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Protein

PH-interacting protein

Gene

PHIP

Organism
Homo sapiens (Human)
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.2 Publications

GO - Molecular functioni

  • insulin receptor binding Source: UniProtKB
  • lysine-acetylated histone binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ8WWQ0.

Names & Taxonomyi

Protein namesi
Recommended name:
PH-interacting protein
Short name:
PHIP
Alternative name(s):
IRS-1 PH domain-binding protein
WD repeat-containing protein 11
Gene namesi
Name:PHIP
Synonyms:WDR11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:15673. PHIP.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33265.

Chemistry

ChEMBLiCHEMBL2176773.

Polymorphism and mutation databases

BioMutaiPHIP.
DMDMi308153472.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18211821PH-interacting proteinPRO_0000297757Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8WWQ0.
MaxQBiQ8WWQ0.
PaxDbiQ8WWQ0.
PRIDEiQ8WWQ0.

PTM databases

iPTMnetiQ8WWQ0.
PhosphoSiteiQ8WWQ0.

Expressioni

Tissue specificityi

Expressed in myeloma and epidermoid carcinoma cell lines.1 Publication

Gene expression databases

BgeeiQ8WWQ0.
CleanExiHS_PHIP.
GenevisibleiQ8WWQ0. HS.

Organism-specific databases

HPAiHPA019140.
HPA019838.

Interactioni

Subunit structurei

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).By similarity1 Publication

GO - Molecular functioni

  • insulin receptor binding Source: UniProtKB
  • lysine-acetylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120353. 28 interactions.
IntActiQ8WWQ0. 21 interactions.
MINTiMINT-1422606.
STRINGi9606.ENSP00000275034.

Structurei

Secondary structure

1
1821
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1321 – 133414Combined sources
Helixi1336 – 13416Combined sources
Turni1347 – 13493Combined sources
Helixi1353 – 13564Combined sources
Helixi1363 – 13719Combined sources
Helixi1378 – 139518Combined sources
Helixi1402 – 142827Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MB3X-ray2.25A1302-1434[»]
ProteinModelPortaliQ8WWQ0.
SMRiQ8WWQ0. Positions 1316-1431.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WWQ0.

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 IRS1By similarityAdd
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.
GeneTreeiENSGT00720000108687.
HOVERGENiHBG108248.
InParanoidiQ8WWQ0.
KOiK11797.
OMAiCYDIIPL.
OrthoDBiEOG7N37BR.
PhylomeDBiQ8WWQ0.
TreeFamiTF324197.

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.

Q8WWQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCERKGLSE 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 PAKFTERPRP 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
KIRSYFNMIE GQGHGAVFDC KCSPDGQHFA CTDSHGHLLI FGFGSSSKYD
560 570 580 590 600
KIADQMFFHS DYRPLIRDAN NFVLDEQTQQ APHLMPPPFL VDVDGNPHPS
610 620 630 640 650
RYQRLVPGRE NCREEQLIPQ MGVTSSGLNQ VLSQQANQEI SPLDSMIQRL
660 670 680 690 700
QQEQDLRRSG EAVISNTSRL SRGSISSTSE VHSPPNVGLR RSGQIEGVRQ
710 720 730 740 750
MHSNAPRSEI ATERDLVAWS RRVVVPELSA GVASRQEEWR TAKGEEEIKT
760 770 780 790 800
YRSEEKRKHL TVPKENKIPT VSKNHAHEHF LDLGESKKQQ TNQHNYRTRS
810 820 830 840 850
ALEETPRPSE EIENGSSSSD EGEVVAVSGG TSEEEERAWH SDGSSSDYSS
860 870 880 890 900
DYSDWTADAG INLQPPKKVP KNKTKKAESS SDEEEESEKQ KQKQIKKEKK
910 920 930 940 950
KVNEEKDGPI SPKKKKPKER KQKRLAVGEL TENGLTLEEW LPSTWITDTI
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 AKYRRWNIGD RFRSVIDDAW WFGTIESQEP LQLEYPDSLF
1110 1120 1130 1140 1150
QCYNVCWDNG DTEKMSPWDM ELIPNNAVFP EELGTSVPLT DGECRSLIYK
1160 1170 1180 1190 1200
PLDGEWGTNP RDEECERIVA GINQLMTLDI ASAFVAPVDL QAYPMYCTVV
1210 1220 1230 1240 1250
AYPTDLSTIK QRLENRFYRR VSSLMWEVRY IEHNTRTFNE PGSPIVKSAK
1260 1270 1280 1290 1300
FVTDLLLHFI KDQTCYNIIP LYNSMKKKVL SDSEDEEKDA DVPGTSTRKR
1310 1320 1330 1340 1350
KDHQPRRRLR NRAQSYDIQA WKKQCEELLN LIFQCEDSEP FRQPVDLLEY
1360 1370 1380 1390 1400
PDYRDIIDTP MDFATVRETL EAGNYESPME LCKDVRLIFS NSKAYTPSKR
1410 1420 1430 1440 1450
SRIYSMSLRL SAFFEEHISS VLSDYKSALR FHKRNTITKR RKKRNRSSSV
1460 1470 1480 1490 1500
SSSAASSPER KKRILKPQLK SESSTSAFST PTRSIPPRHN AAQINGKTES
1510 1520 1530 1540 1550
SSVVRTRSNR VVVDPVVTEQ PSTSSAAKTF ITKANASAIP GKTILENSVK
1560 1570 1580 1590 1600
HSKALNTLSS PGQSSFSHGT RNNSAKENME KEKPVKRKMK SSVLPKASTL
1610 1620 1630 1640 1650
SKSSAVIEQG DCKNNALVPG TIQVNGHGGQ PSKLVKRGPG RKPKVEVNTN
1660 1670 1680 1690 1700
SGEIIHKKRG RKPKKLQYAK PEDLEQNNVH PIRDEVLPSS TCNFLSETNN
1710 1720 1730 1740 1750
VKEDLLQKKN RGGRKPKRKM KTQKLDADLL VPASVKVLRR SNRKKIDDPI
1760 1770 1780 1790 1800
DEEEEFEELK GSEPHMRTRN QGRRTAFYNE DDSEEEQRQL LFEDTSLTFG
1810 1820
TSSRGRVRKL TEKAKANLIG W
Length:1,821
Mass (Da):206,689
Last modified:October 5, 2010 - v2
Checksum:i88688EF8743C980F
GO

Sequence cautioni

The sequence AAH21905.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAC11417.1 differs from that shown. Reason: Frameshift at position 1648. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → P in BAB71353 (PubMed:14702039).Curated
Sequence conflicti770 – 7701T → I in BAB71353 (PubMed:14702039).Curated
Sequence conflicti1648 – 16481N → I in BAC11417 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti469 – 4691V → I in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036238
Natural varianti663 – 6631V → G.Combined sources5 Publications
Corresponds to variant rs7747479 [ dbSNP | Ensembl ].
VAR_034683
Natural varianti874 – 8741T → I.1 Publication
Corresponds to variant rs11547228 [ dbSNP | Ensembl ].
VAR_034684
Natural varianti1093 – 10931L → P.2 Publications
Corresponds to variant rs9350797 [ dbSNP | Ensembl ].
VAR_034685
Natural varianti1135 – 11351T → P.
Corresponds to variant rs34841569 [ dbSNP | Ensembl ].
VAR_034686
Natural varianti1445 – 14451N → T.
Corresponds to variant rs36048894 [ dbSNP | Ensembl ].
VAR_034687
Natural varianti1767 – 17671R → I in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036239

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ924532 mRNA. Translation: ABK76299.1.
AJ303102 mRNA. Translation: CAC83118.1.
AL450327, AL356776 Genomic DNA. Translation: CAH70884.1.
AL356776, AL450327 Genomic DNA. Translation: CAI14406.1.
CH471051 Genomic DNA. Translation: EAW48718.1.
BC008909 mRNA. Translation: AAH08909.2.
BC021905 mRNA. Translation: AAH21905.1. Sequence problems.
BC081569 mRNA. Translation: AAH81569.1.
BC137488 mRNA. Translation: AAI37489.1.
AK057039 mRNA. Translation: BAB71353.1.
AK075124 mRNA. Translation: BAC11417.1. Frameshift.
AL161957 mRNA. Translation: CAH10776.1.
AF310250 mRNA. Translation: AAG45145.1.
CCDSiCCDS4987.1.
RefSeqiNP_060404.3. NM_017934.5.
UniGeneiHs.511817.
Hs.606356.

Genome annotation databases

EnsembliENST00000275034; ENSP00000275034; ENSG00000146247.
GeneIDi55023.
KEGGihsa:55023.
UCSCiuc003pir.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ924532 mRNA. Translation: ABK76299.1.
AJ303102 mRNA. Translation: CAC83118.1.
AL450327, AL356776 Genomic DNA. Translation: CAH70884.1.
AL356776, AL450327 Genomic DNA. Translation: CAI14406.1.
CH471051 Genomic DNA. Translation: EAW48718.1.
BC008909 mRNA. Translation: AAH08909.2.
BC021905 mRNA. Translation: AAH21905.1. Sequence problems.
BC081569 mRNA. Translation: AAH81569.1.
BC137488 mRNA. Translation: AAI37489.1.
AK057039 mRNA. Translation: BAB71353.1.
AK075124 mRNA. Translation: BAC11417.1. Frameshift.
AL161957 mRNA. Translation: CAH10776.1.
AF310250 mRNA. Translation: AAG45145.1.
CCDSiCCDS4987.1.
RefSeqiNP_060404.3. NM_017934.5.
UniGeneiHs.511817.
Hs.606356.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MB3X-ray2.25A1302-1434[»]
ProteinModelPortaliQ8WWQ0.
SMRiQ8WWQ0. Positions 1316-1431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120353. 28 interactions.
IntActiQ8WWQ0. 21 interactions.
MINTiMINT-1422606.
STRINGi9606.ENSP00000275034.

Chemistry

ChEMBLiCHEMBL2176773.

PTM databases

iPTMnetiQ8WWQ0.
PhosphoSiteiQ8WWQ0.

Polymorphism and mutation databases

BioMutaiPHIP.
DMDMi308153472.

Proteomic databases

EPDiQ8WWQ0.
MaxQBiQ8WWQ0.
PaxDbiQ8WWQ0.
PRIDEiQ8WWQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000275034; ENSP00000275034; ENSG00000146247.
GeneIDi55023.
KEGGihsa:55023.
UCSCiuc003pir.4. human.

Organism-specific databases

CTDi55023.
GeneCardsiPHIP.
H-InvDBHIX0032894.
HGNCiHGNC:15673. PHIP.
HPAiHPA019140.
HPA019838.
MIMi612870. gene.
neXtProtiNX_Q8WWQ0.
PharmGKBiPA33265.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0644. Eukaryota.
ENOG410YCD8. LUCA.
GeneTreeiENSGT00720000108687.
HOVERGENiHBG108248.
InParanoidiQ8WWQ0.
KOiK11797.
OMAiCYDIIPL.
OrthoDBiEOG7N37BR.
PhylomeDBiQ8WWQ0.
TreeFamiTF324197.

Enzyme and pathway databases

SignaLinkiQ8WWQ0.

Miscellaneous databases

ChiTaRSiPHIP. human.
EvolutionaryTraceiQ8WWQ0.
GenomeRNAii55023.
NextBioi58406.
PROiQ8WWQ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WWQ0.
CleanExiHS_PHIP.
GenevisibleiQ8WWQ0. HS.

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. "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: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-663.
  2. Antonarakis S.E.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-663.
  3. "The DNA sequence and analysis of human chromosome 6."
    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.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-663.
  5. "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 GLY-663; ILE-874 AND PRO-1093.
    Tissue: Brain, Lymph and Skin.
  6. "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 1-912, NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1230-1821, VARIANT GLY-663.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 905-1821, VARIANT PRO-1093.
    Tissue: Amygdala.
  8. "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 960-1821, TISSUE SPECIFICITY.
  9. "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.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-1281; SER-1283; SER-1296; SER-1405; SER-1479 AND SER-1783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-1281; SER-1283; SER-1315 AND SER-1783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1497 AND LYS-1533, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
    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.
    BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "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-683; SER-692; SER-879; SER-880; SER-881; SER-911; SER-1315 AND SER-1783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-1315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "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."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-421 AND LYS-1470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1302-1434, SUBUNIT.
  22. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-469 AND ILE-1767.

Entry informationi

Entry nameiPHIP_HUMAN
AccessioniPrimary (citable) accession number: Q8WWQ0
Secondary accession number(s): A7J992
, B2RPK4, Q05CQ9, Q5VVH4, Q66I29, Q69YV1, Q8NBZ5, Q96H52, Q96ME2, Q9H261
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: October 5, 2010
Last modified: May 11, 2016
This is version 125 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 6
    Human chromosome 6: 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

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.