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Protein

Phosphatidylinositide phosphatase SAC2

Gene

INPP5F

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Inositol 4-phosphatase which mainly acts on phosphatidylinositol 4-phosphate. May be functionally linked to OCRL, which converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol, for a sequential dephosphorylation of phosphatidylinositol 4,5-bisphosphate at the 5 and 4 position of inositol, thus playing an important role in the endocytic recycling (PubMed:25869669). Regulator of TF:TFRC and integrins recycling pathway, is also involved in cell migration mechanisms (PubMed:25869669). Modulates AKT/GSK3B pathway by decreasing AKT and GSK3B phosphorylation (PubMed:17322895). Negatively regulates STAT3 signaling pathway through inhibition of STAT3 phosphorylation and translocation to the nucleus (PubMed:25476455). Functionally important modulator of cardiac myocyte size and of the cardiac response to stress (By similarity). May play a role as negative regulator of axon regeneration after central nervous system injuries (By similarity).By similarity3 Publications

Catalytic activityi

Myo-inositol phosphate + H2O = myo-inositol + phosphate.2 Publications

Kineticsi

  1. KM=14.3 µM for PtdIns(4,5)P2 (at pH 6.0)1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • cardiac muscle hypertrophy in response to stress Source: UniProtKB
    • clathrin-mediated endocytosis Source: UniProtKB
    • dephosphorylation Source: ParkinsonsUK-UCL
    • negative regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
    • phosphatidylinositol catabolic process Source: UniProtKB
    • phosphatidylinositol-mediated signaling Source: UniProtKB
    • regulation of cell motility Source: UniProtKB
    • regulation of endocytic recycling Source: UniProtKB
    • regulation of protein kinase B signaling Source: Ensembl
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS12255-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositide phosphatase SAC2Curated (EC:3.1.3.252 Publications)
    Alternative name(s):
    Inositol polyphosphate 5-phosphatase FImported
    Sac domain-containing inositol phosphatase 2
    Sac domain-containing phosphoinositide 4-phosphatase 22 Publications
    Short name:
    hSAC2
    Gene namesi
    Name:INPP5FImported
    Synonyms:KIAA0966, SAC2
    ORF Names:MSTP007, MSTP047
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:17054. INPP5F.

    Subcellular locationi

    • Membraneclathrin-coated pit 1 Publication
    • Early endosome 1 Publication
    • Recycling endosome 1 Publication

    • Note: Also found on macropinosomes.By similarity

    GO - Cellular componenti

    • clathrin-coated endocytic vesicle Source: UniProtKB
    • coated pit Source: UniProtKB-KW
    • early endosome Source: UniProtKB
    • recycling endosome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Coated pit, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi458 – 4581C → S: Loss of inositol 4-phosphatase activity. Alters TFRC distribution and delays TF recycling. 1 Publication

    Organism-specific databases

    PharmGKBiPA134927878.

    Polymorphism and mutation databases

    BioMutaiINPP5F.
    DMDMi187611527.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11321132Phosphatidylinositide phosphatase SAC2PRO_0000331621Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei827 – 8271PhosphoserineBy similarity
    Modified residuei830 – 8301PhosphoserineBy similarity
    Modified residuei878 – 8781PhosphoserineBy similarity
    Modified residuei881 – 8811PhosphoserineBy similarity
    Modified residuei907 – 9071PhosphoserineBy similarity
    Modified residuei910 – 9101PhosphoserineBy similarity
    Modified residuei1103 – 11031PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    EPDiQ9Y2H2.
    MaxQBiQ9Y2H2.
    PaxDbiQ9Y2H2.
    PRIDEiQ9Y2H2.

    PTM databases

    DEPODiQ9Y2H2.
    iPTMnetiQ9Y2H2.
    PhosphoSiteiQ9Y2H2.
    SwissPalmiQ9Y2H2.

    Expressioni

    Tissue specificityi

    Ubiquitous (PubMed:11274189). Highly expressed in brain (PubMed:26203138).2 Publications

    Gene expression databases

    BgeeiQ9Y2H2.
    CleanExiHS_INPP5F.
    ExpressionAtlasiQ9Y2H2. baseline and differential.
    GenevisibleiQ9Y2H2. HS.

    Organism-specific databases

    HPAiHPA035297.
    HPA042605.

    Interactioni

    Subunit structurei

    Homodimer (PubMed:25869669). Interacts with OCRL and RAB5A (PubMed:25869668). Interacts with INPP5B and INPP4A (PubMed:25869668). Interacts with STAT3; the interaction is independent of STAT3 'TYR-705' phosphorylation status (PubMed:25476455).By similarity3 Publications

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi116543. 1 interaction.
    IntActiQ9Y2H2. 1 interaction.
    STRINGi9606.ENSP00000354519.

    Structurei

    Secondary structure

    1
    1132
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi595 – 61016Combined sources
    Beta strandi617 – 6259Combined sources
    Beta strandi639 – 65416Combined sources
    Beta strandi656 – 66813Combined sources
    Helixi669 – 6713Combined sources
    Beta strandi672 – 6798Combined sources
    Beta strandi683 – 6853Combined sources
    Beta strandi689 – 69810Combined sources
    Beta strandi701 – 71010Combined sources
    Helixi720 – 73617Combined sources
    Beta strandi743 – 7464Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4XUUX-ray2.62A/B/C/D593-760[»]
    ProteinModelPortaliQ9Y2H2.
    SMRiQ9Y2H2. Positions 593-760.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini167 – 518352SACPROSITE-ProRule annotationAdd
    BLAST
    Domaini593 – 760168hSac2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 hSac2 domain.PROSITE-ProRule annotation
    Contains 1 SAC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiKOG1890. Eukaryota.
    COG5329. LUCA.
    GeneTreeiENSGT00530000063393.
    HOGENOMiHOG000139946.
    HOVERGENiHBG095361.
    InParanoidiQ9Y2H2.
    OMAiENTGVMD.
    OrthoDBiEOG73803W.
    PhylomeDBiQ9Y2H2.
    TreeFamiTF313543.

    Family and domain databases

    InterProiIPR022158. Inositol_phosphatase.
    IPR002013. SAC_dom.
    [Graphical view]
    PfamiPF12456. hSac2. 1 hit.
    PF02383. Syja_N. 1 hit.
    [Graphical view]
    PROSITEiPS51791. HSAC2. 1 hit.
    PS50275. SAC. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9Y2H2-1) [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
    MELFQAKDHY ILQQGERALW CSRRDGGLQL RPATDLLLAW NPICLGLVEG
    60 70 80 90 100
    VIGKIQLHSD LPWWLILIRQ KALVGKLPGD HEVCKVTKIA VLSLSEMEPQ
    110 120 130 140 150
    DLELELCKKH HFGINKPEKI IPSPDDSKFL LKTFTHIKSN VSAPNKKKVK
    160 170 180 190 200
    ESKEKEKLER RLLEELLKMF MDSESFYYSL TYDLTNSVQR QSTGERDGRP
    210 220 230 240 250
    LWQKVDDRFF WNKYMIQDLT EIGTPDVDFW IIPMIQGFVQ IEELVVNYTE
    260 270 280 290 300
    SSDDEKSSPE TPPQESTCVD DIHPRFLVAL ISRRSRHRAG MRYKRRGVDK
    310 320 330 340 350
    NGNVANYVET EQLIHVHNHT LSFVQTRGSV PVFWSQVGYR YNPRPRLDRS
    360 370 380 390 400
    EKETVAYFCA HFEEQLNIYK KQVIINLVDQ AGREKIIGDA YLKQVLLFNN
    410 420 430 440 450
    SHLTYVSFDF HEHCRGMKFE NVQTLTDAIY DIILDMKWCW VDEAGVICKQ
    460 470 480 490 500
    EGIFRVNCMD CLDRTNVVQA AIARVVMEQQ LKKLGVMPPE QPLPVKCNRI
    510 520 530 540 550
    YQIMWANNGD SISRQYAGTA ALKGDFTRTG ERKLAGVMKD GVNSANRYYL
    560 570 580 590 600
    NRFKDAYRQA VIDLMQGIPV TEDLYSIFTK EKEHEALHKE NQRSHQELIS
    610 620 630 640 650
    QLLQSYMKLL LPDDEKFHGG WALIDCDPSL IDATHRDVDV LLLLSNSAYY
    660 670 680 690 700
    VAYYDDEVDK VNQYQRLSLE NLEKIEIGPE PTLFGKPKFS CMRLHYRYKE
    710 720 730 740 750
    ASGYFHTLRA VMRNPEEDGK DTLQCIAEML QITKQAMGSD LPIIEKKLER
    760 770 780 790 800
    KSSKPHEDII GIRSQNQGSL AQGKNFLMSK FSSLNQKVKQ TKSNVNIGNL
    810 820 830 840 850
    RKLGNFTKPE MKVNFLKPNL KVNLWKSDSS LETMENTGVM DKVQAESDGD
    860 870 880 890 900
    MSSDNDSYHS DEFLTNSKSD EDRQLANSLE SVGPIDYVLP SCGIIASAPR
    910 920 930 940 950
    LGSRSQSLSS TDSSVHAPSE ITVAHGSGLG KGQESPLKKS PSAGDVHILT
    960 970 980 990 1000
    GFAKPMDIYC HRFVQDAQNK VTHLSETRSV SQQASQERNQ MTNQVSNETQ
    1010 1020 1030 1040 1050
    SESTEQTPSR PSQLDVSLSA TGPQFLSVEP AHSVASQKTP TSASSMLELE
    1060 1070 1080 1090 1100
    TGLHVTPSPS ESSSSRAVSP FAKIRSSMVQ VASITQAGLT HGINFAVSKV
    1110 1120 1130
    QKSPPEPEII NQVQQNELKK MFIQCQTRII QI
    Length:1,132
    Mass (Da):128,407
    Last modified:April 29, 2008 - v3
    Checksum:i853719FC0AD455CD
    GO
    Isoform 2 (identifier: Q9Y2H2-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         373-375: VII → QQK
         376-1132: Missing.

    Show »
    Length:375
    Mass (Da):43,817
    Checksum:iE9A76393F10C6CC3
    GO
    Isoform 3 (identifier: Q9Y2H2-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         206-219: DDRFFWNKYMIQDL → PLTARRAGFALGKK
         220-1132: Missing.

    Show »
    Length:219
    Mass (Da):25,174
    Checksum:i8AAA498682414245
    GO
    Isoform 4 (identifier: Q9Y2H2-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-19: MELFQAKDHYILQQGERAL → MCHDVIFMAWLKQQFSECT
         20-629: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:522
    Mass (Da):57,800
    Checksum:i8A15030B00C8E9A1
    GO

    Sequence cautioni

    The sequence BAA76810.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti386 – 3861I → V in AAI11494 (PubMed:15489334).Curated
    Sequence conflicti654 – 6541Y → N in BAG52363 (PubMed:14702039).Curated
    Sequence conflicti1008 – 10081P → L in BAG52363 (PubMed:14702039).Curated
    Sequence conflicti1019 – 10191S → P in BAG52363 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti453 – 4531I → V.
    Corresponds to variant rs3736822 [ dbSNP | Ensembl ].
    VAR_042907
    Natural varianti997 – 9971N → D.2 Publications
    Corresponds to variant rs3188055 [ dbSNP | Ensembl ].
    VAR_042908

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1919MELFQ…GERAL → MCHDVIFMAWLKQQFSECT in isoform 4. 1 PublicationVSP_046366Add
    BLAST
    Alternative sequencei20 – 629610Missing in isoform 4. 1 PublicationVSP_046367Add
    BLAST
    Alternative sequencei206 – 21914DDRFF…MIQDL → PLTARRAGFALGKK in isoform 3. 1 PublicationVSP_033266Add
    BLAST
    Alternative sequencei220 – 1132913Missing in isoform 3. 1 PublicationVSP_033267Add
    BLAST
    Alternative sequencei373 – 3753VII → QQK in isoform 2. 1 PublicationVSP_033268
    Alternative sequencei376 – 1132757Missing in isoform 2. 1 PublicationVSP_033269Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB023183 mRNA. Translation: BAA76810.2. Different initiation.
    AK091448 mRNA. Translation: BAG52363.1.
    AC027672 Genomic DNA. No translation available.
    AL133461, AL158014 Genomic DNA. Translation: CAH72974.1.
    AL158014, AL133461 Genomic DNA. Translation: CAI16957.1.
    CH471066 Genomic DNA. Translation: EAW49379.1.
    CH471066 Genomic DNA. Translation: EAW49380.1.
    CH471066 Genomic DNA. Translation: EAW49381.1.
    BC052367 mRNA. Translation: AAH52367.1.
    BC067820 mRNA. Translation: AAH67820.1.
    BC082755 mRNA. Translation: AAH82755.1.
    BC111493 mRNA. Translation: AAI11494.1.
    AL137528 mRNA. Translation: CAB70792.1.
    AF113227 mRNA. Translation: AAG39298.1.
    AF109361 mRNA. Translation: AAQ13509.1.
    CCDSiCCDS58098.1. [Q9Y2H2-4]
    CCDS7616.1. [Q9Y2H2-1]
    PIRiT46372.
    RefSeqiNP_001230123.1. NM_001243194.1. [Q9Y2H2-4]
    NP_001230124.1. NM_001243195.1. [Q9Y2H2-3]
    NP_055752.1. NM_014937.3. [Q9Y2H2-1]
    UniGeneiHs.369755.

    Genome annotation databases

    EnsembliENST00000361976; ENSP00000354519; ENSG00000198825. [Q9Y2H2-1]
    ENST00000369080; ENSP00000358076; ENSG00000198825. [Q9Y2H2-4]
    GeneIDi22876.
    KEGGihsa:22876.
    UCSCiuc001leo.4. human. [Q9Y2H2-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB023183 mRNA. Translation: BAA76810.2. Different initiation.
    AK091448 mRNA. Translation: BAG52363.1.
    AC027672 Genomic DNA. No translation available.
    AL133461, AL158014 Genomic DNA. Translation: CAH72974.1.
    AL158014, AL133461 Genomic DNA. Translation: CAI16957.1.
    CH471066 Genomic DNA. Translation: EAW49379.1.
    CH471066 Genomic DNA. Translation: EAW49380.1.
    CH471066 Genomic DNA. Translation: EAW49381.1.
    BC052367 mRNA. Translation: AAH52367.1.
    BC067820 mRNA. Translation: AAH67820.1.
    BC082755 mRNA. Translation: AAH82755.1.
    BC111493 mRNA. Translation: AAI11494.1.
    AL137528 mRNA. Translation: CAB70792.1.
    AF113227 mRNA. Translation: AAG39298.1.
    AF109361 mRNA. Translation: AAQ13509.1.
    CCDSiCCDS58098.1. [Q9Y2H2-4]
    CCDS7616.1. [Q9Y2H2-1]
    PIRiT46372.
    RefSeqiNP_001230123.1. NM_001243194.1. [Q9Y2H2-4]
    NP_001230124.1. NM_001243195.1. [Q9Y2H2-3]
    NP_055752.1. NM_014937.3. [Q9Y2H2-1]
    UniGeneiHs.369755.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4XUUX-ray2.62A/B/C/D593-760[»]
    ProteinModelPortaliQ9Y2H2.
    SMRiQ9Y2H2. Positions 593-760.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116543. 1 interaction.
    IntActiQ9Y2H2. 1 interaction.
    STRINGi9606.ENSP00000354519.

    PTM databases

    DEPODiQ9Y2H2.
    iPTMnetiQ9Y2H2.
    PhosphoSiteiQ9Y2H2.
    SwissPalmiQ9Y2H2.

    Polymorphism and mutation databases

    BioMutaiINPP5F.
    DMDMi187611527.

    Proteomic databases

    EPDiQ9Y2H2.
    MaxQBiQ9Y2H2.
    PaxDbiQ9Y2H2.
    PRIDEiQ9Y2H2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000361976; ENSP00000354519; ENSG00000198825. [Q9Y2H2-1]
    ENST00000369080; ENSP00000358076; ENSG00000198825. [Q9Y2H2-4]
    GeneIDi22876.
    KEGGihsa:22876.
    UCSCiuc001leo.4. human. [Q9Y2H2-1]

    Organism-specific databases

    CTDi22876.
    GeneCardsiINPP5F.
    HGNCiHGNC:17054. INPP5F.
    HPAiHPA035297.
    HPA042605.
    MIMi609389. gene.
    neXtProtiNX_Q9Y2H2.
    PharmGKBiPA134927878.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1890. Eukaryota.
    COG5329. LUCA.
    GeneTreeiENSGT00530000063393.
    HOGENOMiHOG000139946.
    HOVERGENiHBG095361.
    InParanoidiQ9Y2H2.
    OMAiENTGVMD.
    OrthoDBiEOG73803W.
    PhylomeDBiQ9Y2H2.
    TreeFamiTF313543.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS12255-MONOMER.

    Miscellaneous databases

    ChiTaRSiINPP5F. human.
    GenomeRNAii22876.
    NextBioi35469521.
    PROiQ9Y2H2.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9Y2H2.
    CleanExiHS_INPP5F.
    ExpressionAtlasiQ9Y2H2. baseline and differential.
    GenevisibleiQ9Y2H2. HS.

    Family and domain databases

    InterProiIPR022158. Inositol_phosphatase.
    IPR002013. SAC_dom.
    [Graphical view]
    PfamiPF12456. hSac2. 1 hit.
    PF02383. Syja_N. 1 hit.
    [Graphical view]
    PROSITEiPS51791. HSAC2. 1 hit.
    PS50275. SAC. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification and characterization of a sac domain-containing phosphoinositide 5-phosphatase."
      Minagawa T., Ijuin T., Mochizuki Y., Takenawa T.
      J. Biol. Chem. 276:22011-22015(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, CAUTION.
    2. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-997.
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Brain.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1; 2 AND 3), VARIANT ASP-997.
      Tissue: Placenta and Skin.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 274-1132 (ISOFORM 1).
      Tissue: Testis.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 956-1132 (ISOFORM 1).
      Tissue: Aorta.
    9. Cited for: FUNCTION.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    14. "Inositol Polyphosphate-5-Phosphatase F (INPP5F) inhibits STAT3 activity and suppresses gliomas tumorigenicity."
      Kim H.S., Li A., Ahn S., Song H., Zhang W.
      Sci. Rep. 4:7330-7330(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH STAT3.
    15. "Sac2/INPP5F is an inositol 4-phosphatase that functions in the endocytic pathway."
      Nakatsu F., Messa M., Nandez R., Czapla H., Zou Y., Strittmatter S.M., De Camilli P.
      J. Cell Biol. 209:85-95(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP4A; INPP5B AND OCRL.
    16. "Gene-silencing screen for mammalian axon regeneration identifies Inpp5f (Sac2) as an endogenous suppressor of repair after spinal cord injury."
      Zou Y., Stagi M., Wang X., Yigitkanli K., Siegel C.S., Nakatsu F., Cafferty W.B., Strittmatter S.M.
      J. Neurosci. 35:10429-10439(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    17. "Spatiotemporal control of phosphatidylinositol 4-phosphate by Sac2 regulates endocytic recycling."
      Hsu F., Hu F., Mao Y.
      J. Cell Biol. 209:97-110(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 593-760, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-458.

    Entry informationi

    Entry nameiSAC2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2H2
    Secondary accession number(s): B3KRF1
    , D3DRD1, Q2T9J4, Q5W135, Q5W136, Q6NVY2, Q86U97, Q9H3D9, Q9NT51
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: April 29, 2008
    Last modified: May 11, 2016
    This is version 112 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    INPP5F has been initially described as an inositol polyphosphate 5-phosphatase.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.