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Q92835 (SHIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1189 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processApoptosis
Immunity
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
SH2 domain
SH3-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT 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: Ensembl

immunoglobulin mediated immune response

Inferred from electronic annotation. Source: Ensembl

inositol phosphate metabolic process

Traceable author statement. Source: Reactome

intracellular signal transduction

Inferred from electronic annotation. Source: Ensembl

leukocyte migration

Traceable author statement. Source: Reactome

negative regulation of B cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of bone resorption

Inferred from electronic annotation. Source: Ensembl

negative regulation of immune response

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-6 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of monocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of neutrophil differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of signal transduction

Inferred from electronic annotation. Source: Ensembl

phosphate-containing compound metabolic process

Traceable author statement Ref.1. Source: ProtInc

phosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylinositol dephosphorylation

Inferred from electronic annotation. Source: InterPro

phospholipid metabolic process

Traceable author statement. Source: Reactome

positive regulation of B cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioninositol-polyphosphate 5-phosphatase activity

Traceable author statement Ref.1. Source: ProtInc

phosphatidylinositol trisphosphate phosphatase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 21712384. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FCGR2BP319942EBI-1380477,EBI-724784
SH3KBP1Q96B976EBI-1380477,EBI-346595

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11891189Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
PRO_0000302866

Regions

Domain5 – 10197SH2
Region1016 – 103015Interaction with DAB2 By similarity
Motif124 – 1296SH3-binding 1
Motif912 – 9154NPXY motif 1
Motif969 – 9746SH3-binding 2
Motif1019 – 10224NPXY motif 2
Motif1040 – 105112SH3-binding 3
Compositional bias920 – 1148229Pro-rich

Amino acid modifications

Modified residue9151Phosphotyrosine Ref.10
Modified residue9341Phosphoserine By similarity
Modified residue9441Phosphotyrosine By similarity
Modified residue10221Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 212212Missing in isoform 3.
VSP_027977
Alternative sequence1171Missing in isoform 2.
VSP_027978
Alternative sequence213 – 22210TTLLCKELYG → MFTLSPAPR in isoform 3.
VSP_027979
Natural variant6851V → E in one patient with acute myeloid leukemya; somatic mutation. Ref.14
VAR_034979
Natural variant11691H → Y. Ref.1 Ref.6
Corresponds to variant rs9247 [ dbSNP | Ensembl ].
VAR_059358

Experimental info

Sequence conflict25 – 262DG → GT in AAB49680. Ref.4
Sequence conflict10291P → H in AAB49680. Ref.4

Secondary structure

.................... 1189
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: 7958E91A64A4B68B

FASTA1,189133,292
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 335673E161C5FFAD
Show »

FASTA1,188133,193
Isoform 3 (SIP-110) [UniParc].

Checksum: 2B90E6DD584DD048
Show »

FASTA976109,294

References

« Hide '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, 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]"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.
PIRJC4889.
RefSeqNP_001017915.1. NM_001017915.2. [Q92835-1]
NP_005532.2. NM_005541.4. [Q92835-2]
UniGeneHs.262886.
Hs.601911.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YSXNMR-A1-112[»]
ProteinModelPortalQ92835.
SMRQ92835. Positions 1-112, 402-714.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109847. 33 interactions.
IntActQ92835. 16 interactions.
MINTMINT-123561.
STRING9606.ENSP00000352575.

Chemistry

ChEMBLCHEMBL1781870.

PTM databases

PhosphoSiteQ92835.

Polymorphism databases

DMDM158564077.

Proteomic databases

MaxQBQ92835.
PaxDbQ92835.
PRIDEQ92835.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359570; ENSP00000352575; ENSG00000168918.
GeneID3635.
KEGGhsa:3635.
UCSCuc010zmo.2. human. [Q92835-1]
uc010zmp.2. human. [Q92835-2]

Organism-specific databases

CTD3635.
GeneCardsGC02P233924.
H-InvDBHIX0057065.
HGNCHGNC:6079. INPP5D.
HPACAB016300.
MIM601582. gene.
neXtProtNX_Q92835.
PharmGKBPA29887.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5411.
HOVERGENHBG106726.
KOK03084.
OrthoDBEOG75F4CD.
PhylomeDBQ92835.
TreeFamTF323475.

Enzyme and pathway databases

BioCycMetaCyc:HS09849-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkQ92835.

Gene expression databases

ArrayExpressQ92835.
BgeeQ92835.
CleanExHS_INPP5D.
GenevestigatorQ92835.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
3.60.10.10. 1 hit.
InterProIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR000980. SH2.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
SMARTSM00128. IPPc. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF55550. SSF55550. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSINPP5D. human.
EvolutionaryTraceQ92835.
GeneWikiINPP5D.
GenomeRNAi3635.
NextBio14225.
PROQ92835.
SOURCESearch...

Entry information

Entry nameSHIP1_HUMAN
AccessionPrimary (citable) accession number: Q92835
Secondary accession number(s): O00145 expand/collapse secondary AC list , Q13544, Q13545, Q6P5A4, Q92656, Q9UE80
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM