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Q92835

- SHIP1_HUMAN

UniProt

Q92835 - SHIP1_HUMAN

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Protein

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

Gene

INPP5D

Organism
Homo sapiens (Human)
Status
Reviewed - 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 InsP6.2 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3,4-diphosphate + phosphate.2 Publications

Enzyme regulationi

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

GO - Molecular functioni

  1. inositol-polyphosphate 5-phosphatase activity Source: ProtInc
  2. phosphatidylinositol trisphosphate phosphatase activity Source: Ensembl

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. blood coagulation Source: Reactome
  3. determination of adult lifespan Source: Ensembl
  4. immunoglobulin mediated immune response Source: Ensembl
  5. inositol phosphate metabolic process Source: Reactome
  6. intracellular signal transduction Source: Ensembl
  7. leukocyte migration Source: Reactome
  8. negative regulation of B cell proliferation Source: Ensembl
  9. negative regulation of bone resorption Source: Ensembl
  10. negative regulation of immune response Source: Ensembl
  11. negative regulation of interleukin-6 biosynthetic process Source: Ensembl
  12. negative regulation of monocyte differentiation Source: Ensembl
  13. negative regulation of neutrophil differentiation Source: Ensembl
  14. negative regulation of osteoclast differentiation Source: Ensembl
  15. negative regulation of signal transduction Source: Ensembl
  16. phosphate-containing compound metabolic process Source: ProtInc
  17. phosphatidylinositol biosynthetic process Source: Reactome
  18. phosphatidylinositol dephosphorylation Source: InterPro
  19. phospholipid metabolic process Source: Reactome
  20. positive regulation of apoptotic process Source: Ensembl
  21. positive regulation of B cell differentiation Source: Ensembl
  22. positive regulation of erythrocyte differentiation Source: Ensembl
  23. signal transduction Source: ProtInc
  24. small molecule metabolic process Source: Reactome
  25. T cell receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Apoptosis, Immunity

Enzyme and pathway databases

BioCyciMetaCyc:HS09849-MONOMER.
ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_12519. PECAM1 interactions.
REACT_12555. Downstream TCR signaling.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_23891. Interleukin receptor SHC signaling.
SignaLinkiQ92835.

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
Short name:
hp51CN
Gene namesi
Name:INPP5D
Synonyms:SHIP, SHIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6079. INPP5D.

Subcellular locationi

Cytoplasm 1 Publication. Membrane 1 Publication; Peripheral membrane protein 1 Publication
Note: Translocates to the plasma membrane when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. Partly translocated via its SH2 domain which mediates interaction with tyrosine phosphorylated receptors such as the FC-gamma-RIIB receptor (FCGR2B) or CD16/FCGR3. Tyrosine phosphorylation may also participate in membrane localization By similarity.By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29887.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11891189Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1PRO_0000302866Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei915 – 9151Phosphotyrosine1 Publication
Modified residuei934 – 9341PhosphoserineBy similarity
Modified residuei944 – 9441PhosphotyrosineBy similarity
Modified residuei1022 – 10221PhosphotyrosineBy similarity

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.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92835.
PaxDbiQ92835.
PRIDEiQ92835.

PTM databases

PhosphoSiteiQ92835.

Expressioni

Tissue specificityi

Specifically expressed in immune and hematopoietic cells. Expressed in bone marrow and blood cells. Levels vary considerably within this compartment. Present in at least 74% of immature CD34+ cells, whereas within the more mature population of CD33+ cells, it is present in only 10% of cells. Present in the majority of T-cells, while it is present in a minority of B-cells (at protein level).4 Publications

Gene expression databases

BgeeiQ92835.
CleanExiHS_INPP5D.
ExpressionAtlasiQ92835. baseline and differential.
GenevestigatoriQ92835.

Organism-specific databases

HPAiCAB016300.

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 By similarity. Interacts with MILR1 (tyrosine-phosphorylated). Can weakly interact (via NPXY motif 2) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif By similarity.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
FCGR2BP319942EBI-1380477,EBI-724784
SH3KBP1Q96B976EBI-1380477,EBI-346595

Protein-protein interaction databases

BioGridi109847. 33 interactions.
IntActiQ92835. 16 interactions.
MINTiMINT-123561.
STRINGi9606.ENSP00000352575.

Structurei

Secondary structure

1
1189
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96
Helixi12 – 2211
Beta strandi27 – 326
Beta strandi39 – 457
Beta strandi50 – 578
Beta strandi63 – 653
Beta strandi70 – 723
Beta strandi76 – 783
Helixi79 – 857
Beta strandi88 – 958

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YSXNMR-A1-112[»]
ProteinModelPortaliQ92835.
SMRiQ92835. Positions 1-112, 402-714.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92835.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 10197SH2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1016 – 103015Interaction with DAB2By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi124 – 1296SH3-binding 1
Motifi912 – 9154NPXY motif 1
Motifi969 – 9746SH3-binding 2
Motifi1019 – 10224NPXY motif 2
Motifi1040 – 105112SH3-binding 3Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi920 – 1148229Pro-richAdd
BLAST

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 By similarity.By similarity
The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain.By similarity

Sequence similaritiesi

Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain, SH3-binding

Phylogenomic databases

eggNOGiCOG5411.
GeneTreeiENSGT00760000119075.
HOVERGENiHBG106726.
InParanoidiQ92835.
KOiK03084.
OrthoDBiEOG75F4CD.
PhylomeDBiQ92835.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92835-1) [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
MVPCWNHGNI TRSKAEELLS RTGKDGSFLV RASESISRAY ALCVLYRNCV
60 70 80 90 100
YTYRILPNED DKFTVQASEG VSMRFFTKLD QLIEFYKKEN MGLVTHLQYP
110 120 130 140 150
VPLEEEDTGD DPEEDTVESV VSPPELPPRN IPLTASSCEA KEVPFSNENP
160 170 180 190 200
RATETSRPSL SETLFQRLQS MDTSGLPEEH LKAIQDYLST QLAQDSEFVK
210 220 230 240 250
TGSSSLPHLK KLTTLLCKEL YGEVIRTLPS LESLQRLFDQ QLSPGLRPRP
260 270 280 290 300
QVPGEANPIN MVSKLSQLTS LLSSIEDKVK ALLHEGPESP HRPSLIPPVT
310 320 330 340 350
FEVKAESLGI PQKMQLKVDV ESGKLIIKKS KDGSEDKFYS HKKILQLIKS
360 370 380 390 400
QKFLNKLVIL VETEKEKILR KEYVFADSKK REGFCQLLQQ MKNKHSEQPE
410 420 430 440 450
PDMITIFIGT WNMGNAPPPK KITSWFLSKG QGKTRDDSAD YIPHDIYVIG
460 470 480 490 500
TQEDPLSEKE WLEILKHSLQ EITSVTFKTV AIHTLWNIRI VVLAKPEHEN
510 520 530 540 550
RISHICTDNV KTGIANTLGN KGAVGVSFMF NGTSLGFVNS HLTSGSEKKL
560 570 580 590 600
RRNQNYMNIL RFLALGDKKL SPFNITHRFT HLFWFGDLNY RVDLPTWEAE
610 620 630 640 650
TIIQKIKQQQ YADLLSHDQL LTERREQKVF LHFEEEEITF APTYRFERLT
660 670 680 690 700
RDKYAYTKQK ATGMKYNLPS WCDRVLWKSY PLVHVVCQSY GSTSDIMTSD
710 720 730 740 750
HSPVFATFEA GVTSQFVSKN GPGTVDSQGQ IEFLRCYATL KTKSQTKFYL
760 770 780 790 800
EFHSSCLESF VKSQEGENEE GSEGELVVKF GETLPKLKPI ISDPEYLLDQ
810 820 830 840 850
HILISIKSSD SDESYGEGCI ALRLEATETQ LPIYTPLTHH GELTGHFQGE
860 870 880 890 900
IKLQTSQGKT REKLYDFVKT ERDESSGPKT LKSLTSHDPM KQWEVTSRAP
910 920 930 940 950
PCSGSSITEI INPNYMGVGP FGPPMPLHVK QTLSPDQQPT AWSYDQPPKD
960 970 980 990 1000
SPLGPCRGES PPTPPGQPPI SPKKFLPSTA NRGLPPRTQE SRPSDLGKNA
1010 1020 1030 1040 1050
GDTLPQEDLP LTKPEMFENP LYGSLSSFPK PAPRKDQESP KMPRKEPPPC
1060 1070 1080 1090 1100
PEPGILSPSI VLTKAQEADR GEGPGKQVPA PRLRSFTCSS SAEGRAAGGD
1110 1120 1130 1140 1150
KSQGKPKTPV SSQAPVPAKR PIKPSRSEIN QQTPPTPTPR PPLPVKSPAV
1160 1170 1180
LHLQHSKGRD YRDNTELPHH GKHRPEEGPP GPLGRTAMQ
Length:1,189
Mass (Da):133,292
Last modified:September 11, 2007 - v2
Checksum:i7958E91A64A4B68B
GO
Isoform 2 (identifier: Q92835-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     117-117: Missing.

Show »
Length:1,188
Mass (Da):133,193
Checksum:i335673E161C5FFAD
GO
Isoform 3 (identifier: Q92835-3) [UniParc]FASTAAdd to Basket

Also known as: SIP-110

The sequence of this isoform differs from the canonical sequence as follows:
     1-212: Missing.
     213-222: TTLLCKELYG → MFTLSPAPR

Show »
Length:976
Mass (Da):109,294
Checksum:i2B90E6DD584DD048
GO

Sequence cautioni

The sequence AAC50454.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 262DG → GT in AAB49680. (PubMed:9058707)Curated
Sequence conflicti1029 – 10291P → H in AAB49680. (PubMed:9058707)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti685 – 6851V → E in one patient with acute myeloid leukemya; somatic mutation. 1 Publication
VAR_034979
Natural varianti1169 – 11691H → Y.2 Publications
Corresponds to variant rs9247 [ dbSNP | Ensembl ].
VAR_059358

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 212212Missing in isoform 3. 1 PublicationVSP_027977Add
BLAST
Alternative sequencei117 – 1171Missing in isoform 2. 3 PublicationsVSP_027978
Alternative sequencei213 – 22210TTLLCKELYG → MFTLSPAPR in isoform 3. 1 PublicationVSP_027979

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98429 mRNA. Translation: CAA67071.1.
U57650 mRNA. Translation: AAB53573.1.
U50040 mRNA. Translation: AAC50453.1.
U50041 mRNA. Translation: AAC50454.1. Different initiation.
U84400 mRNA. Translation: AAB49680.1.
U53470 mRNA. Translation: AAD00081.1.
BC062985 mRNA. Translation: AAH62985.1.
BC099920 mRNA. Translation: AAH99920.1.
BC113580 mRNA. Translation: AAI13581.1.
BC113582 mRNA. Translation: AAI13583.1.
CCDSiCCDS74672.1. [Q92835-1]
PIRiJC4889.
RefSeqiNP_001017915.1. NM_001017915.2. [Q92835-1]
NP_005532.2. NM_005541.4. [Q92835-2]
UniGeneiHs.262886.
Hs.601911.

Genome annotation databases

EnsembliENST00000359570; ENSP00000352575; ENSG00000168918. [Q92835-1]
GeneIDi3635.
KEGGihsa:3635.
UCSCiuc010zmo.2. human. [Q92835-1]
uc010zmp.2. human. [Q92835-2]

Polymorphism databases

DMDMi158564077.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98429 mRNA. Translation: CAA67071.1 .
U57650 mRNA. Translation: AAB53573.1 .
U50040 mRNA. Translation: AAC50453.1 .
U50041 mRNA. Translation: AAC50454.1 . Different initiation.
U84400 mRNA. Translation: AAB49680.1 .
U53470 mRNA. Translation: AAD00081.1 .
BC062985 mRNA. Translation: AAH62985.1 .
BC099920 mRNA. Translation: AAH99920.1 .
BC113580 mRNA. Translation: AAI13581.1 .
BC113582 mRNA. Translation: AAI13583.1 .
CCDSi CCDS74672.1. [Q92835-1 ]
PIRi JC4889.
RefSeqi NP_001017915.1. NM_001017915.2. [Q92835-1 ]
NP_005532.2. NM_005541.4. [Q92835-2 ]
UniGenei Hs.262886.
Hs.601911.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YSX NMR - A 1-112 [» ]
ProteinModelPortali Q92835.
SMRi Q92835. Positions 1-112, 402-714.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109847. 33 interactions.
IntActi Q92835. 16 interactions.
MINTi MINT-123561.
STRINGi 9606.ENSP00000352575.

Chemistry

ChEMBLi CHEMBL1781870.

PTM databases

PhosphoSitei Q92835.

Polymorphism databases

DMDMi 158564077.

Proteomic databases

MaxQBi Q92835.
PaxDbi Q92835.
PRIDEi Q92835.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359570 ; ENSP00000352575 ; ENSG00000168918 . [Q92835-1 ]
GeneIDi 3635.
KEGGi hsa:3635.
UCSCi uc010zmo.2. human. [Q92835-1 ]
uc010zmp.2. human. [Q92835-2 ]

Organism-specific databases

CTDi 3635.
GeneCardsi GC02P233924.
H-InvDB HIX0057065.
HGNCi HGNC:6079. INPP5D.
HPAi CAB016300.
MIMi 601582. gene.
neXtProti NX_Q92835.
PharmGKBi PA29887.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5411.
GeneTreei ENSGT00760000119075.
HOVERGENi HBG106726.
InParanoidi Q92835.
KOi K03084.
OrthoDBi EOG75F4CD.
PhylomeDBi Q92835.
TreeFami TF323475.

Enzyme and pathway databases

BioCyci MetaCyc:HS09849-MONOMER.
Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_12519. PECAM1 interactions.
REACT_12555. Downstream TCR signaling.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_23891. Interleukin receptor SHC signaling.
SignaLinki Q92835.

Miscellaneous databases

ChiTaRSi INPP5D. human.
EvolutionaryTracei Q92835.
GeneWikii INPP5D.
GenomeRNAii 3635.
NextBioi 14225.
PROi Q92835.
SOURCEi Search...

Gene expression databases

Bgeei Q92835.
CleanExi HS_INPP5D.
ExpressionAtlasi Q92835. baseline and differential.
Genevestigatori Q92835.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
3.60.10.10. 1 hit.
InterProi IPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR000980. SH2.
[Graphical view ]
Pfami PF03372. Exo_endo_phos. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
SMARTi SM00128. IPPc. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEi PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase."
    Drayer A.L., Pesesse X., De Smedt F., Woscholski R., Parker P., Erneux C.
    Biochem. Biophys. Res. Commun. 225:243-249(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ENZYME ACTIVITY, TISSUE SPECIFICITY, VARIANT TYR-1169.
  2. "Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation."
    Ware M.D., Rosten P., Damen J.E., Liu L., Humphries R.K., Krystal G.
    Blood 88:2833-2840(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, INTERACTION WITH SHC1.
  3. "Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2."
    Kavanaugh W.M., Pot D.A., Chin S.M., Deuter-Reinhard M., Jefferson A.B., Norris F.A., Masiarz F.R., Cousens L.S., Majerus P.W., Williams L.T.
    Curr. Biol. 6:438-445(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-1139 (ISOFORM 1), ENZYME ACTIVITY, INTERACTION WITH GRB2.
    Tissue: Lung.
  4. "The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood."
    Geier S.J., Algate P.A., Carlberg K., Flowers D., Friedman C., Trask B., Rohrschneider L.R.
    Blood 89:1876-1885(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  5. "Purification and molecular cloning of SH2- and SH3-containing inositol polyphosphate-5-phosphatase, which is involved in the signaling pathway of granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-Abl."
    Odai H., Sasaki K., Iwamatsu A., Nakamoto T., Ueno H., Yamagata T., Mitani K., Yazaki Y., Hirai H.
    Blood 89:2745-2756(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH GRB2.
  6. "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] (ISOFORM 2), VARIANT TYR-1169.
    Tissue: B-cell and Lymph.
  7. "CDw150 associates with src-homology 2-containing inositol phosphatase and modulates CD95-mediated apoptosis."
    Mikhalap S.V., Shlapatska L.M., Berdova A.G., Law C.L., Clark E.A., Sidorenko S.P.
    J. Immunol. 162:5719-5727(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLAMF1.
  8. "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells."
    Dunant N.M., Wisniewski D., Strife A., Clarkson B., Resh M.D.
    Cell. Signal. 12:317-326(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH DOK1.
  9. "Evidence that SHIP-1 contributes to phosphatidylinositol 3,4,5-trisphosphate metabolism in T lymphocytes and can regulate novel phosphoinositide 3-kinase effectors."
    Freeburn R.W., Wright K.L., Burgess S.J., Astoul E., Cantrell D.A., Ward S.G.
    J. Immunol. 169:5441-5450(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-915, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "The Src homology 2-containing inositol 5-phosphatase 1 (SHIP1) is involved in CD32a signaling in human neutrophils."
    Vaillancourt M., Levasseur S., Tremblay M.-L., Marois L., Rollet-Labelle E., Naccache P.H.
    Cell. Signal. 18:2022-2032(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Solution structure of the human SHIP SH2 domain."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-112.
  14. "Possible dominant-negative mutation of the SHIP gene in acute myeloid leukemia."
    Luo J.-M., Yoshida H., Komura S., Ohishi N., Pan L., Shigeno K., Hanamura I., Miura K., Iida S., Ueda R., Naoe T., Akao Y., Ohno R., Ohnishi K.
    Leukemia 17:1-8(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GLU-685.

Entry informationi

Entry nameiSHIP1_HUMAN
AccessioniPrimary (citable) accession number: Q92835
Secondary accession number(s): O00145
, Q13544, Q13545, Q6P5A4, Q92656, Q9UE80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: October 29, 2014
This is version 115 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 2
    Human chromosome 2: 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

External Data

Dasty 3