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Protein

Septin-2

Gene

Sept2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements (By similarity). In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein.By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781GTP
Binding sitei104 – 1041GTP; via amide nitrogen
Sitei156 – 1561Important for dimerizationBy similarity
Binding sitei241 – 2411GTP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei256 – 2561GTP
Binding sitei258 – 2581GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 529GTP
Nucleotide bindingi183 – 1864GTP

GO - Molecular functioni

  • enzyme regulator activity Source: MGI
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • identical protein binding Source: MGI
  • protein complex scaffold Source: MGI

GO - Biological processi

  • cilium assembly Source: UniProtKB
  • cytokinesis Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • neuron projection development Source: Ensembl
  • protein polymerization Source: MGI
  • regulation of L-glutamate transport Source: MGI
  • regulation of protein localization Source: MGI
  • smoothened signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-5620912. Anchoring of the basal body to the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-2
Alternative name(s):
Neural precursor cell expressed developmentally down-regulated protein 5
Short name:
NEDD-5
Gene namesi
Name:Sept2
Synonyms:Nedd-5, Nedd5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:97298. Sept2.

Subcellular locationi

  • Cytoplasm
  • Cytoplasmcytoskeleton
  • Cytoplasmcytoskeletonspindle By similarity
  • Chromosomecentromerekinetochore By similarity
  • Cleavage furrow By similarity
  • Midbody By similarity
  • Cytoplasmcell cortex By similarity
  • Cell projectioncilium membrane

  • Note: In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle (By similarity). In interphase and postmitotic cells, localised to fibrous or granular structures, depending on the growth state of the cell. Localizes at the base of the cilia near the morphological distinction between the cilia and plasma membranes.By similarity

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • actomyosin contractile ring Source: UniProtKB
  • axoneme Source: MGI
  • cell cortex Source: MGI
  • cell projection Source: MGI
  • cell surface Source: MGI
  • ciliary membrane Source: UniProtKB
  • ciliary transition zone Source: MGI
  • cleavage furrow Source: UniProtKB-SubCell
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • exocyst Source: Ensembl
  • extracellular exosome Source: MGI
  • microtubule cytoskeleton Source: MGI
  • midbody Source: MGI
  • myelin sheath Source: UniProtKB
  • nonmotile primary cilium Source: MGI
  • nucleolus Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: Ensembl
  • photoreceptor connecting cilium Source: MGI
  • plasma membrane Source: MGI
  • septin complex Source: MGI
  • spindle microtubule Source: MGI
  • synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461S → D: Loss of GTP-binding. 1 Publication
Mutagenesisi47 – 471G → V: Loss of GTP-binding activity. 1 Publication
Mutagenesisi51 – 511S → N: Loss of GTP-binding activity. 1 Publication
Mutagenesisi78 – 781T → G: Reduces affinity for GTP 20-fold. 1 Publication
Mutagenesisi125 – 1251Q → L: Loss of GTP-binding activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 361361Septin-2PRO_0000173516Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphotyrosineCombined sources
Modified residuei190 – 1901N6-acetyllysineBy similarity
Modified residuei211 – 2111PhosphotyrosineBy similarity
Modified residuei218 – 2181PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP42208.
MaxQBiP42208.
PaxDbiP42208.
PeptideAtlasiP42208.
PRIDEiP42208.

2D gel databases

REPRODUCTION-2DPAGEIPI00114945.
P42208.

PTM databases

iPTMnetiP42208.
PhosphoSiteiP42208.
SwissPalmiP42208.

Expressioni

Tissue specificityi

Widely expressed.

Developmental stagei

Expressed at 17 dpc in the brain with levels remaining relatively stable up to adulthood (at protein level).1 Publication

Gene expression databases

BgeeiP42208.
CleanExiMM_SEPT2.
ExpressionAtlasiP42208. baseline and differential.
GenevisibleiP42208. MM.

Interactioni

Subunit structurei

Septins polymerize into heterooligomeric protein complexes that form filaments, and associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation. Septin filaments are assembled from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate head-to-head to form a hexameric unit. Interaction between SEPT2 and SEPT7 seems indirect. Interacts also with SEPT9 and SEPT5. Interaction with SEPT4 not detected. Interacts with MAP4 (By similarity).By similarity

GO - Molecular functioni

  • identical protein binding Source: MGI
  • protein complex scaffold Source: MGI

Protein-protein interaction databases

BioGridi201724. 18 interactions.
DIPiDIP-32438N.
IntActiP42208. 17 interactions.
MINTiMINT-3378243.
STRINGi10090.ENSMUSP00000027495.

Structurei

Secondary structure

1
361
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 4511Combined sources
Helixi50 – 556Combined sources
Beta strandi59 – 613Combined sources
Beta strandi82 – 909Combined sources
Beta strandi93 – 1019Combined sources
Beta strandi105 – 1095Combined sources
Helixi111 – 13323Combined sources
Beta strandi148 – 1536Combined sources
Beta strandi157 – 1604Combined sources
Helixi162 – 17110Combined sources
Turni172 – 1743Combined sources
Beta strandi177 – 1826Combined sources
Helixi184 – 1863Combined sources
Helixi189 – 20517Combined sources
Helixi222 – 23312Combined sources
Beta strandi236 – 2383Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi249 – 25810Combined sources
Beta strandi261 – 2644Combined sources
Turni268 – 2703Combined sources
Helixi273 – 29321Combined sources
Helixi295 – 3039Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FTQX-ray2.90A/B/C/D33-306[»]
ProteinModelPortaliP42208.
SMRiP42208. Positions 34-305.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42208.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 306273Septin-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni260 – 27011Important for dimerizationBy similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00760000118899.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiP42208.
KOiK16942.
OMAiQDCFSTI.
OrthoDBiEOG79KPF0.
PhylomeDBiP42208.
TreeFamiTF101079.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008113. Septin2.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
PRINTSiPR01740. SEPTIN2.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42208-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK
60 70 80 90 100
STLINSLFLT DLYPERIIPG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV
110 120 130 140 150
DTPGYGDAIN CRDCFKTIIS YIDEQFERYL HDESGLNRRH IIDNRVHCCF
160 170 180 190 200
YFISPFGHGL KPLDVAFMKA IHNKVNIVPV IAKADTLTLK ERERLKKRIL
210 220 230 240 250
DEIEEHSIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV GSNQLIEAKG
260 270 280 290 300
KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR
310 320 330 340 350
SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG
360
DSDSGALGQH V
Length:361
Mass (Da):41,526
Last modified:February 1, 1996 - v2
Checksum:iC4BFFB3F1815E081
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49382 mRNA. Translation: BAA08380.1.
AK028072 mRNA. Translation: BAC25737.1.
AK146616 mRNA. Translation: BAE27305.1.
AK151591 mRNA. Translation: BAE30531.1.
AK171331 mRNA. Translation: BAE42396.1.
CH466520 Genomic DNA. Translation: EDL39946.1.
CH466520 Genomic DNA. Translation: EDL39948.1.
BC138636 mRNA. Translation: AAI38637.1.
BC138637 mRNA. Translation: AAI38638.1.
CCDSiCCDS15190.1.
RefSeqiNP_001153189.1. NM_001159717.1.
NP_001153190.1. NM_001159718.1.
NP_001153191.1. NM_001159719.1.
NP_035021.1. NM_010891.2.
XP_006529304.1. XM_006529241.2.
XP_006529305.1. XM_006529242.1.
XP_011246238.1. XM_011247936.1.
UniGeneiMm.428652.

Genome annotation databases

EnsembliENSMUST00000027495; ENSMUSP00000027495; ENSMUSG00000026276.
ENSMUST00000168776; ENSMUSP00000132850; ENSMUSG00000026276.
ENSMUST00000179353; ENSMUSP00000136366; ENSMUSG00000026276.
GeneIDi18000.
KEGGimmu:18000.
UCSCiuc007cea.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49382 mRNA. Translation: BAA08380.1.
AK028072 mRNA. Translation: BAC25737.1.
AK146616 mRNA. Translation: BAE27305.1.
AK151591 mRNA. Translation: BAE30531.1.
AK171331 mRNA. Translation: BAE42396.1.
CH466520 Genomic DNA. Translation: EDL39946.1.
CH466520 Genomic DNA. Translation: EDL39948.1.
BC138636 mRNA. Translation: AAI38637.1.
BC138637 mRNA. Translation: AAI38638.1.
CCDSiCCDS15190.1.
RefSeqiNP_001153189.1. NM_001159717.1.
NP_001153190.1. NM_001159718.1.
NP_001153191.1. NM_001159719.1.
NP_035021.1. NM_010891.2.
XP_006529304.1. XM_006529241.2.
XP_006529305.1. XM_006529242.1.
XP_011246238.1. XM_011247936.1.
UniGeneiMm.428652.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FTQX-ray2.90A/B/C/D33-306[»]
ProteinModelPortaliP42208.
SMRiP42208. Positions 34-305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201724. 18 interactions.
DIPiDIP-32438N.
IntActiP42208. 17 interactions.
MINTiMINT-3378243.
STRINGi10090.ENSMUSP00000027495.

PTM databases

iPTMnetiP42208.
PhosphoSiteiP42208.
SwissPalmiP42208.

2D gel databases

REPRODUCTION-2DPAGEIPI00114945.
P42208.

Proteomic databases

EPDiP42208.
MaxQBiP42208.
PaxDbiP42208.
PeptideAtlasiP42208.
PRIDEiP42208.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027495; ENSMUSP00000027495; ENSMUSG00000026276.
ENSMUST00000168776; ENSMUSP00000132850; ENSMUSG00000026276.
ENSMUST00000179353; ENSMUSP00000136366; ENSMUSG00000026276.
GeneIDi18000.
KEGGimmu:18000.
UCSCiuc007cea.2. mouse.

Organism-specific databases

CTDi4735.
MGIiMGI:97298. Sept2.

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00760000118899.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiP42208.
KOiK16942.
OMAiQDCFSTI.
OrthoDBiEOG79KPF0.
PhylomeDBiP42208.
TreeFamiTF101079.

Enzyme and pathway databases

ReactomeiR-MMU-5620912. Anchoring of the basal body to the plasma membrane.

Miscellaneous databases

ChiTaRSiSept2. mouse.
EvolutionaryTraceiP42208.
PROiP42208.
SOURCEiSearch...

Gene expression databases

BgeeiP42208.
CleanExiMM_SEPT2.
ExpressionAtlasiP42208. baseline and differential.
GenevisibleiP42208. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008113. Septin2.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
PRINTSiPR01740. SEPTIN2.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures."
    Kinoshita M., Kumar S., Noda M.
    Genes Dev. 11:1535-1547(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLY-47; SER-51 AND GLN-125.
    Tissue: Neural tube.
  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].
    Strain: C57BL/6J.
    Tissue: Bone marrow and Placenta.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Brain.
  5. Lubec G., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 51-66; 97-112 AND 117-128, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Hippocampus.
  6. "The septin CDCrel-1 is dispensable for normal development and neurotransmitter release."
    Peng X.-R., Jia Z., Zhang Y., Ware J., Trimble W.S.
    Mol. Cell. Biol. 22:378-387(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SEPT5 AND SEPT7, LACK OF INTERACTION WITH SEPT4, DEVELOPMENTAL STAGE.
  7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  14. "A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution."
    Hu Q., Milenkovic L., Jin H., Scott M.P., Nachury M.V., Spiliotis E.T., Nelson W.J.
    Science 329:436-439(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "A ciliopathy complex at the transition zone protects the cilia as a privileged membrane domain."
    Chih B., Liu P., Chinn Y., Chalouni C., Komuves L.G., Hass P.E., Sandoval W., Peterson A.S.
    Nat. Cell Biol. 14:61-72(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  16. "GTP-induced conformational changes in septins and implications for function."
    Sirajuddin M., Farkasovsky M., Zent E., Wittinghofer A.
    Proc. Natl. Acad. Sci. U.S.A. 106:16592-16597(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 33-306 IN COMPLEX WITH GPPNHP, MUTAGENESIS OF SER-46 AND THR-78.

Entry informationi

Entry nameiSEPT2_MOUSE
AccessioniPrimary (citable) accession number: P42208
Secondary accession number(s): B2RRZ2, Q3U9Y5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: February 1, 1996
Last modified: July 6, 2016
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Coordinated expression with SEPT6 and SEPT7.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.