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Q15019

- SEPT2_HUMAN

UniProt

Q15019 - SEPT2_HUMAN

Protein

Septin-2

Gene

SEPT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    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. 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. May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri.4 Publications

    Sites

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi44 – 518GTP
    Nucleotide bindingi183 – 1919GTP

    GO - Molecular functioni

    1. enzyme regulator activity Source: Ensembl
    2. GTP binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cilium assembly Source: UniProtKB
    2. mitotic nuclear division Source: UniProtKB-KW
    3. neuron projection development Source: Ensembl
    4. regulation of L-glutamate transport Source: Ensembl
    5. regulation of protein localization Source: Ensembl
    6. smoothened signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    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:DIFF6, KIAA0158, NEDD5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:7729. SEPT2.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeleton 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication. Chromosomecentromerekinetochore 1 Publication. Cleavage furrow 1 Publication. Midbody 1 Publication. Cytoplasmcell cortex 1 Publication. Cell projectioncilium membrane By similarity
    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. During bacterial infection, displays a collar shape structure next to actin at the pole of invading bacteria. In epithelial cells, colocalizes with polyglutamylated tubulin around the trans-Golgi network, as well as juxatnuclear and proximal Golgi apparatus. Localizes at the base of the cilia near the morphological distinction between the cilia and plasma membranes.

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. ciliary membrane Source: UniProtKB
    3. cleavage furrow Source: UniProtKB-SubCell
    4. condensed chromosome kinetochore Source: UniProtKB-SubCell
    5. cytoplasm Source: UniProtKB
    6. exocyst Source: Ensembl
    7. extracellular vesicular exosome Source: UniProt
    8. midbody Source: UniProtKB-SubCell
    9. nucleolus Source: HPA
    10. nucleus Source: UniProtKB
    11. perinuclear region of cytoplasm Source: Ensembl
    12. septin complex Source: InterPro
    13. spindle Source: UniProtKB-SubCell
    14. synapse Source: Ensembl

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi156 – 1561F → D: Loss of dimerization. 1 Publication
    Mutagenesisi218 – 2181S → A: Loss of phosphorylation. 1 Publication
    Mutagenesisi260 – 2601W → A: Loss of dimerization. 1 Publication
    Mutagenesisi270 – 2701H → D: Loss of dimerization. 1 Publication

    Organism-specific databases

    PharmGKBiPA31535.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 361361Septin-2PRO_0000173515Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171PhosphotyrosineBy similarity
    Modified residuei190 – 1901N6-acetyllysine1 Publication
    Modified residuei218 – 2181Phosphoserine12 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15019.
    PaxDbiQ15019.
    PRIDEiQ15019.

    2D gel databases

    OGPiQ15019.

    PTM databases

    PhosphoSiteiQ15019.

    Expressioni

    Tissue specificityi

    Widely expressed. Up-regulated in liver cancer.2 Publications

    Gene expression databases

    ArrayExpressiQ15019.
    BgeeiQ15019.
    CleanExiHS_SEPT2.
    GenevestigatoriQ15019.

    Organism-specific databases

    HPAiCAB017190.
    HPA018481.

    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. 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 with SEPT5 By similarity. Interaction with SEPT4 not detected By similarity. Interacts with SEPT9. Interacts with MAP4.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SEPT6Q141416EBI-741220,EBI-745901

    Protein-protein interaction databases

    BioGridi110812. 59 interactions.
    DIPiDIP-38220N.
    IntActiQ15019. 12 interactions.
    MINTiMINT-1433588.
    STRINGi9606.ENSP00000353157.

    Structurei

    Secondary structure

    1
    361
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi23 – 3412
    Beta strandi38 – 458
    Helixi50 – 589
    Beta strandi85 – 884
    Beta strandi95 – 1028
    Helixi118 – 13316
    Beta strandi148 – 1536
    Beta strandi155 – 1595
    Helixi162 – 17110
    Turni172 – 1743
    Beta strandi177 – 1815
    Helixi184 – 1863
    Helixi189 – 20517
    Helixi225 – 2328
    Beta strandi236 – 2383
    Beta strandi243 – 2453
    Beta strandi254 – 2585
    Beta strandi261 – 2644
    Turni268 – 2703
    Helixi273 – 28210
    Helixi284 – 29310
    Helixi295 – 30511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QA5X-ray3.40A/B1-315[»]
    2QAGX-ray4.00A1-361[»]
    2QNRX-ray2.60A/B22-320[»]
    ProteinModelPortaliQ15019.
    SMRiQ15019. Positions 34-305.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15019.

    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 dimerizationAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5019.
    HOGENOMiHOG000233586.
    HOVERGENiHBG065093.
    KOiK16942.
    OrthoDBiEOG79KPF0.
    PhylomeDBiQ15019.
    TreeFamiTF101079.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR000038. Cell_div_GTP-bd.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15019-1) [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

    MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK    50
    STLINSLFLT DLYPERVIPG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV 100
    DTPGYGDAIN CRDCFKTIIS YIDEQFERYL HDESGLNRRH IIDNRVHCCF 150
    YFISPFGHGL KPLDVAFMKA IHNKVNIVPV IAKADTLTLK ERERLKKRIL 200
    DEIEEHNIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV GSNQLIEAKG 250
    KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR 300
    SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG 350
    DGDGGALGHH V 361
    Length:361
    Mass (Da):41,487
    Last modified:November 1, 1997 - v1
    Checksum:i12CCBBE30806F92F
    GO
    Isoform 2 (identifier: Q15019-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MPWISEGRATRPCLRVPSARRGDEGLHQRDEASQKM

    Note: No experimental confirmation available.

    Show »
    Length:396
    Mass (Da):45,461
    Checksum:i4BD59305219D99B5
    GO
    Isoform 3 (identifier: Q15019-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         72-72: A → AALNTRKTLLW

    Note: No experimental confirmation available.

    Show »
    Length:371
    Mass (Da):42,685
    Checksum:i0ED0C05E2DA308B4
    GO

    Sequence cautioni

    The sequence BAA09928.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAY14718.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691P → S in AAH14455. (PubMed:15489334)Curated
    Sequence conflicti360 – 3612HV → TCKVMCTYKKSEKTLSWIKK KTFQMHDPAVCFQSLGGCHP HFNSTCA in BAA05893. (PubMed:8697812)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MPWISEGRATRPCLRVPSAR RGDEGLHQRDEASQKM in isoform 2. 1 PublicationVSP_038271
    Alternative sequencei72 – 721A → AALNTRKTLLW in isoform 3. 1 PublicationVSP_055176

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63878 mRNA. Translation: BAA09928.2. Different initiation.
    D28540 mRNA. Translation: BAA05893.1.
    AF038404 mRNA. Translation: AAB92377.1.
    AK294563 mRNA. Translation: BAG57759.1.
    AC005104 Genomic DNA. No translation available.
    AC104841 Genomic DNA. Translation: AAY14718.1. Sequence problems.
    BC014455 mRNA. Translation: AAH14455.1.
    BC033559 mRNA. Translation: AAH33559.1.
    CCDSiCCDS2548.1. [Q15019-1]
    CCDS63195.1. [Q15019-3]
    RefSeqiNP_001008491.1. NM_001008491.2. [Q15019-1]
    NP_001008492.1. NM_001008492.2. [Q15019-1]
    NP_001269901.1. NM_001282972.1. [Q15019-2]
    NP_001269902.1. NM_001282973.1.
    NP_004395.1. NM_004404.4. [Q15019-1]
    NP_006146.1. NM_006155.2. [Q15019-1]
    XP_005247068.1. XM_005247011.1. [Q15019-1]
    XP_005247069.1. XM_005247012.1. [Q15019-1]
    XP_005247070.1. XM_005247013.1. [Q15019-1]
    XP_006712611.1. XM_006712548.1. [Q15019-1]
    XP_006712612.1. XM_006712549.1. [Q15019-1]
    UniGeneiHs.721234.

    Genome annotation databases

    EnsembliENST00000360051; ENSP00000353157; ENSG00000168385. [Q15019-1]
    ENST00000391971; ENSP00000375832; ENSG00000168385. [Q15019-1]
    ENST00000391973; ENSP00000375834; ENSG00000168385. [Q15019-1]
    ENST00000401990; ENSP00000385109; ENSG00000168385. [Q15019-3]
    ENST00000402092; ENSP00000385172; ENSG00000168385. [Q15019-1]
    GeneIDi4735.
    KEGGihsa:4735.
    UCSCiuc002wbc.3. human. [Q15019-1]
    uc010zop.2. human. [Q15019-2]

    Polymorphism databases

    DMDMi2500769.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63878 mRNA. Translation: BAA09928.2 . Different initiation.
    D28540 mRNA. Translation: BAA05893.1 .
    AF038404 mRNA. Translation: AAB92377.1 .
    AK294563 mRNA. Translation: BAG57759.1 .
    AC005104 Genomic DNA. No translation available.
    AC104841 Genomic DNA. Translation: AAY14718.1 . Sequence problems.
    BC014455 mRNA. Translation: AAH14455.1 .
    BC033559 mRNA. Translation: AAH33559.1 .
    CCDSi CCDS2548.1. [Q15019-1 ]
    CCDS63195.1. [Q15019-3 ]
    RefSeqi NP_001008491.1. NM_001008491.2. [Q15019-1 ]
    NP_001008492.1. NM_001008492.2. [Q15019-1 ]
    NP_001269901.1. NM_001282972.1. [Q15019-2 ]
    NP_001269902.1. NM_001282973.1.
    NP_004395.1. NM_004404.4. [Q15019-1 ]
    NP_006146.1. NM_006155.2. [Q15019-1 ]
    XP_005247068.1. XM_005247011.1. [Q15019-1 ]
    XP_005247069.1. XM_005247012.1. [Q15019-1 ]
    XP_005247070.1. XM_005247013.1. [Q15019-1 ]
    XP_006712611.1. XM_006712548.1. [Q15019-1 ]
    XP_006712612.1. XM_006712549.1. [Q15019-1 ]
    UniGenei Hs.721234.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QA5 X-ray 3.40 A/B 1-315 [» ]
    2QAG X-ray 4.00 A 1-361 [» ]
    2QNR X-ray 2.60 A/B 22-320 [» ]
    ProteinModelPortali Q15019.
    SMRi Q15019. Positions 34-305.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110812. 59 interactions.
    DIPi DIP-38220N.
    IntActi Q15019. 12 interactions.
    MINTi MINT-1433588.
    STRINGi 9606.ENSP00000353157.

    PTM databases

    PhosphoSitei Q15019.

    Polymorphism databases

    DMDMi 2500769.

    2D gel databases

    OGPi Q15019.

    Proteomic databases

    MaxQBi Q15019.
    PaxDbi Q15019.
    PRIDEi Q15019.

    Protocols and materials databases

    DNASUi 4735.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360051 ; ENSP00000353157 ; ENSG00000168385 . [Q15019-1 ]
    ENST00000391971 ; ENSP00000375832 ; ENSG00000168385 . [Q15019-1 ]
    ENST00000391973 ; ENSP00000375834 ; ENSG00000168385 . [Q15019-1 ]
    ENST00000401990 ; ENSP00000385109 ; ENSG00000168385 . [Q15019-3 ]
    ENST00000402092 ; ENSP00000385172 ; ENSG00000168385 . [Q15019-1 ]
    GeneIDi 4735.
    KEGGi hsa:4735.
    UCSCi uc002wbc.3. human. [Q15019-1 ]
    uc010zop.2. human. [Q15019-2 ]

    Organism-specific databases

    CTDi 4735.
    GeneCardsi GC02P242254.
    HGNCi HGNC:7729. SEPT2.
    HPAi CAB017190.
    HPA018481.
    MIMi 601506. gene.
    neXtProti NX_Q15019.
    PharmGKBi PA31535.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5019.
    HOGENOMi HOG000233586.
    HOVERGENi HBG065093.
    KOi K16942.
    OrthoDBi EOG79KPF0.
    PhylomeDBi Q15019.
    TreeFami TF101079.

    Miscellaneous databases

    ChiTaRSi SEPT2. human.
    EvolutionaryTracei Q15019.
    GeneWikii SEPT2.
    GenomeRNAii 4735.
    NextBioi 18256.
    PROi Q15019.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15019.
    Bgeei Q15019.
    CleanExi HS_SEPT2.
    Genevestigatori Q15019.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR000038. Cell_div_GTP-bd.
    IPR027417. P-loop_NTPase.
    IPR016491. Septin.
    IPR008113. Septin2.
    [Graphical view ]
    PANTHERi PTHR18884. PTHR18884. 1 hit.
    Pfami PF00735. Septin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006698. Septin. 1 hit.
    PRINTSi PR01740. SEPTIN2.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS51719. G_SEPTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
      DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Bone marrow.
    2. "Isolation and mapping of a human gene (DIFF6) homologous to yeast CDC3, CDC10, CDC11, and CDC12, and mouse Diff6."
      Mori T., Miura K., Fujiwara T., Shin S., Inazawa J., Nakamura Y.
      Cytogenet. Cell Genet. 73:224-227(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "Human homolog of mouse Nedd5 mRNA."
      Hu G.
      Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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.
      , 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 2).
      Tissue: Amygdala.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Muscle and Testis.
    7. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 51-66, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    8. "Septin 2 phosphorylation: theoretical and mass spectrometric evidence for the existence of a single phosphorylation site in vivo."
      She Y.M., Huang Y.W., Zhang L., Trimble W.S.
      Rapid Commun. Mass Spectrom. 18:1123-1130(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-218.
    9. "Expression profiling the human septin gene family."
      Hall P.A., Jung K., Hillan K.J., Russell S.E.H.
      J. Pathol. 206:269-278(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    10. "Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4."
      Kremer B.E., Haystead T., Macara I.G.
      Mol. Biol. Cell 16:4648-4659(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP4, COORDINATED EXPRESSION WITH SEPT2 AND SEPT7.
    11. "A mitotic septin scaffold required for mammalian chromosome congression and segregation."
      Spiliotis E.T., Kinoshita M., Nelson W.J.
      Science 307:1781-1785(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Structural analysis of septin 2, 6, and 7 complexes."
      Low C., Macara I.G.
      J. Biol. Chem. 281:30697-30706(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEPT6 AND SEPT7.
    14. "Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7."
      Kremer B.E., Adang L.A., Macara I.G.
      Cell 130:837-850(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Epithelial polarity requires septin coupling of vesicle transport to polyglutamylated microtubules."
      Spiliotis E.T., Hunt S.J., Hu Q., Kinoshita M., Nelson W.J.
      J. Cell Biol. 180:295-303(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COLOCALIZATION WITH POLYGLUTAMYLATED TUBULIN.
    16. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    18. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    21. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "The phosphorylation of SEPT2 on Ser218 by casein kinase 2 is important to hepatoma carcinoma cell proliferation."
      Yu W., Ding X., Chen F., Liu M., Shen S., Gu X., Yu L.
      Mol. Cell. Biochem. 325:61-67(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-218, MUTAGENESIS OF SER-218, TISSUE SPECIFICITY.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: INTERACTION WITH SEPT9, ROLE IN BACTERIAL INFECTION.
    25. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    26. "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-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-315 IN COMPLEXES WITH GTP, ELECTRON MICROSCOPY, MUTAGENESIS OF PHE-156; TRP-260 AND HIS-270, SUBUNIT.
    31. "Human septin 2 in complex with GDP."
      Structural genomics consortium (SGC)
      Submitted (AUG-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-320 IN COMPLEX WITH GDP, SUBUNIT.

    Entry informationi

    Entry nameiSEPT2_HUMAN
    AccessioniPrimary (citable) accession number: Q15019
    Secondary accession number(s): B4DGE8
    , Q14132, Q53QU3, Q8IUK9, Q96CB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 158 of the entry and version 1 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

    Coordinated expression with SEPT6 and SEPT7.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3