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Q9UH03

- SEPT3_HUMAN

UniProt

Q9UH03 - SEPT3_HUMAN

Protein

Neuronal-specific septin-3

Gene

SEPT3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 3 (15 May 2007)
      Previous versions | rss
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    Functioni

    Filament-forming cytoskeletal GTPase By similarity. May play a role in cytokinesis Potential.By similarityCurated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei102 – 1021GTP
    Binding sitei265 – 2651GTP; via amide nitrogen and carbonyl oxygen
    Binding sitei280 – 2801GTP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi68 – 758GTP
    Nucleotide bindingi208 – 2169GTP

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neuronal-specific septin-3
    Gene namesi
    Name:SEPT3
    Synonyms:SEP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:10750. SEPT3.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeleton By similarity. Cell junctionsynapse By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. septin complex Source: InterPro
    3. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24355.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 358358Neuronal-specific septin-3PRO_0000173517Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei91 – 911PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by PKG on serine residues. Phosphorylated by PKG on Ser-91 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UH03.
    PaxDbiQ9UH03.
    PRIDEiQ9UH03.

    PTM databases

    PhosphoSiteiQ9UH03.

    Expressioni

    Tissue specificityi

    Brain-specific.2 Publications

    Inductioni

    Up-regulated during neuronal differentiation.1 Publication

    Gene expression databases

    ArrayExpressiQ9UH03.
    BgeeiQ9UH03.
    CleanExiHS_SEPT3.
    GenevestigatoriQ9UH03.

    Organism-specific databases

    HPAiCAB017633.
    HPA003548.

    Interactioni

    Subunit structurei

    Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation By similarity.By similarity

    Protein-protein interaction databases

    BioGridi121011. 3 interactions.
    IntActiQ9UH03. 2 interactions.
    MINTiMINT-1385903.
    STRINGi9606.ENSP00000379704.

    Structurei

    Secondary structure

    1
    358
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi61 – 7313
    Helixi74 – 8512
    Beta strandi107 – 1115
    Beta strandi120 – 1245
    Helixi140 – 15718
    Beta strandi173 – 1786
    Beta strandi182 – 1843
    Helixi187 – 19711
    Beta strandi200 – 2067
    Helixi209 – 2113
    Helixi214 – 23017
    Helixi246 – 25611
    Beta strandi260 – 2623
    Beta strandi269 – 2724
    Beta strandi275 – 2806
    Beta strandi287 – 2904
    Turni292 – 2943
    Helixi297 – 3059
    Turni306 – 3083
    Helixi309 – 31810
    Helixi320 – 3289

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3SOPX-ray2.88A/B60-329[»]
    ProteinModelPortaliQ9UH03.
    SMRiQ9UH03. Positions 60-329.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 331274Septin-type GAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5019.
    HOVERGENiHBG065093.
    InParanoidiQ9UH03.
    KOiK16938.
    OMAiRKELTAM.
    PhylomeDBiQ9UH03.
    TreeFamiTF101078.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR000038. Cell_div_GTP-bd.
    IPR027417. P-loop_NTPase.
    IPR016491. Septin.
    IPR008114. Septin3.
    [Graphical view]
    PANTHERiPTHR18884. PTHR18884. 1 hit.
    PfamiPF00735. Septin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006698. Septin. 1 hit.
    PRINTSiPR01741. SEPTIN3.
    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: Q9UH03-1) [UniParc]FASTAAdd to Basket

    Also known as: A, SEP3A

    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

    MSKGLPETRT DAAMSELVPE PRPKPAVPMK PMSINSNLLG YIGIDTIIEQ    50
    MRKKTMKTGF DFNIMVVGQS GLGKSTLVNT LFKSQVSRKA SSWNREEKIP 100
    KTVEIKAIGH VIEEGGVKMK LTVIDTPGFG DQINNENCWE PIEKYINEQY 150
    EKFLKEEVNI ARKKRIPDTR VHCCLYFISP TGHSLRPLDL EFMKHLSKVV 200
    NIIPVIAKAD TMTLEEKSEF KQRVRKELEV NGIEFYPQKE FDEDLEDKTE 250
    NDKIRQESMP FAVVGSDKEY QVNGKRVLGR KTPWGIIEVE NLNHCEFALL 300
    RDFVIRTHLQ DLKEVTHNIH YETYRAKRLN DNGGLPPGEG LLGTVLPPVP 350
    ATPCPTAE 358
    Length:358
    Mass (Da):40,704
    Last modified:May 15, 2007 - v3
    Checksum:iB49B0D1FBD9DE43B
    GO
    Isoform 2 (identifier: Q9UH03-2) [UniParc]FASTAAdd to Basket

    Also known as: B, SEP3B

    The sequence of this isoform differs from the canonical sequence as follows:
         338-358: GEGLLGTVLPPVPATPCPTAE → VSVDTEESHDSNP

    Show »
    Length:350
    Mass (Da):40,100
    Checksum:i71D66D57E04D6C93
    GO
    Isoform 3 (identifier: Q9UH03-3) [UniParc]FASTAAdd to Basket

    Also known as: C, SEP3C

    The sequence of this isoform differs from the canonical sequence as follows:
         68-83: GQSGLGKSTLVNTLFK → AGSPLRSTSMSSTRSS
         84-358: Missing.

    Show »
    Length:83
    Mass (Da):9,061
    Checksum:iA1008153DB5F8F76
    GO

    Sequence cautioni

    The sequence AAG00517.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAG00518.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAG00519.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAI11780.2 differs from that shown. Reason: Erroneous initiation.
    The sequence CAD38797.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAG30458.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei68 – 8316GQSGL…NTLFK → AGSPLRSTSMSSTRSS in isoform 3. 1 PublicationVSP_025398Add
    BLAST
    Alternative sequencei84 – 358275Missing in isoform 3. 1 PublicationVSP_025399Add
    BLAST
    Alternative sequencei338 – 35821GEGLL…CPTAE → VSVDTEESHDSNP in isoform 2. 4 PublicationsVSP_006049Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF285107 mRNA. Translation: AAG00517.1. Different initiation.
    AF285108 mRNA. Translation: AAG00518.1. Different initiation.
    AF285109 mRNA. Translation: AAG00519.1. Different initiation.
    CR456572 mRNA. Translation: CAG30458.1. Different initiation.
    AL833942 mRNA. Translation: CAD38797.1. Different initiation.
    Z99716 Genomic DNA. Translation: CAI41693.1.
    Z99716 Genomic DNA. Translation: CAQ07552.1.
    CH471095 Genomic DNA. Translation: EAW60480.1.
    BC111779 mRNA. Translation: AAI11780.2. Different initiation.
    AB209152 mRNA. Translation: BAD92389.1.
    CCDSiCCDS14026.2. [Q9UH03-1]
    CCDS14027.2. [Q9UH03-2]
    PIRiJC7681.
    RefSeqiNP_061979.3. NM_019106.5. [Q9UH03-2]
    NP_663786.2. NM_145733.2. [Q9UH03-1]
    UniGeneiHs.120483.

    Genome annotation databases

    EnsembliENST00000396417; ENSP00000379695; ENSG00000100167. [Q9UH03-3]
    ENST00000396425; ENSP00000379703; ENSG00000100167. [Q9UH03-2]
    ENST00000396426; ENSP00000379704; ENSG00000100167. [Q9UH03-1]
    GeneIDi55964.
    KEGGihsa:55964.
    UCSCiuc003bbr.4. human. [Q9UH03-1]
    uc003bbs.4. human. [Q9UH03-2]

    Polymorphism databases

    DMDMi147744590.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF285107 mRNA. Translation: AAG00517.1 . Different initiation.
    AF285108 mRNA. Translation: AAG00518.1 . Different initiation.
    AF285109 mRNA. Translation: AAG00519.1 . Different initiation.
    CR456572 mRNA. Translation: CAG30458.1 . Different initiation.
    AL833942 mRNA. Translation: CAD38797.1 . Different initiation.
    Z99716 Genomic DNA. Translation: CAI41693.1 .
    Z99716 Genomic DNA. Translation: CAQ07552.1 .
    CH471095 Genomic DNA. Translation: EAW60480.1 .
    BC111779 mRNA. Translation: AAI11780.2 . Different initiation.
    AB209152 mRNA. Translation: BAD92389.1 .
    CCDSi CCDS14026.2. [Q9UH03-1 ]
    CCDS14027.2. [Q9UH03-2 ]
    PIRi JC7681.
    RefSeqi NP_061979.3. NM_019106.5. [Q9UH03-2 ]
    NP_663786.2. NM_145733.2. [Q9UH03-1 ]
    UniGenei Hs.120483.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3SOP X-ray 2.88 A/B 60-329 [» ]
    ProteinModelPortali Q9UH03.
    SMRi Q9UH03. Positions 60-329.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121011. 3 interactions.
    IntActi Q9UH03. 2 interactions.
    MINTi MINT-1385903.
    STRINGi 9606.ENSP00000379704.

    PTM databases

    PhosphoSitei Q9UH03.

    Polymorphism databases

    DMDMi 147744590.

    Proteomic databases

    MaxQBi Q9UH03.
    PaxDbi Q9UH03.
    PRIDEi Q9UH03.

    Protocols and materials databases

    DNASUi 55964.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000396417 ; ENSP00000379695 ; ENSG00000100167 . [Q9UH03-3 ]
    ENST00000396425 ; ENSP00000379703 ; ENSG00000100167 . [Q9UH03-2 ]
    ENST00000396426 ; ENSP00000379704 ; ENSG00000100167 . [Q9UH03-1 ]
    GeneIDi 55964.
    KEGGi hsa:55964.
    UCSCi uc003bbr.4. human. [Q9UH03-1 ]
    uc003bbs.4. human. [Q9UH03-2 ]

    Organism-specific databases

    CTDi 55964.
    GeneCardsi GC22P042372.
    HGNCi HGNC:10750. SEPT3.
    HPAi CAB017633.
    HPA003548.
    MIMi 608314. gene.
    neXtProti NX_Q9UH03.
    PharmGKBi PA24355.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5019.
    HOVERGENi HBG065093.
    InParanoidi Q9UH03.
    KOi K16938.
    OMAi RKELTAM.
    PhylomeDBi Q9UH03.
    TreeFami TF101078.

    Miscellaneous databases

    ChiTaRSi SEPT3. human.
    GeneWikii SEPT3.
    GenomeRNAii 55964.
    NextBioi 61373.
    PROi Q9UH03.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UH03.
    Bgeei Q9UH03.
    CleanExi HS_SEPT3.
    Genevestigatori Q9UH03.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR000038. Cell_div_GTP-bd.
    IPR027417. P-loop_NTPase.
    IPR016491. Septin.
    IPR008114. Septin3.
    [Graphical view ]
    PANTHERi PTHR18884. PTHR18884. 1 hit.
    Pfami PF00735. Septin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006698. Septin. 1 hit.
    PRINTSi PR01741. SEPTIN3.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS51719. G_SEPTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human septin 3 on chromosome 22q13.2 is upregulated by neuronal differentiation."
      Methner A., Leypoldt F., Joost P., Lewerenz J.
      Biochem. Biophys. Res. Commun. 283:48-56(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), INDUCTION, TISSUE SPECIFICITY.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Amygdala.
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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).
    7. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-358 (ISOFORM 2).
      Tissue: Brain.
    8. "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.
    9. "The structure and properties of septin 3: a possible missing link in septin filament formation."
      Macedo J.N., Valadares N.F., Marques I.A., Ferreira F.M., Damalio J.C., Pereira H.M., Garratt R.C., Araujo A.P.
      Biochem. J. 450:95-105(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 60-329, GTP-BINDING SITES.

    Entry informationi

    Entry nameiSEPT3_HUMAN
    AccessioniPrimary (citable) accession number: Q9UH03
    Secondary accession number(s): B1AHR0
    , Q2NKJ7, Q59GF7, Q6IBZ6, Q8N3P3, Q9HD35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: May 15, 2007
    Last modified: October 1, 2014
    This is version 125 of the entry and version 3 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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