Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1

Gene

Inpp5d

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

Functioni

Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6.19 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3,4-diphosphate + phosphate.3 Publications

Enzyme regulationi

Activated upon translocation to the sites of synthesis of PtdIns(3,4,5)P3 in the membrane.

GO - Molecular functioni

  • inositol-polyphosphate 5-phosphatase activity Source: MGI
  • phosphatidylinositol trisphosphate phosphatase activity Source: MGI
  • PTB domain binding Source: MGI
  • SH3 domain binding Source: MGI

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • determination of adult lifespan Source: MGI
  • immunoglobulin mediated immune response Source: MGI
  • intracellular signal transduction Source: MGI
  • negative regulation of B cell activation Source: MGI
  • negative regulation of B cell proliferation Source: MGI
  • negative regulation of bone resorption Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of granulocyte differentiation Source: MGI
  • negative regulation of immune response Source: MGI
  • negative regulation of interleukin-6 biosynthetic process Source: MGI
  • negative regulation of monocyte differentiation Source: MGI
  • negative regulation of neutrophil differentiation Source: MGI
  • negative regulation of osteoclast differentiation Source: MGI
  • negative regulation of signal transduction Source: MGI
  • phosphatidylinositol dephosphorylation Source: InterPro
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of B cell differentiation Source: MGI
  • positive regulation of erythrocyte differentiation Source: MGI
  • positive regulation of lymphocyte differentiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Apoptosis, Immunity

Enzyme and pathway databases

ReactomeiR-MMU-1660499. Synthesis of PIPs at the plasma membrane.
R-MMU-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-MMU-202424. Downstream TCR signaling.
R-MMU-912526. Interleukin receptor SHC signaling.

Chemistry databases

SwissLipidsiSLP:000000873.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC:3.1.3.86)
Alternative name(s):
Inositol polyphosphate-5-phosphatase of 145 kDa
Short name:
SIP-145
SH2 domain-containing inositol 5'-phosphatase 1
Short name:
SH2 domain-containing inositol phosphatase 1
Short name:
SHIP-1
p150Ship
Gene namesi
Name:Inpp5d
Synonyms:7a33, Ship, Ship1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:107357. Inpp5d.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cell membrane 1 Publication; Peripheral membrane protein 1 Publication
  • Membrane raft 1 Publication
  • Cytoplasmcytoskeleton 1 Publication

  • Note: Translocates to the plasma membrane when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type (PubMed:12393695). Translocates from the cytoplasm to membrane ruffles in a FCGR3/CD16-dependent manner (PubMed:12393695). Colocalizes with FC-gamma-RIIB receptor (FCGR2B) or FCGR3/CD16 at membrane ruffles (PubMed:12393695). Tyrosine phosphorylation may also participate in membrane localization (PubMed:12393695).1 Publication
Isoform 5 :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile. They however fail to thrive and only 40% survive by 14 weeks of age. Mortality is associated with extensive consolidation of the lungs resulting from infiltration by myeloid cells. Increased numbers of granulocyte-macrophage progenitors are observed in both the bone marrow and spleen. Absence of Inpp5d leads to steel factor-induced degranulation of mast cells. They also display increased numbers of osteoclast precursors leading to a severe osteoporosis.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi676D → G: Loss of function. 1 Publication1
Mutagenesisi918Y → F: Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-1021. 3 Publications1
Mutagenesisi1021Y → F: Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-918. 3 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003028671 – 1191Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1Add BLAST1191

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei246PhosphoserineCombined sources1
Modified residuei918Phosphotyrosine1 Publication1
Modified residuei935PhosphoserineCombined sources1
Modified residuei945PhosphotyrosineCombined sources1
Modified residuei964PhosphothreonineCombined sources1
Modified residuei967PhosphoserineCombined sources1
Modified residuei972PhosphoserineCombined sources1
Modified residuei1021Phosphotyrosine1 Publication1

Post-translational modificationi

Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as cytokines, growth factors, antibodies, chemokines, integrin ligands and hypertonic and oxidative stress. Phosphorylated upon IgG receptor FCGR2B-binding.7 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9ES52.
PeptideAtlasiQ9ES52.
PRIDEiQ9ES52.

PTM databases

iPTMnetiQ9ES52.
PhosphoSitePlusiQ9ES52.

Expressioni

Tissue specificityi

Specifically expressed in immune and hematopoietic cells. Levels vary considerably within this compartment. Lost during erythropoiesis when erythroid cells become Ter119+. Increases substantially with T-cell maturation and when resting B-cells are activated. Also present in mature granulocytes, monocyte/macrophages, mast cells and platelets. Isoform 5 is the only form expressed in embryonic stem (ES) cells and is coexpressed with other isoforms in hematopoietic stem cells, and disappears with differentiation.4 Publications

Developmental stagei

Expressed in late primitive-streak stage embryos (7.5 dpc), when hematopoiesis is thought to begin, and the expression is restricted to the hematopoietic lineage in embryo. In adults expression continues to be in the majority of cells from hematopoietic origin, including granulocytes, monocytes and lymphocytes, and is also found in the spermatids of the testis.2 Publications

Inductioni

By activin/TGF-beta (at protein level). Regulated by the Smad pathway. Isoform 3 is expressed during myeloid development.1 Publication

Gene expression databases

BgeeiENSMUSG00000026288.
CleanExiMM_INPP5D.
ExpressionAtlasiQ9ES52. baseline and differential.
GenevisibleiQ9ES52. MM.

Interactioni

Subunit structurei

Interacts with tyrosine phosphorylated forms of SHC1, DOK1, DOK3, PTPN11/SHP-2, SLAMF1/CD150. Interacts with PTPN11 in response to IL-3. Interacts with receptors EPOR, MS4A2/FCER1B and FCER1G, FCGR2A, FCGR2B and FCGR3. Interacts with GRB2 and PLCG1. Interacts with tyrosine kinases SRC and TEC. Interacts with FCGR2A, leading to regulate gene expression during the phagocytic process. Interacts with c-Met/MET. Interacts with MILR1 (tyrosine-phosphorylated). Isoform 5 interacts with IL6ST/gp130. Can weakly interact (via NPXY motif 2) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif.23 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PIK3R1P237272EBI-1452545,EBI-520244From a different organism.
Plcg2Q8CIH53EBI-300210,EBI-617954

GO - Molecular functioni

  • PTB domain binding Source: MGI
  • SH3 domain binding Source: MGI

Protein-protein interaction databases

BioGridi200769. 24 interactors.
IntActiQ9ES52. 11 interactors.
MINTiMINT-205819.
STRINGi10090.ENSMUSP00000127941.

Structurei

3D structure databases

ProteinModelPortaliQ9ES52.
SMRiQ9ES52.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 104SH2PROSITE-ProRule annotationAdd BLAST97

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1015 – 1029Interaction with DAB21 PublicationAdd BLAST15

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi127 – 132SH3-binding 16
Motifi915 – 918NPXY motif 14
Motifi970 – 975SH3-binding 26
Motifi1018 – 1021NPXY motif 24
Motifi1039 – 1050SH3-binding 3Add BLAST12

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi962 – 1153Pro-richAdd BLAST192

Domaini

The SH2 domain interacts with tyrosine phosphorylated forms of proteins such as SHC1 or PTPN11/SHP-2. It competes with that of GRB2 for binding to phosphorylated SHC1 to inhibit the Ras pathway. It is also required for tyrosine phosphorylation.1 Publication
The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain.1 Publication

Sequence similaritiesi

Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain, SH3-binding

Phylogenomic databases

eggNOGiKOG0565. Eukaryota.
COG5411. LUCA.
GeneTreeiENSGT00760000119075.
HOVERGENiHBG106726.
InParanoidiQ9ES52.
KOiK03084.
OMAiLTKPEMF.
OrthoDBiEOG091G00P6.
PhylomeDBiQ9ES52.
TreeFamiTF323475.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR000980. SH2.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00128. IPPc. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ES52-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPAMVPGWNH GNITRSKAEE LLSRAGKDGS FLVRASESIP RAYALCVLFR
60 70 80 90 100
NCVYTYRILP NEDDKFTVQA SEGVPMRFFT KLDQLIDFYK KENMGLVTHL
110 120 130 140 150
QYPVPLEEED AIDEAEEDTV ESVMSPPELP PRNIPMSAGP SEAKDLPLAT
160 170 180 190 200
ENPRAPEVTR LSLSETLFQR LQSMDTSGLP EEHLKAIQDY LSTQLLLDSD
210 220 230 240 250
FLKTGSSNLP HLKKLMSLLC KELHGEVIRT LPSLESLQRL FDQQLSPGLR
260 270 280 290 300
PRPQVPGEAS PITMVAKLSQ LTSLLSSIED KVKSLLHEGS ESTNRRSLIP
310 320 330 340 350
PVTFEVKSES LGIPQKMHLK VDVESGKLIV KKSKDGSEDK FYSHKKILQL
360 370 380 390 400
IKSQKFLNKL VILVETEKEK ILRKEYVFAD SKKREGFCQL LQQMKNKHSE
410 420 430 440 450
QPEPDMITIF IGTWNMGNAP PPKKITSWFL SKGQGKTRDD SADYIPHDIY
460 470 480 490 500
VIGTQEDPLG EKEWLELLRH SLQEVTSMTF KTVAIHTLWN IRIVVLAKPE
510 520 530 540 550
HENRISHICT DNVKTGIANT LGNKGAVGVS FMFNGTSLGF VNSHLTSGSE
560 570 580 590 600
KKLRRNQNYM NILRFLALGD KKLSPFNITH RFTHLFWLGD LNYRVELPTW
610 620 630 640 650
EAEAIIQKIK QQQYSDLLAH DQLLLERKDQ KVFLHFEEEE ITFAPTYRFE
660 670 680 690 700
RLTRDKYAYT KQKATGMKYN LPSWCDRVLW KSYPLVHVVC QSYGSTSDIM
710 720 730 740 750
TSDHSPVFAT FEAGVTSQFV SKNGPGTVDS QGQIEFLACY ATLKTKSQTK
760 770 780 790 800
FYLEFHSSCL ESFVKSQEGE NEEGSEGELV VRFGETLPKL KPIISDPEYL
810 820 830 840 850
LDQHILISIK SSDSDESYGE GCIALRLETT EAQHPIYTPL THHGEMTGHF
860 870 880 890 900
RGEIKLQTSQ GKMREKLYDF VKTERDESSG MKCLKNLTSH DPMRQWEPSG
910 920 930 940 950
RVPACGVSSL NEMINPNYIG MGPFGQPLHG KSTLSPDQQL TAWSYDQLPK
960 970 980 990 1000
DSSLGPGRGE GPPTPPSQPP LSPKKFSSST ANRGPCPRVQ EARPGDLGKV
1010 1020 1030 1040 1050
EALLQEDLLL TKPEMFENPL YGSVSSFPKL VPRKEQESPK MLRKEPPPCP
1060 1070 1080 1090 1100
DPGISSPSIV LPKAQEVESV KGTSKQAPVP VLGPTPRIRS FTCSSSAEGR
1110 1120 1130 1140 1150
MTSGDKSQGK PKASASSQAP VPVKRPVKPS RSEMSQQTTP IPAPRPPLPV
1160 1170 1180 1190
KSPAVLQLQH SKGRDYRDNT ELPHHGKHRQ EEGLLGRTAM Q
Length:1,191
Mass (Da):133,542
Last modified:September 11, 2007 - v2
Checksum:iAF9F21326A59EC7A
GO
Isoform 2 (identifier: Q9ES52-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     120-120: Missing.

Show »
Length:1,190
Mass (Da):133,443
Checksum:iDF81F3046F33A07F
GO
Isoform 3 (identifier: Q9ES52-3) [UniParc]FASTAAdd to basket
Also known as: 135 kDa SHIP

The sequence of this isoform differs from the canonical sequence as follows:
     920-980: Missing.

Show »
Length:1,130
Mass (Da):127,199
Checksum:iC3E2F1EB206034BF
GO
Isoform 4 (identifier: Q9ES52-4) [UniParc]FASTAAdd to basket
Also known as: SHIPdelta

The sequence of this isoform differs from the canonical sequence as follows:
     120-120: Missing.
     920-960: GMGPFGQPLH...DSSLGPGRGE → VFIFHSQPRS...GPAADEARDV
     961-1191: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:959
Mass (Da):108,345
Checksum:iB95D49476957345E
GO
Isoform 5 (identifier: Q9ES52-5) [UniParc]FASTAAdd to basket
Also known as: s-SHIP

The sequence of this isoform differs from the canonical sequence as follows:
     1-263: Missing.

Show »
Length:928
Mass (Da):104,101
Checksum:i7390D08E57505B82
GO
Isoform 6 (identifier: Q9ES52-6) [UniParc]FASTAAdd to basket
Also known as: s-SHIPD183

The sequence of this isoform differs from the canonical sequence as follows:
     1-263: Missing.
     920-980: Missing.

Show »
Length:867
Mass (Da):97,758
Checksum:iF848515DE853AD65
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti43Y → C in AAB18937 (PubMed:8643691).Curated1
Sequence conflicti527V → A in AAC53023 (PubMed:9027494).Curated1
Sequence conflicti534N → I in AAC53023 (PubMed:9027494).Curated1
Sequence conflicti905C → E AA sequence (PubMed:8643691).Curated1
Sequence conflicti981A → T in AAB18937 (PubMed:8643691).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0279801 – 263Missing in isoform 5 and isoform 6. 1 PublicationAdd BLAST263
Alternative sequenceiVSP_027981120Missing in isoform 2 and isoform 4. 4 Publications1
Alternative sequenceiVSP_027982920 – 980Missing in isoform 3 and isoform 6. 1 PublicationAdd BLAST61
Alternative sequenceiVSP_027983920 – 960GMGPF…PGRGE → VFIFHSQPRSLPQGARGKTW GSGKGGSSAPGGPAADEARD V in isoform 4. 1 PublicationAdd BLAST41
Alternative sequenceiVSP_027984961 – 1191Missing in isoform 4. 1 PublicationAdd BLAST231

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51742 mRNA. Translation: AAC52606.1.
U39203 mRNA. Translation: AAB18937.1.
U52044 mRNA. Translation: AAC53023.1.
AF125996 mRNA. Translation: AAD37118.1.
AF235502
, AF235496, AF235498, AF235499, AF235500, AF235501 Genomic DNA. Translation: AAG23922.1.
AF228679 mRNA. Translation: AAF69143.1.
AF184912 mRNA. Translation: AAF25823.1.
AF184913 mRNA. Translation: AAF25824.1.
AK143560 mRNA. Translation: BAE25436.1.
BC108328 mRNA. Translation: AAI08329.1.
CCDSiCCDS35655.1. [Q9ES52-1]
CCDS48310.1. [Q9ES52-3]
CCDS48311.1. [Q9ES52-2]
PIRiJC6118.
RefSeqiNP_001103662.1. NM_001110192.2. [Q9ES52-2]
NP_001103663.1. NM_001110193.2. [Q9ES52-3]
NP_034696.2. NM_010566.3. [Q9ES52-1]
UniGeneiMm.15105.

Genome annotation databases

EnsembliENSMUST00000042275; ENSMUSP00000044647; ENSMUSG00000026288. [Q9ES52-2]
ENSMUST00000072999; ENSMUSP00000072763; ENSMUSG00000026288. [Q9ES52-4]
ENSMUST00000167032; ENSMUSP00000126569; ENSMUSG00000026288. [Q9ES52-5]
ENSMUST00000168783; ENSMUSP00000131244; ENSMUSG00000026288. [Q9ES52-3]
ENSMUST00000169754; ENSMUSP00000127941; ENSMUSG00000026288. [Q9ES52-1]
ENSMUST00000170300; ENSMUSP00000132384; ENSMUSG00000026288. [Q9ES52-6]
GeneIDi16331.
KEGGimmu:16331.
UCSCiuc007bxc.3. mouse. [Q9ES52-1]
uc007bxd.3. mouse. [Q9ES52-3]
uc007bxf.3. mouse. [Q9ES52-2]
uc007bxg.3. mouse. [Q9ES52-6]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51742 mRNA. Translation: AAC52606.1.
U39203 mRNA. Translation: AAB18937.1.
U52044 mRNA. Translation: AAC53023.1.
AF125996 mRNA. Translation: AAD37118.1.
AF235502
, AF235496, AF235498, AF235499, AF235500, AF235501 Genomic DNA. Translation: AAG23922.1.
AF228679 mRNA. Translation: AAF69143.1.
AF184912 mRNA. Translation: AAF25823.1.
AF184913 mRNA. Translation: AAF25824.1.
AK143560 mRNA. Translation: BAE25436.1.
BC108328 mRNA. Translation: AAI08329.1.
CCDSiCCDS35655.1. [Q9ES52-1]
CCDS48310.1. [Q9ES52-3]
CCDS48311.1. [Q9ES52-2]
PIRiJC6118.
RefSeqiNP_001103662.1. NM_001110192.2. [Q9ES52-2]
NP_001103663.1. NM_001110193.2. [Q9ES52-3]
NP_034696.2. NM_010566.3. [Q9ES52-1]
UniGeneiMm.15105.

3D structure databases

ProteinModelPortaliQ9ES52.
SMRiQ9ES52.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200769. 24 interactors.
IntActiQ9ES52. 11 interactors.
MINTiMINT-205819.
STRINGi10090.ENSMUSP00000127941.

Chemistry databases

SwissLipidsiSLP:000000873.

PTM databases

iPTMnetiQ9ES52.
PhosphoSitePlusiQ9ES52.

Proteomic databases

PaxDbiQ9ES52.
PeptideAtlasiQ9ES52.
PRIDEiQ9ES52.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042275; ENSMUSP00000044647; ENSMUSG00000026288. [Q9ES52-2]
ENSMUST00000072999; ENSMUSP00000072763; ENSMUSG00000026288. [Q9ES52-4]
ENSMUST00000167032; ENSMUSP00000126569; ENSMUSG00000026288. [Q9ES52-5]
ENSMUST00000168783; ENSMUSP00000131244; ENSMUSG00000026288. [Q9ES52-3]
ENSMUST00000169754; ENSMUSP00000127941; ENSMUSG00000026288. [Q9ES52-1]
ENSMUST00000170300; ENSMUSP00000132384; ENSMUSG00000026288. [Q9ES52-6]
GeneIDi16331.
KEGGimmu:16331.
UCSCiuc007bxc.3. mouse. [Q9ES52-1]
uc007bxd.3. mouse. [Q9ES52-3]
uc007bxf.3. mouse. [Q9ES52-2]
uc007bxg.3. mouse. [Q9ES52-6]

Organism-specific databases

CTDi3635.
MGIiMGI:107357. Inpp5d.

Phylogenomic databases

eggNOGiKOG0565. Eukaryota.
COG5411. LUCA.
GeneTreeiENSGT00760000119075.
HOVERGENiHBG106726.
InParanoidiQ9ES52.
KOiK03084.
OMAiLTKPEMF.
OrthoDBiEOG091G00P6.
PhylomeDBiQ9ES52.
TreeFamiTF323475.

Enzyme and pathway databases

ReactomeiR-MMU-1660499. Synthesis of PIPs at the plasma membrane.
R-MMU-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-MMU-202424. Downstream TCR signaling.
R-MMU-912526. Interleukin receptor SHC signaling.

Miscellaneous databases

PROiQ9ES52.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026288.
CleanExiMM_INPP5D.
ExpressionAtlasiQ9ES52. baseline and differential.
GenevisibleiQ9ES52. MM.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR000980. SH2.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00128. IPPc. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSHIP1_MOUSE
AccessioniPrimary (citable) accession number: Q9ES52
Secondary accession number(s): Q3UPF9
, Q4U212, Q61034, Q61173, Q61181, Q9JKR7, Q9JLF9, Q9JLG0, Q9QVN8, Q9WUC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: November 2, 2016
This is version 136 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.