,
Bosch D.G.M., Andersen U.A., Baker C., Bauters M., Bernier R.A.,
van Bon B.W., Claahsen-van der Grinten H.L., Gecz J., Gilissen C.,
Grillo L., Hackett A., Kleefstra T., Koolen D., Kvarnung M.,
Larsen M.J., Marcelis C., McKenzie F., Monin M.L., Nava C.,
Schuurs-Hoeijmakers J.H., Pfundt R., Steehouwer M., Stevens S.J.C.,
Stumpel C.T., Vansenne F., Vinci M., van de Vorst M., Vries P.,
Witherspoon K., Veltman J.A., Brunner H.G., Mefford H.C., Romano C.,
Vissers L.E.L.M., Eichler E.E., de Vries B.B.A.;
"A genotype-first approach identifies an intellectual disability-
overweight syndrome caused by PHIP haploinsufficiency.";
Eur. J. Hum. Genet. 26:54-63(2018).
-!- FUNCTION: Probable regulator of the insulin and insulin-like
growth factor signaling pathways. Stimulates cell proliferation
through regulation of cyclin transcription and has an anti-
apoptotic activity through AKT1 phosphorylation and activation.
Plays a role in the regulation of cell morphology and cytoskeletal
organization. {ECO:0000269|PubMed:12242307,
ECO:0000269|PubMed:21834987}.
-!- SUBUNIT: Interacts with IRS1 and IRS2 (By similarity). Interacts
(via bromo domain) with acetylated lysine residues on histone
H1.4, histone H3 and H4 (in vitro). {ECO:0000250,
ECO:0000269|PubMed:22464331}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in myeloma and epidermoid carcinoma
cell lines. {ECO:0000269|PubMed:11018022}.
-!- DISEASE: Developmental delay, intellectual disability, obesity,
and dysmorphic features (DIDOD) [MIM:617991]: An autosomal
dominant disorder characterized by developmental delay,
intellectual disability, autistic features, anxiety, hypotonia,
obesity, and dysmorphic features. {ECO:0000269|PubMed:23033978,
ECO:0000269|PubMed:27900362, ECO:0000269|PubMed:29209020}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAH21905.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAC11417.1; Type=Frameshift; Positions=1648; Evidence={ECO:0000305};
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EMBL; DQ924532; ABK76299.1; -; mRNA.
EMBL; AJ303102; CAC83118.1; -; mRNA.
EMBL; AL450327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL356776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48718.1; -; Genomic_DNA.
EMBL; BC008909; AAH08909.2; -; mRNA.
EMBL; BC021905; AAH21905.1; ALT_SEQ; mRNA.
EMBL; BC081569; AAH81569.1; -; mRNA.
EMBL; BC137488; AAI37489.1; -; mRNA.
EMBL; AK057039; BAB71353.1; -; mRNA.
EMBL; AK075124; BAC11417.1; ALT_FRAME; mRNA.
EMBL; AL161957; CAH10776.1; -; mRNA.
EMBL; AF310250; AAG45145.1; -; mRNA.
CCDS; CCDS4987.1; -.
RefSeq; NP_060404.4; NM_017934.6.
UniGene; Hs.511817; -.
UniGene; Hs.606356; -.
PDB; 3MB3; X-ray; 2.25 A; A=1302-1434.
PDB; 5ENB; X-ray; 1.73 A; A=1315-1440.
PDB; 5ENC; X-ray; 1.59 A; A=1315-1440.
PDB; 5ENE; X-ray; 1.49 A; A=1315-1440.
PDB; 5ENF; X-ray; 1.37 A; A=1315-1440.
PDB; 5ENH; X-ray; 1.95 A; A=1315-1440.
PDB; 5ENI; X-ray; 1.69 A; A=1315-1440.
PDB; 5ENJ; X-ray; 1.63 A; A=1315-1440.
PDBsum; 3MB3; -.
PDBsum; 5ENB; -.
PDBsum; 5ENC; -.
PDBsum; 5ENE; -.
PDBsum; 5ENF; -.
PDBsum; 5ENH; -.
PDBsum; 5ENI; -.
PDBsum; 5ENJ; -.
ProteinModelPortal; Q8WWQ0; -.
SMR; Q8WWQ0; -.
BioGrid; 120353; 61.
IntAct; Q8WWQ0; 25.
STRING; 9606.ENSP00000275034; -.
ChEMBL; CHEMBL2176773; -.
iPTMnet; Q8WWQ0; -.
PhosphoSitePlus; Q8WWQ0; -.
BioMuta; PHIP; -.
DMDM; 308153472; -.
EPD; Q8WWQ0; -.
jPOST; Q8WWQ0; -.
MaxQB; Q8WWQ0; -.
PaxDb; Q8WWQ0; -.
PeptideAtlas; Q8WWQ0; -.
PRIDE; Q8WWQ0; -.
ProteomicsDB; 74919; -.
Ensembl; ENST00000275034; ENSP00000275034; ENSG00000146247.
GeneID; 55023; -.
KEGG; hsa:55023; -.
UCSC; uc003pir.4; human.
CTD; 55023; -.
DisGeNET; 55023; -.
EuPathDB; HostDB:ENSG00000146247.13; -.
GeneCards; PHIP; -.
H-InvDB; HIX0032894; -.
HGNC; HGNC:15673; PHIP.
HPA; HPA019140; -.
HPA; HPA019838; -.
MalaCards; PHIP; -.
MIM; 612870; gene.
MIM; 617991; phenotype.
neXtProt; NX_Q8WWQ0; -.
OpenTargets; ENSG00000146247; -.
PharmGKB; PA33265; -.
eggNOG; KOG0644; Eukaryota.
eggNOG; ENOG410YCD8; LUCA.
GeneTree; ENSGT00940000153647; -.
HOVERGEN; HBG108248; -.
InParanoid; Q8WWQ0; -.
KO; K11797; -.
OMA; PTVSKNH; -.
OrthoDB; 240778at2759; -.
PhylomeDB; Q8WWQ0; -.
TreeFam; TF324197; -.
SignaLink; Q8WWQ0; -.
ChiTaRS; PHIP; human.
EvolutionaryTrace; Q8WWQ0; -.
GenomeRNAi; 55023; -.
PRO; PR:Q8WWQ0; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000146247; Expressed in 244 organ(s), highest expression level in cerebral cortex.
Genevisible; Q8WWQ0; HS.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005158; F:insulin receptor binding; NAS:UniProtKB.
GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; NAS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:MGI.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
Gene3D; 1.20.920.10; -; 2.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR028738; PHIP.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR16266:SF4; PTHR16266:SF4; 1.
Pfam; PF00439; Bromodomain; 2.
Pfam; PF00400; WD40; 5.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 2.
SMART; SM00320; WD40; 8.
SUPFAM; SSF47370; SSF47370; 2.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 2.
PROSITE; PS00678; WD_REPEATS_1; 2.
PROSITE; PS50082; WD_REPEATS_2; 5.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Bromodomain; Complete proteome;
Disease mutation; Isopeptide bond; Mental retardation; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Ubl conjugation; WD repeat.
CHAIN 1 1821 PH-interacting protein.
/FTId=PRO_0000297757.
REPEAT 181 222 WD 1.
REPEAT 224 262 WD 2.
REPEAT 265 310 WD 3.
REPEAT 319 360 WD 4.
REPEAT 363 402 WD 5.
REPEAT 422 461 WD 6.
REPEAT 464 504 WD 7.
REPEAT 512 551 WD 8.
DOMAIN 1176 1246 Bromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 1333 1403 Bromo 2. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
REGION 924 1129 Mediates interaction with IRS1.
{ECO:0000250}.
COMPBIAS 867 923 Lys-rich.
COMPBIAS 1752 1758 Poly-Glu.
MOD_RES 136 136 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 641 641 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 659 659 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 674 674 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 677 677 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 683 683 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 692 692 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 879 879 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 880 880 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 881 881 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 911 911 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1281 1281 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1283 1283 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1296 1296 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1315 1315 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1359 1359 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1405 1405 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 1479 1479 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1497 1497 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1525 1525 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1533 1533 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1560 1560 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1651 1651 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1762 1762 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1783 1783 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 421 421 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1470 1470 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 1470 1470 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1644 1644 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1670 1670 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 17 17 F -> S (in DIDOD; unknown pathological
significance; dbSNP:rs878854420).
{ECO:0000269|PubMed:27900362}.
/FTId=VAR_080981.
VARIANT 110 110 R -> C (in DIDOD; unknown pathological
significance; dbSNP:rs768324201).
{ECO:0000269|PubMed:29209020}.
/FTId=VAR_080982.
VARIANT 110 110 R -> S (in DIDOD; unknown pathological
significance).
{ECO:0000269|PubMed:29209020}.
/FTId=VAR_080983.
VARIANT 274 1821 Missing (in DIDOD).
{ECO:0000269|PubMed:29209020}.
/FTId=VAR_080984.
VARIANT 469 469 V -> I (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036238.
VARIANT 555 1821 Missing (in DIDOD).
{ECO:0000269|PubMed:29209020}.
/FTId=VAR_080985.
VARIANT 634 1821 Missing (in DIDOD).
{ECO:0000269|PubMed:29209020}.
/FTId=VAR_080986.
VARIANT 663 663 V -> G (in dbSNP:rs7747479).
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17636024,
ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
/FTId=VAR_034683.
VARIANT 874 874 T -> I (in dbSNP:rs11547228).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_034684.
VARIANT 968 1821 Missing (in DIDOD).
{ECO:0000269|PubMed:29209020}.
/FTId=VAR_080987.
VARIANT 1093 1093 L -> P (in dbSNP:rs9350797).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_034685.
VARIANT 1135 1135 T -> P (in dbSNP:rs34841569).
/FTId=VAR_034686.
VARIANT 1149 1821 Missing (in DIDOD).
{ECO:0000269|PubMed:23033978,
ECO:0000269|PubMed:29209020}.
/FTId=VAR_078691.
VARIANT 1191 1821 Missing (in DIDOD).
{ECO:0000269|PubMed:29209020}.
/FTId=VAR_080988.
VARIANT 1263 1263 Q -> E (in DIDOD; unknown pathological
significance; found in a patient who also
carries a de novo missense variant in
TBC1D8B). {ECO:0000269|PubMed:29209020}.
/FTId=VAR_080989.
VARIANT 1298 1821 Missing (in DIDOD).
{ECO:0000269|PubMed:29209020}.
/FTId=VAR_080990.
VARIANT 1354 1821 Missing (in DIDOD).
{ECO:0000269|PubMed:29209020}.
/FTId=VAR_080991.
VARIANT 1445 1445 N -> T (in dbSNP:rs36048894).
/FTId=VAR_034687.
VARIANT 1767 1767 R -> I (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036239.
CONFLICT 2 2 S -> P (in Ref. 6; BAB71353).
{ECO:0000305}.
CONFLICT 770 770 T -> I (in Ref. 6; BAB71353).
{ECO:0000305}.
CONFLICT 1648 1648 N -> I (in Ref. 6; BAC11417).
{ECO:0000305}.
TURN 1318 1320 {ECO:0000244|PDB:5ENF}.
HELIX 1321 1334 {ECO:0000244|PDB:5ENF}.
HELIX 1336 1341 {ECO:0000244|PDB:5ENF}.
TURN 1347 1349 {ECO:0000244|PDB:5ENF}.
HELIX 1353 1356 {ECO:0000244|PDB:5ENF}.
HELIX 1363 1371 {ECO:0000244|PDB:5ENF}.
HELIX 1378 1395 {ECO:0000244|PDB:5ENF}.
HELIX 1402 1434 {ECO:0000244|PDB:5ENF}.
SEQUENCE 1821 AA; 206689 MW; 88688EF8743C980F CRC64;
MSCERKGLSE LRSELYFLIA RFLEDGPCQQ AAQVLIREVA EKELLPRRTD WTGKEHPRTY
QNLVKYYRHL APDHLLQICH RLGPLLEQEI PQSVPGVQTL LGAGRQSLLR TNKSCKHVVW
KGSALAALHC GRPPESPVNY GSPPSIADTL FSRKLNGKYR LERLVPTAVY QHMKMHKRIL
GHLSSVYCVT FDRTGRRIFT GSDDCLVKIW ATDDGRLLAT LRGHAAEISD MAVNYENTMI
AAGSCDKMIR VWCLRTCAPL AVLQGHSASI TSLQFSPLCS GSKRYLSSTG ADGTICFWLW
DAGTLKINPR PAKFTERPRP GVQMICSSFS AGGMFLATGS TDHIIRVYFF GSGQPEKISE
LEFHTDKVDS IQFSNTSNRF VSGSRDGTAR IWQFKRREWK SILLDMATRP AGQNLQGIED
KITKMKVTMV AWDRHDNTVI TAVNNMTLKV WNSYTGQLIH VLMGHEDEVF VLEPHPFDPR
VLFSAGHDGN VIVWDLARGV KIRSYFNMIE GQGHGAVFDC KCSPDGQHFA CTDSHGHLLI
FGFGSSSKYD KIADQMFFHS DYRPLIRDAN NFVLDEQTQQ APHLMPPPFL VDVDGNPHPS
RYQRLVPGRE NCREEQLIPQ MGVTSSGLNQ VLSQQANQEI SPLDSMIQRL QQEQDLRRSG
EAVISNTSRL SRGSISSTSE VHSPPNVGLR RSGQIEGVRQ MHSNAPRSEI ATERDLVAWS
RRVVVPELSA GVASRQEEWR TAKGEEEIKT YRSEEKRKHL TVPKENKIPT VSKNHAHEHF
LDLGESKKQQ TNQHNYRTRS ALEETPRPSE EIENGSSSSD EGEVVAVSGG TSEEEERAWH
SDGSSSDYSS DYSDWTADAG INLQPPKKVP KNKTKKAESS SDEEEESEKQ KQKQIKKEKK
KVNEEKDGPI SPKKKKPKER KQKRLAVGEL TENGLTLEEW LPSTWITDTI PRRCPFVPQM
GDEVYYFRQG HEAYVEMARK NKIYSINPKK QPWHKMELRE QELMKIVGIK YEVGLPTLCC
LKLAFLDPDT GKLTGGSFTM KYHDMPDVID FLVLRQQFDD AKYRRWNIGD RFRSVIDDAW
WFGTIESQEP LQLEYPDSLF QCYNVCWDNG DTEKMSPWDM ELIPNNAVFP EELGTSVPLT
DGECRSLIYK PLDGEWGTNP RDEECERIVA GINQLMTLDI ASAFVAPVDL QAYPMYCTVV
AYPTDLSTIK QRLENRFYRR VSSLMWEVRY IEHNTRTFNE PGSPIVKSAK FVTDLLLHFI
KDQTCYNIIP LYNSMKKKVL SDSEDEEKDA DVPGTSTRKR KDHQPRRRLR NRAQSYDIQA
WKKQCEELLN LIFQCEDSEP FRQPVDLLEY PDYRDIIDTP MDFATVRETL EAGNYESPME
LCKDVRLIFS NSKAYTPSKR SRIYSMSLRL SAFFEEHISS VLSDYKSALR FHKRNTITKR
RKKRNRSSSV SSSAASSPER KKRILKPQLK SESSTSAFST PTRSIPPRHN AAQINGKTES
SSVVRTRSNR VVVDPVVTEQ PSTSSAAKTF ITKANASAIP GKTILENSVK HSKALNTLSS
PGQSSFSHGT RNNSAKENME KEKPVKRKMK SSVLPKASTL SKSSAVIEQG DCKNNALVPG
TIQVNGHGGQ PSKLVKRGPG RKPKVEVNTN SGEIIHKKRG RKPKKLQYAK PEDLEQNNVH
PIRDEVLPSS TCNFLSETNN VKEDLLQKKN RGGRKPKRKM KTQKLDADLL VPASVKVLRR
SNRKKIDDPI DEEEEFEELK GSEPHMRTRN QGRRTAFYNE DDSEEEQRQL LFEDTSLTFG
TSSRGRVRKL TEKAKANLIG W


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP1689: Porphyrin and chlorophyll metabolism
WP2292: Chemokine signaling pathway
WP731: Sterol regulatory element binding protein related
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation

Related Genes :
[Irs1 Irs-1] Insulin receptor substrate 1 (IRS-1) (pp185)
[Irs1 Irs-1] Insulin receptor substrate 1 (IRS-1)
[PHLPP1 KIAA0606 PHLPP PLEKHE1 SCOP] PH domain leucine-rich repeat-containing protein phosphatase 1 (EC 3.1.3.16) (Pleckstrin homology domain-containing family E member 1) (PH domain-containing family E member 1) (Suprachiasmatic nucleus circadian oscillatory protein) (hSCOP)
[PLEKHO1 CKIP1 OC120 HQ0024c] Pleckstrin homology domain-containing family O member 1 (PH domain-containing family O member 1) (C-Jun-binding protein) (JBP) (Casein kinase 2-interacting protein 1) (CK2-interacting protein 1) (CKIP-1) (Osteoclast maturation-associated gene 120 protein)
[Sh2b1 Sh2-b Sh2bpsm1] SH2B adapter protein 1 (FceRI gamma-chain-interacting protein SH2-B) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)
[PHLPP2 KIAA0931 PHLPPL] PH domain leucine-rich repeat-containing protein phosphatase 2 (EC 3.1.3.16) (PH domain leucine-rich repeat-containing protein phosphatase-like) (PHLPP-like)
[Sh2b1 Sh2bpsm1] SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)
[IRS1] Insulin receptor substrate 1 (IRS-1)
[Wdfy3] WD repeat and FYVE domain-containing protein 3 (Beach domain, WD repeat and FYVE domain-containing protein 1) (BWF1)
[APPL1 APPL DIP13A KIAA1428] DCC-interacting protein 13-alpha (Dip13-alpha) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 1)
[AGAP3 CENTG3] Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3 (AGAP-3) (CRAM-associated GTPase) (CRAG) (Centaurin-gamma-3) (Cnt-g3) (MR1-interacting protein) (MRIP-1)
[Appl1 Dip13a Kiaa1428] DCC-interacting protein 13-alpha (Dip13-alpha) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 1)
[SH2B1 KIAA1299 SH2B] SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B)
[Asap1 Ddef1 Kiaa1249 Shag1] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[APPL2 DIP13B] DCC-interacting protein 13-beta (Dip13-beta) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 2)
[WDR45 WDRX1 WDRXI4 WIPI4 JM5] WD repeat domain phosphoinositide-interacting protein 4 (WIPI-4) (WD repeat-containing protein 45)
[ASAP1 DDEF1 KIAA1249] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[Appl2 Dip13b Dip3b] DCC-interacting protein 13-beta (Dip13-beta) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 2)
[WDR45B WDR45L WIPI3] WD repeat domain phosphoinositide-interacting protein 3 (WIPI-3) (WD repeat-containing protein 45-like) (WDR45-like protein) (WD repeat-containing protein 45B) (WIPI49-like protein)
[ACAP1 CENTB1 KIAA0050] Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 (Centaurin-beta-1) (Cnt-b1)
[WDFY1 FENS1 KIAA1435 WDF1 ZFYVE17] WD repeat and FYVE domain-containing protein 1 (FYVE domain-containing protein localized to endosomes 1) (FENS-1) (Phosphoinositide-binding protein 1) (WD40- and FYVE domain-containing protein 1) (Zinc finger FYVE domain-containing protein 17)
[WDR48 KIAA1449 UAF1] WD repeat-containing protein 48 (USP1-associated factor 1) (WD repeat endosomal protein) (p80)
[WDFY3 KIAA0993] WD repeat and FYVE domain-containing protein 3 (Autophagy-linked FYVE protein) (Alfy)
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[Appl2] DCC-interacting protein 13-beta (Adapter protein containing PH domain, PTB domain and leucine zipper motif 2)
[IRS4] Insulin receptor substrate 4 (IRS-4) (160 kDa phosphotyrosine protein) (py160) (Phosphoprotein of 160 kDa) (pp160)
[FBXW11 BTRCP2 FBW1B FBXW1B KIAA0696] F-box/WD repeat-containing protein 11 (F-box and WD repeats protein beta-TrCP2) (F-box/WD repeat-containing protein 1B) (Homologous to Slimb protein) (HOS)
[PLEKHM1 KIAA0356] Pleckstrin homology domain-containing family M member 1 (PH domain-containing family M member 1) (162 kDa adapter protein) (AP162)
[aip1 wdpA DDB_G0278733] Actin-interacting protein 1 (DAip1) (WD repeat-containing protein 2 homolog)
[Plekhb1 Evt1 Phr1] Pleckstrin homology domain-containing family B member 1 (PH domain-containing family B member 1) (Evectin-1) (PH domain-containing protein in retina 1) (PHRET1) (Pleckstrin homology domain retinal protein 1)

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