Q92835 (SHIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	INPP5D
Synonyms:	SHIP, SHIP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1189 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.9 Ref.11
Catalytic activity	1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3,4-diphosphate + phosphate. Ref.1 Ref.3
Enzyme regulation	Activated upon translocation to the sites of synthesis of PtdIns(3,4,5)P3 in the membrane By similarity.
Subunit structure	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. Ref.2 Ref.3 Ref.5 Ref.7 Ref.8
Subcellular location	Cytoplasm. Membrane; Peripheral membrane protein. 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. Ref.8
Tissue specificity	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). Ref.1 Ref.2 Ref.4 Ref.5
Domain	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. The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain By similarity.
Post-translational modification	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. Ref.5 Ref.8
Sequence similarities	Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family. Contains 1 SH2 domain.
Sequence caution	The sequence AAC50454.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Apoptosis Immunity
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat SH2 domain SH3-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell receptor signaling pathway Traceable author statement. Source: Reactome apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW blood coagulation Traceable author statement. Source: Reactome determination of adult lifespan Inferred from electronic annotation. Source: Compara immunoglobulin mediated immune response Inferred from electronic annotation. Source: Compara intracellular signal transduction Inferred from electronic annotation. Source: Compara leukocyte migration Traceable author statement. Source: Reactome negative regulation of B cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of bone resorption Inferred from electronic annotation. Source: Compara negative regulation of immune response Inferred from electronic annotation. Source: Compara negative regulation of interleukin-6 biosynthetic process Inferred from electronic annotation. Source: Compara negative regulation of monocyte differentiation Inferred from electronic annotation. Source: Compara negative regulation of neutrophil differentiation Inferred from electronic annotation. Source: Compara negative regulation of osteoclast differentiation Inferred from electronic annotation. Source: Compara negative regulation of signal transduction Inferred from electronic annotation. Source: Compara phosphatidylinositol biosynthetic process Traceable author statement. Source: Reactome phosphatidylinositol phosphorylation Inferred from electronic annotation. Source: InterPro positive regulation of B cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of erythrocyte differentiation Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	inositol-polyphosphate 5-phosphatase activity Traceable author statement Ref.1. Source: ProtInc phosphatidylinositol trisphosphate phosphatase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92835-1)

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.

Isoform 2 (identifier: Q92835-2)

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

Isoform 3 (identifier: Q92835-3)

Also known as: SIP-110;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1189

1189

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

PRO_0000302866

Regions

Domain

5 – 101

97

SH2

Region

1016 – 1030

15

Interaction with DAB2 By similarity

Motif

124 – 129

6

SH3-binding 1

Motif

912 – 915

4

NPXY motif 1

Motif

969 – 974

6

SH3-binding 2

Motif

1019 – 1022

4

NPXY motif 2

Motif

1040 – 1051

12

SH3-binding 3

Compositional bias

920 – 1148

229

Pro-rich

Amino acid modifications

Modified residue

865

1

Phosphotyrosine By similarity

Modified residue

915

1

Phosphotyrosine Ref.10

Modified residue

934

1

Phosphoserine By similarity

Modified residue

944

1

Phosphotyrosine By similarity

Modified residue

971

1

Phosphoserine By similarity

Modified residue

1022

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

1 – 212

212

Missing in isoform 3.

VSP_027977

Alternative sequence

117

1

Missing in isoform 2.

VSP_027978

Alternative sequence

213 – 222

10

TTLLCKELYG → MFTLSPAPR in isoform 3.

VSP_027979

Natural variant

685

1

V → E in one patient with acute myeloid leukemya; somatic mutation. Ref.14

VAR_034979

Natural variant

1169

1

H → Y. Ref.1 Ref.6
Corresponds to variant rs9247 [ dbSNP | Ensembl ].

VAR_059358

Experimental info

Sequence conflict

25 – 26

2

DG → GT in AAB49680. Ref.4

Sequence conflict

1029

1

P → H in AAB49680. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1189

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Helix

12 – 22

11

Beta strand

27 – 32

6

Beta strand

39 – 45

7

Beta strand

50 – 57

8

Beta strand

63 – 65

3

Beta strand

70 – 72

3

Beta strand

76 – 78

3

Helix

79 – 85

7

Beta strand

88 – 95

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: 7958E91A64A4B68B	FASTA	1,189	133,292
	10 20 30 40 50 60 MVPCWNHGNI TRSKAEELLS RTGKDGSFLV RASESISRAY ALCVLYRNCV YTYRILPNED 70 80 90 100 110 120 DKFTVQASEG VSMRFFTKLD QLIEFYKKEN MGLVTHLQYP VPLEEEDTGD DPEEDTVESV 130 140 150 160 170 180 VSPPELPPRN IPLTASSCEA KEVPFSNENP RATETSRPSL SETLFQRLQS MDTSGLPEEH 190 200 210 220 230 240 LKAIQDYLST QLAQDSEFVK TGSSSLPHLK KLTTLLCKEL YGEVIRTLPS LESLQRLFDQ 250 260 270 280 290 300 QLSPGLRPRP QVPGEANPIN MVSKLSQLTS LLSSIEDKVK ALLHEGPESP HRPSLIPPVT 310 320 330 340 350 360 FEVKAESLGI PQKMQLKVDV ESGKLIIKKS KDGSEDKFYS HKKILQLIKS QKFLNKLVIL 370 380 390 400 410 420 VETEKEKILR KEYVFADSKK REGFCQLLQQ MKNKHSEQPE PDMITIFIGT WNMGNAPPPK 430 440 450 460 470 480 KITSWFLSKG QGKTRDDSAD YIPHDIYVIG TQEDPLSEKE WLEILKHSLQ EITSVTFKTV 490 500 510 520 530 540 AIHTLWNIRI VVLAKPEHEN RISHICTDNV KTGIANTLGN KGAVGVSFMF NGTSLGFVNS 550 560 570 580 590 600 HLTSGSEKKL RRNQNYMNIL RFLALGDKKL SPFNITHRFT HLFWFGDLNY RVDLPTWEAE 610 620 630 640 650 660 TIIQKIKQQQ YADLLSHDQL LTERREQKVF LHFEEEEITF APTYRFERLT RDKYAYTKQK 670 680 690 700 710 720 ATGMKYNLPS WCDRVLWKSY PLVHVVCQSY GSTSDIMTSD HSPVFATFEA GVTSQFVSKN 730 740 750 760 770 780 GPGTVDSQGQ IEFLRCYATL KTKSQTKFYL EFHSSCLESF VKSQEGENEE GSEGELVVKF 790 800 810 820 830 840 GETLPKLKPI ISDPEYLLDQ HILISIKSSD SDESYGEGCI ALRLEATETQ LPIYTPLTHH 850 860 870 880 890 900 GELTGHFQGE IKLQTSQGKT REKLYDFVKT ERDESSGPKT LKSLTSHDPM KQWEVTSRAP 910 920 930 940 950 960 PCSGSSITEI INPNYMGVGP FGPPMPLHVK QTLSPDQQPT AWSYDQPPKD SPLGPCRGES 970 980 990 1000 1010 1020 PPTPPGQPPI SPKKFLPSTA NRGLPPRTQE SRPSDLGKNA GDTLPQEDLP LTKPEMFENP 1030 1040 1050 1060 1070 1080 LYGSLSSFPK PAPRKDQESP KMPRKEPPPC PEPGILSPSI VLTKAQEADR GEGPGKQVPA 1090 1100 1110 1120 1130 1140 PRLRSFTCSS SAEGRAAGGD KSQGKPKTPV SSQAPVPAKR PIKPSRSEIN QQTPPTPTPR 1150 1160 1170 1180 PPLPVKSPAV LHLQHSKGRD YRDNTELPHH GKHRPEEGPP GPLGRTAMQ
	Isoform 2 [UniParc]. Checksum: 335673E161C5FFAD	FASTA	1,188	133,193
	10 20 30 40 50 60 MVPCWNHGNI TRSKAEELLS RTGKDGSFLV RASESISRAY ALCVLYRNCV YTYRILPNED 70 80 90 100 110 120 DKFTVQASEG VSMRFFTKLD QLIEFYKKEN MGLVTHLQYP VPLEEEDTGD DPEEDTESVV 130 140 150 160 170 180 SPPELPPRNI PLTASSCEAK EVPFSNENPR ATETSRPSLS ETLFQRLQSM DTSGLPEEHL 190 200 210 220 230 240 KAIQDYLSTQ LAQDSEFVKT GSSSLPHLKK LTTLLCKELY GEVIRTLPSL ESLQRLFDQQ 250 260 270 280 290 300 LSPGLRPRPQ VPGEANPINM VSKLSQLTSL LSSIEDKVKA LLHEGPESPH RPSLIPPVTF 310 320 330 340 350 360 EVKAESLGIP QKMQLKVDVE SGKLIIKKSK DGSEDKFYSH KKILQLIKSQ KFLNKLVILV 370 380 390 400 410 420 ETEKEKILRK EYVFADSKKR EGFCQLLQQM KNKHSEQPEP DMITIFIGTW NMGNAPPPKK 430 440 450 460 470 480 ITSWFLSKGQ GKTRDDSADY IPHDIYVIGT QEDPLSEKEW LEILKHSLQE ITSVTFKTVA 490 500 510 520 530 540 IHTLWNIRIV VLAKPEHENR ISHICTDNVK TGIANTLGNK GAVGVSFMFN GTSLGFVNSH 550 560 570 580 590 600 LTSGSEKKLR RNQNYMNILR FLALGDKKLS PFNITHRFTH LFWFGDLNYR VDLPTWEAET 610 620 630 640 650 660 IIQKIKQQQY ADLLSHDQLL TERREQKVFL HFEEEEITFA PTYRFERLTR DKYAYTKQKA 670 680 690 700 710 720 TGMKYNLPSW CDRVLWKSYP LVHVVCQSYG STSDIMTSDH SPVFATFEAG VTSQFVSKNG 730 740 750 760 770 780 PGTVDSQGQI EFLRCYATLK TKSQTKFYLE FHSSCLESFV KSQEGENEEG SEGELVVKFG 790 800 810 820 830 840 ETLPKLKPII SDPEYLLDQH ILISIKSSDS DESYGEGCIA LRLEATETQL PIYTPLTHHG 850 860 870 880 890 900 ELTGHFQGEI KLQTSQGKTR EKLYDFVKTE RDESSGPKTL KSLTSHDPMK QWEVTSRAPP 910 920 930 940 950 960 CSGSSITEII NPNYMGVGPF GPPMPLHVKQ TLSPDQQPTA WSYDQPPKDS PLGPCRGESP 970 980 990 1000 1010 1020 PTPPGQPPIS PKKFLPSTAN RGLPPRTQES RPSDLGKNAG DTLPQEDLPL TKPEMFENPL 1030 1040 1050 1060 1070 1080 YGSLSSFPKP APRKDQESPK MPRKEPPPCP EPGILSPSIV LTKAQEADRG EGPGKQVPAP 1090 1100 1110 1120 1130 1140 RLRSFTCSSS AEGRAAGGDK SQGKPKTPVS SQAPVPAKRP IKPSRSEINQ QTPPTPTPRP 1150 1160 1170 1180 PLPVKSPAVL HLQHSKGRDY RDNTELPHHG KHRPEEGPPG PLGRTAMQ
	Isoform 3 (SIP-110) [UniParc]. Checksum: 2B90E6DD584DD048	FASTA	976	109,294
	10 20 30 40 50 60 MFTLSPAPRE VIRTLPSLES LQRLFDQQLS PGLRPRPQVP GEANPINMVS KLSQLTSLLS 70 80 90 100 110 120 SIEDKVKALL HEGPESPHRP SLIPPVTFEV KAESLGIPQK MQLKVDVESG KLIIKKSKDG 130 140 150 160 170 180 SEDKFYSHKK ILQLIKSQKF LNKLVILVET EKEKILRKEY VFADSKKREG FCQLLQQMKN 190 200 210 220 230 240 KHSEQPEPDM ITIFIGTWNM GNAPPPKKIT SWFLSKGQGK TRDDSADYIP HDIYVIGTQE 250 260 270 280 290 300 DPLSEKEWLE ILKHSLQEIT SVTFKTVAIH TLWNIRIVVL AKPEHENRIS HICTDNVKTG 310 320 330 340 350 360 IANTLGNKGA VGVSFMFNGT SLGFVNSHLT SGSEKKLRRN QNYMNILRFL ALGDKKLSPF 370 380 390 400 410 420 NITHRFTHLF WFGDLNYRVD LPTWEAETII QKIKQQQYAD LLSHDQLLTE RREQKVFLHF 430 440 450 460 470 480 EEEEITFAPT YRFERLTRDK YAYTKQKATG MKYNLPSWCD RVLWKSYPLV HVVCQSYGST 490 500 510 520 530 540 SDIMTSDHSP VFATFEAGVT SQFVSKNGPG TVDSQGQIEF LRCYATLKTK SQTKFYLEFH 550 560 570 580 590 600 SSCLESFVKS QEGENEEGSE GELVVKFGET LPKLKPIISD PEYLLDQHIL ISIKSSDSDE 610 620 630 640 650 660 SYGEGCIALR LEATETQLPI YTPLTHHGEL TGHFQGEIKL QTSQGKTREK LYDFVKTERD 670 680 690 700 710 720 ESSGPKTLKS LTSHDPMKQW EVTSRAPPCS GSSITEIINP NYMGVGPFGP PMPLHVKQTL 730 740 750 760 770 780 SPDQQPTAWS YDQPPKDSPL GPCRGESPPT PPGQPPISPK KFLPSTANRG LPPRTQESRP 790 800 810 820 830 840 SDLGKNAGDT LPQEDLPLTK PEMFENPLYG SLSSFPKPAP RKDQESPKMP RKEPPPCPEP 850 860 870 880 890 900 GILSPSIVLT KAQEADRGEG PGKQVPAPRL RSFTCSSSAE GRAAGGDKSQ GKPKTPVSSQ 910 920 930 940 950 960 APVPAKRPIK PSRSEINQQT PPTPTPRPPL PVKSPAVLHL QHSKGRDYRD NTELPHHGKH 970 RPEEGPPGPL GRTAMQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, MASS SPECTROMETRY.
[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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00329213.
IPI00604549.
IPI00847557.

PIR

JC4889.

RefSeq

NP_001017915.1. NM_001017915.1.
NP_005532.2. NM_005541.3.

UniGene

Hs.262886.
Hs.601911.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YSX	NMR	-	A	1-112	[»]

ProteinModelPortal

Q92835.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92835. 6 interactions.

MINT

MINT-123561.

STRING

9606.ENSP00000352575.

PTM databases

PhosphoSite

Q92835.

Polymorphism databases

DMDM

158564077.

Proteomic databases

PaxDb

Q92835.

PRIDE

Q92835.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359570; ENSP00000352575; ENSG00000168918.

GeneID

3635.

KEGG

hsa:3635.

UCSC

uc010zmo.2. human.
uc010zmp.2. human.

Organism-specific databases

CTD

3635.

GeneCards

GC02P233924.

H-InvDB

HIX0057065.

HGNC

HGNC:6079. INPP5D.

HPA

CAB016300.

MIM

601582. gene.

neXtProt

NX_Q92835.

PharmGKB

PA29887.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5411.

HOVERGEN

HBG106726.

KO

K03084.

Enzyme and pathway databases

BioCyc

MetaCyc:HS09849-MONOMER.

Reactome

REACT_111217. Metabolism.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q92835.

Bgee

Q92835.

CleanEx

HS_INPP5D.

Genevestigator

Q92835.

Family and domain databases

Gene3D

3.30.505.10. 1 hit.

InterPro

IPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR000980. SH2.
[Graphical view]

Pfam

PF03372. Exo_endo_phos. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.

SMART

SM00128. IPPc. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]

SUPFAM

SSF56219. Exo_endo_phos. 1 hit.

PROSITE

PS50001. SH2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1781870.

ChiTaRS

INPP5D. human.

EvolutionaryTrace

Q92835.

GenomeRNAi

3635.

NextBio

14225.

SOURCE

Search...

Entry information

Entry name

SHIP1_HUMAN

Accession

Primary (citable) accession number: Q92835
Secondary accession number(s): O00145 , Q13544, Q13545, Q6P5A4, Q92656, Q9UE80

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.