Q8VDD9 · PHIP_MOUSE
- ProteinPH-interacting protein
- GenePhip
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1821 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePH-interacting protein
- Short namesPHIP
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8VDD9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000297758 | 1-1821 | PH-interacting protein | |||
Sequence: MSRERKGLSELRSELYFLIARFLEDGPCQQAAQVLIREVAEKELLPRRTDWTGKEHPRTYQNLVKYYRHLAPDHLLQICHRLGPLLEQEIPQSVPGVQTLLGAGRQSLLRTNKSCKHVVWKGSALAALHCGRPPESPVNYGSPPSIADTLFSRKLNGKYRLERLVPTAVYQHMKMHKRILGHLSSVYCVTFDRTGRRIFTGSDDCLVKIWATDDGRLLATLRGHAAEISDMAVNYENTMIAAGSCDKMIRVWCLRTCAPLAVLQGHSASITSLQFSPLCSGSKRYLSSTGADGTICFWLWDAGTLKINPRPTKFTERPRPGVQMICSSFSAGGMFLATGSTDHIIRVYFFGSGQPEKISELEFHTDKVDSIQFSNTSNRFVSGSRDGTARIWQFKRREWKSILLDMATRPAGQNLQGIEDKITKMKVTMVAWDRHDNTVITAVNNMTLKVWNSYTGQLIHVLMGHEDEVFVLEPHPFDPRVLFSAGHDGNVIVWDLARGVKVRSYFNMIEGQGHGAVFDCKCSPDGQHFACTDSHGHLLIFGFGSSSKYDKIADQMFFHSDYRPLIRDANNFVLDEQTQQAPHLMPPPFLVDVDGNPHPSRYQRLVPGRENCREEQLIPQMGVTSSGLNQVLSQQANQDISPLDSMIQRLQQEQDLRRSGEAGVSNASRVNRGSVSSTSEVHSPPNIGLRRSGQIEGVRQMHSNAPRSEIATERDLVAWSRRVVVPELSAGVASRQEEWRTAKGEEEIKSYRSEEKRKHLTVAKENKILTVSKNHAHEHFLDLGDSKKQQANQHNYRTRSALEETPRPLEELENGTSSSDEGEVLAVSGGTSEEEERAWHSDGSSSDYSSDYSDWTADAGINLQPPKKVPKHKTKKPESSSDEEEESENQKQKHIKKERKKANEEKDGPTSPKKKKPKERKQKRLAVGELTENGLTLEEWLPSAWITDTLPRRCPFVPQMGDEVYYFRQGHEAYVEMARKNKIYSINPKKQPWHKMELREQELMKIVGIKYEVGLPTLCCLKLAFLDPDTGKLTGGSFTMKYHDMPDVIDFLVLRQQFDDAKYRPWNIGDRFRSVIDDAWWFGTIESQEPLQPEYPDSLFQCYNVCWDNGDTEKMSPWDMELIPNNAVFPEELGTSVPLTDVECRSLIYKPLDGEWGANPRDEECERIVGGINQLMTLDIASAFVAPVDLQAYPMYCTVVAYPTDLSTIKQRLENRFYRRFSSLMWEVRYIEHNTRTFNEPGSPIVKSAKFVTDLLLHFIKDQTCYNIIPLYNSMKKKVLSDSEEEEKDADVPGTSTRKRKDHQPRRRLRNRAQSYDIQAWKKQCQELLNLIFQCEDSEPFRQPVDLLEYPDYRDIIDTPMDFATVRETLEAGNYESPMELCKDVRLIFSNFKAYTPSKRSRIYSMSLRLSAFFEEHISSVLSDYKSALRFHKRNTISKKRKKRNRSSSLSSSAASSPERKKRILKPQLKSEVSTSPFSIPTRSVLPRHNAAQMNGKPESSSVVRTRSNRVAVDPVVTEQPSTSSATKAFVSKTNTSAMPGKAMLENSVRHSKALSTLSSPDPLTFSHATKNNSAKENMEKEKPVKRKMKSSVFSKASPLPKSAAVIEQGECKNNVLIPGTIQVNGHGGQPSKLVKRGPGRKPKVEVNTSSGEVTHKKRGRKPKNLQCAKQENSEQNNMHPIRADVLPSSTCNFLSETNAVKEDLLQKKSRGGRKPKRKMKTHNLDSELIVPTNVKVLRRSNRKKTDDPIDEEEEFEELKGSEPHMRTRNQGRRTAFYNEDDSEEEQRQLLFEDTSLTFGTSSRGRVRKLTEKAKANLIGW | ||||||
Modified residue | 136 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 421 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 641 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 659 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 674 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 677 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 683 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 692 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 879 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 880 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 881 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 911 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1281 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1283 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1296 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1315 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1359 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1405 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 1470 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | ||||||
Cross-link | 1470 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 1479 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1497 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 1525 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1533 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 1560 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 1644 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1651 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 1670 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1762 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1783 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
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).
Induction
In motor neurons after injury.
Developmental stage
Expressed at highest levels at 17.5 dpc in the neural layer of the retina and olfactory epithelia.
Interaction
Subunit
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
Interacts with IRS1 and IRS2
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q8VDD9 | Irs1 P35570 | 2 | EBI-1369766, EBI-520230 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 181-222 | WD 1 | ||||
Sequence: GHLSSVYCVTFDRTGRRIFTGSDDCLVKIWATDDGRLLATLR | ||||||
Repeat | 224-262 | WD 2 | ||||
Sequence: HAAEISDMAVNYENTMIAAGSCDKMIRVWCLRTCAPLAV | ||||||
Repeat | 265-310 | WD 3 | ||||
Sequence: GHSASITSLQFSPLCSGSKRYLSSTGADGTICFWLWDAGTLKINPR | ||||||
Repeat | 319-360 | WD 4 | ||||
Sequence: RPGVQMICSSFSAGGMFLATGSTDHIIRVYFFGSGQPEKISE | ||||||
Repeat | 363-402 | WD 5 | ||||
Sequence: FHTDKVDSIQFSNTSNRFVSGSRDGTARIWQFKRREWKSI | ||||||
Repeat | 422-461 | WD 6 | ||||
Sequence: ITKMKVTMVAWDRHDNTVITAVNNMTLKVWNSYTGQLIHV | ||||||
Repeat | 464-504 | WD 7 | ||||
Sequence: GHEDEVFVLEPHPFDPRVLFSAGHDGNVIVWDLARGVKVRS | ||||||
Repeat | 512-551 | WD 8 | ||||
Sequence: QGHGAVFDCKCSPDGQHFACTDSHGHLLIFGFGSSSKYDK | ||||||
Compositional bias | 653-685 | Polar residues | ||||
Sequence: EQDLRRSGEAGVSNASRVNRGSVSSTSEVHSPP | ||||||
Region | 653-695 | Disordered | ||||
Sequence: EQDLRRSGEAGVSNASRVNRGSVSSTSEVHSPPNIGLRRSGQI | ||||||
Region | 782-927 | Disordered | ||||
Sequence: DLGDSKKQQANQHNYRTRSALEETPRPLEELENGTSSSDEGEVLAVSGGTSEEEERAWHSDGSSSDYSSDYSDWTADAGINLQPPKKVPKHKTKKPESSSDEEEESENQKQKHIKKERKKANEEKDGPTSPKKKKPKERKQKRLAV | ||||||
Compositional bias | 811-825 | Polar residues | ||||
Sequence: ELENGTSSSDEGEVL | ||||||
Compositional bias | 843-857 | Polar residues | ||||
Sequence: GSSSDYSSDYSDWTA | ||||||
Compositional bias | 875-914 | Basic and acidic residues | ||||
Sequence: KKPESSSDEEEESENQKQKHIKKERKKANEEKDGPTSPKK | ||||||
Region | 924-1129 | Mediates interaction with IRS1 | ||||
Sequence: RLAVGELTENGLTLEEWLPSAWITDTLPRRCPFVPQMGDEVYYFRQGHEAYVEMARKNKIYSINPKKQPWHKMELREQELMKIVGIKYEVGLPTLCCLKLAFLDPDTGKLTGGSFTMKYHDMPDVIDFLVLRQQFDDAKYRPWNIGDRFRSVIDDAWWFGTIESQEPLQPEYPDSLFQCYNVCWDNGDTEKMSPWDMELIPNNAVF | ||||||
Domain | 1176-1246 | Bromo 1 | ||||
Sequence: MTLDIASAFVAPVDLQAYPMYCTVVAYPTDLSTIKQRLENRFYRRFSSLMWEVRYIEHNTRTFNEPGSPIV | ||||||
Compositional bias | 1282-1299 | Basic and acidic residues | ||||
Sequence: DSEEEEKDADVPGTSTRK | ||||||
Region | 1282-1310 | Disordered | ||||
Sequence: DSEEEEKDADVPGTSTRKRKDHQPRRRLR | ||||||
Domain | 1333-1403 | Bromo 2 | ||||
Sequence: FQCEDSEPFRQPVDLLEYPDYRDIIDTPMDFATVRETLEAGNYESPMELCKDVRLIFSNFKAYTPSKRSRI | ||||||
Region | 1435-1507 | Disordered | ||||
Sequence: NTISKKRKKRNRSSSLSSSAASSPERKKRILKPQLKSEVSTSPFSIPTRSVLPRHNAAQMNGKPESSSVVRTR | ||||||
Compositional bias | 1469-1507 | Polar residues | ||||
Sequence: LKSEVSTSPFSIPTRSVLPRHNAAQMNGKPESSSVVRTR | ||||||
Compositional bias | 1556-1573 | Polar residues | ||||
Sequence: STLSSPDPLTFSHATKNN | ||||||
Region | 1556-1596 | Disordered | ||||
Sequence: STLSSPDPLTFSHATKNNSAKENMEKEKPVKRKMKSSVFSK | ||||||
Compositional bias | 1574-1589 | Basic and acidic residues | ||||
Sequence: SAKENMEKEKPVKRKM | ||||||
Region | 1623-1676 | Disordered | ||||
Sequence: QVNGHGGQPSKLVKRGPGRKPKVEVNTSSGEVTHKKRGRKPKNLQCAKQENSEQ | ||||||
Region | 1740-1785 | Disordered | ||||
Sequence: RSNRKKTDDPIDEEEEFEELKGSEPHMRTRNQGRRTAFYNEDDSEE | ||||||
Compositional bias | 1759-1785 | Basic and acidic residues | ||||
Sequence: LKGSEPHMRTRNQGRRTAFYNEDDSEE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,821
- Mass (Da)206,726
- Last updated2007-08-21 v2
- Checksum92E8DF0833F60FFA
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A087WP89 | A0A087WP89_MOUSE | Phip | 92 | ||
A0A087WPP7 | A0A087WPP7_MOUSE | Phip | 84 | ||
A0A087WR26 | A0A087WR26_MOUSE | Phip | 360 | ||
F8VQ93 | F8VQ93_MOUSE | Phip | 1821 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 653-685 | Polar residues | ||||
Sequence: EQDLRRSGEAGVSNASRVNRGSVSSTSEVHSPP | ||||||
Sequence conflict | 672 | in Ref. 3; AAH49950 | ||||
Sequence: R → G | ||||||
Compositional bias | 811-825 | Polar residues | ||||
Sequence: ELENGTSSSDEGEVL | ||||||
Compositional bias | 843-857 | Polar residues | ||||
Sequence: GSSSDYSSDYSDWTA | ||||||
Compositional bias | 875-914 | Basic and acidic residues | ||||
Sequence: KKPESSSDEEEESENQKQKHIKKERKKANEEKDGPTSPKK | ||||||
Sequence conflict | 1065 | in Ref. 4; BAE36779 and 5; AAG45146 | ||||
Sequence: P → R | ||||||
Sequence conflict | 1155 | in Ref. 5; AAG45146 | ||||
Sequence: E → D | ||||||
Compositional bias | 1282-1299 | Basic and acidic residues | ||||
Sequence: DSEEEEKDADVPGTSTRK | ||||||
Sequence conflict | 1392 | in Ref. 4; BAE36779 and 5; AAG45146 | ||||
Sequence: F → S | ||||||
Compositional bias | 1469-1507 | Polar residues | ||||
Sequence: LKSEVSTSPFSIPTRSVLPRHNAAQMNGKPESSSVVRTR | ||||||
Compositional bias | 1556-1573 | Polar residues | ||||
Sequence: STLSSPDPLTFSHATKNN | ||||||
Compositional bias | 1574-1589 | Basic and acidic residues | ||||
Sequence: SAKENMEKEKPVKRKM | ||||||
Compositional bias | 1759-1785 | Basic and acidic residues | ||||
Sequence: LKGSEPHMRTRNQGRRTAFYNEDDSEE | ||||||
Sequence conflict | 1776 | in Ref. 5; AAG45146 | ||||
Sequence: A → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ303103 EMBL· GenBank· DDBJ | CAC83119.1 EMBL· GenBank· DDBJ | mRNA | ||
AB049460 EMBL· GenBank· DDBJ | BAB16299.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC049950 EMBL· GenBank· DDBJ | AAH49950.1 EMBL· GenBank· DDBJ | mRNA | Different termination. | |
AK162189 EMBL· GenBank· DDBJ | BAE36779.1 EMBL· GenBank· DDBJ | mRNA | ||
AF310251 EMBL· GenBank· DDBJ | AAG45146.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |