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Q9NTJ5 (SAC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositide phosphatase SAC1

EC=3.1.3.-
Alternative name(s):
Suppressor of actin mutations 1-like protein
Gene names
Name:SACM1L
Synonyms:KIAA0851
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphoinositide phosphatase that hydrolyzes PtdIns3P and PtdIns4P. Has low activity towards PtdIns(3,5)P2 By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Detected in heart, brain, lung, liver, kidney, pancreas and testis. Ref.2

Sequence similarities

Contains 1 SAC domain.

Sequence caution

The sequence BAA74874.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processphosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylinositol dephosphorylation

Inferred from electronic annotation. Source: Ensembl

phospholipid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: LIFEdb

Golgi membrane

Traceable author statement. Source: Reactome

alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionphosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol bisphosphate phosphatase activity

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-3-phosphatase activity

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-4-phosphate phosphatase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 14527956. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

COPG1Q9Y6783EBI-3917235,EBI-1049127

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 587587Phosphatidylinositide phosphatase SAC1
PRO_0000317171

Regions

Transmembrane56 – 7621Helical; Potential
Transmembrane521 – 54121Helical; Potential
Transmembrane549 – 56921Helical; Potential
Domain122 – 451330SAC

Amino acid modifications

Modified residue4561N6-acetyllysine Ref.6

Natural variations

Natural variant4341Y → F. Ref.3 Ref.4 Ref.5
Corresponds to variant rs1468542 [ dbSNP | Ensembl ].
VAR_038484

Experimental info

Sequence conflict451K → E in BAF83831. Ref.4
Sequence conflict3761Q → R in CAB66765. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9NTJ5 [UniParc].

Last modified February 5, 2008. Version 2.
Checksum: 3E0FC7515D15A071

FASTA58766,967
        10         20         30         40         50         60 
MATAAYEQLK LHITPEKFYV EACDDGADDV LTIDRVSTEV TLAVKKDVPP SAVTRPIFGI 

        70         80         90        100        110        120 
LGTIHLVAGN YLIVITKKIK VGEFFSHVVW KATDFDVLSY KKTMLHLTDI QLQDNKTFLA 

       130        140        150        160        170        180 
MLNHVLNVDG FYFSTTYDLT HTLQRLSNTS PEFQEMSLLE RADQRFVWNG HLLRELSAQP 

       190        200        210        220        230        240 
EVHRFALPVL HGFITMHSCS INGKYFDWIL ISRRSCFRAG VRYYVRGIDS EGHAANFVET 

       250        260        270        280        290        300 
EQIVHYNGSK ASFVQTRGSI PVFWSQRPNL KYKPLPQISK VANHMDGFQR HFDSQVIIYG 

       310        320        330        340        350        360 
KQVIINLINQ KGSEKPLEQT FATMVSSLGS GMMRYIAFDF HKECKNMRWD RLSILLDQVA 

       370        380        390        400        410        420 
EMQDELSYFL VDSAGQVVAN QEGVFRSNCM DCLDRTNVIQ SLLARRSLQA QLQRLGVLHV 

       430        440        450        460        470        480 
GQKLEEQDEF EKIYKNAWAD NANACAKQYA GTGALKTDFT RTGKRTHLGL IMDGWNSMIR 

       490        500        510        520        530        540 
YYKNNFSDGF RQDSIDLFLG NYSVDELESH SPLSVPRDWK FLALPIIMVV AFSMCIICLL 

       550        560        570        580 
MAGDTWTETL AYVLFWGVAS IGTFFIILYN GKDFVDAPRL VQKEKID 

« Hide

References

« Hide 'large scale' references
[1]"The LZTFL1 gene is a part of a transcriptional map covering 250 kb within the common eliminated region 1 (C3CER1) in 3p21.3."
Kiss H., Kedra D., Kiss C., Kost-Alimova M., Yang Y., Klein G., Imreh S., Dumanski J.P.
Genomics 73:10-19(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Prediction of the coding sequences of unidentified human genes. XII. 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. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY.
Tissue: Brain.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PHE-434.
Tissue: Testis.
[4]"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. expand/collapse author list , 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], VARIANT PHE-434.
[5]"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], VARIANT PHE-434.
Tissue: Placenta.
[6]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ297357 Genomic DNA. Translation: CAB95945.1.
AJ289880 Genomic DNA. Translation: CAB96871.1.
AB020658 mRNA. Translation: BAA74874.2. Different initiation.
AL136831 mRNA. Translation: CAB66765.1.
AK291142 mRNA. Translation: BAF83831.1.
BC016559 mRNA. Translation: AAH16559.1.
CCDSCCDS33745.1.
PIRT46447.
RefSeqNP_054735.3. NM_014016.3.
UniGeneHs.156509.

3D structure databases

ProteinModelPortalQ9NTJ5.
SMRQ9NTJ5. Positions 46-453.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116572. 7 interactions.
IntActQ9NTJ5. 9 interactions.
MINTMINT-4723852.
STRING9606.ENSP00000373713.

PTM databases

PhosphoSiteQ9NTJ5.

Polymorphism databases

DMDM167016563.

Proteomic databases

MaxQBQ9NTJ5.
PaxDbQ9NTJ5.
PRIDEQ9NTJ5.

Protocols and materials databases

DNASU22908.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000389061; ENSP00000373713; ENSG00000211456.
GeneID22908.
KEGGhsa:22908.
UCSCuc003cos.2. human.

Organism-specific databases

CTD22908.
GeneCardsGC03P045730.
H-InvDBHIX0021677.
HGNCHGNC:17059. SACM1L.
HPAHPA039573.
MIM606569. gene.
neXtProtNX_Q9NTJ5.
PharmGKBPA34925.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5329.
HOVERGENHBG108454.
InParanoidQ9NTJ5.
OMAISKVANH.
OrthoDBEOG73803W.
PhylomeDBQ9NTJ5.
TreeFamTF313543.

Enzyme and pathway databases

BioCycMetaCyc:HS11932-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9NTJ5.
BgeeQ9NTJ5.
CleanExHS_SACM1L.
GenevestigatorQ9NTJ5.

Family and domain databases

InterProIPR002013. Syja_N.
[Graphical view]
PfamPF02383. Syja_N. 1 hit.
[Graphical view]
PROSITEPS50275. SAC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSACM1L. human.
GeneWikiSACM1L.
GenomeRNAi22908.
NextBio43577.
PROQ9NTJ5.
SOURCESearch...

Entry information

Entry nameSAC1_HUMAN
AccessionPrimary (citable) accession number: Q9NTJ5
Secondary accession number(s): A8K527 expand/collapse secondary AC list , O94935, Q7LA14, Q7LA22, Q96AX7, Q9NQ46, Q9NQ57
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: July 9, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM