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Protein

Phosphatidylinositide phosphatase SAC2

Gene

Inpp5f

Organism
Mus musculus (Mouse)
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:25869668, PubMed:25869669). Regulator of TF:TFRC and integrins recycling pathway, is also involved in cell migration mechanisms (By similarity). 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 (By similarity). Functionally important modulator of cardiac myocyte size and of the cardiac response to stress (PubMed:19875726). May play a role as negative regulator of axon regeneration after central nervous system injuries (PubMed:26203138).By similarity5 Publications

Catalytic activityi

Myo-inositol phosphate + H2O = myo-inositol + phosphate.By similarity

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

ReactomeiR-MMU-1660516. Synthesis of PIPs at the early endosome membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositide phosphatase SAC2 (EC:3.1.3.25By similarity1 Publication)
Alternative name(s):
Inositol polyphosphate 5-phosphatase FImported
Sac domain-containing inositol phosphatase 2
Sac domain-containing phosphoinositide 4-phosphatase 21 Publication
Short name:
hSAC2
Gene namesi
Name:Inpp5fImported
Synonyms:Kiaa0966, Sac2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2141867. Inpp5f.

Subcellular locationi

GO - Cellular componenti

  • axon Source: ParkinsonsUK-UCL
  • clathrin-coated endocytic vesicle Source: UniProtKB
  • coated pit Source: UniProtKB-SubCell
  • cytoplasm Source: ParkinsonsUK-UCL
  • dendrite Source: ParkinsonsUK-UCL
  • early endosome Source: UniProtKB
  • neuronal cell body Source: ParkinsonsUK-UCL
  • recycling endosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Animals develop normal corticospinal tract and raphespinal tract. Mutants show greater axonal growth and functional recovery after central nervous system trauma (PubMed:26203138). Knockout mice have normal cardiac form and function but show augmented hypertrophy and reactivation of the fetal gene program in response to stress compared to wild-type littermates (PubMed:19875726).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi460 – 4601D → A: Has a diffuse cytosolic localization. 1 Publication
Mutagenesisi460 – 4601D → N: Loss of inositol 4-phosphatase activity. No effect on subcellular localization. No effect on interaction with OCRL, INPP5B and IPP4A. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11321132Phosphatidylinositide phosphatase SAC2PRO_0000331622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei714 – 7141PhosphoserineCombined sources
Modified residuei827 – 8271PhosphoserineCombined sources
Modified residuei830 – 8301PhosphoserineCombined sources
Modified residuei879 – 8791PhosphoserineCombined sources
Modified residuei882 – 8821PhosphoserineCombined sources
Modified residuei908 – 9081PhosphoserineCombined sources
Modified residuei911 – 9111PhosphoserineCombined sources
Modified residuei1103 – 11031PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8CDA1.
MaxQBiQ8CDA1.
PaxDbiQ8CDA1.
PeptideAtlasiQ8CDA1.
PRIDEiQ8CDA1.

PTM databases

iPTMnetiQ8CDA1.
PhosphoSiteiQ8CDA1.

Expressioni

Tissue specificityi

Highly expressed in brain and hypothalamus, expressed in lung and pancreas, and detected at low levels in liver and heart (at protein level).2 Publications

Inductioni

Up-regulated in the absence of histone deacetylase 2/HDAC2 in the heart from HDAC2-null mice.1 Publication

Gene expression databases

BgeeiQ8CDA1.
ExpressionAtlasiQ8CDA1. baseline and differential.
GenevisibleiQ8CDA1. MM.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with OCRL and RAB5. Interacts with INPP5B and INPP4A (PubMed:25869668). Interacts with STAT3; the interaction is independent of STAT3 'TYR-705' phosphorylation status (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000045910.

Structurei

3D structure databases

ProteinModelPortaliQ8CDA1.
SMRiQ8CDA1. 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.
HOGENOMiHOG000046510.
HOVERGENiHBG095361.
InParanoidiQ8CDA1.
OMAiENTGVMD.
OrthoDBiEOG73803W.
PhylomeDBiQ8CDA1.
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: Q8CDA1-1) [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
ELELELCKKH HFGINKPEKI IPSPDDSKFL LKTFTNIKSN VSAPNKKKVK
160 170 180 190 200
ESKEKEKLER RLLEELLKMF MDSESFYYSL TYDLTNSVQR QSTGERDGRP
210 220 230 240 250
LWQKVDDRFF WNKYMIQALT EIGTPDVDFW IIPIIQGFVQ IEELVVNYNE
260 270 280 290 300
SSDDDKSSPE TPPQDSTCVD DIHPRFLVAL ISRRSRHRAG MRYKRRGVDK
310 320 330 340 350
NGNVANYVET EQLIHVHHHT LSFIQTRGSV PVFWSQVGYR YNPRPRLDKS
360 370 380 390 400
EKETVDCFCA HFEEQLKIYK KQVIVNLVDQ AGREKIIGDA YLKQVLLFNN
410 420 430 440 450
PKLTYVSFDF HEHCRGMKFE NVQTLTDAIH DIIIDMKWCW VDQAGVICKQ
460 470 480 490 500
EGIFRVNCMD CLDRTNVVQA AIARVVMEQQ LKKLGVMPPE QPLPVKCNRT
510 520 530 540 550
YQIMWANNGD SISRQYAGTA ALKGDFTRTG ERKLAGVMKD GVNSANRYYL
560 570 580 590 600
SRFKDAYRQA VIDLMQGVPV TEDLYSIFTK EKEHEALHKE SQRSHQELIS
610 620 630 640 650
QLLQSYMQLL LPGDEKFHGG WALVDCDPSL TDAAHRDVEV LLLLSNAAYY
660 670 680 690 700
VAYYDDEVDK VNQYQRLGLE DLERIEIGPE PTLFGKPKFS CMRLHYRCKE
710 720 730 740 750
AGGYFHTLRA VPRSPEEDGK DTLQCIAEML QITKQAMGLD VPIIEKKLER
760 770 780 790 800
KSSKPHEDII GIRSQNQGSL AQGKSFLMSK FSSLNQKVKQ TKSNVNIGNL
810 820 830 840 850
RKLGNFTKPE MKVNFLKPNL KVNLWKSDSS LETMENPGVM GNKVQGESDG
860 870 880 890 900
DISSDNDSYH SDEFLTNSKS EEDKQLANSL ESVGPIDYIL PSCGIIVSAP
910 920 930 940 950
RLGSRSQSAS SIDVSTHAPS EAAAGPGSEL GKGLESPLKK SPSADSIHTR
960 970 980 990 1000
TGFTKPMDVY CQRFVQDAQN KMNDLSEIRS VAQKSEEGSH KTNRVSNEET
1010 1020 1030 1040 1050
QSEPMGQTPP RPSQLNVSCS VAGPPFLSVE PVHSVLSQKT PSSGSSLLEL
1060 1070 1080 1090 1100
EAGLCVTPSS ESSSSRAVSP FAKIRSSMVQ VANITQAGLT HGINLAVAKV
1110 1120 1130
QKSPAEPEAV NEIQQNELKN MFTQCQTRII QI
Length:1,132
Mass (Da):127,608
Last modified:March 1, 2003 - v1
Checksum:i4EDEA936E95D486C
GO
Isoform 2 (identifier: Q8CDA1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-627: Missing.
     628-629: PS → MH

Show »
Length:505
Mass (Da):55,241
Checksum:iD23C6ACE913BFB85
GO
Isoform 3 (identifier: Q8CDA1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-691: Missing.

Show »
Length:441
Mass (Da):47,885
Checksum:i4C855E8EBE10F926
GO
Isoform 4 (identifier: Q8CDA1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     373-414: VIVNLVDQAG...YVSFDFHEHC → RIWVWSQHPL...REEKRREEVT
     415-1132: Missing.

Show »
Length:414
Mass (Da):48,995
Checksum:i851CDFAF785F1EF6
GO

Sequence cautioni

The sequence BAC28723.1 differs from that shown. Reason: Frameshift at position 692. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti728 – 7281E → D in AAH67200 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 691691Missing in isoform 3. 1 PublicationVSP_033270Add
BLAST
Alternative sequencei1 – 627627Missing in isoform 2. 1 PublicationVSP_033271Add
BLAST
Alternative sequencei373 – 41442VIVNL…FHEHC → RIWVWSQHPLTQREEKRREE KRREEKRREEKRREEKRREE VT in isoform 4. 1 PublicationVSP_033272Add
BLAST
Alternative sequencei415 – 1132718Missing in isoform 4. 1 PublicationVSP_033273Add
BLAST
Alternative sequencei628 – 6292PS → MH in isoform 2. 1 PublicationVSP_033274

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129249 mRNA. Translation: BAC98059.1.
AK030870 mRNA. Translation: BAC27166.1.
AK034482 mRNA. Translation: BAC28723.1. Frameshift.
AK047166 mRNA. Translation: BAC32978.1.
AK150418 mRNA. Translation: BAE29542.1.
BC067200 mRNA. Translation: AAH67200.1.
BC125437 mRNA. Translation: AAI25438.1.
CCDSiCCDS21899.1. [Q8CDA1-1]
RefSeqiNP_848756.2. NM_178641.5. [Q8CDA1-1]
XP_006507217.1. XM_006507154.2. [Q8CDA1-2]
XP_006507218.1. XM_006507155.2. [Q8CDA1-2]
UniGeneiMm.490344.

Genome annotation databases

EnsembliENSMUST00000043138; ENSMUSP00000045910; ENSMUSG00000042105. [Q8CDA1-1]
ENSMUST00000118605; ENSMUSP00000113700; ENSMUSG00000042105. [Q8CDA1-2]
ENSMUST00000151237; ENSMUSP00000146197; ENSMUSG00000042105. [Q8CDA1-3]
GeneIDi101490.
KEGGimmu:101490.
UCSCiuc009jzc.1. mouse. [Q8CDA1-1]
uc009jzf.1. mouse. [Q8CDA1-3]
uc009jzg.1. mouse. [Q8CDA1-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129249 mRNA. Translation: BAC98059.1.
AK030870 mRNA. Translation: BAC27166.1.
AK034482 mRNA. Translation: BAC28723.1. Frameshift.
AK047166 mRNA. Translation: BAC32978.1.
AK150418 mRNA. Translation: BAE29542.1.
BC067200 mRNA. Translation: AAH67200.1.
BC125437 mRNA. Translation: AAI25438.1.
CCDSiCCDS21899.1. [Q8CDA1-1]
RefSeqiNP_848756.2. NM_178641.5. [Q8CDA1-1]
XP_006507217.1. XM_006507154.2. [Q8CDA1-2]
XP_006507218.1. XM_006507155.2. [Q8CDA1-2]
UniGeneiMm.490344.

3D structure databases

ProteinModelPortaliQ8CDA1.
SMRiQ8CDA1. Positions 593-760.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000045910.

PTM databases

iPTMnetiQ8CDA1.
PhosphoSiteiQ8CDA1.

Proteomic databases

EPDiQ8CDA1.
MaxQBiQ8CDA1.
PaxDbiQ8CDA1.
PeptideAtlasiQ8CDA1.
PRIDEiQ8CDA1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043138; ENSMUSP00000045910; ENSMUSG00000042105. [Q8CDA1-1]
ENSMUST00000118605; ENSMUSP00000113700; ENSMUSG00000042105. [Q8CDA1-2]
ENSMUST00000151237; ENSMUSP00000146197; ENSMUSG00000042105. [Q8CDA1-3]
GeneIDi101490.
KEGGimmu:101490.
UCSCiuc009jzc.1. mouse. [Q8CDA1-1]
uc009jzf.1. mouse. [Q8CDA1-3]
uc009jzg.1. mouse. [Q8CDA1-2]

Organism-specific databases

CTDi22876.
MGIiMGI:2141867. Inpp5f.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1890. Eukaryota.
COG5329. LUCA.
GeneTreeiENSGT00530000063393.
HOGENOMiHOG000046510.
HOVERGENiHBG095361.
InParanoidiQ8CDA1.
OMAiENTGVMD.
OrthoDBiEOG73803W.
PhylomeDBiQ8CDA1.
TreeFamiTF313543.

Enzyme and pathway databases

ReactomeiR-MMU-1660516. Synthesis of PIPs at the early endosome membrane.

Miscellaneous databases

PROiQ8CDA1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CDA1.
ExpressionAtlasiQ8CDA1. baseline and differential.
GenevisibleiQ8CDA1. MM.

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. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Embryonic tail.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Bone marrow, Cerebellum, Diencephalon and Thymus.
  3. "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 AND 2).
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Cited for: FUNCTION, INDUCTION.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Inpp5f is a polyphosphoinositide phosphatase that regulates cardiac hypertrophic responsiveness."
    Zhu W., Trivedi C.M., Zhou D., Yuan L., Lu M.M., Epstein J.A.
    Circ. Res. 105:1240-1247(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714; SER-827; SER-830; SER-879; SER-882; SER-908; SER-911 AND SER-1103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "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: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH INPP4A; INPP5B; OCRL AND RAB5A, MUTAGENESIS OF ASP-460.
  9. "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: FUNCTION, TISSUE SPECIFICITY.
  10. "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: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiSAC2_MOUSE
AccessioniPrimary (citable) accession number: Q8CDA1
Secondary accession number(s): Q3UCS0
, Q6NX83, Q6ZQ16, Q8C8G7, Q8CBW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

INPP5F has been initially described as an inositol polyphosphate 5-phosphatase.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.