Phosphatidylinositide phosphatase SAC1

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Q9NTJ5 (SAC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phosphatidylinositide phosphatase SAC1
EC=3.1.3.-

Alternative name(s):
Suppressor of actin mutations 1-like protein

Gene names

Name:	SACM1L
Synonyms:	KIAA0851

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	587 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phosphatidylinositol biosynthetic process Traceable author statement. Source: Reactome phosphatidylinositol dephosphorylation Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to endoplasmic reticulum membrane Inferred from electronic annotation. Source: Compara
Molecular_function	phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylinositol bisphosphate phosphatase activity Inferred from electronic annotation. Source: Compara phosphatidylinositol-3-phosphatase activity Inferred from electronic annotation. Source: Compara phosphatidylinositol-4-phosphate phosphatase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 587

587

Phosphatidylinositide phosphatase SAC1

PRO_0000317171

Regions

Transmembrane

56 – 76

Helical; Potential

Transmembrane

521 – 541

Helical; Potential

Transmembrane

549 – 569

Helical; Potential

Domain

122 – 451

330

SAC

Amino acid modifications

Modified residue

456

N6-acetyllysine Ref.6

Natural variations

Natural variant

434

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

VAR_038484

Experimental info

Sequence conflict

K → E in BAF83831. Ref.4

Sequence conflict

376

Q → R in CAB66765. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q9NTJ5 [UniParc].

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

FASTA

587

66,967

        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' referencesShow '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. 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. 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, MASS SPECTROMETRY.
[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.
IPI	IPI00022275.
PIR	T46447.
RefSeq	NP_054735.3. NM_014016.3.
UniGene	Hs.156509.
3D structure databases
ProteinModelPortal	Q9NTJ5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NTJ5. 3 interactions.
STRING	9606.ENSP00000373713.
PTM databases
PhosphoSite	Q9NTJ5.
Polymorphism databases
DMDM	167016563.
Proteomic databases
PaxDb	Q9NTJ5.
PRIDE	Q9NTJ5.
Protocols and materials databases
DNASU	22908.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000389061; ENSP00000373713; ENSG00000211456.
GeneID	22908.
KEGG	hsa:22908.
UCSC	uc003cos.2. human.
Organism-specific databases
CTD	22908.
GeneCards	GC03P045730.
H-InvDB	HIX0021677.
HGNC	HGNC:17059. SACM1L.
HPA	HPA039573.
MIM	606569. gene.
neXtProt	NX_Q9NTJ5.
PharmGKB	PA34925.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5329.
HOVERGEN	HBG108454.
InParanoid	Q9NTJ5.
OMA	NVDGFYF.
OrthoDB	EOG4RR6H1.
Enzyme and pathway databases
BioCyc	MetaCyc:HS11932-MONOMER.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q9NTJ5.
Bgee	Q9NTJ5.
CleanEx	HS_SACM1L.
Genevestigator	Q9NTJ5.
Family and domain databases
InterPro	IPR002013. Syja_N. [Graphical view]
Pfam	PF02383. Syja_N. 1 hit. [Graphical view]
PROSITE	PS50275. SAC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SACM1L. human.
GenomeRNAi	22908.
NextBio	43577.
SOURCE	Search...

Entry information

Entry name

SAC1_HUMAN

Accession

Primary (citable) accession number: Q9NTJ5
Secondary accession number(s): A8K527

Q9NQ57

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

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

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents