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Protein

Phosphatidylinositide phosphatase SAC2

Gene

INPP5F

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Inositol 5-phosphatase which acts on phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Hydrolyzes phosphatidylinositol 4,5-bisphosphate most effectively. Modulates AKT/GSK3B pathway by decreasing AKT and GSK3B phosphorylation.2 Publications

Kineticsi

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

GO - Molecular functioni

  1. phosphoric ester hydrolase activity Source: InterPro

GO - Biological processi

  1. cardiac muscle hypertrophy in response to stress Source: Ensembl
  2. phosphatidylinositol catabolic process Source: Ensembl
  3. phosphatidylinositol-mediated signaling Source: Ensembl
  4. 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 SAC2 (EC:3.1.3.-)
Alternative name(s):
Inositol polyphosphate 5-phosphatase F
Sac domain-containing inositol phosphatase 2
Sac domain-containing phosphoinositide 5-phosphatase 2
Short name:
hSAC2
Gene namesi
Name:INPP5F
Synonyms:KIAA0966, SAC2
ORF Names:MSTP007, MSTP047
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:17054. INPP5F.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi460 – 4601D → A: Loss of phosphatase activity. 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

Proteomic databases

MaxQBiQ9Y2H2.
PaxDbiQ9Y2H2.
PRIDEiQ9Y2H2.

PTM databases

DEPODiQ9Y2H2.
PhosphoSiteiQ9Y2H2.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9Y2H2.
CleanExiHS_INPP5F.
ExpressionAtlasiQ9Y2H2. baseline and differential.
GenevestigatoriQ9Y2H2.

Organism-specific databases

HPAiHPA035297.
HPA042605.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XUUX-ray2.62A/B/C/D593-760[»]
SMRiQ9Y2H2. Positions 165-513.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 SAC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5329.
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]
PROSITEiPS50275. 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. 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.
UCSCiuc001len.4. human. [Q9Y2H2-3]
uc001leo.3. human. [Q9Y2H2-1]

Polymorphism and mutation databases

BioMutaiINPP5F.

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[»]
SMRiQ9Y2H2. Positions 165-513.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

DEPODiQ9Y2H2.
PhosphoSiteiQ9Y2H2.

Polymorphism and mutation databases

BioMutaiINPP5F.
DMDMi187611527.

Proteomic databases

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.
UCSCiuc001len.4. human. [Q9Y2H2-3]
uc001leo.3. human. [Q9Y2H2-1]

Organism-specific databases

CTDi22876.
GeneCardsiGC10P121485.
HGNCiHGNC:17054. INPP5F.
HPAiHPA035297.
HPA042605.
MIMi609389. gene.
neXtProtiNX_Q9Y2H2.
PharmGKBiPA134927878.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5329.
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.
GenevestigatoriQ9Y2H2.

Family and domain databases

InterProiIPR022158. Inositol_phosphatase.
IPR002013. SAC_dom.
[Graphical view]
PfamiPF12456. hSac2. 1 hit.
PF02383. Syja_N. 1 hit.
[Graphical view]
PROSITEiPS50275. 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), FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-460, TISSUE SPECIFICITY.
  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.

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: April 29, 2015
This is version 101 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

Miscellaneous

Inositol polyphosphate 5-phosphatases usually have 2 conserved motifs that are essential for 5-phosphatase activity. However, INPP5F does not contain such motifs, and phosphatase activity seems to exist in the SAC domain, suggesting a new type of phosphoinositide 5-phosphatase.

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

External Data

Dasty 3

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 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.