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Entry version 45 (16 Oct 2019)
Sequence version 2 (03 Jul 2019)
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Protein

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

Gene

INPPL1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (PubMed:12847108). 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. 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 (By similarity).By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>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.By similarity

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processImmunity

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SSC-1660499 Synthesis of PIPs at the plasma membrane
R-SSC-1855204 Synthesis of IP3 and IP4 in the cytosol

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000861

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC:3.1.3.861 Publication)
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:INPPL1
Synonyms:SHIP2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSus scrofa (Pig)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9823 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008227 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004476051 – 1260Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2Add BLAST1260

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei136PhosphoserineBy similarity1
Modified residuei243PhosphoserineBy similarity1
Modified residuei355PhosphoserineBy similarity1
Modified residuei888PhosphotyrosineBy similarity1
Modified residuei892PhosphoserineBy similarity1
Modified residuei960PhosphothreonineBy similarity1
Modified residuei988PhosphotyrosineBy similarity1
Modified residuei1133PhosphoserineBy similarity1
Modified residuei1164PhosphotyrosineBy similarity1
Modified residuei1259PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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-988 following cell attachment and spreading. Phosphorylated at Tyr-1164 following EGF signaling pathway stimulation.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
F1SUW7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed abundantly in skeletal muscle tissue.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSSSCG00000014811 Expressed in 6 organ(s), highest expression level in lung

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
D7PF45 SS

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with tyrosine phosphorylated form of SHC1.

Interacts with EGFR. Upon stimulation by the EGF signaling pathway, it forms a complex with SHC1 and EGFR.

Interacts with cytoskeletal protein SORBS3/vinexin, promoting its localization to the periphery of cells.

Forms a complex with filamin (FLNA or FLNB), actin, GPIb (GP1BA or GP1BB) that regulates cortical and submembraneous actin.

Interacts with c-Met/MET, when c-Met/MET is phosphorylated on 'Tyr-1356'.

Interacts with p130Cas/BCAR1.

Interacts with CENTD3/ARAP3 via its SAM domain.

Interacts with c-Cbl/CBL and CAP/SORBS1.

Interacts with activated EPHA2 receptor.

Interacts with receptor FCGR2A.

Interacts with receptor FCGR2B.

Interacts with tyrosine kinase ABL1 (By similarity).

Interacts with tyrosine kinase TEC (By similarity).

Interacts with CSF1R (By similarity).

Interacts (via N-terminus) with SH3YL1 (via SH3 domain).

Interacts with FCRL6 (tyrosine phosphorylated form) (By similarity).

By similarity

GO - Molecular functioni

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini25 – 121SH2PROSITE-ProRule annotationAdd BLAST97
Domaini1198 – 1260SAMPROSITE-ProRule annotationAdd BLAST63

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi946 – 951SH3-bindingBy similarity6
Motifi985 – 988NPXY motifBy similarity4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

SH2 domain, SH3-binding

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0565 Eukaryota
KOG4384 Eukaryota
COG5411 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156576

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
F1SUW7

KEGG Orthology (KO)

More...
KOi
K15909

Identification of Orthologs from Complete Genome Data

More...
OMAi
HDYLKGS

Database of Orthologous Groups

More...
OrthoDBi
311217at2759

TreeFam database of animal gene trees

More...
TreeFami
TF323475

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.150.50, 1 hit
3.30.505.10, 1 hit
3.60.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03372 Exo_endo_phos, 1 hit
PF00536 SAM_1, 1 hit
PF00017 SH2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00401 SH2DOMAIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00128 IPPc, 1 hit
SM00454 SAM, 1 hit
SM00252 SH2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47769 SSF47769, 1 hit
SSF55550 SSF55550, 1 hit
SSF56219 SSF56219, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50105 SAM_DOMAIN, 1 hit
PS50001 SH2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

D7PF45-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASACGAPGP GAGPGAALGS PAPAWYHRDL SRAAAEELLA RAGRDGSFLV
60 70 80 90 100
RDSESVAGAF ALCVLYQKHV HTYRILPDGE DFLAVQTSQG VPVRRFQTLG
110 120 130 140 150
ELIGLYAQPN QGLVCALLLP VERERELDPP DERDASDGED EKPPLPPRSG
160 170 180 190 200
TSVSAPLGPS SPPAAPEPPT PAVESAPNGL STVSHEYLKG SYGLDLEAVR
210 220 230 240 250
GGASNLPHLT RTLAASCRRL HSEVDKVLSG LEILSKVFDQ QSSPMVTRLL
260 270 280 290 300
QQQNPPQTGE QELESLVLKL SVLKDFLSGI QKKALKALQD MSSTAPPAPV
310 320 330 340 350
QPSTRKAKTI PVQAFEVKLD VTLGDLTKIG KSQKFTLSVD VEGGRLVLLR
360 370 380 390 400
RQRDSQEDWT TFTHDRIRQL IKSQRVQNKL GVVFEKEKER TQRKDFIFVS
410 420 430 440 450
ARKREAFCQL LQLMKNKHSK QDEPDMISVF IGTWNMGSVP PPRNVTSWFT
460 470 480 490 500
SKGLGKTLDE VTVTIPHDIY VFGTQENSVG DREWLDLLRG GLKELTDLDY
510 520 530 540 550
RPIAMQSLWN IKVAVLVKPE HENRISHVST SSVKTGIANT LGNKGAVGVS
560 570 580 590 600
FMFNGTSFGF VNCHLTSGNE KTARRNQNYL DILRLLSLGD RQLGAFDISL
610 620 630 640 650
RFTHLFWFGD LNYRLDMDIQ EILNYISRKE FEPLLRVDQL NLEREKHKVF
660 670 680 690 700
LRFSEEEISF PPTYRYERGS RDTYAWHKQK PTGVRTNVPS WCDRILWKSH
710 720 730 740 750
PETHIICNSY GCTDDIVTSD HSPVFGTFEV GVTSQFISKK GLSKTADQAY
760 770 780 790 800
IEFESIEAIV KTASRTKFFI EFYSTCLEEY KKSFENDAQS SDNVNFLKVQ
810 820 830 840 850
WSSRQLPTLK PILDIEYLQD QHLLLTVKSM DGYESYGECV VALKSMIGST
860 870 880 890 900
AQQFLTFLSH RGEETGNIRG SMKVRVPTER LGTRERLYEW ISIDKDEAGA
910 920 930 940 950
KSKAPSVSRG SQEPRSGSRK PAPAEASCPL SKLFEEPEKP PPTGRPPAPP
960 970 980 990 1000
RAAPREEPLT PRLKPEGAPE PEGVAAPPPK NSFNNPAYYV LEGVPHQLLP
1010 1020 1030 1040 1050
PEPPSPARAP VPPATKNKVA ITVPAPQLGR HRPPRVGEGS SSDEESGGTL
1060 1070 1080 1090 1100
PPPDFPPPPL PDSAIFLPPS REPLPGPGVR GRSGGEARAL PPPKAHPRPP
1110 1120 1130 1140 1150
LPPGPLPPGT FLGEAAGGDD RSCSVLQVAK KLSEVDSAPP GPGRCLLLPG
1160 1170 1180 1190 1200
PLELQPARAL PSDYGRPLSF PPPRIRESVQ EDLAEEAPCP QAGRTGGLGE
1210 1220 1230 1240 1250
AGMGAWLRAI GLERYEEGLV HNGWDDLEFL SDITEEDLEE AGVQDPAHKR
1260
LLLDTLQLSK
Length:1,260
Mass (Da):138,538
Last modified:July 3, 2019 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iED57E0C2F7A68145
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti11G → GG in ADG23056 (PubMed:21935613).Curated1
Sequence conflicti150G → GS in ADG23056 (PubMed:21935613).Curated1
Sequence conflicti167E → ET in ADG23056 (PubMed:21935613).Curated1
Sequence conflicti813L → LA in ADG23056 (PubMed:21935613).Curated1
Sequence conflicti943T → N in ADG23056 (PubMed:21935613).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
GU391030 mRNA Translation: ADG23056.1
AEMK02000070 Genomic DNA No translation available.

NCBI Reference Sequences

More...
RefSeqi
NP_001177208.1, NM_001190279.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSSSCT00000016162; ENSSSCP00000015729; ENSSSCG00000014811

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100462718

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ssc:100462718

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GU391030 mRNA Translation: ADG23056.1
AEMK02000070 Genomic DNA No translation available.
RefSeqiNP_001177208.1, NM_001190279.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Chemistry databases

SwissLipidsiSLP:000000861

Proteomic databases

PaxDbiF1SUW7

Genome annotation databases

EnsembliENSSSCT00000016162; ENSSSCP00000015729; ENSSSCG00000014811
GeneIDi100462718
KEGGissc:100462718

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3636

Phylogenomic databases

eggNOGiKOG0565 Eukaryota
KOG4384 Eukaryota
COG5411 LUCA
GeneTreeiENSGT00940000156576
InParanoidiF1SUW7
KOiK15909
OMAiHDYLKGS
OrthoDBi311217at2759
TreeFamiTF323475

Enzyme and pathway databases

ReactomeiR-SSC-1660499 Synthesis of PIPs at the plasma membrane
R-SSC-1855204 Synthesis of IP3 and IP4 in the cytosol

Gene expression databases

BgeeiENSSSCG00000014811 Expressed in 6 organ(s), highest expression level in lung
GenevisibleiD7PF45 SS

Family and domain databases

Gene3Di1.10.150.50, 1 hit
3.30.505.10, 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSHIP2_PIG
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: D7PF45
Secondary accession number(s): F1SUW7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 3, 2019
Last sequence update: July 3, 2019
Last modified: October 16, 2019
This is version 45 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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