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Protein

PH-interacting protein

Gene

Phip

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

GO - Biological processi

  • cytoskeleton organization Source: UniProtKB
  • insulin receptor signaling pathway Source: MGI
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of extrinsic apoptotic signaling pathway Source: MGI
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of insulin-like growth factor receptor signaling pathway Source: UniProtKB
  • positive regulation of mitotic nuclear division Source: UniProtKB
  • positive regulation of peptidyl-serine phosphorylation Source: MGI
  • positive regulation of peptidyl-threonine phosphorylation Source: MGI
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein import into nucleus Source: MGI
  • regulation of cell morphogenesis Source: UniProtKB
  • regulation of growth Source: MGI
  • regulation of protein phosphorylation Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
PH-interacting protein
Short name:
PHIP
Alternative name(s):
IRS-1 PH domain-binding protein
Neuronal differentiation-related protein
Short name:
NDRP
WD repeat-containing protein 11
Gene namesi
Name:Phip
Synonyms:Ndrp, Phip1, Wdr11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1932404. Phip.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18211821PH-interacting proteinPRO_0000297758Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei136 – 1361PhosphoserineBy similarity
Cross-linki421 – 421Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei641 – 6411PhosphoserineBy similarity
Modified residuei659 – 6591PhosphoserineBy similarity
Modified residuei683 – 6831PhosphoserineBy similarity
Modified residuei692 – 6921PhosphoserineBy similarity
Modified residuei879 – 8791PhosphoserineBy similarity
Modified residuei880 – 8801PhosphoserineBy similarity
Modified residuei881 – 8811PhosphoserineBy similarity
Modified residuei911 – 9111PhosphoserineBy similarity
Modified residuei1281 – 12811PhosphoserineCombined sources
Modified residuei1283 – 12831PhosphoserineCombined sources
Modified residuei1296 – 12961PhosphoserineBy similarity
Modified residuei1315 – 13151PhosphoserineCombined sources
Modified residuei1359 – 13591PhosphothreonineBy similarity
Modified residuei1405 – 14051PhosphoserineBy similarity
Cross-linki1470 – 1470Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1479 – 14791PhosphoserineBy similarity
Modified residuei1497 – 14971N6-acetyllysineBy similarity
Modified residuei1525 – 15251PhosphoserineBy similarity
Modified residuei1533 – 15331N6-acetyllysineCombined sources
Modified residuei1651 – 16511PhosphoserineBy similarity
Modified residuei1762 – 17621PhosphoserineBy similarity
Modified residuei1783 – 17831PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8VDD9.
MaxQBiQ8VDD9.
PaxDbiQ8VDD9.
PRIDEiQ8VDD9.

PTM databases

iPTMnetiQ8VDD9.
PhosphoSiteiQ8VDD9.

Expressioni

Tissue specificityi

Widely expressed with most abundant expression detected in pancreatic islets, brain and skeletal muscle. Predominantly expressed in developing and regenerating neurons. Expressed in adult brain (granular layer of the olfactorium bulb, hippocampus, dentate gyrus and cerebellum internal granular layer). Expressed in the CA3 region of adult hippocampus, adult and fetal retina, perinatal dorsal root ganglion and embryonal olfactory epithelia (at protein level).3 Publications

Developmental stagei

Expressed at highest levels at 17.5 dpc in the neural layer of the retina and olfactory epithelia.1 Publication

Inductioni

In motor neurons after injury.1 Publication

Gene expression databases

CleanExiMM_PHIP.

Interactioni

Subunit structurei

Interacts (via bromo domain) with acetylated lysine residues on histone H1.4, histone H3 and H4 (in vitro) (By similarity). Interacts with IRS1 and IRS2.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Irs1P355702EBI-1369766,EBI-520230From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ8VDD9. 6 interactions.
MINTiMINT-4119794.
STRINGi10090.ENSMUSP00000034787.

Structurei

3D structure databases

ProteinModelPortaliQ8VDD9.
SMRiQ8VDD9. Positions 1316-1431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati181 – 22242WD 1Add
BLAST
Repeati224 – 26239WD 2Add
BLAST
Repeati265 – 31046WD 3Add
BLAST
Repeati319 – 36042WD 4Add
BLAST
Repeati363 – 40240WD 5Add
BLAST
Repeati422 – 46140WD 6Add
BLAST
Repeati464 – 50441WD 7Add
BLAST
Repeati512 – 55140WD 8Add
BLAST
Domaini1176 – 124671Bromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini1333 – 140371Bromo 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni924 – 1129206Mediates interaction with IRS1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi867 – 92357Lys-richAdd
BLAST
Compositional biasi1752 – 17587Poly-Glu

Sequence similaritiesi

Contains 2 bromo domains.PROSITE-ProRule annotation
Contains 8 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain, Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0644. Eukaryota.
ENOG410YCD8. LUCA.
HOGENOMiHOG000095265.
HOVERGENiHBG108248.
InParanoidiQ8VDD9.
PhylomeDBiQ8VDD9.

Family and domain databases

Gene3Di1.20.920.10. 2 hits.
2.130.10.10. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR028738. PHIP.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR16266:SF4. PTHR16266:SF4. 1 hit.
PfamiPF00439. Bromodomain. 2 hits.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 2 hits.
SM00320. WD40. 8 hits.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 2 hits.
SSF50978. SSF50978. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 2 hits.
PS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VDD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRERKGLSE LRSELYFLIA RFLEDGPCQQ AAQVLIREVA EKELLPRRTD
60 70 80 90 100
WTGKEHPRTY QNLVKYYRHL APDHLLQICH RLGPLLEQEI PQSVPGVQTL
110 120 130 140 150
LGAGRQSLLR TNKSCKHVVW KGSALAALHC GRPPESPVNY GSPPSIADTL
160 170 180 190 200
FSRKLNGKYR LERLVPTAVY QHMKMHKRIL GHLSSVYCVT FDRTGRRIFT
210 220 230 240 250
GSDDCLVKIW ATDDGRLLAT LRGHAAEISD MAVNYENTMI AAGSCDKMIR
260 270 280 290 300
VWCLRTCAPL AVLQGHSASI TSLQFSPLCS GSKRYLSSTG ADGTICFWLW
310 320 330 340 350
DAGTLKINPR PTKFTERPRP GVQMICSSFS AGGMFLATGS TDHIIRVYFF
360 370 380 390 400
GSGQPEKISE LEFHTDKVDS IQFSNTSNRF VSGSRDGTAR IWQFKRREWK
410 420 430 440 450
SILLDMATRP AGQNLQGIED KITKMKVTMV AWDRHDNTVI TAVNNMTLKV
460 470 480 490 500
WNSYTGQLIH VLMGHEDEVF VLEPHPFDPR VLFSAGHDGN VIVWDLARGV
510 520 530 540 550
KVRSYFNMIE GQGHGAVFDC KCSPDGQHFA CTDSHGHLLI FGFGSSSKYD
560 570 580 590 600
KIADQMFFHS DYRPLIRDAN NFVLDEQTQQ APHLMPPPFL VDVDGNPHPS
610 620 630 640 650
RYQRLVPGRE NCREEQLIPQ MGVTSSGLNQ VLSQQANQDI SPLDSMIQRL
660 670 680 690 700
QQEQDLRRSG EAGVSNASRV NRGSVSSTSE VHSPPNIGLR RSGQIEGVRQ
710 720 730 740 750
MHSNAPRSEI ATERDLVAWS RRVVVPELSA GVASRQEEWR TAKGEEEIKS
760 770 780 790 800
YRSEEKRKHL TVAKENKILT VSKNHAHEHF LDLGDSKKQQ ANQHNYRTRS
810 820 830 840 850
ALEETPRPLE ELENGTSSSD EGEVLAVSGG TSEEEERAWH SDGSSSDYSS
860 870 880 890 900
DYSDWTADAG INLQPPKKVP KHKTKKPESS SDEEEESENQ KQKHIKKERK
910 920 930 940 950
KANEEKDGPT SPKKKKPKER KQKRLAVGEL TENGLTLEEW LPSAWITDTL
960 970 980 990 1000
PRRCPFVPQM GDEVYYFRQG HEAYVEMARK NKIYSINPKK QPWHKMELRE
1010 1020 1030 1040 1050
QELMKIVGIK YEVGLPTLCC LKLAFLDPDT GKLTGGSFTM KYHDMPDVID
1060 1070 1080 1090 1100
FLVLRQQFDD AKYRPWNIGD RFRSVIDDAW WFGTIESQEP LQPEYPDSLF
1110 1120 1130 1140 1150
QCYNVCWDNG DTEKMSPWDM ELIPNNAVFP EELGTSVPLT DVECRSLIYK
1160 1170 1180 1190 1200
PLDGEWGANP RDEECERIVG GINQLMTLDI ASAFVAPVDL QAYPMYCTVV
1210 1220 1230 1240 1250
AYPTDLSTIK QRLENRFYRR FSSLMWEVRY IEHNTRTFNE PGSPIVKSAK
1260 1270 1280 1290 1300
FVTDLLLHFI KDQTCYNIIP LYNSMKKKVL SDSEEEEKDA DVPGTSTRKR
1310 1320 1330 1340 1350
KDHQPRRRLR NRAQSYDIQA WKKQCQELLN LIFQCEDSEP FRQPVDLLEY
1360 1370 1380 1390 1400
PDYRDIIDTP MDFATVRETL EAGNYESPME LCKDVRLIFS NFKAYTPSKR
1410 1420 1430 1440 1450
SRIYSMSLRL SAFFEEHISS VLSDYKSALR FHKRNTISKK RKKRNRSSSL
1460 1470 1480 1490 1500
SSSAASSPER KKRILKPQLK SEVSTSPFSI PTRSVLPRHN AAQMNGKPES
1510 1520 1530 1540 1550
SSVVRTRSNR VAVDPVVTEQ PSTSSATKAF VSKTNTSAMP GKAMLENSVR
1560 1570 1580 1590 1600
HSKALSTLSS PDPLTFSHAT KNNSAKENME KEKPVKRKMK SSVFSKASPL
1610 1620 1630 1640 1650
PKSAAVIEQG ECKNNVLIPG TIQVNGHGGQ PSKLVKRGPG RKPKVEVNTS
1660 1670 1680 1690 1700
SGEVTHKKRG RKPKNLQCAK QENSEQNNMH PIRADVLPSS TCNFLSETNA
1710 1720 1730 1740 1750
VKEDLLQKKS RGGRKPKRKM KTHNLDSELI VPTNVKVLRR SNRKKTDDPI
1760 1770 1780 1790 1800
DEEEEFEELK GSEPHMRTRN QGRRTAFYNE DDSEEEQRQL LFEDTSLTFG
1810 1820
TSSRGRVRKL TEKAKANLIG W
Length:1,821
Mass (Da):206,726
Last modified:August 21, 2007 - v2
Checksum:i92E8DF0833F60FFA
GO

Sequence cautioni

The sequence AAG45146.1 differs from that shown.Intron retention. This sequence is incomplete at the 5' end and extensively differs from that shown.Curated
The sequence AAH49950.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAB16299.1 differs from that shown.Intron retention. This sequence is incomplete at the 3' end and extensively differs from that shown.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti672 – 6721R → G in AAH49950 (PubMed:15489334).Curated
Sequence conflicti1065 – 10651P → R in BAE36779 (PubMed:16141072).Curated
Sequence conflicti1065 – 10651P → R in AAG45146 (PubMed:11018022).Curated
Sequence conflicti1155 – 11551E → D in AAG45146 (PubMed:11018022).Curated
Sequence conflicti1392 – 13921F → S in BAE36779 (PubMed:16141072).Curated
Sequence conflicti1392 – 13921F → S in AAG45146 (PubMed:11018022).Curated
Sequence conflicti1776 – 17761A → T in AAG45146 (PubMed:11018022).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ303103 mRNA. Translation: CAC83119.1.
AB049460 mRNA. Translation: BAB16299.1. Sequence problems.
BC049950 mRNA. Translation: AAH49950.1. Different termination.
AK162189 mRNA. Translation: BAE36779.1.
AF310251 mRNA. Translation: AAG45146.1. Sequence problems.
CCDSiCCDS40706.1.
UniGeneiMm.221688.

Genome annotation databases

UCSCiuc009qvw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ303103 mRNA. Translation: CAC83119.1.
AB049460 mRNA. Translation: BAB16299.1. Sequence problems.
BC049950 mRNA. Translation: AAH49950.1. Different termination.
AK162189 mRNA. Translation: BAE36779.1.
AF310251 mRNA. Translation: AAG45146.1. Sequence problems.
CCDSiCCDS40706.1.
UniGeneiMm.221688.

3D structure databases

ProteinModelPortaliQ8VDD9.
SMRiQ8VDD9. Positions 1316-1431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8VDD9. 6 interactions.
MINTiMINT-4119794.
STRINGi10090.ENSMUSP00000034787.

PTM databases

iPTMnetiQ8VDD9.
PhosphoSiteiQ8VDD9.

Proteomic databases

EPDiQ8VDD9.
MaxQBiQ8VDD9.
PaxDbiQ8VDD9.
PRIDEiQ8VDD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiuc009qvw.1. mouse.

Organism-specific databases

MGIiMGI:1932404. Phip.

Phylogenomic databases

eggNOGiKOG0644. Eukaryota.
ENOG410YCD8. LUCA.
HOGENOMiHOG000095265.
HOVERGENiHBG108248.
InParanoidiQ8VDD9.
PhylomeDBiQ8VDD9.

Miscellaneous databases

ChiTaRSiPhip. mouse.
PROiQ8VDD9.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PHIP.

Family and domain databases

Gene3Di1.20.920.10. 2 hits.
2.130.10.10. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR028738. PHIP.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR16266:SF4. PTHR16266:SF4. 1 hit.
PfamiPF00439. Bromodomain. 2 hits.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 2 hits.
SM00320. WD40. 8 hits.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 2 hits.
SSF50978. SSF50978. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 2 hits.
PS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Antonarakis S.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1779.
  2. "Identification of a novel WD repeat-containing gene predominantly expressed in developing and regenerating neurons."
    Kato H., Chen S., Kiyama H., Ikeda K., Kimura N., Nakashima K., Taga T.
    J. Biochem. 128:923-932(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-999, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
    Strain: Swiss Webster / NIH.
  3. "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] OF 1-893.
    Strain: Czech II.
    Tissue: Mammary tumor.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 745-1458.
    Strain: C57BL/6J.
    Tissue: Egg.
  5. "Cloning and characterization of PHIP, a novel insulin receptor substrate-1 pleckstrin homology domain interacting protein."
    Farhang-Fallah J., Yin X., Trentin G., Cheng A.M., Rozakis-Adcock M.
    J. Biol. Chem. 275:40492-40497(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 924-1821, FUNCTION, INTERACTION WITH IRS1 AND IRS2, TISSUE SPECIFICITY.
  6. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1589-1596, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  7. "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."
    Farhang-Fallah J., Randhawa V.K., Nimnual A., Klip A., Bar-Sagi D., Rozakis-Adcock M.
    Mol. Cell. Biol. 22:7325-7336(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Identification of a WD40 repeat-containing isoform of PHIP as a novel regulator of beta-cell growth and survival."
    Podcheko A., Northcott P., Bikopoulos G., Lee A., Bommareddi S.R., Kushner J.A., Farhang-Fallah J., Rozakis-Adcock M.
    Mol. Cell. Biol. 27:6484-6496(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281 AND SER-1283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281 AND SER-1283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281; SER-1283; SER-1315 AND SER-1783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.
  12. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1533, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPHIP_MOUSE
AccessioniPrimary (citable) accession number: Q8VDD9
Secondary accession number(s): Q3TS96
, Q80VI6, Q9EPY1, Q9ESL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: August 21, 2007
Last modified: May 11, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.