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Protein

Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2

Gene

INPPL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (PubMed:21624956). Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification.10 Publications

Miscellaneous

Its ability to confer resistance to dietary obesity suggests that it may serve as a possible therapeutic target in cases of type 2 diabetes and obesity.

Catalytic activityi

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

Activity regulationi

Activated upon translocation to the sites of synthesis of PtdIns(3,4,5)P3 in the membrane. Enzymatic activity is enhanced in the presence of phosphatidylserine.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActin-binding, Hydrolase
Biological processCell adhesion, Immunity

Enzyme and pathway databases

BioCyciMetaCyc:HS09233-MONOMER
BRENDAi3.1.3.86 2681
ReactomeiR-HSA-1660499 Synthesis of PIPs at the plasma membrane
R-HSA-1855204 Synthesis of IP3 and IP4 in the cytosol
R-HSA-912526 Interleukin receptor SHC signaling
SABIO-RKiO15357
SignaLinkiO15357
SIGNORiO15357

Chemistry databases

SwissLipidsiSLP:000000953

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC:3.1.3.86)
Alternative name(s):
Inositol polyphosphate phosphatase-like protein 1
Short name:
INPPL-1
Protein 51C
SH2 domain-containing inositol 5'-phosphatase 2
Short name:
SH2 domain-containing inositol phosphatase 2
Short name:
SHIP-2
Gene namesi
Name:INPPL1
Synonyms:SHIP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000165458.13
HGNCiHGNC:6080 INPPL1
MIMi600829 gene
neXtProtiNX_O15357

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Diabetes mellitus, non-insulin-dependent (NIDDM)2 Publications
Disease susceptibility may be associated with variations affecting the gene represented in this entry.
Disease descriptionA multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
See also OMIM:125853
Genetic variations in INPPL1 may be a cause of susceptibility to metabolic syndrome. Metabolic syndrome is characterized by diabetes, insulin resistance, hypertension, and hypertriglyceridemia is absent.2 Publications
Opsismodysplasia (OPSMD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare skeletal dysplasia involving delayed bone maturation. Clinical signs observed at birth include short limbs, small hands and feet, relative macrocephaly with a large anterior fontanel, and characteristic craniofacial abnormalities including a prominent brow, depressed nasal bridge, a small anteverted nose, and a relatively long philtrum. Death secondary to respiratory failure during the first few years of life has been reported, but there can be long-term survival. Typical radiographic findings include shortened long bones with very delayed epiphyseal ossification, severe platyspondyly, metaphyseal cupping, and characteristic abnormalities of the metacarpals and phalanges.
See also OMIM:258480
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069586401R → W in OPSMD. 1 PublicationCorresponds to variant dbSNP:rs397514511EnsemblClinVar.1
Natural variantiVAR_069587659P → S in OPSMD. 1 PublicationCorresponds to variant dbSNP:rs397514510EnsemblClinVar.1
Natural variantiVAR_069588688W → C in OPSMD. 1 Publication1
Natural variantiVAR_069589722F → I in OPSMD. 1 PublicationCorresponds to variant dbSNP:rs397514512EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi47R → G: Abolishes interaction with p130Cas/BCAR1 and its ability to induce increased adhesion. Abolishes phosphorylation upon FCGR2A clustering. 2 Publications1
Mutagenesisi140 – 141PL → AA: Abolishes interaction with SH3YL1. 1 Publication2
Mutagenesisi607D → A: Abolishes enzyme activity but not phosphorylation upon FCGR2A clustering. 1 Publication1
Mutagenesisi958T → A: Reduces PDGF-stimulated tyrosine phosphorylation and association with SHC1. 1 Publication1
Mutagenesisi986 – 987YY → FF: Inducer a strong reduction of phosphorylation upon re-plating on collagen I. 1 Publication2

Keywords - Diseasei

Diabetes mellitus, Disease mutation

Organism-specific databases

DisGeNETi3636
MalaCardsiINPPL1
MIMi125853 phenotype
258480 phenotype
OpenTargetsiENSG00000165458
Orphaneti2746 Opsismodysplasia
PharmGKBiPA29888

Chemistry databases

ChEMBLiCHEMBL2331064
GuidetoPHARMACOLOGYi1459

Polymorphism and mutation databases

BioMutaiINPPL1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003028701 – 1258Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2Add BLAST1258

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei132PhosphoserineCombined sources1
Modified residuei165PhosphothreonineCombined sources1
Modified residuei241PhosphoserineCombined sources1
Modified residuei352PhosphoserineCombined sources1
Modified residuei886PhosphotyrosineCombined sources1
Modified residuei890PhosphoserineCombined sources1
Modified residuei958PhosphothreonineCombined sources1 Publication1
Modified residuei986Phosphotyrosine; by SRC2 Publications1
Modified residuei1131PhosphoserineCombined sources1
Modified residuei1135PhosphotyrosineCombined sources1
Modified residuei1162PhosphotyrosineCombined sources1 Publication1
Modified residuei1257PhosphoserineCombined sources1

Post-translational modificationi

Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as insulin, growth factors such as EGF or PDGF, chemokines, integrin ligands and hypertonic and oxidative stress. May be phosphorylated upon IgG receptor FCGR2B-binding. Phosphorylated at Tyr-986 following cell attachment and spreading. Phosphorylated at Tyr-1162 following EGF signaling pathway stimulation. Phosphorylated at Thr-958 in response to PDGF.8 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO15357
MaxQBiO15357
PaxDbiO15357
PeptideAtlasiO15357
PRIDEiO15357
ProteomicsDBi48609
48610 [O15357-2]

PTM databases

DEPODiO15357
iPTMnetiO15357
PhosphoSitePlusiO15357

Expressioni

Tissue specificityi

Widely expressed, most prominently in skeletal muscle, heart and brain. Present in platelets. Expressed in transformed myeloid cells and in primary macrophages, but not in peripheral blood monocytes.5 Publications

Inductioni

By bacterial lipopolysaccharides (LPS).1 Publication

Gene expression databases

BgeeiENSG00000165458 Expressed in 191 organ(s), highest expression level in left lobe of thyroid gland
CleanExiHS_INPPL1
ExpressionAtlasiO15357 baseline and differential
GenevisibleiO15357 HS

Organism-specific databases

HPAiHPA037601

Interactioni

Subunit structurei

Interacts with tyrosine phosphorylated form of SHC1 (PubMed:9660833, PubMed:10194451, PubMed:11349134). Interacts with EGFR (PubMed:11349134). Upon stimulation by the EGF signaling pathway, it forms a complex with SHC1 and EGFR (PubMed:11349134). Interacts with cytoskeletal protein SORBS3/vinexin, promoting its localization to the periphery of cells (PubMed:16302969). Forms a complex with filamin (FLNA or FLNB), actin, GPIb (GP1BA or GP1BB) that regulates cortical and submembraneous actin (PubMed:11739414, PubMed:12676785). Interacts with c-Met/MET, when c-Met/MET is phosphorylated on 'Tyr-1356' (PubMed:15735664). Interacts with p130Cas/BCAR1 (PubMed:11158326). Interacts with CENTD3/ARAP3 via its SAM domain (PubMed:17314030). Interacts with c-Cbl/CBL and CAP/SORBS1 (PubMed:12504111). Interacts with activated EPHA2 receptor (PubMed:17135240). Interacts with receptor FCGR2A (PubMed:12690104). Interacts with receptor FCGR2B (PubMed:11016922). Interacts with tyrosine kinase ABL1 (PubMed:10194451). Interacts with tyrosine kinase TEC (By similarity). Interacts with CSF1R (By similarity). Interacts (via N-terminus) with SH3YL1 (via SH3 domain) (PubMed:21624956). Interacts with FCRL6 (tyrosine phosphorylated form) (PubMed:20933011).By similarity14 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi109848, 118 interactors
DIPiDIP-39733N
IntActiO15357, 30 interactors
MINTiO15357
STRINGi9606.ENSP00000298229

Chemistry databases

BindingDBiO15357

Structurei

Secondary structure

11258
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliO15357
SMRiO15357
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15357

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 117SH2PROSITE-ProRule annotationAdd BLAST97
Domaini1196 – 1258SAMPROSITE-ProRule annotationAdd BLAST63

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi944 – 949SH3-binding6
Motifi983 – 986NPXY motif4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi935 – 1105Pro-richAdd BLAST171

Domaini

The SH2 domain interacts with tyrosine phosphorylated forms of proteins such as SHC1 or FCGR2A. It also mediates the interaction with p130Cas/BCAR1.
The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain.By similarity

Sequence similaritiesi

Keywords - Domaini

SH2 domain, SH3-binding

Phylogenomic databases

eggNOGiKOG0565 Eukaryota
KOG4384 Eukaryota
COG5411 LUCA
GeneTreeiENSGT00760000119075
HOGENOMiHOG000004836
HOVERGENiHBG106726
InParanoidiO15357
KOiK15909
OMAiVKSMDGY
OrthoDBiEOG091G00P6
PhylomeDBiO15357
TreeFamiTF323475

Family and domain databases

Gene3Di3.30.505.10, 1 hit
3.60.10.10, 1 hit
InterProiView protein in InterPro
IPR036691 Endo/exonu/phosph_ase_sf
IPR005135 Endo/exonuclease/phosphatase
IPR000300 IPPc
IPR001660 SAM
IPR013761 SAM/pointed_sf
IPR000980 SH2
IPR036860 SH2_dom_sf
PfamiView protein in Pfam
PF03372 Exo_endo_phos, 1 hit
PF00536 SAM_1, 1 hit
PF00017 SH2, 1 hit
PRINTSiPR00401 SH2DOMAIN
SMARTiView protein in SMART
SM00128 IPPc, 1 hit
SM00454 SAM, 1 hit
SM00252 SH2, 1 hit
SUPFAMiSSF47769 SSF47769, 1 hit
SSF55550 SSF55550, 1 hit
SSF56219 SSF56219, 1 hit
PROSITEiView protein in PROSITE
PS50105 SAM_DOMAIN, 1 hit
PS50001 SH2, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O15357-1) [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
MASACGAPGP GGALGSQAPS WYHRDLSRAA AEELLARAGR DGSFLVRDSE
60 70 80 90 100
SVAGAFALCV LYQKHVHTYR ILPDGEDFLA VQTSQGVPVR RFQTLGELIG
110 120 130 140 150
LYAQPNQGLV CALLLPVEGE REPDPPDDRD ASDGEDEKPP LPPRSGSTSI
160 170 180 190 200
SAPTGPSSPL PAPETPTAPA AESAPNGLST VSHDYLKGSY GLDLEAVRGG
210 220 230 240 250
ASHLPHLTRT LATSCRRLHS EVDKVLSGLE ILSKVFDQQS SPMVTRLLQQ
260 270 280 290 300
QNLPQTGEQE LESLVLKLSV LKDFLSGIQK KALKALQDMS STAPPAPQPS
310 320 330 340 350
TRKAKTIPVQ AFEVKLDVTL GDLTKIGKSQ KFTLSVDVEG GRLVLLRRQR
360 370 380 390 400
DSQEDWTTFT HDRIRQLIKS QRVQNKLGVV FEKEKDRTQR KDFIFVSARK
410 420 430 440 450
REAFCQLLQL MKNKHSKQDE PDMISVFIGT WNMGSVPPPK NVTSWFTSKG
460 470 480 490 500
LGKTLDEVTV TIPHDIYVFG TQENSVGDRE WLDLLRGGLK ELTDLDYRPI
510 520 530 540 550
AMQSLWNIKV AVLVKPEHEN RISHVSTSSV KTGIANTLGN KGAVGVSFMF
560 570 580 590 600
NGTSFGFVNC HLTSGNEKTA RRNQNYLDIL RLLSLGDRQL NAFDISLRFT
610 620 630 640 650
HLFWFGDLNY RLDMDIQEIL NYISRKEFEP LLRVDQLNLE REKHKVFLRF
660 670 680 690 700
SEEEISFPPT YRYERGSRDT YAWHKQKPTG VRTNVPSWCD RILWKSYPET
710 720 730 740 750
HIICNSYGCT DDIVTSDHSP VFGTFEVGVT SQFISKKGLS KTSDQAYIEF
760 770 780 790 800
ESIEAIVKTA SRTKFFIEFY STCLEEYKKS FENDAQSSDN INFLKVQWSS
810 820 830 840 850
RQLPTLKPIL ADIEYLQDQH LLLTVKSMDG YESYGECVVA LKSMIGSTAQ
860 870 880 890 900
QFLTFLSHRG EETGNIRGSM KVRVPTERLG TRERLYEWIS IDKDEAGAKS
910 920 930 940 950
KAPSVSRGSQ EPRSGSRKPA FTEASCPLSR LFEEPEKPPP TGRPPAPPRA
960 970 980 990 1000
APREEPLTPR LKPEGAPEPE GVAAPPPKNS FNNPAYYVLE GVPHQLLPPE
1010 1020 1030 1040 1050
PPSPARAPVP SATKNKVAIT VPAPQLGHHR HPRVGEGSSS DEESGGTLPP
1060 1070 1080 1090 1100
PDFPPPPLPD SAIFLPPSLD PLPGPVVRGR GGAEARGPPP PKAHPRPPLP
1110 1120 1130 1140 1150
PGPSPASTFL GEVASGDDRS CSVLQMAKTL SEVDYAPAGP ARSALLPGPL
1160 1170 1180 1190 1200
ELQPPRGLPS DYGRPLSFPP PRIRESIQED LAEEAPCLQG GRASGLGEAG
1210 1220 1230 1240 1250
MSAWLRAIGL ERYEEGLVHN GWDDLEFLSD ITEEDLEEAG VQDPAHKRLL

LDTLQLSK
Length:1,258
Mass (Da):138,599
Last modified:November 24, 2009 - v2
Checksum:iD76B5AA8ACDE8CBA
GO
Isoform 2 (identifier: O15357-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-242: Missing.

Show »
Length:1,016
Mass (Da):113,176
Checksum:iF99D2FBEDA102C1F
GO

Computationally mapped potential isoform sequencesi

There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0A0MTP6A0A0A0MTP6_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
1,146Annotation score:
H7BXR2H7BXR2_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
149Annotation score:
F5GY16F5GY16_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
127Annotation score:
H0YFZ4H0YFZ4_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
197Annotation score:
F5H588F5H588_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
33Annotation score:
F5GYK9F5GYK9_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
22Annotation score:
F5GWY9F5GWY9_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
17Annotation score:
H0YFB4H0YFB4_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
INPPL1
41Annotation score:

Sequence cautioni

The sequence AAA50503 differs from that shown. Reason: Frameshift at position 1153.Curated
The sequence AAA96658 differs from that shown. Reason: Frameshift at several positions.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti307I → M in AAA96658 (PubMed:8530088).Curated1
Sequence conflicti1142R → A in AAA50503 (PubMed:8530088).Curated1
Sequence conflicti1142R → A in AAA96658 (PubMed:8530088).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069586401R → W in OPSMD. 1 PublicationCorresponds to variant dbSNP:rs397514511EnsemblClinVar.1
Natural variantiVAR_034980632L → I Associated with susceptibility to NIDDM. 1 PublicationCorresponds to variant dbSNP:rs61749195Ensembl.1
Natural variantiVAR_069587659P → S in OPSMD. 1 PublicationCorresponds to variant dbSNP:rs397514510EnsemblClinVar.1
Natural variantiVAR_069588688W → C in OPSMD. 1 Publication1
Natural variantiVAR_034981721V → M1 PublicationCorresponds to variant dbSNP:rs116848359Ensembl.1
Natural variantiVAR_069589722F → I in OPSMD. 1 PublicationCorresponds to variant dbSNP:rs397514512EnsemblClinVar.1
Natural variantiVAR_034982982N → S Associated with susceptibility to NIDDM. 1 PublicationCorresponds to variant dbSNP:rs70940821Ensembl.1
Natural variantiVAR_0349831083A → G1 PublicationCorresponds to variant dbSNP:rs11548491Ensembl.1
Natural variantiVAR_0349841114A → G3 PublicationsCorresponds to variant dbSNP:rs1049472Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0279851 – 242Missing in isoform 2. 1 PublicationAdd BLAST242

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24444 mRNA Translation: AAA50503.1 Frameshift.
L36818 mRNA Translation: AAA96658.1 Frameshift.
Y14385 mRNA Translation: CAA74743.1
AP000593 Genomic DNA No translation available.
CH471076 Genomic DNA Translation: EAW74855.1
BC140853 mRNA Translation: AAI40854.1
CCDSiCCDS8213.1 [O15357-1]
PIRiJC5765
RefSeqiNP_001558.3, NM_001567.3 [O15357-1]
XP_011543301.1, XM_011544999.2 [O15357-1]
UniGeneiHs.523875

Genome annotation databases

EnsembliENST00000298229; ENSP00000298229; ENSG00000165458 [O15357-1]
ENST00000538751; ENSP00000444619; ENSG00000165458 [O15357-2]
GeneIDi3636
KEGGihsa:3636
UCSCiuc001osf.4 human [O15357-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24444 mRNA Translation: AAA50503.1 Frameshift.
L36818 mRNA Translation: AAA96658.1 Frameshift.
Y14385 mRNA Translation: CAA74743.1
AP000593 Genomic DNA No translation available.
CH471076 Genomic DNA Translation: EAW74855.1
BC140853 mRNA Translation: AAI40854.1
CCDSiCCDS8213.1 [O15357-1]
PIRiJC5765
RefSeqiNP_001558.3, NM_001567.3 [O15357-1]
XP_011543301.1, XM_011544999.2 [O15357-1]
UniGeneiHs.523875

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K4PNMR-A1194-1258[»]
2KSONMR-B1200-1258[»]
2MK2NMR-A20-117[»]
3NR8X-ray2.80A/B419-732[»]
4A9CX-ray2.10A/B419-732[»]
5OKMX-ray1.96A/B/C/D/E/F/G/H420-878[»]
5OKNX-ray2.65A/B/C/D/E/F/G/H420-878[»]
5OKOX-ray1.94A/B420-878[»]
5OKPX-ray1.85A420-878[»]
ProteinModelPortaliO15357
SMRiO15357
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109848, 118 interactors
DIPiDIP-39733N
IntActiO15357, 30 interactors
MINTiO15357
STRINGi9606.ENSP00000298229

Chemistry databases

BindingDBiO15357
ChEMBLiCHEMBL2331064
GuidetoPHARMACOLOGYi1459
SwissLipidsiSLP:000000953

PTM databases

DEPODiO15357
iPTMnetiO15357
PhosphoSitePlusiO15357

Polymorphism and mutation databases

BioMutaiINPPL1

Proteomic databases

EPDiO15357
MaxQBiO15357
PaxDbiO15357
PeptideAtlasiO15357
PRIDEiO15357
ProteomicsDBi48609
48610 [O15357-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298229; ENSP00000298229; ENSG00000165458 [O15357-1]
ENST00000538751; ENSP00000444619; ENSG00000165458 [O15357-2]
GeneIDi3636
KEGGihsa:3636
UCSCiuc001osf.4 human [O15357-1]

Organism-specific databases

CTDi3636
DisGeNETi3636
EuPathDBiHostDB:ENSG00000165458.13
GeneCardsiINPPL1
H-InvDBiHIX0201720
HGNCiHGNC:6080 INPPL1
HPAiHPA037601
MalaCardsiINPPL1
MIMi125853 phenotype
258480 phenotype
600829 gene
neXtProtiNX_O15357
OpenTargetsiENSG00000165458
Orphaneti2746 Opsismodysplasia
PharmGKBiPA29888
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0565 Eukaryota
KOG4384 Eukaryota
COG5411 LUCA
GeneTreeiENSGT00760000119075
HOGENOMiHOG000004836
HOVERGENiHBG106726
InParanoidiO15357
KOiK15909
OMAiVKSMDGY
OrthoDBiEOG091G00P6
PhylomeDBiO15357
TreeFamiTF323475

Enzyme and pathway databases

BioCyciMetaCyc:HS09233-MONOMER
BRENDAi3.1.3.86 2681
ReactomeiR-HSA-1660499 Synthesis of PIPs at the plasma membrane
R-HSA-1855204 Synthesis of IP3 and IP4 in the cytosol
R-HSA-912526 Interleukin receptor SHC signaling
SABIO-RKiO15357
SignaLinkiO15357
SIGNORiO15357

Miscellaneous databases

ChiTaRSiINPPL1 human
EvolutionaryTraceiO15357
GeneWikiiINPPL1
GenomeRNAii3636
PROiPR:O15357
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000165458 Expressed in 191 organ(s), highest expression level in left lobe of thyroid gland
CleanExiHS_INPPL1
ExpressionAtlasiO15357 baseline and differential
GenevisibleiO15357 HS

Family and domain databases

Gene3Di3.30.505.10, 1 hit
3.60.10.10, 1 hit
InterProiView protein in InterPro
IPR036691 Endo/exonu/phosph_ase_sf
IPR005135 Endo/exonuclease/phosphatase
IPR000300 IPPc
IPR001660 SAM
IPR013761 SAM/pointed_sf
IPR000980 SH2
IPR036860 SH2_dom_sf
PfamiView protein in Pfam
PF03372 Exo_endo_phos, 1 hit
PF00536 SAM_1, 1 hit
PF00017 SH2, 1 hit
PRINTSiPR00401 SH2DOMAIN
SMARTiView protein in SMART
SM00128 IPPc, 1 hit
SM00454 SAM, 1 hit
SM00252 SH2, 1 hit
SUPFAMiSSF47769 SSF47769, 1 hit
SSF55550 SSF55550, 1 hit
SSF56219 SSF56219, 1 hit
PROSITEiView protein in PROSITE
PS50105 SAM_DOMAIN, 1 hit
PS50001 SH2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSHIP2_HUMAN
AccessioniPrimary (citable) accession number: O15357
Secondary accession number(s): B2RTX5, Q13577, Q13578
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: November 24, 2009
Last modified: September 12, 2018
This is version 147 of the entry and version 2 of the sequence. See 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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