Full text data of SACM1L
SACM1L
(KIAA0851)
[Confidence: high (present in two of the MS resources)]
Phosphatidylinositide phosphatase SAC1; 3.1.3.- (Suppressor of actin mutations 1-like protein)
Phosphatidylinositide phosphatase SAC1; 3.1.3.- (Suppressor of actin mutations 1-like protein)
hRBCD
IPI00022275
IPI00022275 KIAA0851 protein KIAA0851 protein membrane n/a n/a n/a n/a 2 n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a 2 n/a n/a n/a n/a cytoskeleton associated n/a found at its expected molecular weight found at molecular weight
IPI00022275 KIAA0851 protein KIAA0851 protein membrane n/a n/a n/a n/a 2 n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a 2 n/a n/a n/a n/a cytoskeleton associated n/a found at its expected molecular weight found at molecular weight
UniProt
Q9NTJ5
ID SAC1_HUMAN Reviewed; 587 AA.
AC Q9NTJ5; A8K527; O94935; Q7LA14; Q7LA22; Q96AX7; Q9NQ46; Q9NQ57;
read moreDT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 22-JAN-2014, entry version 85.
DE RecName: Full=Phosphatidylinositide phosphatase SAC1;
DE EC=3.1.3.-;
DE AltName: Full=Suppressor of actin mutations 1-like protein;
GN Name=SACM1L; Synonyms=KIAA0851;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11352561; DOI=10.1006/geno.2000.6498;
RA Kiss H., Kedra D., Kiss C., Kost-Alimova M., Yang Y., Klein G.,
RA Imreh S., Dumanski J.P.;
RT "The LZTFL1 gene is a part of a transcriptional map covering 250 kb
RT within the common eliminated region 1 (C3CER1) in 3p21.3.";
RL Genomics 73:10-19(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-434.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-434.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-434.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-456, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P
CC and PtdIns(4)P. Has low activity towards PtdIns(3,5)P2 (By
CC similarity).
CC -!- INTERACTION:
CC Q9Y678:COPG1; NbExp=3; IntAct=EBI-3917235, EBI-1049127;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein (By similarity).
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, lung, liver, kidney,
CC pancreas and testis.
CC -!- SIMILARITY: Contains 1 SAC domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74874.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ297357; CAB95945.1; -; Genomic_DNA.
DR EMBL; AJ289880; CAB96871.1; -; Genomic_DNA.
DR EMBL; AB020658; BAA74874.2; ALT_INIT; mRNA.
DR EMBL; AL136831; CAB66765.1; -; mRNA.
DR EMBL; AK291142; BAF83831.1; -; mRNA.
DR EMBL; BC016559; AAH16559.1; -; mRNA.
DR PIR; T46447; T46447.
DR RefSeq; NP_054735.3; NM_014016.3.
DR UniGene; Hs.156509; -.
DR ProteinModelPortal; Q9NTJ5; -.
DR SMR; Q9NTJ5; 46-453.
DR IntAct; Q9NTJ5; 9.
DR MINT; MINT-4723852; -.
DR STRING; 9606.ENSP00000373713; -.
DR PhosphoSite; Q9NTJ5; -.
DR DMDM; 167016563; -.
DR PaxDb; Q9NTJ5; -.
DR PRIDE; Q9NTJ5; -.
DR DNASU; 22908; -.
DR Ensembl; ENST00000389061; ENSP00000373713; ENSG00000211456.
DR GeneID; 22908; -.
DR KEGG; hsa:22908; -.
DR UCSC; uc003cos.2; human.
DR CTD; 22908; -.
DR GeneCards; GC03P045730; -.
DR H-InvDB; HIX0021677; -.
DR HGNC; HGNC:17059; SACM1L.
DR HPA; HPA039573; -.
DR MIM; 606569; gene.
DR neXtProt; NX_Q9NTJ5; -.
DR PharmGKB; PA34925; -.
DR eggNOG; COG5329; -.
DR HOVERGEN; HBG108454; -.
DR InParanoid; Q9NTJ5; -.
DR OMA; ISKVANH; -.
DR OrthoDB; EOG73803W; -.
DR BioCyc; MetaCyc:HS11932-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; SACM1L; human.
DR GeneWiki; SACM1L; -.
DR GenomeRNAi; 22908; -.
DR NextBio; 43577; -.
DR PRO; PR:Q9NTJ5; -.
DR ArrayExpress; Q9NTJ5; -.
DR Bgee; Q9NTJ5; -.
DR CleanEx; HS_SACM1L; -.
DR Genevestigator; Q9NTJ5; -.
DR GO; GO:0032281; C:alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral to endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0034593; F:phosphatidylinositol bisphosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IEA:Ensembl.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:Ensembl.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR InterPro; IPR002013; Syja_N.
DR Pfam; PF02383; Syja_N; 1.
DR PROSITE; PS50275; SAC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Endoplasmic reticulum; Hydrolase;
KW Membrane; Polymorphism; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 587 Phosphatidylinositide phosphatase SAC1.
FT /FTId=PRO_0000317171.
FT TRANSMEM 56 76 Helical; (Potential).
FT TRANSMEM 521 541 Helical; (Potential).
FT TRANSMEM 549 569 Helical; (Potential).
FT DOMAIN 122 451 SAC.
FT MOD_RES 456 456 N6-acetyllysine.
FT VARIANT 434 434 Y -> F (in dbSNP:rs1468542).
FT /FTId=VAR_038484.
FT CONFLICT 45 45 K -> E (in Ref. 4; BAF83831).
FT CONFLICT 376 376 Q -> R (in Ref. 3; CAB66765).
SQ SEQUENCE 587 AA; 66967 MW; 3E0FC7515D15A071 CRC64;
MATAAYEQLK LHITPEKFYV EACDDGADDV LTIDRVSTEV TLAVKKDVPP SAVTRPIFGI
LGTIHLVAGN YLIVITKKIK VGEFFSHVVW KATDFDVLSY KKTMLHLTDI QLQDNKTFLA
MLNHVLNVDG FYFSTTYDLT HTLQRLSNTS PEFQEMSLLE RADQRFVWNG HLLRELSAQP
EVHRFALPVL HGFITMHSCS INGKYFDWIL ISRRSCFRAG VRYYVRGIDS EGHAANFVET
EQIVHYNGSK ASFVQTRGSI PVFWSQRPNL KYKPLPQISK VANHMDGFQR HFDSQVIIYG
KQVIINLINQ KGSEKPLEQT FATMVSSLGS GMMRYIAFDF HKECKNMRWD RLSILLDQVA
EMQDELSYFL VDSAGQVVAN QEGVFRSNCM DCLDRTNVIQ SLLARRSLQA QLQRLGVLHV
GQKLEEQDEF EKIYKNAWAD NANACAKQYA GTGALKTDFT RTGKRTHLGL IMDGWNSMIR
YYKNNFSDGF RQDSIDLFLG NYSVDELESH SPLSVPRDWK FLALPIIMVV AFSMCIICLL
MAGDTWTETL AYVLFWGVAS IGTFFIILYN GKDFVDAPRL VQKEKID
//
ID SAC1_HUMAN Reviewed; 587 AA.
AC Q9NTJ5; A8K527; O94935; Q7LA14; Q7LA22; Q96AX7; Q9NQ46; Q9NQ57;
read moreDT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 22-JAN-2014, entry version 85.
DE RecName: Full=Phosphatidylinositide phosphatase SAC1;
DE EC=3.1.3.-;
DE AltName: Full=Suppressor of actin mutations 1-like protein;
GN Name=SACM1L; Synonyms=KIAA0851;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11352561; DOI=10.1006/geno.2000.6498;
RA Kiss H., Kedra D., Kiss C., Kost-Alimova M., Yang Y., Klein G.,
RA Imreh S., Dumanski J.P.;
RT "The LZTFL1 gene is a part of a transcriptional map covering 250 kb
RT within the common eliminated region 1 (C3CER1) in 3p21.3.";
RL Genomics 73:10-19(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-434.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-434.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-434.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-456, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P
CC and PtdIns(4)P. Has low activity towards PtdIns(3,5)P2 (By
CC similarity).
CC -!- INTERACTION:
CC Q9Y678:COPG1; NbExp=3; IntAct=EBI-3917235, EBI-1049127;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein (By similarity).
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, lung, liver, kidney,
CC pancreas and testis.
CC -!- SIMILARITY: Contains 1 SAC domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74874.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ297357; CAB95945.1; -; Genomic_DNA.
DR EMBL; AJ289880; CAB96871.1; -; Genomic_DNA.
DR EMBL; AB020658; BAA74874.2; ALT_INIT; mRNA.
DR EMBL; AL136831; CAB66765.1; -; mRNA.
DR EMBL; AK291142; BAF83831.1; -; mRNA.
DR EMBL; BC016559; AAH16559.1; -; mRNA.
DR PIR; T46447; T46447.
DR RefSeq; NP_054735.3; NM_014016.3.
DR UniGene; Hs.156509; -.
DR ProteinModelPortal; Q9NTJ5; -.
DR SMR; Q9NTJ5; 46-453.
DR IntAct; Q9NTJ5; 9.
DR MINT; MINT-4723852; -.
DR STRING; 9606.ENSP00000373713; -.
DR PhosphoSite; Q9NTJ5; -.
DR DMDM; 167016563; -.
DR PaxDb; Q9NTJ5; -.
DR PRIDE; Q9NTJ5; -.
DR DNASU; 22908; -.
DR Ensembl; ENST00000389061; ENSP00000373713; ENSG00000211456.
DR GeneID; 22908; -.
DR KEGG; hsa:22908; -.
DR UCSC; uc003cos.2; human.
DR CTD; 22908; -.
DR GeneCards; GC03P045730; -.
DR H-InvDB; HIX0021677; -.
DR HGNC; HGNC:17059; SACM1L.
DR HPA; HPA039573; -.
DR MIM; 606569; gene.
DR neXtProt; NX_Q9NTJ5; -.
DR PharmGKB; PA34925; -.
DR eggNOG; COG5329; -.
DR HOVERGEN; HBG108454; -.
DR InParanoid; Q9NTJ5; -.
DR OMA; ISKVANH; -.
DR OrthoDB; EOG73803W; -.
DR BioCyc; MetaCyc:HS11932-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; SACM1L; human.
DR GeneWiki; SACM1L; -.
DR GenomeRNAi; 22908; -.
DR NextBio; 43577; -.
DR PRO; PR:Q9NTJ5; -.
DR ArrayExpress; Q9NTJ5; -.
DR Bgee; Q9NTJ5; -.
DR CleanEx; HS_SACM1L; -.
DR Genevestigator; Q9NTJ5; -.
DR GO; GO:0032281; C:alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral to endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0034593; F:phosphatidylinositol bisphosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IEA:Ensembl.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:Ensembl.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR InterPro; IPR002013; Syja_N.
DR Pfam; PF02383; Syja_N; 1.
DR PROSITE; PS50275; SAC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Endoplasmic reticulum; Hydrolase;
KW Membrane; Polymorphism; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 587 Phosphatidylinositide phosphatase SAC1.
FT /FTId=PRO_0000317171.
FT TRANSMEM 56 76 Helical; (Potential).
FT TRANSMEM 521 541 Helical; (Potential).
FT TRANSMEM 549 569 Helical; (Potential).
FT DOMAIN 122 451 SAC.
FT MOD_RES 456 456 N6-acetyllysine.
FT VARIANT 434 434 Y -> F (in dbSNP:rs1468542).
FT /FTId=VAR_038484.
FT CONFLICT 45 45 K -> E (in Ref. 4; BAF83831).
FT CONFLICT 376 376 Q -> R (in Ref. 3; CAB66765).
SQ SEQUENCE 587 AA; 66967 MW; 3E0FC7515D15A071 CRC64;
MATAAYEQLK LHITPEKFYV EACDDGADDV LTIDRVSTEV TLAVKKDVPP SAVTRPIFGI
LGTIHLVAGN YLIVITKKIK VGEFFSHVVW KATDFDVLSY KKTMLHLTDI QLQDNKTFLA
MLNHVLNVDG FYFSTTYDLT HTLQRLSNTS PEFQEMSLLE RADQRFVWNG HLLRELSAQP
EVHRFALPVL HGFITMHSCS INGKYFDWIL ISRRSCFRAG VRYYVRGIDS EGHAANFVET
EQIVHYNGSK ASFVQTRGSI PVFWSQRPNL KYKPLPQISK VANHMDGFQR HFDSQVIIYG
KQVIINLINQ KGSEKPLEQT FATMVSSLGS GMMRYIAFDF HKECKNMRWD RLSILLDQVA
EMQDELSYFL VDSAGQVVAN QEGVFRSNCM DCLDRTNVIQ SLLARRSLQA QLQRLGVLHV
GQKLEEQDEF EKIYKNAWAD NANACAKQYA GTGALKTDFT RTGKRTHLGL IMDGWNSMIR
YYKNNFSDGF RQDSIDLFLG NYSVDELESH SPLSVPRDWK FLALPIIMVV AFSMCIICLL
MAGDTWTETL AYVLFWGVAS IGTFFIILYN GKDFVDAPRL VQKEKID
//
MIM
606569
*RECORD*
*FIELD* NO
606569
*FIELD* TI
*606569 SUPPRESSOR OF ACTIN MUTATIONS 1-LIKE; SACM1L
;;SUPPRESSOR OF ACTIN 1; SAC1;;
read moreKIAA0851
*FIELD* TX
CLONING
By screening for cDNAs with the potential to encode large proteins
expressed in brain, Nagase et al. (2000) identified a cDNA encoding
SAC1, which they called KIAA0851, a 587-amino acid protein with 34%
sequence identity with the yeast RSD1 (recessive suppressor of secretory
defect) protein. RT-PCR detected expression of SAC1 in heart, brain,
lung, liver, kidney, pancreas, testis, and ovary, and less abundant
expression in skeletal muscle and spleen.
Kiss et al. (2001) cloned mouse Sac1 which encodes a protein sharing 95%
sequence identity with human SAC1. Both contain 2 transmembrane regions
and a leucine zipper pattern. Both are predicted to be cytoplasmic
proteins in the endoplasmic reticulum. Northern blot analysis in mouse
showed high expression of a 4-kb transcript in brain, lung, liver, and
kidney. A lower level of expression was seen in spleen and skeletal
muscle, and no expression was observed in heart or testis.
GENE STRUCTURE
Kiss et al. (2001) determined that the SAC1 gene contains 20 exons and
spans 55.7 kb. It has a large first intron of approximately 14 kb.
MAPPING
By sequence analysis, Kiss et al. (2001) mapped the SAC1 gene within a
250-kb putative tumor suppressor region on chromosome 3p21.3.
*FIELD* RF
1. Kiss, H.; Kedra, D.; Kiss, C.; Kost-Alimova, M.; Yang, Y.; Klein,
G.; Imreh, S.; Dumanski, J. P.: The LZTFL1 gene is a part of a transcriptional
map covering 250 kb within the common eliminated region 1 (C3CER1)
in 3p21.3. Genomics 73: 10-19, 2001.
2. Nagase, T.; Kikuno, R.; Hattori, A.; Kondo, Y.; Okumura, K.; Ohara,
O.: Prediction of the coding sequences of unidentified human genes.
XIX. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro. DNA Res. 7: 347-355, 2000.
*FIELD* CD
Carol A. Bocchini: 12/18/2001
*FIELD* ED
carol: 01/15/2002
carol: 12/20/2001
terry: 12/19/2001
carol: 12/18/2001
*RECORD*
*FIELD* NO
606569
*FIELD* TI
*606569 SUPPRESSOR OF ACTIN MUTATIONS 1-LIKE; SACM1L
;;SUPPRESSOR OF ACTIN 1; SAC1;;
read moreKIAA0851
*FIELD* TX
CLONING
By screening for cDNAs with the potential to encode large proteins
expressed in brain, Nagase et al. (2000) identified a cDNA encoding
SAC1, which they called KIAA0851, a 587-amino acid protein with 34%
sequence identity with the yeast RSD1 (recessive suppressor of secretory
defect) protein. RT-PCR detected expression of SAC1 in heart, brain,
lung, liver, kidney, pancreas, testis, and ovary, and less abundant
expression in skeletal muscle and spleen.
Kiss et al. (2001) cloned mouse Sac1 which encodes a protein sharing 95%
sequence identity with human SAC1. Both contain 2 transmembrane regions
and a leucine zipper pattern. Both are predicted to be cytoplasmic
proteins in the endoplasmic reticulum. Northern blot analysis in mouse
showed high expression of a 4-kb transcript in brain, lung, liver, and
kidney. A lower level of expression was seen in spleen and skeletal
muscle, and no expression was observed in heart or testis.
GENE STRUCTURE
Kiss et al. (2001) determined that the SAC1 gene contains 20 exons and
spans 55.7 kb. It has a large first intron of approximately 14 kb.
MAPPING
By sequence analysis, Kiss et al. (2001) mapped the SAC1 gene within a
250-kb putative tumor suppressor region on chromosome 3p21.3.
*FIELD* RF
1. Kiss, H.; Kedra, D.; Kiss, C.; Kost-Alimova, M.; Yang, Y.; Klein,
G.; Imreh, S.; Dumanski, J. P.: The LZTFL1 gene is a part of a transcriptional
map covering 250 kb within the common eliminated region 1 (C3CER1)
in 3p21.3. Genomics 73: 10-19, 2001.
2. Nagase, T.; Kikuno, R.; Hattori, A.; Kondo, Y.; Okumura, K.; Ohara,
O.: Prediction of the coding sequences of unidentified human genes.
XIX. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro. DNA Res. 7: 347-355, 2000.
*FIELD* CD
Carol A. Bocchini: 12/18/2001
*FIELD* ED
carol: 01/15/2002
carol: 12/20/2001
terry: 12/19/2001
carol: 12/18/2001